[go: up one dir, main page]

WO2012068236A2 - Novel fungal oxidoreductases - Google Patents

Novel fungal oxidoreductases Download PDF

Info

Publication number
WO2012068236A2
WO2012068236A2 PCT/US2011/060970 US2011060970W WO2012068236A2 WO 2012068236 A2 WO2012068236 A2 WO 2012068236A2 US 2011060970 W US2011060970 W US 2011060970W WO 2012068236 A2 WO2012068236 A2 WO 2012068236A2
Authority
WO
WIPO (PCT)
Prior art keywords
seq
acid sequence
enzyme
amino acid
activity
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Ceased
Application number
PCT/US2011/060970
Other languages
French (fr)
Other versions
WO2012068236A3 (en
Inventor
Johannes Visser
Sandra Hinz
Jan Werij
Jacob Visser
Vivi Joosten
Martijn Koetsier
Mark Emalfarb
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Dyadic International USA Inc
Original Assignee
Dyadic International USA Inc
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Dyadic International USA Inc filed Critical Dyadic International USA Inc
Publication of WO2012068236A2 publication Critical patent/WO2012068236A2/en
Publication of WO2012068236A3 publication Critical patent/WO2012068236A3/en
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/37—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from fungi
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/0004—Oxidoreductases (1.)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P19/00—Preparation of compounds containing saccharide radicals
    • C12P19/02—Monosaccharides
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P19/00—Preparation of compounds containing saccharide radicals
    • C12P19/14—Preparation of compounds containing saccharide radicals produced by the action of a carbohydrase (EC 3.2.x), e.g. by alpha-amylase, e.g. by cellulase, hemicellulase
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P7/00—Preparation of oxygen-containing organic compounds
    • C12P7/02—Preparation of oxygen-containing organic compounds containing a hydroxy group
    • C12P7/04—Preparation of oxygen-containing organic compounds containing a hydroxy group acyclic
    • C12P7/06—Ethanol, i.e. non-beverage
    • C12P7/08—Ethanol, i.e. non-beverage produced as by-product or from waste or cellulosic material substrate
    • C12P7/10—Ethanol, i.e. non-beverage produced as by-product or from waste or cellulosic material substrate substrate containing cellulosic material
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P2203/00—Fermentation products obtained from optionally pretreated or hydrolyzed cellulosic or lignocellulosic material as the carbon source
    • Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
    • Y02E—REDUCTION OF GREENHOUSE GAS [GHG] EMISSIONS, RELATED TO ENERGY GENERATION, TRANSMISSION OR DISTRIBUTION
    • Y02E50/00—Technologies for the production of fuel of non-fossil origin
    • Y02E50/10—Biofuels, e.g. bio-diesel

Definitions

  • This invention relates to novel enzymes and novel methods for producing the same.
  • Oxidoreductases represent a category of various enzymes including but not limited to oxidases, monooxygenases, Baeyer- Villiger monooxygenases, hydroxylases, peroxidases, dioxygenases, dehydrogenases, and reductases that catalyze an oxidation-reduction reaction.
  • the invention also relates to a method to aid in the conversion of plant biomass to biofuels by degrading lignin to allow enzymes used in the processing of plant biomass to more easily access the cellulose and hemicellulose and to novel combinations of enzymes, including those that provide a combined or synergistic release of sugars from plant biomass.
  • the invention also relates to methods of using the novel enzymes and compositions of such enzymes in a variety of other processes, such as bleaching pulp, cotton and flour; disinfecting food; preserving and increasing shelf life of food and beverages improving baking products; producing sugar alcohols; synthesizing amino acids, steroids, and other fine chemicals; manufacturing of products; and controlling pollution.
  • Oxidoreductases are enzymes that catalyze the transfer of electrons from one molecule (the reductant or electron donor) to another (the oxidant or electron acceptor).
  • Oxidoreductases can be oxidases or dehydrogenases.
  • Oxidases are enzymes that utilize molecular oxygen as an electron acceptor
  • dehydrogenases are enzymes that oxidize a substrate by transferring a hydride to an acceptor that is either an NAD /NADP + or a flavin-dependent enzyme.
  • Other oxidoreductases include peroxidases, oxygenases, hydroxylases, and reductases. Peroxidases catalyze the reduction of a peroxide..
  • Oxygenases catalyze the incorporation of oxygen from molecular oxygen into organic substrates.
  • Hydroxylases are a class of oxygenases that catalyze the introduction of hydroxyl groups to organic substrates.
  • Monooxygenases are a class of oxygenases that catalyze the incorporation of one atom of oxygen from molecular oxygen into organic substrates.
  • Dioxygenases are a class of oxygenases that catalyze the incorporation of both atoms of oxygen from molecular oxygen into organic substrates.
  • Baeyer-Villiger monooxygenases are a class of oxygenases that catalyze the insertion of an oxygen atom from molecular oxygen in a ketone, next to the carbonyl carbon atom.
  • Reductases catalyze reductions, in most cases reductases can act like an oxidase. Many pathways of biogenesis and bio degradation require oxidoreductase (dehydrogenase or reductase) activity, coupled to the reduction or oxidation of a donor or acceptor cofactor.
  • oxidoreductase dehydrogenase or reductase
  • Potential cofactors include cytochromes, oxygen, disulfide, iron-sulfur proteins, flavin adenine dinucleotide (FAD), and the nicotinamide adenine dinucleotides NAD and NADP (Newsholme, E. A. and Leech, A. R. (1983) Biochemistry for the Medical Sciences, John Wiley and Sons, Chichester, U. K. pp. 779-793).
  • Oxidoreductases have found a great number of uses in industry such as aiding in the production of bio fuels; bleaching pulp, cotton and flour; cleansing of food such as vegetables; improving the structure of baked goods; clarification of beer or wine; increasing shelf life of food and beverages; producing xylitol and other sugar alcohols such as sorbitol; synthesizing amino acids, steroids, and other fine chemicals; acting as biosensors; manufacturing adhesives, computer chips, and other products; controlling pollution and soil detoxification; whitening skin/hair, and teeth; various bioremediative processes and textile applications, such as denim treatment, stain removal, treatment of various fibers for textile industry, methods for decolorizing dyes and methods for treating dye house effluents, or use in hair dyeing composition, in hard-surface cleaning or in detergent formulations; and stimulating the immune system to name just a few applications.
  • Oxidoreductases such as laccases
  • have many industrially potential applications such as delignification of wood pulps, methods for treating lignin containing fibers, methods for treating wood fibers in order to functionalize them, improving of the production of fuel ethanol from renewable raw materials.
  • Plant biomass is being touted as the up-and-coming source for biofuels and chemical building blocks
  • biomass such as corn stover, switchgrass and other feedstocks
  • Lignin is a complex chemical compound that is an integral part of the secondary cell walls of many plants and some algae.
  • Lignin acts like a kind of glue holding together cellulose and hemicelluose, which are important ingredients in making ethanol or chemical building blocks
  • Oxidoreductases can act upon lignin or as reductases in the degradation of (hemi-) cellulose to allow the enzymes used in the processing of plant biomass to more easily access the cellulose and hemicellulose to create biofuels such as ethanol or chemical intermediates such as succinic acid.
  • biofuels such as ethanol or chemical intermediates such as succinic acid.
  • Pulp manufactured by the kraft process must be bleached to provide the desired whiteness of fine paper, tissue, and similar products. Traditionally, this was achieved using reactions involving chlorine and sodium hydroxide. More recently, chlorine dioxide has been increasingly substituted for chlorine. Due to environmental concerns over chloroorganic compounds present in the bleaching effluents, non-chlorine bleaching reactions are currently being introduced. These reactions include oxygen delignification followed by chelation and hydrogen peroxide oxidation, and combinations of ozone and other non-chlorine compounds. These processes are presently more costly and less selective for lignin than chlorine bleaching. Thus, there exists the need for more efficient oxidoreductase enzymes to create a more cost effective and environmentally friendly process for whitening paper and tissue products, and the novel enzymes of the present invention fulfil such a need.
  • the "stone washed" look has been used by the denim industry to produce a product that appears faded and worn. Because traditional stone washing with pumice stones reduces the strength of fabric and burdens the laundering apparatuses, the industry has turned towards an enzymatic denim finishing processes.
  • a "bleached look" of denim is normally obtained by means of bleaching chemicals, e.g. sodium hypochlorite.
  • bleaching chemicals e.g. sodium hypochlorite.
  • the hypochlorite process is environmentally very harmful, damages the fabric easily, and is possibly harmful for the user. Furthermore, it cannot be used for Lycra containing products, and antichlor treatment with several rinsing/washing steps is required.
  • oxidoreductases that are able to function at low temperatures to accommodate the newer dyes and finishes that must be washed at a lower temperature. Therefore, there exists a need for developing an ecologically less harmful alternative for sodium hypochlorite that can function at lower temperatures, in particular the oxidoreductases of the present invention, (e.g., laccases), can serve that purpose.
  • the oxidoreductases of the present invention e.g., laccases
  • Oxidoreductases are useful in the production of cheese.
  • Lactobionic acid can be used as the sole acidulent for direct acidification of cheese, or in conjunction with reduced amounts of lactic acid culture.
  • a lactose oxidase is used in one embodiment to convert lactose intrinsically present in the dairy liquid ingredient(s) into lactobionic acid. It is desirable to manufacture cheeses with reduced lactose content while preserving flavor, texture, and appearance comparable with conventional cheese products.
  • the present invention provides such enzymes to aid in the production of lactobionic acid.
  • Flavor problems caused by non-specific oxidants due to oxidation of other components of a food system can be eliminated due to the specificity of an enzyme catalyzed reaction.
  • One example of such a use includes a process in which treatment with sulfhydryl oxidase aids in the removal of a burnt flavor from Ultra- High Temperature (UHT) sterilized milk.
  • UHT Ultra- High Temperature
  • Filamentous fungi are a rich source of oxidoreductases, such as but not limited to oxidases, monooxygenases, Baeyer-Villiger monooxygenases, hydroxylases, peroxidases, dioxygenases, dehydrogenases, and reductases that catalyze an oxidation-reduction reaction. It is desirable to produce inexpensive enzymes and enzyme mixtures that efficiently aid in the conversion of (plant) biomass for use in a variety of industrial applications.
  • the present invention comprises an isolated nucleic acid sequence selected from the group consisting of:
  • nucleic acid sequence encoding an amino acid sequence that is at least about 70% identical to an amino acid sequence of (a) and has a biological activity of the protein comprising the amino acid sequence.
  • the nucleic acid sequence encodes an amino acid sequence that is at least about 90%, at least about 95%, at least about 97% or at least about 99% identical to the amino acid sequence of (a) and has a biological activity of the protein comprising the amino acid sequence.
  • the nucleic acid sequence encodes a protein comprising an amino acid sequence selected from SEQ ID NO: 2, SEQ ID No: 4, SEQ ID No: 6, SEQ ID No: 8, SEQ ID No: 10, SEQ ID No: 12, SEQ ID No: 14, SEQ ID No: 16, SEQ ID No: 18, SEQ ID No: 20, SEQ ID No: 22, SEQ ID No: 24, SEQ ID No: 26, SEQ ID No: 28, SEQ ID No: 30, SEQ ID No: 32, SEQ ID No: 34, SEQ ID No: 36, SEQ ID No: 38, SEQ ID No: 40, SEQ ID No: 42, SEQ ID No: 44, SEQ ID No: 46, SEQ ID No: 48, SEQ ID No: 50, SEQ ID No: 52, SEQ ID No: 54, SEQ ID No: 56, SEQ ID No: 58, SEQ ID No: 60, SEQ ID No: 62, SEQ ID No: 64, SEQ ID No: 66, SEQ ID No: 68,
  • the nucleic acid sequence comprises a nucleic acid sequence selected from SEQ ID No: 1, SEQ ID No: 3, SEQ ID No: 5, SEQ ID No: 7, SEQ ID No: 9, SEQ ID No: 11, SEQ ID No: 13, SEQ ID No: 15, SEQ ID No: 17, SEQ ID No: 19, SEQ ID No: 21, SEQ ID No: 23, SEQ ID No: 25, SEQ ID No: 27, SEQ ID No: 29, SEQ ID No: 31, SEQ ID No: 33, SEQ ID No: 35, SEQ ID No: 37, SEQ ID No: 39, SEQ ID No: 41, SEQ ID No: 43, SEQ ID No: 45, SEQ ID No: 47, SEQ ID No: 49, SEQ ID No: 51, SEQ ID No: 53, SEQ ID No: 55, SEQ ID No: 56, SEQ ID No: 57, SEQ ID No: 59, SEQ ID No: 61, SEQ ID No: 63, SEQ ID No: 65, SEQ ID No: 67,
  • the present invention comprises nucleic acid sequences that are fully complementary to any of the nucleic acid sequences described above.
  • the present invention comprises an isolated protein comprising an amino acid sequence encoded by any of the nucleic acid molecules described above.
  • the present invention comprises an isolated fusion protein comprising an isolated protein of the present invention fused to a protein comprising an amino acid sequence that is heterologous to the isolated protein.
  • the present invention comprises a kit for degrading a plant biomass to comprising at least one isolated protein of the present invention.
  • the present invention comprises a bleach comprising at least one isolated protein of the present invention.
  • the present invention comprises a composition for the degradation of lignin comprising at least one isolated protein of the present invention.
  • the present invention comprises a recombinant nucleic acid molecule comprising an isolated nucleic acid molecule of the present invention, operatively linked to at least one expression control sequence.
  • the recombinant nucleic acid molecule comprises an expression vector.
  • the recombinant nucleic acid molecule comprises a targeting vector.
  • the present invention comprises an isolated host cell transfected with a nucleic acid molecule of the present invention.
  • the host cell is a fungus.
  • the host cell is a filamentous fungus.
  • the filamentous fungus is from a genus selected from the group consisting of: Chrysosporium, Thielavia, Talaromyces, Neurospora, Aureobasidium, Filibasidium, Piromyces, Corynascus, Cryptococcus, Acremonium, Tolypocladium, Scytalidium, Schizophyllum, Sporotrichum, Penicillium, Gibberella, Myceliophthora, Mucor, Aspergillus, Fusarium, Humicola, and Trichoderma, and anamorphs and teleomorphs thereof.
  • the host cell is a bacterium.
  • the present invention comprises an oligonucleotide consisting essentially of at least 12 consecutive nucleotides of a nucleic acid sequence selected from SEQ ID No: 1, SEQ ID No: 3, SEQ ID No: 5, SEQ ID No: 7, SEQ ID No: 9, SEQ ID No: 11, SEQ ID No: 13, SEQ ID No: 15, SEQ ID No: 17, SEQ ID No: 19, SEQ ID No: 21, SEQ ID No: 23, SEQ ID No: 25, SEQ ID No: 27, SEQ ID No: 29, SEQ ID No: 31, SEQ ID No: 33, SEQ ID No: 35, SEQ ID No: 37, SEQ ID No: 39, SEQ ID No: 41, SEQ ID No: 43, SEQ ID No: 45, SEQ ID No: 47, SEQ ID No: 49, SEQ ID No: 51, SEQ ID No: 53, SEQ ID No: 55, SEQ ID No: 56, SEQ ID No: 57, SEQ ID No: 59, SEQ ID No:
  • the present invention comprises a kit comprising at least one oligonucleotide of the present invention.
  • the present invention comprises methods for producing a protein of the present invention, comprising culturing a cell that has been transfected with a nucleic acid molecule comprising a nucleic acid sequence encoding the protein, and expressing the protein with the transfected cell. In some embodiments, the present invention further comprises recovering the protein from the cell or from a culture comprising the cell.
  • the present invention comprises a genetically modified organism comprising components suitable for degrading lignin, wherein the organism has been genetically modified to express at least one protein of the present invention.
  • the genetically modified organism is a plant, alga, fungus or bacterium.
  • the fungus is yeast, mushroom or filamentous fungus.
  • the filamentous fungus is from a genus selected from the group consisting of: Chrysosporium, Thielavia, Neurospora, Aureobasidium, Filibasidium, Piromyces, Corynascus, Cryptococcus, Acremonium, Tolypocladium, Scytalidium, Schizophyllum, Sporotrichum, Penicillium, Talaromyces, Gibberella, Myceliophthora, Mucor, Aspergillus, Fusarium, Humicola, and Trichoderma.
  • the filamentous fungus is selected from the group consisting of: Trichoderma reesei, Trichoderma harzanium, Myceliophthora thermophila, Aspergillus niger, Aspergillus oryzae, Aspergillus japonicus, Aspergillus niger Penicillium canescens, Penicillium solitum, Penicillium funiculosum, Talaromyces emersonii, Talaromyces flavus, Talaromyces emersonii and Myceliophthora thermophila.
  • the genetically modified organism has been genetically modified to express at least one additional enzyme.
  • the additional enzyme is an enzyme selected from the group consisting of: cellulase, glucosidase, xylanase, xylosidase, ligninase, glucuronidase, arabinofuranosidase, arabinase, arabinogalactanase, esterase, lipase, pectinase, glucomannanase, amylase, laminarinase, xyloglucanase, galactanase, galactosidase, glucoamylase, pectate and pectin lyase, chitosanases, exo-P-D-glucosaminidase, and cellobiose dehydrogenase.
  • the genetically modified organism is a plant.
  • the present invention comprises a recombinant enzyme isolated from a genetically modified microorganism of the present invention.
  • the recombinant enzyme has been subjected to a purification step.
  • the present invention comprises a crude fermentation product produced by culturing the cells from the genetically modified organism of the present invention, wherein the crude fermentation product contains at least one protein of the present invention.
  • the present invention comprises a multi-enzyme composition comprising enzymes produced by a genetically modified organism of the present invention , and recovered therefrom.
  • the present invention comprises a multi-enzyme composition comprising at least one protein of the present inventions, and at least one additional protein for degrading a biomass material or a fragment thereof that has biological activity.
  • the present invention comprises a multi-enzyme composition comprising at least one protein selected from SEQ ID No: 1892, SEQ ID No: 1894, SEQ ID No: 1896, SEQ ID No: 1898, SEQ ID No: 1900, SEQ ID No: 1902, SEQ ID No: 1904, SEQ ID No: 1906, SEQ ID No: 1908, SEQ ID No: 1910, SEQ ID No: 1912, SEQ ID No: 1914, SEQ ID No: 1916, SEQ ID No: 1918, SEQ ID No: 1920, SEQ ID No: 1922, SEQ ID No: 1924, SEQ ID No: 1926, SEQ ID No: 1928, SEQ ID No: 1930, SEQ ID No: 1932, SEQ ID No: 1934, SEQ ID No: 1936, SEQ ID No: 1938, SEQ ID No: 1940, SEQ ID No: 1942, SEQ ID No: 1944, SEQ ID No: 1946, SEQ ID No: 1948, SEQ ID No: 1950, SEQ ID No:
  • the present invention comprises a multi-enzyme composition comprising at least one protein selected from SEQ ID No: 1892, SEQ ID No: 1894, SEQ ID No: 1896, SEQ ID No: 1898, SEQ ID No: 1900, SEQ ID No: 1902, SEQ ID No: 1904, SEQ ID No: 1906, SEQ ID No: 1908, SEQ ID No: 1910, SEQ ID No: 1912, SEQ ID No: 1914, SEQ ID No: 1916, SEQ ID No: 1918, SEQ ID No: 1920, SEQ ID No: 1922, SEQ ID No: 1924, SEQ ID No: 1926, SEQ ID No: 1928, SEQ ID No: 1930, SEQ ID No: 1932, SEQ ID No: 1934, SEQ ID No: 1936, SEQ ID No: 1938, SEQ ID No: 1940, SEQ ID No: 1942, SEQ ID No: 1944, SEQ ID No: 1946, SEQ ID No: 1948, SEQ ID No: 1950, SEQ ID No:
  • the present invention comprises a multi-enzyme composition
  • a multi-enzyme composition comprising at least one protein selected from SEQ ID NO: 234, SEQ ID NO: 786, SEQ ID NO: 828, SEQ ID NO: 836, SEQ ID NO: 1000, SEQ ID NO: 1774, SEQ ID NO: 1884, SEQ ID NO: 1886, SEQ ID NO: 1888 and SEQ ID NO: 1990, and at least one additional protein for degrading a biomass material or a fragment thereof that has biological activity.
  • the present invention relates generally to proteins that play a role in reduction- oxidation reactions.
  • the present invention relates to enzymes isolated from a filamentous fungal strain denoted herein as CI (Accession No. VKM F- 3500-D), nucleic acids encoding the enzymes, and methods of producing and using the enzymes.
  • the invention also provides compositions that include at least one of the enzymes described herein for uses including, but not limited to, the degradation/modification of lignin or (hemi-) cellulose.
  • the invention stems, in part, from the discovery of a variety of novel oxidoreductases produced by the CI fungus that exhibit high activity toward plant biomass.
  • the present invention also provides methods and compositions for aiding in the conversion of plant biomass to fermentable sugars that can, in turn, be converted to useful products.
  • Such products may include, without limitation, metabolites, and bio fuels.
  • the methods include methods for degrading lignin and lignocellulosic material using enzyme mixtures to liberate sugars.
  • the compositions of the invention include enzyme combinations that break down lignin and ligno cellulose.
  • lignin or "lignen” refers to complex polymers, the chief noncarbohydrate constituent of wood, that binds to cellulose fibers and hardens and strengthens the cell walls of plants. Lignin is an integral part of the secondary cell walls of many plants and some algae. Lignin acts to hold together cellulose and hemicelluose, which are important ingredients in making ethanol.
  • biomass or "lignocellulosic material” includes materials containing cellulose and/or hemicellulose. Generally, these materials also contain pectin, lignin, protein, carbohydrates (such as starch and sugar) and ash. Ligno cellulose is generally found, for example, in the stems, leaves, hulls, husks, and cobs of plants or leaves, branches, and wood of trees.
  • Fermentable sugars refers to simple sugars, such as glucose, xylose, arabinose, galactose, mannose, rhamnose, sucrose and fructose.
  • Biomass can include virgin biomass and/or non-virgin biomass such as agricultural biomass, commercial organics, construction and demolition debris, municipal solid waste, waste paper and yard waste.
  • biomass include trees, shrubs and grasses, wheat, wheat straw, sugar cane bagasse, sugar beet, soybean, corn, corn husks, corn kernel including fiber from kernels, products and byproducts from milling of grains such as corn, tobacco, wheat and barley (including wet milling and dry milling) as well as municipal solid waste, waste paper and yard waste.
  • the biomass can also be, but is not limited to, herbaceous material, agricultural residues, forestry residues, municipal solid wastes, waste paper, and pulp and paper mill residues.
  • Agricultural biomass includes branches, bushes, canes, corn and corn husks, energy crops, algae, fruits, flowers, grains, grasses, herbaceous crops, leaves, bark, needles, logs, roots, saplings, short rotation woody crops, shrubs, switch grasses, trees, vegetables, fruit peels, vines, sugar beet pulp, wheat midlings, oat hulls, peat moss, mushroom compost and hard and soft woods (not including woods with deleterious materials).
  • agricultural biomass includes organic waste materials generated from agricultural processes including farming and forestry activities, specifically including forestry wood waste. Agricultural biomass may be any of the aforestated singularly or in any combination or mixture thereof.
  • Energy crops are fast-growing crops that are grown for the specific purpose of producing energy, including without limitation, biofuels, from all or part of the plant.
  • Energy crops can include crops that are grown (or are designed to grow) for their increased cellulose, xylose and sugar contents. Examples of such plants include, without limitation, switchgrass, willow and poplar.
  • Energy crops may also include algae, for example, designer algae that are genetically engineered for enhanced production of hydrogen, alcohols, and oils, which can be further processed into diesel and jet fuels, as well as other bio-based products.
  • biomass high in starch, sugar, or protein such as corn, grains, fruits and vegetables are usually consumed as food.
  • biomass high in cellulose, hemicellulose and lignin are not readily digestible and are primarily utilized for wood and paper products, animal feed, fuel, or are typically disposed.
  • the substrate is of high ligno cellulose content, including distillers' dried grains corn stover, corn cobs, rice straw, wheat straw, hay, sugarcane bagasse, sugar cane pulp, citrus peels and other agricultural biomass, switchgrass, forestry wastes, poplar wood chips, pine wood chips, sawdust, yard waste, and the like, including any combination thereof.
  • the present invention includes enzymes or compositions thereof with, for example, oxidoreductases, cellobiohydrolase, endoglucanase, xylanase, ⁇ -glucosidase, and hemicellulase activities.
  • Fermentable sugars can be converted to useful value-added fermentation products, non-limiting examples of which include amino acids, vitamins, pharmaceuticals, animal feed supplements, specialty chemicals, chemical feedstocks, plastics, solvents, fuels, or other organic polymers, lactic acid, and ethanol, including fuel ethanol.
  • Specific value-added products that may be produced by the methods of the invention include, but not limited to, biofuels (including ethanol and butanol); lactic acid; plastics; specialty chemicals; organic acids, including citric acid, succinic acid and maleic acid; solvents; animal feed supplements; pharmaceuticals; vitamins; amino acids, such as lysine, methionine, tryptophan, threonine, and aspartic acid; industrial enzymes, such as proteases, cellulases, amylases, glucanases, xylanases, arabinanases, lactases, lipases, esterases, lyases, oxidoreductases, transferases ; and chemical feedstocks.
  • the enzymes of the present invention may be used alone, or in combination with other enzymes, chemicals or biological materials.
  • the enzymes of the present invention may be used for in vitro applications in which the enzymes or mixtures thereof are added to or mixed with the appropriate substrates to catalyze the desired reactions. Additionally, the enzymes of the present invention may be used for in vivo applications in which nucleic acid molecules encoding the enzymes are introduced into cells and are expressed therein to produce the enzymes and catalyze the desired reactions within the cells.
  • enzymes capable of promoting cell wall degradation may be added to algal cells suspended in solutions to degrade the algal cell walls and release their content, whereas in some embodiments, nucleic acid molecules encoding such enzymes may be introduced into the algal cells to express the enzymes therein, so that these enzymes can degrade the algal cell walls from within.
  • Some embodiments may combine the in vitro applications with the in vivo applications. In some embodiments, the enzymes used for in vitro applications may be different from the enzymes used for in vivo applications.
  • the present invention includes proteins isolated from, or derived from the knowledge of enzymes from, a fungus such as Myceliophthora thermophila or a mutant or other derivative thereof, and more particularly, from the fungal strain denoted herein as CI (Accession No. VKM F-3500-D).
  • M. thermophila has previously appeared in patent applications and in the literature as Myceliophthora thermophila or Sporotrichum thermophile.
  • the proteins of the invention possess enzymatic activity.
  • U.S. Patent No. 6,015,707 or U.S. Patent No. 6,573,086 a strain called CI (Accession No.
  • VKM F-3500-D was isolated from samples of forest alkaline soil from Sola Lake, Far East of the Russian Federation. This strain was deposited at the All-Russian Collection of Microorganisms of Russian Academy of Sciences (VKM), Bakhurhina St. 8, Moscow, Russia, 113184, under the terms of the Budapest Treaty on the International Regulation of the Deposit of Microorganisms for the Purposes of Patent Procedure on August 29, 1996, as Myceliophthora thermophila Garg 27K, VKM-F 3500 D. Various mutant strains of M. thermophila (C. lucknowense) CI have been produced and these strains have also been deposited at the All-Russian Collection of Microorganisms of Russian Academy of Sciences (VKM), Bakhurhina St.
  • Strain CI was mutagenised by subjecting it to ultraviolet light to generate strain UV13-6 (Accession No. VKM F-3632 D). This strain was subsequently further mutated with N-methyl-N- nitro-N-nitrosoguanidine to generate strain NG7C-19 (Accession No. VKM F-3633 D).
  • strain UV18-25 (Accession No. VKM F-3631 D).
  • strain W1L (Accession No. CBS 122189), which was subsequently subjected to mutation by ultraviolet light, resulting in strain W1L#100L (Accession No. CBS122190).
  • Strain CI was initially classified as a Myceliophthora thermophila based on morphological and growth characteristics of the microorganism, as discussed in detail in U.S. Patent No. 6,015,707, U.S. Patent No. 6,573,086 and patent PCT/NL2010/000045. The CI strain was subsequently reclassified as M. thermophila based on genetic tests.
  • a protein of the invention comprises, consists essentially of, or consists of an amino acid sequence selected from SEQ ID NO: 2, SEQ ID No: 4, SEQ ID No: 6, SEQ ID No: 8, SEQ ID No: 10, SEQ ID No: 12, SEQ ID No: 14, SEQ ID No: 16, SEQ ID No: 18, SEQ ID No: 20, SEQ ID No: 22, SEQ ID No: 24, SEQ ID No: 26, SEQ ID No: 28, SEQ ID No: 30, SEQ ID No: 32, SEQ ID No: 34, SEQ ID No: 36, SEQ ID No: 38, SEQ ID No: 40, SEQ ID No: 42, SEQ ID No: 44, SEQ ID No: 46, SEQ ID No: 48, SEQ ID No: 50, SEQ ID No: 52, SEQ ID No: 54, SEQ ID No: 56, SEQ ID No: 58, SEQ ID No: 60, SEQ ID No: 62, SEQ ID No: 64, SEQ ID No: 66, SEQ ID
  • the present invention also includes homologues or variants of any of the above sequences, including fragments and sequences having a given identity to any of the above sequences, wherein the homologue, variant, or fragment has at least one biological activity of the wild-type protein, as described herein.
  • oxidoreductase refers to an enzyme that catalyzes the transfer of electrons from one molecule (the reductant, also called the hydride or electron donor) to another (the oxidant, also called the idem or electron acceptor).
  • reductant also called the hydride or electron donor
  • oxidant also called the idem or electron acceptor
  • Oxidase refers to any enzyme that catalyzes an oxidation-reduction reaction involving molecular oxygen (O 2 ) as the electron acceptor.
  • oxidoreductases are oxidoreductases that induce the incorporation of one atom of oxygen from 0 2 into the substance being oxidized.
  • Baeyer-Villiger Monooxygenases are oxidoreductases that induce the incorporation of one atom of oxygen from O 2 next to the carbonyl goup of the ketone substance being oxidized.
  • Peroxidases are enzymes that typically catalyze a reaction of the form: ROOR' + electron donor (2 e " ) + 2H + ⁇ ROH + R'OH.
  • Hydroxylases are oxidoreductases that induce the introduction of a hydroxyl group in the substance being oxidized.
  • Dioxygenases are enzymes that incorporate both atoms of O 2 into one substrate.
  • Dehydrogenases refer to enzymes that catalyze the removal of hydrogen from organic compounds.
  • Reductases refers to any enzyme that catalyzes the reduction of a substrate.
  • Cytochrome-c oxidase is an enzyme that receives an electron from each of four cytochrome c molecules, and transfers them to one oxygen molecule, converting molecular oxygen to two molecules of water.
  • Xanthine oxidoreductase is an enzyme that generates reactive oxygen species.
  • Xanthine oxidase is an enzyme that catalyzes the oxidation of hypoxanthine to xanthine and can further catalyze the oxidation of xanthine to uric acid.
  • Redwood dehydrogenase refers to a protein that oxidizes cellobiose to cellobiono lactone .
  • Sulfhydryl oxidases or SOX are enzymes known to catalyze the conversion of thio compounds to the corresponding disulfides. Sulfhydryl oxidases are therefore of interest in applications where oxidation of free sulfhydryl groups to disulfide linkages is sought.
  • oxidases are those catalyzing the oxidation of sugars such as glucose oxidase, galactose oxidase and hexose oxidase .
  • Laccases belong to a family of multi-copper oxidases. Laccases are characterized by low substrate specificity, oxidizing various substrate, including diphenols, polyphenols, different substituted phenols, diamines, aromatic amines, and even inorganic compounds like iodine. Laccases oxidize their substrates by a one- electron oxidation mechanism, and they use molecular oxygen as an electron acceptor. Among laccases the primary sequence, induction mechanism, physico- chemical (e.g. isoelectric point and carbohydrate content) and biochemical characteristics are variable. The copper binding sites of laccases are, however, strictly conserved.
  • proteins disclosed herein possess oxidoreductase activity.
  • the proteins of the present invention can be combined with various enzymes as discussed below to aid in the production of bio fuels.
  • carbohydrase refers to any protein that catalyzes the hydrolysis of carbohydrates.
  • glycoside hydrolase refers to a protein that catalyzes the hydrolysis of the glycosidic bonds between carbohydrates or between a carbohydrate and a non-carbohydrate residue.
  • Endoglucanases cellobiohydrolases, ⁇ -glucosidases, a-glucosidases, xylanases, ⁇ - xylosidases, alpha- xylosidases, galactanases, a-galactosidases, ⁇ -galactosidases, a- amylases, glucoamylases, endo-arabinases, arabinofuranosidases, mannanases, ⁇ - mannosidases, pectinases, acetyl xylan esterases, acetyl mannan esterases, ferulic acid esterases, coumaric acid esterases, pectin methyl esterases, and chitosanases are examples of glycosidases.
  • Cellulose is a linear beta-(l-4) glucan consisting of anhydrocellobiose units.
  • Cellulases include endoglucanases, cellobiohydrolases, and ⁇ -glucosidases.
  • Cellulase refers to a protein that catalyzes the hydrolysis of l,4 ⁇ -D-glycosidic linkages in cellulose; cellulose derivatives (such as carboxymethylcellulose and hydroxyethylcellulose); plant lignocellulosic materials, beta-D-glucans or xyloglucans.
  • Endoglucanase refers to a protein that catalyzes the hydrolysis of cellulose to oligosaccharide chains at random locations by means of an endoglucanase activity.
  • Cellobiohydrolase refers to a protein that catalyzes the hydrolysis of cellulose to cellobiose via an exoglucanase activity, sequentially releasing molecules of cellobiose from the reducing or non-reducing ends of cellulose or cello - oligosaccharides.
  • ⁇ -glucosidase refers to an enzyme that catalyzes the conversion of cellobiose and oligosaccharides to glucose.
  • Hemicellulase refers to a protein that catalyzes the hydrolysis of hemicellulose, such as that found in lignocellulosic materials. Hemicelluloses are complex polymers, and their composition often varies widely from organism to organism, and from one tissue type to another. Hemicelluloses include a variety of compounds, such as xylans, arabinoxylans, xyloglucans, mannans, glucomannans, pectins, polygalacturonan, rhamnogalacturonan, xylogalacturonan and galacto(gluco)mannans. Hemicellulose can also contain glucan, which is a general term for beta-linked glucose residues.
  • a main component of hemicellulose is beta-l,4-linked xylose, a five carbon sugar.
  • this xylose is often branched as beta- 1,3 linkages or beta- 1,2 linkages, and can be substituted with linkages to arabinose, galactose, mannose, glucuronic acid, or by esterification to acetic acid.
  • hemicellulose is very different in dicotyledonous plants (dicots, i.e., plant whose seeds have two cotyledons or seed leaves such as lima beans, peanuts, almonds, peas, kidney beans) as compared to monocotyledonous plants (monocots; i.e., plants having a single cotyledon or seed leaf such as corn, wheat, rice, grasses, barley).
  • dicots i.e., plants having a single cotyledon or seed leaf such as corn, wheat, rice, grasses, barley.
  • hemicellulose is comprised mainly of xyloglucans that are 1,4- beta-linked glucose chains with 1,6-alpha-linked xylosyl side chains.
  • hetero xylans In monocots, including most grain crops, the principal components of hemicellulose are hetero xylans. These are primarily comprised of 1 ,4-beta- linked xylose backbone polymers with 1,2- or 1,3-alpha linkages to arabinose, linkage of galactose and mannose to arabinose or xylose in side chains, as well as xylose modified by ester- linked acetic acids. Also present are branched beta glucans comprised of 1,3- and 1 ,4-beta- linked glucosyl chains. In monocots, cellulose, hetero xylans and beta glucans are present in roughly equal amounts, each comprising about 15-25% of the dry matter of cell walls.
  • Hemicellulo lytic enzymes include both endo-acting and exo-acting enzymes, such as xylanases, ⁇ -xylosidases. alpha- xylosidases, galactanases, a-galactosidases, ⁇ -galactosidases, endo-arabinases, arabinofuranosidases, mannanases, ⁇ -mannosidases. Hemicellulases also include the accessory enzymes, such as acetylesterases, ferulic acid esterases, and coumaric acid esterases.
  • xylanases and acetyl xylan esterases cleave the xylan and acetyl side chains of xylan and the remaining xylo -oligomers are unsubstituted and can thus be hydro lysed with ⁇ -xylosidase only.
  • xylanases, acetylesterases and ⁇ -xylosidases are examples of hemicellulases.
  • Xylanase specifically refers to an enzyme that hydro lyzes the ⁇ -1,4 bond in the xylan backbone, producing short xylooligosaccharides.
  • ⁇ -Mannanase or "endo-l,4 ⁇ -mannosidase” refers to a protein that hydro lyzes mannan-based hemicelluloses (mannan, glucomannan, galacto(gluco)mannan) and produces short ⁇ -l,4-mannooligosaccharides.
  • Mannan endo-l,6-a-mannosidase refers to a protein that hydro lyzes 1,6-a- mannosidic linkages in unbranched 1,6-mannans.
  • ⁇ -Mannosidase ( ⁇ -l,4-mannoside mannohydrolase; EC 3.2.1.25) refers to a protein that catalyzes the removal of ⁇ -D-mannose residues from the nonreducing ends of oligosaccharides.
  • Galactanase refers to a protein that catalyzes the hydrolysis of ⁇ -1,4- ⁇ - ⁇ - galactosidic linkages in arabinogalactans.
  • Gluco amylase refers to a protein that catalyzes the hydrolysis of terminal 1,4- linked a-D-glucose residues successively from non-reducing ends of the glycosyl chains in starch with the release of ⁇ -D-glucose.
  • ⁇ -hexosaminidase or " ⁇ - ⁇ -acetylglucosaminidase” refers to a protein that catalyzes the hydrolysis of terminal N-acetyl-D-hexosamine residues in N-acetyl- ⁇ -
  • a-L-arabinofuranosidase refers to a protein that hydro lyzes arabinofuranosyl-containing hemicelluloses. Some of these enzymes remove arabino fur ano side residues from 0-2 or 0-3 single substituted xylose residues, as well as from 0-2 and/or 0-3 double substituted xylose residues.
  • Endo-arabinase refers to a protein that catalyzes the hydrolysis of 1,5-a- arabinofuranosidic linkages in 1,5-arabinans.
  • Exo-arabinase refers to a protein that catalyzes the hydrolysis of 1,5-a-linkages in 1,5-arabinans or 1,5-a-L arabino-oligosaccharides, releasing mainly arabinobiose, although a small amount of arabinotriose can also be liberated.
  • ⁇ -xylosidase refers to a protein that hydro lyzes short l,4-P-D-xylooligomers into xylose.
  • Cellobiose dehydrogenase refers to a protein that oxidizes cellobiose to cellobiono lactone .
  • Chitosanase refers to a protein that catalyzes the endohydro lysis of P-l,4-linkages between D-glucosamine residues in acetylated chitosan (i.e., deacetylated chitin).
  • Exo -polygalacturonase refers to a protein that catalyzes the hydrolysis of terminal alpha 1 ,4-linked galacturonic acid residues from non-reducing ends thus converting polygalacturonides to galacturonic acid.
  • Alcohol xylan esterase refers to a protein that catalyzes the removal of the acetyl groups from xylose residues.
  • Alcohol mannan esterase refers to a protein that catalyzes the removal of the acetyl groups from mannose residues
  • ferulic esterase or "ferulic acid esterase” refers to a protein that hydro lyzes the ester bond between the arabinose substituent group and ferulic acid.
  • Coumaric acid esterase refers to a protein that hydro lyzes the ester bond between the arabinose substituent group and coumaric acid.
  • Acetyl xylan esterases, ferulic acid esterases and pectin methyl esterases are examples of carbohydrate esterases.
  • Pectate lyase and pectin lyases refer to proteins that catalyze the cleavage of 1 ,4-a-D-galacturonan by beta-elimination acting on polymeric and/or oligosaccharide substrates (pectates and pectins, respectively).
  • Endo-l,3- -glucanase or “laminarinase” refers to a protein that catalyzes the cleavage of 1,3-linkages in ⁇ -D-glucans such as laminarin or lichenin.
  • Laminarin is a linear polysaccharide made up of ⁇ -1 -glucan with -l,6-linkages.
  • lichenan refers to a protein that catalyzes the hydrolysis of lichenan, a linear, 1,3-1,4- ⁇ - ⁇ glucan.
  • Rhamnogalacturonan is composed of alternating a-l,4-rhamnose and a-l,2-linked galacturonic acid, with side chains linked 1,4 to rhamnose.
  • the side chains include Type I galactan, which is -l,4-linked galactose with a-l,3-linked arabinose substituents; Type II galactan, which is -l,3-l,6-linked galactoses (very branched) with arabinose substituents; and arabinan, which is a-l,5-linked arabinose with a- 1,3-linked arabinose branches.
  • the galacturonic acid substituents may be acetylated and/or methylated.
  • "Exo-rhamnogalacturonanase” refers to a protein that catalyzes the degradation of the rhamnogalacturonan backbone of pectin from the nonreducing end.
  • Rhamnogalacturonan acetylesterase refers to a protein that catalyzes the removal of the acetyl groups ester-linked to the highly branched rhamnogalacturonan (hairy) regions of pectin.
  • Rhamnogalacturonan lyase refers to a protein that catalyzes the degradation of the rhamnogalacturonan backbone of pectin via a ⁇ -elimination mechanism (see, e.g., Pages et al, J. Bacteriol. 185:4727-4733 (2003)).
  • Alpha-rhamnosidase refers to a protein that catalyzes the hydrolysis of terminal non-reducing a-L-rhamnose residues in a-L-rhamno sides.
  • Glycosidases glycoside hydrolases; GH
  • GH glycoside hydrolases
  • Glycosidases such as the proteins of the present invention may be assigned to families on the basis of sequence similarities, and there are now over 100 different such families defined (see the CAZy (Carbohydrate Active EnZymes database) website, maintained by the Architecture of Fonction de Macromolecules Bi Anlagens of the Centre National de la Recherche Scientifique, which describes the families of structurally-related catalytic and carbohydrate- binding modules (or functional domains) of enzymes that degrade, modify, or create glycosidic bonds; Coutinho, P.M. & Henrissat, B. (1999) Carbohydrate-active enzymes: an integrated database approach. In “Recent Advances in Carbohydrate Bioengineering", H.J. Gilbert, G. Davies, B.
  • sequence homology may be used to identify particular domains within proteins, such as carbohydrate binding modules (CBMs; also known as carbohydrate binding domains (CBDs), sometimes called cellulose binding domains).
  • CBMs carbohydrate binding modules
  • CBDs carbohydrate binding domains
  • the CAZy homologies of proteins of the present invention are disclosed below.
  • An enzyme assigned to a particular CAZy family may exhibit one or more of the enzymatic activities or substrate specificities associated with the CAZy family. In other embodiments, the enzymes of the present invention may exhibit one or more of the enzyme activities discussed above.
  • Certain proteins used in the multi-enzyme compositions of the present invention may be classified as "Family 61 glycosidases" based on homology of the polypeptides to CAZy Family GH61.
  • Family 61 glycosidases may exhibit oxidative activity towards biopolymers including, but not limited to, cellulose, hemicellulose, chitin, chitosan, amylose, amylopectin, pectin and lignin.
  • the oxidative activity towards the biopolymers may results in an enhancing effect on the degradation of the corresponding biopolymer.
  • Polynuceo tides encoding "Family 61 glycosidases” and polypetides thereof are provided as SEQ ID NO: 1892 through SEQ ID NO: 1944. Additional information on the properties of Family 61 glycosidases may be found in U.S. Patent Application Publication Nos. 2005/0191736, 2006/0005279, 2007/0077630, and in PCT Publication No. WO 2004/031378.
  • Cellulo lytic enhancing activity refers to a biological activity that enhances the hydrolysis of a cellulo sic material by proteins having cellulo lytic activity. This enhancing activity is expected to be related by the cellulose oxidizing activity of the GH61 enzyme.
  • Hemicellulo lytic enhancing activity refers to a biological activity that enhances the hydrolysis of a hemicellulo sic material by proteins having hemicellulo lytic activity. This enhancing activity is expected to be related by the hemicellulose oxidizing activity of the GH61 enzyme.
  • hemicellulo stic materials include, but are not limited to, xylan, glucuronoxylan, arabinoxylan, glucomannan, and xyloglucan
  • Chitino lytic enhancing activity refers to a biological activity that enhances the hydrolysis of a chitinoic material by proteins having chitinase activity. This enhancing activity is expected to be related by the chitin oxidizing activity of the GH61 enzyme.
  • Amylo lytic enhancing activity refers to a biological activity that enhances the hydrolysis of a amylosic material by proteins having amylase activity. This enhancing activity is expected to be related by the amylose oxidizing activity of the GH61 enzyme.
  • Amylopectino lytic enhancing activity refers to a biological activity that enhances the hydrolysis of a amylopectinoic materials by proteins having amylopectinase activity. This enhancing activity is expected to be related by the amylopectin oxidizing activity of the GH61 enzyme.
  • Pectino lytic enhancing activity refers to a biological activity that enhances the hydrolysis of a pectinoic materials by proteins having pectinase activity. This enhancing activity is expected to be related by the pectin oxidizing activity of the GH61 enzyme.
  • “Lignino lytic enhancing activity” refers to a biological activity that enhances the hydrolysis of a ligno lytic materials by proteins having ligninase activity. This enhancing activity is expected to be related by the lignin oxidizing activity of the GH61 enzyme.
  • Cellobiose dehydrogenases and “cellobiose oxidases” are oxidoreductases that oxidize cellobiose to cellobiono-l,5-lactone and can utilize electron acceptors including, but not limited to, molecular oxygen, CDH-like reductases, GH61 enzymes, cytochrome c and Felll
  • CDH-like reductases are oxidoreductases that can be reduced by an oxidoreductase such as, but not limited to, Cellobiose dehydrogenase, and that can be oxidized by "CDH-like reductases” and GH61 enzymes.
  • the polynucelo tides encoding the CDH-like reductases and the polypeptides thereoff are provided as sequences SEQ ID NO: 234, SEQ ID NO: 1000, SEQ ID NO: 1774, SEQ ID NO: 1884, SEQ ID NO: 1886, SEQ ID NO: 1888 and SEQ ID NO: 1890.
  • This enhancing activity observed for the GH61 enzymes is expected to be related to the reduction of the GH61 enzyme by oxidoreductases such as, but not limited to, cellobiose dehydrogenases and CDH-like reductases.
  • Reduced GH61 in combination hydrogen peroxide can oxidize biopolymers.
  • the oxidation of biopolymers by the GH61 enzyme enhances the degradation of the biopolymer.
  • Proteins used in the multi-enzyme compositions of the present invention may also include homologues, variants, and fragments of the proteins disclosed herein.
  • the protein fragments include, but are not limited to, fragments comprising a catalytic domain (CD) and/or a carbohydrate binding module (CBM) (also known as a cellulose-binding domain; both can be referred to herein as CBM).
  • CD catalytic domain
  • CBM carbohydrate binding module
  • the identity and location of domains within proteins of the present invention are disclosed in detail below.
  • the present invention encompasses all combinations of the disclosed domains.
  • a protein fragment may comprise a CD of a protein but not a CBM of the protein or a CBM of a protein but not a CD.
  • domains from different proteins may be combined. Protein fragments comprising a CD, CBM or combinations thereof for each protein disclosed herein can be readily produced using standard techniques known in the art.
  • a protein fragment comprises a domain of a protein that has at least one biological activity of the full-length protein. Homologues or variants of proteins of the invention that have at least one biological activity of the full-length protein are described in detail below.
  • a protein fragment comprises a domain of a protein that has the catalytic activity of the full-length enzyme.
  • Oxidoreductases represent a category of various enzymes including but not limited to oxidases, oxygenases, monoxygenases, Baeyer-Villiger monooxygenases, dioxygenases, peroxidases, dehydrogenases, reductases that catalyze an oxidation- reduction reaction.
  • Sequence Oxid-1 scaffold00008.G4 is encoded by the nucleotides of SEQ ID No: 1 which encodes the amino acid sequence of SEQ ID NO: 2. This enzyme is believed to have cytochrome-c oxidase activity.
  • Sequence Oxid-2 scaflbld00016.G278 is encoded by the nucleotides of SEQ ID No: 3 which encodes the amino acid sequence of SEQ ID No: 4. This enzyme is believed to have cytochrome-c oxidase activity.
  • Sequence Oxid-3 scaffold00016.G284 is encoded by the nucleotides of SEQ ID No: 5 which encodes the amino acid sequence of SEQ ID No: 6. This enzyme is believed to have ent-kaurene oxidase activity.
  • Sequence Oxid-4 scaffold00016.G642 is encoded by the nucleotides of SEQ ID No: 7 which encodes the amino acid sequence of SEQ ID No: 8. This enzyme is believed to have cytochrome-c oxidase activity.
  • Sequence Oxid-5 scaffold00016.G1015 is encoded by the nucleotides of SEQ ID No: 9 which encodes the amino acid sequence of SEQ ID No: 10. This enzyme is believed to have coproporphyrinogen oxidase activity.
  • Sequence Oxid-6 scaffold00016.Gl 147 is encoded by the nucleotides of SEQ ID No: 11 which encodes the amino acid sequence of SEQ ID No: 12. This enzyme is believed to have xanthine oxidase activity.
  • Sequence Oxid-7 scaffold00031.G10 is encoded by the nucleotides of SEQ ID No: 13 which encodes the amino acid sequence of SEQ ID No: 14. This enzyme is believed to have catalase activity.
  • Sequence Oxid-8 scaffold00031.G81 is encoded by the nucleotides of SEQ ID No: 15 which encodes the amino acid sequence of SEQ ID No: 16. This enzyme is believed to have glutathione peroxidase activity.
  • Sequence Oxid-9 scaffold00031.G109 is encoded by the nucleotides of SEQ ID No: 17 which encodes the amino acid sequence of SEQ ID No: 18. This enzyme is believed to have cytochrome-c oxidase activity.
  • Sequence Oxid-10 scaffold00031.G306 is encoded by the nucleotides of SEQ ID No: 19 which encodes the amino acid sequence of SEQ ID No: 20. This enzyme is believed to have urate oxidase activity.
  • Sequence Oxid-11 scaffold00031.G894 is encoded by the nucleotides of SEQ ID No: 21 which encodes the amino acid sequence of SEQ ID No: 22. This enzyme is believed to have glutathione peroxidase activity.
  • Sequence Oxid-12 scaffold00031.G1329 is encoded by the nucleotides of SEQ ID No: 23 which encodes the amino acid sequence of SEQ ID No: 24. This enzyme is believed to have D-amino-acid oxidase activity.
  • Sequence Oxid-13 scaflbld00031.G1386 is encoded by the nucleotides of SEQ ID No: 25 which encodes the amino acid sequence of SEQ ID No: 26. This enzyme is believed to have dihydroorotate oxidase activity.
  • Sequence Oxid-14 scaffold00050.G316 is encoded by the nucleotides of SEQ ID No: 27 which encodes the amino acid sequence of SEQ ID No: 28. This enzyme is believed to have linoleate diol synthase activity.
  • Sequence Oxid-15 scaffold00050.G973 is encoded by the nucleotides of SEQ ID No: 29 which encodes the amino acid sequence of SEQ ID No: 30. This enzyme is believed to have cytochrome-c oxidase activity.
  • Sequence Oxid-16 scaffold00050.G992 is encoded by the nucleotides of SEQ ID No: 31 which encodes the amino acid sequence of SEQ ID No: 32. This enzyme is believed to have amine oxidase activity.
  • Sequence Oxid-17 scaffold00050.Gl 115 is encoded by the nucleotides of SEQ ID No: 33 which encodes the amino acid sequence of SEQ ID No: 34. This enzyme is believed to have thiol oxidase activity.
  • Sequence Oxid-18 scaffold00050.Gl 138 is encoded by the nucleotides of SEQ ID No: 35 which encodes the amino acid sequence of SEQ ID No: 36. This enzyme is believed to have thioredoxin peroxidase activity.
  • the enzyme identified as Sequence Oxid-19 scaffold00050.Gl 145 is encoded by the nucleotides of SEQ ID No: 37 which encodes the amino acid sequence of SEQ ID No: 38. This enzyme is believed to have glucose oxidase - alcohol oxidase activity.
  • Sequence Oxid-20 scaffold00050.G1403 is encoded by the nucleotides of SEQ ID No: 39 which encodes the amino acid sequence of SEQ ID No: 40. This enzyme is believed to have Peroxidase activity.
  • Sequence Oxid-21 scaffold00050.G1668 is encoded by the nucleotides of SEQ ID No: 41 which encodes the amino acid sequence of SEQ ID No: 42. This enzyme is believed to have ent-kaurene oxidase activity.
  • Sequence Oxid-22 scaffold00071.G641 is encoded by the nucleotides of SEQ ID No: 43 which encodes the amino acid sequence of SEQ ID No: 44. This enzyme is believed to have oxygen-dependent protoporphyrinogen oxidase activity.
  • Sequence Oxid-23 scaffold00071.G707 is encoded by the nucleotides of SEQ ID No: 45 which encodes the amino acid sequence of SEQ ID No: 46. This enzyme is believed to have cytochrome-c peroxidase activity.
  • Sequence Oxid-24 scaffold00071.G1701 is encoded by the nucleotides of SEQ ID No: 47 which encodes the amino acid sequence of SEQ ID No: 48. This enzyme is believed to have D-amino-acid oxidase activity.
  • Sequence Oxid-25 scaffold00071.G2756 is encoded by the nucleotides of SEQ ID No: 49 which encodes the amino acid sequence of SEQ ID No: 50. This enzyme is believed to have peroxiredoxin activity.
  • Sequence Oxid-26 scaffold00071.G2771 is encoded by the nucleotides of SEQ ID No: 51 which encodes the amino acid sequence of SEQ ID No: 52. This enzyme is believed to have D-arabinono-l,4-lactone oxidase activity.
  • Sequence Oxid-27 scaffold00071.G2849 is encoded by the nucleotides of SEQ ID No: 53 which encodes the amino acid sequence of SEQ ID No: 54. This enzyme is believed to have D-arabinono-l,4-lactone oxidase activity.
  • Sequence Oxid-28 scaffold00071.G3230 is encoded by the nucleotides of SEQ ID No: 55 which encodes the amino acid sequence of SEQ ID No: 56. This enzyme is believed to have cytochrome-c oxidase activity.
  • Sequence Oxid-29 scaffold00071.G3441 is encoded by the nucleotides of SEQ ID No: 56 which encodes the amino acid sequence of SEQ ID No: 58. This enzyme is believed to have alcohol oxidase activity.
  • Sequence Oxid-30 scaffold00071.G3442 is encoded by the nucleotides of SEQ ID No: 57 which encodes the amino acid sequence of SEQ ID No: 60. This enzyme is believed to have alcohol oxidase activity.
  • Sequence Oxid-31 scaffold00071.G3476 is encoded by the nucleotides of SEQ ID No: 59 which encodes the amino acid sequence of SEQ ID No: 62. This enzyme is believed to have amine oxidase activity.
  • Sequence Oxid-32 scaffold00075.G779 is encoded by the nucleotides of SEQ ID No: 61 which encodes the amino acid sequence of SEQ ID No: 64. This enzyme is believed to have C-4 methylsterol oxidase activity.
  • Sequence Oxid-33 scaffold00092.G21 is encoded by the nucleotides of SEQ ID No: 63 which encodes the amino acid sequence of SEQ ID No: 66. This enzyme is believed to have glucose oxidase activity.
  • Sequence Oxid-34 scaffold00122.G43 is encoded by the nucleotides of SEQ ID No: 65 which encodes the amino acid sequence of SEQ ID No: 68. This enzyme is believed to have catalase activity.
  • Sequence Oxid-35 scaffold00122.G57 is encoded by the nucleotides of SEQ ID No: 67 which encodes the amino acid sequence of SEQ ID No: 70. This enzyme is believed to have glucose oxidase - alcohol oxidase activity.
  • Sequence Oxid-36 scaffold00131.G269 is encoded by the nucleotides of SEQ ID No: 69 which encodes the amino acid sequence of SEQ ID No: 72. This enzyme is believed to have dihydroorotate oxidase activity.
  • Sequence Oxid-37 scaffold00131.G1286 is encoded by the nucleotides of SEQ ID No: 71 which encodes the amino acid sequence of SEQ ID No: 74. This enzyme is believed to have cytochrome-c oxidase activity.
  • Sequence Oxid-38 scaffold00131.G1420 is encoded by the nucleotides of SEQ ID No: 73 which encodes the amino acid sequence of SEQ ID No: 76. This enzyme is believed to have phospholipid-hydroperoxide glutathione peroxidase activity.
  • Sequence Oxid-39 scaffold00137.G197 is encoded by the nucleotides of SEQ ID No: 75 which encodes the amino acid sequence of SEQ ID No: 78. This enzyme is believed to have alcohol oxidase activity.
  • Sequence Oxid-40 scaffold00142.G451 is encoded by the nucleotides of SEQ ID No: 77 which encodes the amino acid sequence of SEQ ID No: 80. This enzyme is believed to have cytochrome-c oxidase activity.
  • Sequence Oxid-41 scaffold00169.G174 is encoded by the nucleotides of SEQ ID No: 79 which encodes the amino acid sequence of SEQ ID No: 82. This enzyme is believed to have alcohol oxidase activity.
  • Sequence Oxid-42 scaffold00227.G212 is encoded by the nucleotides of SEQ ID No: 81 which encodes the amino acid sequence of SEQ ID No: 84. This enzyme is believed to have versatile peroxidase activity.
  • Sequence Oxid-43 scaffold00227.G247 is encoded by the nucleotides of SEQ ID No: 83 which encodes the amino acid sequence of SEQ ID No: 86. This enzyme is believed to have L-pipecolate oxidase - proline oxidase activity.
  • Sequence Oxid-44 scaffold00227.G400 is encoded by the nucleotides of SEQ ID No: 85 which encodes the amino acid sequence of SEQ ID No: 88. This enzyme is believed to have ent-kaurene oxidase activity.
  • Sequence Oxid-45 scaffold00050.G1500 is encoded by the nucleotides of SEQ ID No: 87 which encodes the amino acid sequence of SEQ ID No: 87
  • Sequence Oxid-46 177_g is encoded by the nucleotides of
  • SEQ ID No: 89 which encodes the amino acid sequence of SEQ ID No: 92. This enzyme is believed to have ent-kaurene oxidase activity.
  • Sequence Oxid-47 578_g is encoded by the nucleotides of
  • SEQ ID No: 91 which encodes the amino acid sequence of SEQ ID No: 94. This enzyme is believed to have cytochrome-c oxidase activity.
  • Sequence Oxid-48 941_g is encoded by the nucleotides of
  • SEQ ID No: 93 which encodes the amino acid sequence of SEQ ID No: 96. This enzyme is believed to have catalase activity.
  • Sequence Oxid-49 1538_g is encoded by the nucleotides of SEQ ID No: 95 which encodes the amino acid sequence of SEQ ID No: 98.
  • This enzyme is believed to have catalase activity.
  • Sequence Oxid-50 1787_g is encoded by the nucleotides of SEQ ID No: 97 which encodes the amino acid sequence of SEQ ID No: 100.
  • This enzyme is believed to have D-amino-acid oxidase activity.
  • Sequence Oxid-51 2870_g is encoded by the nucleotides of SEQ ID No: 99 which encodes the amino acid sequence of SEQ ID No: 102.
  • This enzyme is believed to have flavin-linked sulfhydryl oxidase activity.
  • Sequence Oxid-52 362 l_g is encoded by the nucleotides of SEQ ID No: 101 which encodes the amino acid sequence of SEQ ID No: 104.
  • This enzyme is believed to have oxygen-dependent protoporphyrinogen oxidase activity.
  • Sequence Oxid-53 5878_g is encoded by the nucleotides of SEQ ID No: 103 which encodes the amino acid sequence of SEQ ID No: 106.
  • This enzyme is believed to have pyridoxamine-phosphate oxidase activity.
  • Sequence Oxid-54 6852_g is encoded by the nucleotides of SEQ ID No: 105 which encodes the amino acid sequence of SEQ ID No: 108.
  • This enzyme is believed to have catalase activity.
  • Sequence Oxid-55 7956_g is encoded by the nucleotides of SEQ ID No: 107 which encodes the amino acid sequence of SEQ ID No: 110.
  • This enzyme is believed to have peroxidase activity.
  • Sequence Oxid-56 8774_g is encoded by the nucleotides of SEQ ID No: 109 which encodes the amino acid sequence of SEQ ID No: 112.
  • This enzyme is believed to have cytochrome-c oxidase activity.
  • Sequence Oxid-58 scaffold00122.pathl .genel6 is encoded by the nucleotides of SEQ ID No: 113 which encodes the amino acid sequence of SEQ ID No: 116. This enzyme is believed to have catalase activity.
  • Sequence Oxid-61 scaffold00050.G998 is encoded by the nucleotides of SEQ ID No: 119 which encodes the amino acid sequence of SEQ ID No: 119
  • Sequence Oxid-62 scaffold00071.G2587 is encoded by the nucleotides of SEQ ID No: 121 which encodes the amino acid sequence of SEQ ID No: 121
  • Sequence Oxid-63 scaffold00169.G454 is encoded by the nucleotides of SEQ ID No: 123 which encodes the amino acid sequence of SEQ ID No: 123
  • Sequence Oxid-64 scaffold00169.G455 is encoded by the nucleotides of SEQ ID No: 125 which encodes the amino acid sequence of SEQ ID No: 125
  • Sequence Oxid-65 scaffold00071.G416 is encoded by the nucleotides of SEQ ID No: 127 which encodes the amino acid sequence of SEQ ID No: 130. This enzyme is believed to have thioredoxin-disulfide reductase activity.
  • Sequence Oxid-66 scaffold00071.G1899 is encoded by the nucleotides of SEQ ID No: 129 which encodes the amino acid sequence of SEQ ID No: 132. This enzyme is believed to have arsenate reductase (glutaredoxin) activity.
  • Sequence Oxid-67 scaffold00075.G497 is encoded by the nucleotides of SEQ ID No: 131 which encodes the amino acid sequence of SEQ ID No: 134. This enzyme is believed to have ferredoxin-NADP+ reductase activity.
  • Sequence Oxid-68 scaffold00031.G158 is encoded by the nucleotides of SEQ ID No: 133 which encodes the amino acid sequence of SEQ ID No: 136. This enzyme is believed to have tryptophan 2,3-dioxygenase activity.
  • Sequence Oxid-69 scaffold00031.G227 is encoded by the nucleotides of SEQ ID No: 135 which encodes the amino acid sequence of SEQ ID No: 138. This enzyme is believed to have sulfonate dioxygenase activity.
  • Sequence Oxid-70 scaffold00031.G625 is encoded by the nucleotides of SEQ ID No: 137 which encodes the amino acid sequence of SEQ ID No: 140. This enzyme is believed to have catechol 1 ,2-dioxygenase activity.
  • Sequence Oxid-71 scaffold00031.G776 is encoded by the nucleotides of SEQ ID No: 139 which encodes the amino acid sequence of SEQ ID No: 142. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-72 scaffold00031.G1607 is encoded by the nucleotides of SEQ ID No: 141 which encodes the amino acid sequence of SEQ ID No: 144. This enzyme is believed to have 2-nitropropane dioxygenase activity.
  • Sequence Oxid-73 scaffold00050.G277 is encoded by the nucleotides of SEQ ID No: 143 which encodes the amino acid sequence of SEQ ID No: 146. This enzyme is believed to have nitric oxide dioxygenase activity.
  • Sequence Oxid-74 scaffold00071.G251 is encoded by the nucleotides of SEQ ID No: 145 which encodes the amino acid sequence of SEQ ID No: 148. This enzyme is believed to have 3-hydroxyanthranilate 3,4-dioxygenase activity.
  • Sequence Oxid-75 scaffold00071.G335 is encoded by the nucleotides of SEQ ID No: 147 which encodes the amino acid sequence of SEQ ID No: 150. This enzyme is believed to have nitric oxide dioxygenase activity.
  • sequence Oxid-76 scaflbld00071.G2259 is encoded by the nucleotides of SEQ ID No: 149 which encodes the amino acid sequence of SEQ ID No: 152. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-77 scaffold00071.G3208 is encoded by the nucleotides of SEQ ID No: 151 which encodes the amino acid sequence of SEQ ID No: 154. This enzyme is believed to have catechol 1 ,2-dioxygenase activity.
  • Sequence Oxid-78 scaffold00075.G417 is encoded by the nucleotides of SEQ ID No: 153 which encodes the amino acid sequence of SEQ ID No: 156. This enzyme is believed to have cysteine dioxygenase activity.
  • Sequence Oxid-79 scaffold00075.G1075 is encoded by the nucleotides of SEQ ID No: 155 which encodes the amino acid sequence of SEQ ID No: 158. This enzyme is believed to have sulfonate dioxygenase activity.
  • Sequence Oxid-80 scaffold00075.G1251 is encoded by the nucleotides of SEQ ID No: 157 which encodes the amino acid sequence of SEQ ID No: 160. This enzyme is believed to have sulfonate dioxygenase activity.
  • Sequence Oxid-81 scaffold00131.G595 is encoded by the nucleotides of SEQ ID No: 159 which encodes the amino acid sequence of SEQ ID No: 162. This enzyme is believed to have trimethyllysine dioxygenase activity.
  • Sequence Oxid-82 scaffold00131.G596 is encoded by the nucleotides of SEQ ID No: 161 which encodes the amino acid sequence of SEQ ID No: 164. This enzyme is believed to have trimethyllysine dioxygenase activity.
  • Sequence Oxid-83 scaffold00131.G810 is encoded by the nucleotides of SEQ ID No: 163 which encodes the amino acid sequence of SEQ ID No: 166. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-84 scaffold00131.G1675 is encoded by the nucleotides of SEQ ID No: 165 which encodes the amino acid sequence of SEQ ID No: 168. This enzyme is believed to have 2-nitropropane dioxygenase activity.
  • Sequence Oxid-85 scaffold00131.G2052 is encoded by the nucleotides of SEQ ID No: 167 which encodes the amino acid sequence of SEQ ID No: 170. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-86 scaffold00131.G2141 is encoded by the nucleotides of SEQ ID No: 169 which encodes the amino acid sequence of SEQ ID No: 172. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-87 scaflbld00142.G307 is encoded by the nucleotides of SEQ ID No: 171 which encodes the amino acid sequence of SEQ ID No: 174. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-88 scaffold00142.G386 is encoded by the nucleotides of SEQ ID No: 173 which encodes the amino acid sequence of SEQ ID No: 176. This enzyme is believed to have tryptophan 2,3-dioxygenase activity.
  • Sequence Oxid-89 scaffold00169.G8 is encoded by the nucleotides of SEQ ID No: 175 which encodes the amino acid sequence of SEQ ID No: 178. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-90 scaffold00169.G77 is encoded by the nucleotides of SEQ ID No: 177 which encodes the amino acid sequence of SEQ ID No: 180. This enzyme is believed to have sulfonate dioxygenase activity.
  • Sequence Oxid-91 scaffold00169.G407 is encoded by the nucleotides of SEQ ID No: 179 which encodes the amino acid sequence of SEQ ID No: 182. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-92 scaffold00227.G198 is encoded by the nucleotides of SEQ ID No: 181 which encodes the amino acid sequence of SEQ ID No: 184. This enzyme is believed to have 2-nitropropane dioxygenase activity.
  • Sequence Oxid-93 scaffold00227.G634 is encoded by the nucleotides of SEQ ID No: 183 which encodes the amino acid sequence of SEQ ID No: 186. This enzyme is believed to have catechol 1 ,2-dioxygenase activity.
  • Sequence Oxid-94 2107_g is encoded by the nucleotides of SEQ ID No: 185 which encodes the amino acid sequence of SEQ ID No: 188. This enzyme is believed to have 2-nitropropane dioxygenase activity.
  • Sequence Oxid-95 977 l_g is encoded by the nucleotides of SEQ ID No: 187 which encodes the amino acid sequence of SEQ ID No: 190. This enzyme is believed to have catechol 1 ,2-dioxygenase activity.
  • Sequence Oxid-96 scaffold00031.G1073 is encoded by the nucleotides of SEQ ID No: 189 which encodes the amino acid sequence of SEQ ID No: 192. This enzyme is believed to have prephenate dehydrogenase (NADP+) activity.
  • Sequence Oxid-97 scaffold00227.G60 is encoded by the nucleotides of SEQ ID No: 191 which encodes the amino acid sequence of SEQ ID No: 194. This enzyme is believed to have homogentisate 1 ,2-dioxygenase activity.
  • Sequence Oxid-98 scaffold00016.G898 is encoded by the nucleotides of SEQ ID No: 193 which encodes the amino acid sequence of SEQ ID No: 196. This enzyme is believed to have 4-hydroxyphenylpyruvate dioxygenase activity.
  • Sequence Oxid-99 scaffold00071.G470 is encoded by the nucleotides of SEQ ID No: 195 which encodes the amino acid sequence of SEQ ID No: 198. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-100 scaffold00071.G607 is encoded by the nucleotides of SEQ ID No: 197 which encodes the amino acid sequence of SEQ ID No: 200. This enzyme is believed to have Protein disulfide oxidoreductase activity.
  • Sequence Oxid-101 scaffold00071.G1052 is encoded by the nucleotides of SEQ ID No: 199 which encodes the amino acid sequence of SEQ ID No: 202. This enzyme is believed to have Protein disulfide isomerase activity.
  • Sequence Oxid-102 scaffold00071.G1584 is encoded by the nucleotides of SEQ ID No: 201 which encodes the amino acid sequence of SEQ ID No: 204. This enzyme is believed to have Protein disulfide isomerase activity.
  • Sequence Oxid-103 scaffold00071.G2169 is encoded by the nucleotides of SEQ ID No: 203 which encodes the amino acid sequence of SEQ ID No: 206. This enzyme is believed to have Protein disulfide oxidoreductase activity.
  • Sequence Oxid-104 scaffold00131.G1597 is encoded by the nucleotides of SEQ ID No: 205 which encodes the amino acid sequence of SEQ ID No: 208. This enzyme is believed to have Protein disulfide isomerase activity.
  • Sequence Oxid-105 scaffold00227.G519 is encoded by the nucleotides of SEQ ID No: 207 which encodes the amino acid sequence of SEQ ID No: 210. This enzyme is believed to have Protein disulfide oxidoreductase activity.
  • Sequence Oxid-106 scaffold00016.G594 is encoded by the nucleotides of SEQ ID No: 209 which encodes the amino acid sequence of SEQ ID No: 212. This enzyme is believed to have Protein disulfide oxidoreductase activity.
  • Sequence Oxid-107 scaffold00016.Gl 163 is encoded by the nucleotides of SEQ ID No: 211 which encodes the amino acid sequence of SEQ ID No: 214. This enzyme is believed to have glutathione-disulfide reductase activity.
  • Sequence Oxid-108 scaflbld00031.G1301 is encoded by the nucleotides of SEQ ID No: 213 which encodes the amino acid sequence of SEQ ID No: 216. This enzyme is believed to have Protein disulfide oxidoreductase activity.
  • Sequence Oxid-109 scaffold00050.G952 is encoded by the nucleotides of SEQ ID No: 215 which encodes the amino acid sequence of SEQ ID No: 218. This enzyme is believed to have Protein disulfide oxidoreductase activity.
  • Sequence Oxid-110 scaffold00031.G37 is encoded by the nucleotides of SEQ ID No: 217 which encodes the amino acid sequence of SEQ ID No: 220. This enzyme is believed to have Redox-active center Protein activity.
  • Sequence Oxid-111 scaffold00031.G200 is encoded by the nucleotides of SEQ ID No: 219 which encodes the amino acid sequence of SEQ ID No: 222. This enzyme is believed to have Redox-active center Protein activity.
  • Sequence Oxid-112 scaffold00031.G1677 is encoded by the nucleotides of SEQ ID No: 221 which encodes the amino acid sequence of SEQ ID No: 224. This enzyme is believed to have Redox-active center Protein activity.
  • Sequence Oxid-113 scaffold00071.G1335 is encoded by the nucleotides of SEQ ID No: 223 which encodes the amino acid sequence of SEQ ID No: 226. This enzyme is believed to have Redox-active center Protein activity.
  • Sequence Oxid-114 scaffold00071.G3221 is encoded by the nucleotides of SEQ ID No: 225 which encodes the amino acid sequence of SEQ ID No: 228. This enzyme is believed to have Redox-active center Protein activity.
  • Sequence Oxid-115 scaffold00129.Gl is encoded by the nucleotides of SEQ ID No: 227 which encodes the amino acid sequence of SEQ ID No: 230. This enzyme is believed to have Redox-active center Protein activity.
  • Sequence Oxid-116 scaffold00142.G269 is encoded by the nucleotides of SEQ ID No: 229 which encodes the amino acid sequence of SEQ ID No: 232. This enzyme is believed to have Redox-active center Protein activity.
  • Sequence Oxid-117 scaffold00071.G3389 is encoded by the nucleotides of SEQ ID No: 231 which encodes the amino acid sequence of SEQ ID No: 234. This enzyme is believed to have cellobiose dehydrogenase (acceptor) activity.
  • Sequence Oxid-118 scaflbld00092.G499 is encoded by the nucleotides of SEQ ID No: 233 which encodes the amino acid sequence of SEQ ID No: 236. This enzyme is believed to have cellobiose dehydrogenase (acceptor) activity.
  • Sequence Oxid-119 scaffold00137.G80 is encoded by the nucleotides of SEQ ID No: 235.
  • SEQ ID No: 237 which encodes the amino acid sequence of SEQ ID No: 238. This enzyme is believed to have cellobiose dehydrogenase (acceptor) activity.
  • Sequence Oxid-120 scaffold00142.G279 is encoded by the nucleotides of SEQ ID No: 239 which encodes the amino acid sequence of SEQ ID No: 240. This enzyme is believed to have cellobiose dehydrogenase (acceptor) activity.
  • Sequence Oxid-121 scaffold00142.G282 is encoded by the nucleotides of SEQ ID No: 241 which encodes the amino acid sequence of SEQ ID No: 242. This enzyme is believed to have cellobiose dehydrogenase (acceptor) activity.
  • Sequence Oxid-122 scaffold00050.G528 is encoded by the nucleotides of SEQ ID No: 243 which encodes the amino acid sequence of SEQ ID No: 244. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-123 scaffold00050.Gl 147 is encoded by the nucleotides of SEQ ID No: 245 which encodes the amino acid sequence of SEQ ID No: 246. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-124 scaffold00071.G1252 is encoded by the nucleotides of SEQ ID No: 247 which encodes the amino acid sequence of SEQ ID No: 248. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-125 scaffold00092.G8 is encoded by the nucleotides of SEQ ID No: 249 which encodes the amino acid sequence of SEQ ID No: 250. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-126 scaffold00092.G500 is encoded by the nucleotides of SEQ ID No: 251 which encodes the amino acid sequence of SEQ ID No: 252. This enzyme is believed to have cellobiose dehydrogenase (acceptor) activity.
  • Sequence Oxid-127 scaflbld00122.G120 is encoded by the nucleotides of SEQ ID No: 253 which encodes the amino acid sequence of SEQ ID No: 254. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-128 scaffold00131.G1200 is encoded by the nucleotides of SEQ ID No: 255 which encodes the amino acid sequence of SEQ ID No: 256. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-129 scaffold00169.G243 is encoded by the nucleotides of SEQ ID No: 257 which encodes the amino acid sequence of SEQ ID No: 258. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-130 scaffold00169.G244 is encoded by the nucleotides of SEQ ID No: 259 which encodes the amino acid sequence of SEQ ID No: 260. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-131 scaffold00131.G1201 is encoded by the nucleotides of SEQ ID No: 261 which encodes the amino acid sequence of SEQ ID No: 262. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-132 scaffold00050.G593 is encoded by the nucleotides of SEQ ID No: 263 which encodes the amino acid sequence of SEQ ID No: 264. This enzyme is believed to have nitrate reductase (NADPH) activity.
  • NADPH nitrate reductase
  • Sequence Oxid-133 scaffold00075.G929 is encoded by the nucleotides of SEQ ID No: 265 which encodes the amino acid sequence of SEQ ID No: 266. This enzyme is believed to have nitrate reductase (NADPH) activity.
  • NADPH nitrate reductase
  • Sequence Oxid-134 scaffold00227.G302 is encoded by the nucleotides of SEQ ID No: 267 which encodes the amino acid sequence of SEQ ID No: 268. This enzyme is believed to have nitrite reductase [NAD(P)H] activity.
  • Sequence Oxid-135 scaffold00131.G1207 is encoded by the nucleotides of SEQ ID No: 269 which encodes the amino acid sequence of SEQ ID No: 270. This enzyme is believed to have nitrite reductase (NO-forming) activity.
  • Sequence Oxid-136 scaffold00016.G461 is encoded by the nucleotides of SEQ ID No: 271 which encodes the amino acid sequence of SEQ ID No: 272. This enzyme is believed to have glutamate synthase (NADPH) activity.
  • Sequence Oxid-137 scaffold00031.G1084 is encoded by the nucleotides of SEQ ID No: 273 which encodes the amino acid sequence of SEQ ID No: 274. This enzyme is believed to have glutamate dehydrogenase activity.
  • Sequence Oxid-138 scaffold00050.G21 is encoded by the nucleotides of SEQ ID No: 275 which encodes the amino acid sequence of SEQ ID No: 276. This enzyme is believed to have proline dehydrogenase activity.
  • Sequence Oxid-139 scaffold00075.G589 is encoded by the nucleotides of SEQ ID No: 277 which encodes the amino acid sequence of SEQ ID No: 278. This enzyme is believed to have isocitrate dehydrogenase (NAD+) activity.
  • CCL09102 is encoded by the nucleotides of SEQ ID No: 279 which encodes the amino acid sequence of SEQ ID No: 280. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-142 scaffold00016.G1047 (CL09554) is encoded by the nucleotides of SEQ ID No: 283 which encodes the amino acid sequence of SEQ ID No: 284. This enzyme is believed to have monooxygenase activity.
  • scaffold00019.pathl .gene7 (CL05569) is encoded by the nucleotides of SEQ ID No: 285 which encodes the amino acid sequence of SEQ ID No: 286. This enzyme is believed to have oxidation reduction activity.
  • scaffold00022.pathl .genel (CL08704) is encoded by the nucleotides of SEQ ID No: 287 which encodes the amino acid sequence of SEQ ID No: 288. This enzyme is believed to have oxidation reduction activity.
  • scaffold00031.pathl .genel4 (CL07195) is encoded by the nucleotides of SEQ ID No: 289 which encodes the amino acid sequence of SEQ ID No: 290. This enzyme is believed to have oxidation reduction activity. [0268] The enzyme identified as Sequence Oxid-146 scaffold00031.G86 976_g
  • scafFold00031.pathl .gene42 (CL07149) is encoded by the nucleotides of SEQ ID No: 291 which encodes the amino acid sequence of SEQ ID No: 292. This enzyme is believed to have oxidation reduction activity.
  • scaffold00031.pathl .gene69 (CL07117) is encoded by the nucleotides of SEQ ID No: 293 which encodes the amino acid sequence of SEQ ID No: 294. This enzyme is believed to have oxidation reduction activity.
  • the enzyme identified as Sequence Oxid-148 scaffold00031.G225 1063 9 (partly), scaffold00031. pathl . genel 15 (CL07057) is encoded by the nucleotides of SEQ ID No: 295 which encodes the amino acid sequence of SEQ ID No: 296. This enzyme is believed to have oxidation reduction activity.
  • pathl . gene252 (CL06915) is encoded by the nucleotides of SEQ ID No: 297 which encodes the amino acid sequence of SEQ ID No: 298. This enzyme is believed to have regulation of transcription, DNA-dependent activity.
  • pathl . gene263 (CL06904) is encoded by the nucleotides of SEQ ID No: 299 which encodes the amino acid sequence of SEQ ID No: 300. This enzyme is believed to have oxidation reduction activity.
  • pathl . gene521 (CL06630) is encoded by the nucleotides of SEQ ID No: 301 which encodes the amino acid sequence of SEQ ID No: 302. This enzyme is believed to have oxidation reduction activity.
  • pathl . gene780 (CL02845) is encoded by the nucleotides of SEQ ID No: 303 which encodes the amino acid sequence of SEQ ID No: 304. This enzyme is believed to have oxidation reduction activity.
  • pathl . gene783 (CL02839) is encoded by the nucleotides of SEQ ID No: 305 which encodes the amino acid sequence of SEQ ID No: 306. This enzyme is believed to have oxidation reduction activity.
  • the enzyme identified as Sequence Oxid-154 scaffold00050.G279 1167_g, 2268_g, 2269_g, scaffold00050.pathl .genel l6, scaffold00050.pathl .genel l7 (CL10139 CL10141 CL10140) is encoded by the nucleotides of SEQ ID No: 307 which encodes the amino acid sequence of SEQ ID No: 308. This enzyme is believed to have oxidation reduction activity.
  • the enzyme identified as Sequence Oxid-155 scaffold00050.G298 2280_g, 228 l_g, scaffold00050.pathl .genel29, scaffold00050.pathl .genel30 (CL10151) is encoded by the nucleotides of SEQ ID No: 309 which encodes the amino acid sequence of SEQ ID No: 310. This enzyme is believed to have oxidation reduction activity.
  • Sequence Oxid-156 scaffold00050.G308 (CL10159) is encoded by the nucleotides of SEQ ID No: 311 which encodes the amino acid sequence of SEQ ID No: 312. This enzyme is believed to have monooxygenase activity.
  • the enzyme identified as Sequence Oxid-157 scaffold00050.G397 234 l_g, 2342_g, scaffold00050.pathl .genel87 (CL10213) is encoded by the nucleotides of SEQ ID No: 313 which encodes the amino acid sequence of SEQ ID No: 314. This enzyme is believed to have oxidation reduction activity.
  • scaffold00050.pathl .gene246 (CL10291) is encoded by the nucleotides of SEQ ID No: 315 which encodes the amino acid sequence of SEQ ID No: 316. This enzyme is believed to have flavin-containing monooxygenase activity.
  • scaffold00050.pathl .gene325 (CL10405) is encoded by the nucleotides of SEQ ID No: 317 which encodes the amino acid sequence of SEQ ID No: 318. This enzyme is believed to have kynurenine 3 -monooxygenase activity.
  • scaffold00050.pathl .gene425 (CL10527) is encoded by the nucleotides of SEQ ID No: 319 which encodes the amino acid sequence of SEQ ID No: 320. This enzyme is believed to have flavin-containing monooxygenase activity.
  • scaffold00050.pathl .gene511 (CL10614) is encoded by the nucleotides of SEQ ID No: 321 which encodes the amino acid sequence of SEQ ID No: 322. This enzyme is believed to have monooxygenase activity.
  • sequence Oxid-162 scaffold00050.G1041 2727_g scaffold00050.pathl .gene514 is encoded by the nucleotides of SEQ ID No: 323 which encodes the amino acid sequence of SEQ ID No: 324. This enzyme is believed to have monooxygenase activity.
  • scaffold00050.pathl .gene515 (CL10617) is encoded by the nucleotides of SEQ ID NO: 1
  • scaffold00050.pathl .gene702 (CL10825) is encoded by the nucleotides of SEQ ID NO: 1
  • scaffold00050.pathl .gene747 (CL10883) is encoded by the nucleotides of SEQ ID NO: 1
  • scaffold00050.pathl .gene821 (CL10975) is encoded by the nucleotides of SEQ ID NO: 1
  • scaffold00050.pathl .gene838 (CL10989) is encoded by the nucleotides of SEQ ID NO: 1
  • scaffold00053.pathl .genel3 (CL11584) is encoded by the nucleotides of SEQ ID NO: 1
  • scaffold00053.pathl .gene26 (CL11558) is encoded by the nucleotides of SEQ ID NO: 1
  • scaffold00071.pathl .gene427 (CL00475 CL00476) is encoded by the nucleotides of SEQ ID No: 339 which encodes the amino acid sequence of SEQ ID No: 340. This enzyme is believed to have phenol 2-monooxygenase activity.
  • scaffold00071.pathl .gene427 is encoded by the nucleotides of SEQ ID No: 341 which encodes the amino acid sequence of SEQ ID No: 342. This enzyme is believed to have monooxygenase activity.
  • scaffold00071.pathl .gene459 (CL00510) is encoded by the nucleotides of SEQ ID No: 343 which encodes the amino acid sequence of SEQ ID No: 344. This enzyme is believed to have monophenol monooxygenase activity.
  • scaffold00071.pathl .gene492 (CL00537) is encoded by the nucleotides of SEQ ID No: 345 which encodes the amino acid sequence of SEQ ID No: 346. This enzyme is believed to have dopamine beta-monooxygenase activity.
  • scaffold00071.pathl .gene580 (CL00621) is encoded by the nucleotides of SEQ ID No: 347 which encodes the amino acid sequence of SEQ ID No: 348. This enzyme is believed to have monooxygenase activity.
  • scaffold00071.pathl .gene621 (CL00688 CL08353 CL01496 CL03246) is encoded by the nucleotides of SEQ ID No: 349 which encodes the amino acid sequence of SEQ ID No: 350. This enzyme is believed to have flavin-containing
  • scaffold00071.pathl .gene875 (CL08558 CL00981) is encoded by the nucleotides of SEQ ID No: 351 which encodes the amino acid sequence of SEQ ID No: 352. This enzyme is believed to have flavin-containing monooxygenase activity.
  • scaffold00071.pathl .genel020 (CL01129) is encoded by the nucleotides of SEQ ID No: 353 which encodes the amino acid sequence of SEQ ID No: 354. This enzyme is believed to have lactate 2-monooxygenase activity.
  • scaffold00071.pathl .genel 187, scaffold00071.pathl .genel 188 (CL07578 CL01313) is encoded by the nucleotides of SEQ ID No: 355 which encodes the amino acid sequence of SEQ ID No: 356. This enzyme is believed to have monooxygenase activity.
  • scaffold00071.pathl .genel245, scaffold00071.pathl .genel246 (CL01384) is encoded by the nucleotides of SEQ ID No: 357 which encodes the amino acid sequence of SEQ ID No: 358. This enzyme is believed to have flavin-containing monooxygenase activity.
  • scaffold00071.pathl .genel812 (CL11406) is encoded by the nucleotides of SEQ ID No: 359 which encodes the amino acid sequence of SEQ ID No: 360. This enzyme is believed to have monooxygenase activity.
  • scaffold00075.pathl .gene356 (CL03408) is encoded by the nucleotides of SEQ ID No: 361 which encodes the amino acid sequence of SEQ ID No: 362. This enzyme is believed to have monooxygenase activity.
  • scaffold00075.pathl .gene444 (CL03483) is encoded by the nucleotides of SEQ ID No: 363 which encodes the amino acid sequence of SEQ ID No: 364. This enzyme is believed to have squalene monooxygenase activity.
  • scaffold00075.pathl .gene459 (CL03497) is encoded by the nucleotides of SEQ ID No: 365 which encodes the amino acid sequence of SEQ ID No: 366. This enzyme is believed to have deoxyhypusine monooxygenase activity.
  • Sequence Oxid-184 scaffold00092.G3 (CL05970) is encoded by the nucleotides of SEQ ID No: 367 which encodes the amino acid sequence of SEQ ID No: 368. This enzyme is believed to have monooxygenase activity.
  • scaffold00092.pathl .gene20 (CL05985) is encoded by the nucleotides of SEQ ID No: 369 which encodes the amino acid sequence of SEQ ID No: 370. This enzyme is believed to have monooxygenase activity.
  • sequence Oxid-186 scaffold00092.G71 6289_g scaffold00092.pathl .gene41 (CL06010) is encoded by the nucleotides of SEQ ID No: 371 which encodes the amino acid sequence of SEQ ID No: 372. This enzyme is believed to have monooxygenase activity.
  • scaffold00092.pathl .gene42 (CL06011 CL06012) is encoded by the nucleotides of SEQ ID No: 373 which encodes the amino acid sequence of SEQ ID No: 374. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-188 scaffold00092.G89 (CL06022) is encoded by the nucleotides of SEQ ID No: 375 which encodes the amino acid sequence of SEQ ID No: 376. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-189 scaffold00092.G158 (CL06068) is encoded by the nucleotides of SEQ ID No: 377 which encodes the amino acid sequence of SEQ ID No: 378. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-190 scaffold00092.G332 (CL06172) is encoded by the nucleotides of SEQ ID No: 379 which encodes the amino acid sequence of SEQ ID No: 380. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-191 scaffold00105.G2 is encoded by the nucleotides of SEQ ID No: 381 which encodes the amino acid sequence of SEQ ID No: 382. This enzyme is believed to have flavin-containing monooxygenase activity.
  • Sequence Oxid-193 scaffold00120.Gl is encoded by the nucleotides of SEQ ID No: 385 which encodes the amino acid sequence of SEQ ID No: 386. This enzyme is believed to have monooxygenase activity.
  • CL03832 is encoded by the nucleotides of SEQ ID No: 389 which encodes the amino acid sequence of SEQ ID No: 390. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-196 scaffold00122.G80 (CL03841) is encoded by the nucleotides of SEQ ID No: 391 which encodes the amino acid sequence of SEQ ID No: 392. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-197 scaffold00122.G198 (CL03918) is encoded by the nucleotides of SEQ ID No: 393 which encodes the amino acid sequence of SEQ ID No: 394. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-198 scaffold00122.G199 (CL03919) is encoded by the nucleotides of SEQ ID No: 395 which encodes the amino acid sequence of SEQ ID No: 396. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-199 scaffold00122.G202 (CL03922) is encoded by the nucleotides of SEQ ID No: 397 which encodes the amino acid sequence of SEQ ID No: 398. This enzyme is believed to have monooxygenase activity.
  • CL04267 is encoded by the nucleotides of SEQ ID No: 399 which encodes the amino acid sequence of 400. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-201 scaffold00131.G363 is encoded by the nucleotides of SEQ ID No: 401 which encodes the amino acid sequence of SEQ ID No: 402. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-202 scaffold00131.G364 (CL04453) is encoded by the nucleotides of SEQ ID No: 403 which encodes the amino acid sequence of SEQ ID No: 404. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-203 scaffold00131.G446 is encoded by the nucleotides of SEQ ID No: 405 which encodes the amino acid sequence of SEQ ID No: 406. This enzyme is believed to have flavin-containing monooxygenase activity CL04492 activity.
  • Sequence Oxid-204 scaffold00131.G752 (CL04674) is encoded by the nucleotides of SEQ ID No: 407 which encodes the amino acid sequence of SEQ ID No: 408. This enzyme is believed to have phenol 2- monooxygenase activity.
  • Sequence Oxid-205 scaffold00131.G875 (CL04745) is encoded by the nucleotides of SEQ ID No: 409 which encodes the amino acid sequence of SEQ ID No: 410. This enzyme is believed to have flavin-containing monooxygenase activity.
  • CL04796 is encoded by the nucleotides of SEQ ID No: 411 which encodes the amino acid sequence of SEQ ID No: 412. This enzyme is believed to have benzoate 4-monooxygenase activity.
  • Sequence Oxid-207 scaffold00131.Gl 166 (CL04936) is encoded by the nucleotides of SEQ ID No: 413 which encodes the amino acid sequence of SEQ ID No: 414. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-208 scaffold00131.G1265 is encoded by the nucleotides of SEQ ID No: 415 which encodes the amino acid sequence of SEQ ID No: 416. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-209 scaffold00131.G1806 (CL05310) is encoded by the nucleotides of SEQ ID No: 417 which encodes the amino acid sequence of SEQ ID No: 418. This enzyme is believed to have monooxygenase activity.
  • CL05012 CL08560 CL08557) is encoded by the nucleotides of SEQ ID No: 419 which encodes the amino acid sequence of SEQ ID No: 420. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-211 scaffold00142.G368 is encoded by the nucleotides of SEQ ID No: 421 which encodes the amino acid sequence of SEQ ID No: 422. This enzyme is believed to have flavin-containing monooxygenase activity.
  • Sequence Oxid-212 scaflbld00142.G370 is encoded by the nucleotides of SEQ ID No: 423 which encodes the amino acid sequence of SEQ ID No: 424. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-213 scaffold00142.G465 (CL08624) is encoded by the nucleotides of SEQ ID No: 425 which encodes the amino acid sequence of SEQ ID No: 426. This enzyme is believed to have monooxygenase activity.
  • CL05970 is encoded by the nucleotides of SEQ ID No: 427 which encodes the amino acid sequence of SEQ ID No: 428. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-215 scaffold00142.G589 is encoded by the nucleotides of SEQ ID No: 429 which encodes the amino acid sequence of SEQ ID No: 430. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-216 scaffold00169.G30 (CL07907) is encoded by the nucleotides of SEQ ID No: 431 which encodes the amino acid sequence of SEQ ID No: 432. This enzyme is believed to have monooxygenase activity.
  • CL11558 CL07902 is encoded by the nucleotides of SEQ ID No: 433 which encodes the amino acid sequence of SEQ ID No: 434. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-218 scaffold00169.G288 (CL07724) is encoded by the nucleotides of SEQ ID No: 435 which encodes the amino acid sequence of SEQ ID No: 436. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-219 scaffold00169.G316 (CL07703) is encoded by the nucleotides of SEQ ID No: 437 which encodes the amino acid sequence of SEQ ID No: 438. This enzyme is believed to have flavin-containing monooxygenase activity.
  • Sequence Oxid-220 scaffold00169.G318 (CL07702) is encoded by the nucleotides of SEQ ID No: 439 which encodes the amino acid sequence of SEQ ID No: 440. This enzyme is believed to have flavin-containing monooxygenase activity.
  • Sequence Oxid-221 scaffold00169.G321 (CL07700) is encoded by the nucleotides of SEQ ID No: 441 which encodes the amino acid sequence of SEQ ID No: 442. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-222 scaffold00169.G325 (CL07697) is encoded by the nucleotides of SEQ ID No: 443 which encodes the amino acid sequence of SEQ ID No: 444. This enzyme is believed to have flavin-containing monooxygenase activity.
  • Sequence Oxid-223 scaffold00169.G402 (CL07634) is encoded by the nucleotides of SEQ ID No: 445 which encodes the amino acid sequence of SEQ ID No: 446. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-224 scaffold00169.G442 (CL07610) is encoded by the nucleotides of SEQ ID No: 447 which encodes the amino acid sequence of SEQ ID No: 448. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-225 scaffold00214.G9 (CL02472) is encoded by the nucleotides of SEQ ID No: 449 which encodes the amino acid sequence of SEQ ID No: 450. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-226 scaffold00214.G10 is encoded by the nucleotides of SEQ ID No: 451 which encodes the amino acid sequence of SEQ ID No: 452. This enzyme is believed to have monooxygenase activity.
  • CL02481) is encoded by the nucleotides of SEQ ID No: 453 which encodes the amino acid sequence of SEQ ID No: 454. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-228 scaffold00227.G204 (CL08208) is encoded by the nucleotides of SEQ ID No: 455 which encodes the amino acid sequence of SEQ ID No: 456. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-229 scaffold00227.G683 (CL08810
  • CL07938 is encoded by the nucleotides of SEQ ID No: 457 which encodes the amino acid sequence of SEQ ID No: 458. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-230 scaffold00050.G1657 (CL11016) is encoded by the nucleotides of SEQ ID No: 459 which encodes the amino acid sequence of SEQ ID No: 460. This enzyme is believed to have NADPH-hemo Protein reductase activity.
  • Sequence Oxid-231 scaffold00068.Gl is encoded by the nucleotides of SEQ ID No: 461 which encodes the amino acid sequence of SEQ ID No: 462. This enzyme is believed to have oxidoreductase activity, acting on paired activity.
  • Sequence Oxid-232 scaffold00071.G571 (CL00326) is encoded by the nucleotides of SEQ ID No: 463 which encodes the amino acid sequence of SEQ ID No: 464. This enzyme is believed to have sterol 14- demethylase activity.
  • Sequence Oxid-233 scaffold00071.G633 is encoded by the nucleotides of SEQ ID No: 465 which encodes the amino acid sequence of SEQ ID No: 466. This enzyme is believed to have oxidoreductase activity, acting on paired d activity.
  • Sequence Oxid-234 scaffold00071.G634 (CL00365) is encoded by the nucleotides of SEQ ID No: 467 which encodes the amino acid sequence of SEQ ID No: 468. This enzyme is believed to have oxidoreductase activity, acting on paired d activity.
  • Sequence Oxid-235 scaffold00071.G1361 (CL00816) is encoded by the nucleotides of SEQ ID No: 469 which encodes the amino acid sequence of SEQ ID No: 470. This enzyme is believed to have oxidoreductase activity, acting on paired d activity.
  • Sequence Oxid-236 scaffold00071.G1662 (CL00992) is encoded by the nucleotides of SEQ ID No: 471 which encodes the amino acid sequence of SEQ ID No: 472. This enzyme is believed to have oxidoreductase activity, acting on paired d activity.
  • Sequence Oxid-237 scaffold00071.G1865 (CLOU 14) is encoded by the nucleotides of SEQ ID No: 473 which encodes the amino acid sequence of SEQ ID No: 474. This enzyme is believed to have oxidoreductase activity, acting on paired d activity.
  • Sequence Oxid-238 scaffold00092.G20 (CL05975) is encoded by the nucleotides of SEQ ID No: 475 which encodes the amino acid sequence of SEQ ID No: 476. This enzyme is believed to have NADPH-hemo Protein reductase activity.
  • CL06087) is encoded by the nucleotides of SEQ ID No: 477 which encodes the amino acid sequence of SEQ ID No: 478. This enzyme is believed to have oxidoreductase activity, acting on paired d activity.
  • Sequence Oxid-240 scaffold00227.G102 (CL08261) is encoded by the nucleotides of SEQ ID No: 479 which encodes the amino acid sequence of SEQ ID No: 480. This enzyme is believed to have oxidoreductase activity, acting on paired d activity.
  • Sequence Oxid-241 scaffold00071.G592 (CL00336) is encoded by the nucleotides of SEQ ID No: 481 which encodes the amino acid sequence of SEQ ID No: 482. This enzyme is believed to have succinate dehydrogenase (ubiquinone) activity
  • Sequence Oxid-242 scaffold00142.G540 (CL08666) is encoded by the nucleotides of SEQ ID No: 483 which encodes the amino acid sequence of SEQ ID No: 484. This enzyme is believed to have activity.
  • Sequence Oxid-243 scaffold00031.G1485 (CL02772) is encoded by the nucleotides of SEQ ID No: 485 which encodes the amino acid sequence of SEQ ID No: 486. This enzyme is believed to have chitin binding activity.
  • Sequence Oxid-244 scaffold00071.G1644 (CL00980) is encoded by the nucleotides of SEQ ID No: 487 which encodes the amino acid sequence of SEQ ID No: 488. This enzyme is believed to have ATP-binding Hydrolase Lipid degradation activity.
  • Sequence Oxid-245 scaffold00131.G793 (CL04696) is encoded by the nucleotides of SEQ ID No: 489 which encodes the amino acid sequence of SEQ ID No: 490. This enzyme is believed to have oxidoreductase activity, Glucooligosaccharide oxidase putative activity.
  • Sequence Oxid-246 scaffold00131.G1570 (CL05186) is encoded by the nucleotides of SEQ ID No: 491 which encodes the amino acid sequence of SEQ ID No: 492. This enzyme is believed to have defense response to fungus and seems to be a combination between manganese peroxidase (MnP) and a (number of) carbohydrate binding domain(s). activity.
  • MnP manganese peroxidase
  • Sequence Oxid-247 scaffold00169.G412 (CL07628) is encoded by the nucleotides of SEQ ID No: 493 which encodes the amino acid sequence of SEQ ID No: 494. This enzyme is believed to have oxidoreductase activity, lactose oxidase activity.
  • C04696 is encoded by the nucleotides of SEQ ID No: 495 which encodes the amino acid sequence of SEQ ID No: 496. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-249 scaffold00092.G538 (CL06304) is encoded by the nucleotides of SEQ ID No: 497 which encodes the amino acid sequence of SEQ ID No: 498. This enzyme is believed to have cytochrome-b5 reductase activity.
  • CL 10276 is encoded by the nucleotides of SEQ ID No: 499 which encodes the amino acid sequence of 500. This enzyme is believed to have oxidoreductase activity.
  • C10276 is encoded by the nucleotides of SEQ ID No: 501 which encodes the amino acid sequence of SEQ ID No: 502. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-252 scaffold00071.G2538 (CL01543) is encoded by the nucleotides of SEQ ID No: 503 which encodes the amino acid sequence of SEQ ID No: 504. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-253 scaffold00131.G2158 (CL05501) is encoded by the nucleotides of SEQ ID No: 505 which encodes the amino acid sequence of SEQ ID No: 506. This enzyme is believed to have copper ion binding, oxidoreductase activity, Laccase activity.
  • Sequence Oxid-254 scaffold00142.G37 (CL08347) is encoded by the nucleotides of SEQ ID No: 507 which encodes the amino acid sequence of SEQ ID No: 508. This enzyme is believed to have copper ion binding, oxidoreductase activity.
  • Sequence Oxid-255 scaffold00016.G641 (CL09304) is encoded by the nucleotides of SEQ ID No: 509 which encodes the amino acid sequence of SEQ ID No: 510. This enzyme is believed to have glycerol-3- phosphate dehydrogenase activity.
  • CL06843 (Cytochrome) is encoded by the nucleotides of SEQ ID No: 511 which encodes the amino acid sequence of SEQ ID No: 512. This enzyme is believed to have D-lactate dehydrogenase activity.
  • CL06797 is encoded by the nucleotides of SEQ ID No: 513 which encodes the amino acid sequence of SEQ ID No: 514. This enzyme is believed to have FAD
  • Flavo Protein, tRNA dihydrouridine synthase activity Flavo Protein, tRNA dihydrouridine synthase activity.
  • Sequence Oxid-259 scaffold00031.G1052 (CL06572) activity is encoded by the nucleotides of SEQ ID No: 517 which encodes the amino acid sequence of SEQ ID No: 518. This enzyme is believed to have FAD Flavo
  • Sequence Oxid-260 scaffold00031.Gl 199 (CL02964) is encoded by the nucleotides of SEQ ID No: 519 which encodes the amino acid sequence of SEQ ID No: 520. This enzyme is believed to have FMN Flavo Protein,
  • Sequence Oxid-261 scaffold00031.G1320 (CL02890) is encoded by the nucleotides of SEQ ID No: 521 which encodes the amino acid sequence of SEQ ID No: 522. This enzyme is believed to have FAD flavo protein, acyl-CoA dehydrogenase activity.
  • Sequence Oxid-262 scaffold00050.G972 (CL10574) is encoded by the nucleotides of SEQ ID No: 523 which encodes the amino acid sequence of SEQ ID No: 524. This enzyme is believed to have FAD flavo protein, acyl-CoA dehydrogenase activity.
  • Sequence Oxid-263 scaffold00050.G1269 (CL10770) is encoded by the nucleotides of SEQ ID No: 525 which encodes the amino acid sequence of SEQ ID No: 526. This enzyme is believed to have disulfide bond FAD Flavo Protein, dihydrolipoyl dehydrogenase activity.
  • Sequence Oxid-264 scaffold00050.G1295 (CL10786) is encoded by the nucleotides of SEQ ID No: 527 which encodes the amino acid sequence of SEQ ID No: 528. This enzyme is believed to have electron transport FAD flavo protein mitochondrion respiratory chain transit peptide transport activity.
  • Sequence Oxid-265 scaffold00050.G1321 (CL10801) is encoded by the nucleotides of SEQ ID No: 529 which encodes the amino acid sequence of SEQ ID No: 530. This enzyme is believed to have FMN Flavo Protein, photoreceptor activity, transcription factor activity.
  • Sequence Oxid-266 scaffold00050.G1429 (CL10879) is encoded by the nucleotides of SEQ ID No: 531 which encodes the amino acid sequence of SEQ ID No: 532. This enzyme is believed to have Cadmium Disulfide bond FAD Flavo Protein, oxidoreductase activity, acting on sulfur g activity.
  • Sequence Oxid-267 scaffold00071.G59 (CL00036) is encoded by the nucleotides of SEQ ID No: 533 which encodes the amino acid sequence of SEQ ID No: 534. This enzyme is believed to have FAD Flavo Protein, D-lactate dehydrogenase (Cytochrome) activity.
  • Sequence Oxid-268 scaffold00071.G556 (CL00318) is encoded by the nucleotides of SEQ ID No: 535 which encodes the amino acid sequence of SEQ ID No: 536. This enzyme is believed to have Cytoplasm FAD Flavo Protein, tRNA dihydrouridine synthase activity.
  • Sequence Oxid-269 scaffold00071.G744 (CL00443) is encoded by the nucleotides of SEQ ID No: 537 which encodes the amino acid sequence of SEQ ID No: 538. This enzyme is believed to have Cytoplasm FAD Flavo Protein, tRNA dihydrouridine synthase activity.
  • Sequence Oxid-270 scaffold00071.G1440 (CL00865) is encoded by the nucleotides of SEQ ID No: 539 which encodes the amino acid sequence of SEQ ID No: 540. This enzyme is believed to have FMN Flavo Protein, NADPH dehydrogenase activity.
  • Sequence Oxid-271 scaffold00071.G2386 (CL01424) is encoded by the nucleotides of SEQ ID No: 541 which encodes the amino acid sequence of SEQ ID No: 542. This enzyme is believed to have heme binding, L- lactate dehydrogenase (Cytochrome) activity.
  • Sequence Oxid-272 scaffold00071.G2604 (CL01584) is encoded by the nucleotides of SEQ ID No: 543 which encodes the amino acid sequence of SEQ ID No: 544. This enzyme is believed to have FMN binding activity.
  • Sequence Oxid-273 scaffold00075.G430 (CL03269) is encoded by the nucleotides of SEQ ID No: 545 which encodes the amino acid sequence of SEQ ID No: 546. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-274 scaffold00075.G449 (CL03284) is encoded by the nucleotides of SEQ ID No: 547 which encodes the amino acid sequence of SEQ ID No: 548.
  • This enzyme is believed to have FAD FMN Flavo Protein, oxidoreductase activity TAH18 GIBZE
  • Sequence Oxid-275 scaffold00075.G652 (CL03401) is encoded by the nucleotides of SEQ ID No: 549 which encodes the amino acid sequence of SEQ ID No: 550. This enzyme is believed to have NADPH-hemo Protein reductase activity.
  • Sequence Oxid-276 scaffold00075.G818 (Cytochrome) is encoded by the nucleotides of SEQ ID No: 551 which encodes the amino acid sequence of SEQ ID No: 552. This enzyme is believed to have L-lactate dehydrogenase (Cytochrome) activity.
  • Sequence Oxid-277 scaffold00092.G461 (CL06252) is encoded by the nucleotides of SEQ ID No: 553 which encodes the amino acid sequence of SEQ ID No: 554. This enzyme is believed to have FMN binding activity.
  • Sequence Oxid-278 scaffold00131.G685 (CL04637) is encoded by the nucleotides of SEQ ID No: 555 which encodes the amino acid sequence of SEQ ID No: 556. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-279 scaffold00131.G729 (CL04661) is encoded by the nucleotides of SEQ ID No: 557 which encodes the amino acid sequence of SEQ ID No: 558. This enzyme is believed to have FMN binding activity.
  • Sequence Oxid-280 scaffold00131.G1632 (CL05218) is encoded by the nucleotides of SEQ ID No: 559 which encodes the amino acid sequence of SEQ ID No: 560. This enzyme is believed to have heme binding, L- lactate dehydrogenase (Cytochrome) activity.
  • Sequence Oxid-281 scaffold00214.G35 (CL02491) is encoded by the nucleotides of SEQ ID No: 561 which encodes the amino acid sequence of SEQ ID No: 562. This enzyme is believed to have FMN binding activity.
  • Sequence Oxid-282 scaffold00214.G73 (CL02521) is encoded by the nucleotides of SEQ ID No: 563 which encodes the amino acid sequence of SEQ ID No: 564. This enzyme is believed to have heme binding, sulfite reductase (NADPH)
  • Sequence Oxid-283 scaffold00227.G366 (CL08117) is encoded by the nucleotides of SEQ ID No: 565 which encodes the amino acid sequence of SEQ ID No: 566. This enzyme is believed to have NAD or NADH binding, NADH dehydrogenase (ubiquinone)
  • Sequence Oxid-284 scaffold00227.G646 (CL07959) is encoded by the nucleotides of SEQ ID No: 567 which encodes the amino acid sequence of SEQ ID No: 568. This enzyme is believed to have sulfite reductase (NADPH)
  • Sequence Oxid-285 scaffold00227.G647 (CL07958) is encoded by the nucleotides of SEQ ID No: 569 which encodes the amino acid sequence of SEQ ID No: 570. This enzyme is believed to have Metal-binding Mitochondrion NAD Oxidoreductase, alcohol dehydrogenase activity.
  • Sequence Oxid-286 scaffbld00071.G964 (CL00580) is encoded by the nucleotides of SEQ ID No: 571 which encodes the amino acid sequence of SEQ ID No: 572. This enzyme is believed to have FMN binding, oxidoreductase activity.
  • Sequence Oxid-287 scaffold00071.G874 (CL00522) is encoded by the nucleotides of SEQ ID No: 573 which encodes the amino acid sequence of SEQ ID No: 574. This enzyme is believed to have fumarate reductase
  • Sequence Oxid-288 scaffold00071.G901 (CL00541) is encoded by the nucleotides of SEQ ID No: 575 which encodes the amino acid sequence of SEQ ID No: 576. This enzyme is believed to have FAD binding, tRNA dihydrouridine synthase activity.
  • Sequence Oxid-289 scaffold00071.G1736 (CL01038) is encoded by the nucleotides of SEQ ID No: 577 which encodes the amino acid sequence of SEQ ID No: 578. This enzyme is believed to have cytochrome-b5 reductase activity.
  • Sequence Oxid-290 scaffold00071.G2980 (CL01805) is encoded by the nucleotides of SEQ ID No: 579 which encodes the amino acid sequence of SEQ ID No: 580. This enzyme is believed to have acyl-CoA dehydrogenase activity, FAD binding activity.
  • Sequence Oxid-291 scaffold00071.G3041 (Cytochrome) is encoded by the nucleotides of SEQ ID No: 581 which encodes the amino acid sequence of SEQ ID No: 582. This enzyme is believed to have D-lactate dehydrogenase activityFAD binding (CL01846) activity.
  • Sequence Oxid-292 scaffold00075.G444 (CL03281) is encoded by the nucleotides of SEQ ID No: 583 which encodes the amino acid sequence of SEQ ID No: 584. This enzyme is believed to have FAD Flavo Protein, electron carrier activity.
  • Sequence Oxid-293 scaffold00075.G498 (CL03310) is encoded by the nucleotides of SEQ ID No: 585 which encodes the amino acid sequence of SEQ ID No: 586. This enzyme is believed to have FAD Flavo Protein, electron carrier activity.
  • Sequence Oxid-294 scaffold00075.G582 (CL03364
  • CL05169 DNA scaffold00075.G582
  • CL03364 CL05169 is encoded by the nucleotides of SEQ ID No: 587 which encodes the amino acid sequence of SEQ ID No: 588.
  • This enzyme is believed to have methylenetetrahydro folate reductase (NADPH) and FAD FlavoProtein NADP Oxidoreductase PhosphoProtein PF02219 1 5 1 20 GO:0005829 GO:0005634 GO:0004489 F:methylenetetrahydrofolate reductase (NADPH) GO:0009086 P:methionine biosynthetic process GO:0055114 P:oxidation reduction activity.
  • NADPH methylenetetrahydro folate reductase
  • FADPH methylenetetrahydrofolate reductase
  • Sequence Oxid-295 scaffold00075.G1087 (CL03644) is encoded by the nucleotides of SEQ ID No: 589 which encodes the amino acid sequence of SEQ ID No: 590. This enzyme is believed to have cytochrome-b5 reductase activity.
  • Sequence Oxid-296 scaffold00122.G187 (CL03910) is encoded by the nucleotides of SEQ ID No: 591 which encodes the amino acid sequence of SEQ ID No: 592. This enzyme is believed to have FAD Flavo Protein, oxidoreductase activity.
  • Sequence Oxid-297 scaffold00131.G377 (CL04457) is encoded by the nucleotides of SEQ ID No: 593 which encodes the amino acid sequence of SEQ ID No: 594. This enzyme is believed to have acyl-CoA dehydrogenase activity.
  • Sequence Oxid-298 scaffold00131.G684 (CL04636) is encoded by the nucleotides of SEQ ID No: 595 which encodes the amino acid sequence of SEQ ID No: 596. This enzyme is believed to have FAD FlavoProtein, oxidoreductase activity.
  • Sequence Oxid-299 scaffold00131.G1217 (CL04976) is encoded by the nucleotides of SEQ ID No: 597 which encodes the amino acid sequence of SEQ ID No: 598. This enzyme is believed to have acyl-CoA dehydrogenase activity, FAD binding activity.
  • Sequence Oxid-300 scaffold00142.G588 (CL08704) is encoded by the nucleotides of SEQ ID No: 599 which encodes the amino acid sequence of 600. This enzyme is believed to have 2 iron, 2 sulfur cluster binding, FAD binding, oxidoreductase activity.
  • Sequence Oxid-301 scaffold00214.G90 (CL02529) is encoded by the nucleotides of SEQ ID No: 601 which encodes the amino acid sequence of SEQ ID No: 602. This enzyme is believed to have FAD binding, NADH dehydrogenase (ubiquinone) activity.
  • Sequence Oxid-302 scaffold00227.G251 (CL08179) is encoded by the nucleotides of SEQ ID No: 603 which encodes the amino acid sequence of SEQ ID No: 604. This enzyme is believed to have 4 iron, 4 sulfur cluster binding, electron-transferring-flavoprotein dehydrogenase activity.
  • Sequence Oxid-303 scaffold00008.Gl (CL11660) is encoded by the nucleotides of SEQ ID No: 605 which encodes the amino acid sequence of SEQ ID No: 606. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity GO: 0042773 activity.
  • Sequence Oxid-304 scaffold00016.G15 (CL08920) is encoded by the nucleotides of SEQ ID No: 607 which encodes the amino acid sequence of SEQ ID No: 608. This enzyme is believed to have FAD binding, oxidoreductase activity.
  • Sequence Oxid-305 scaffold00016.G18 (CL08922) is encoded by the nucleotides of SEQ ID No: 609 which encodes the amino acid sequence of SEQ ID No: 610.
  • This enzyme is believed to have alcohol dehydrogenase (NADP+) activity, hydroxymethylfurfural reductase (NADH) activity.
  • Sequence Oxid-306 scaffold00016.G58 (CL08949) is encoded by the nucleotides of SEQ ID No: 611 which encodes the amino acid sequence of SEQ ID No: 612. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-307 scaffold00016.Gl 17 (CL08986) is encoded by the nucleotides of SEQ ID No: 613 which encodes the amino acid sequence of SEQ ID No: 614. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-308 scaffold00016.G162 (CL09014) is encoded by the nucleotides of SEQ ID No: 615 which encodes the amino acid sequence of SEQ ID No: 616. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-309 scaffold00016.G280 (CL09100) is encoded by the nucleotides of SEQ ID No: 617 which encodes the amino acid sequence of SEQ ID No: 618. This enzyme is believed to have L-xylulose reductase (NADP+) activity.
  • Sequence Oxid-310 scaffold00016.G288 (CL09105) is encoded by the nucleotides of SEQ ID No: 619 which encodes the amino acid sequence of SEQ ID No: 620. This enzyme is believed to have chorismate synthase activity, oxidoreductase activity.
  • Sequence Oxid-311 30_g scaffold00016.pathl .gene8 is encoded by the nucleotides of SEQ ID No: 621 which encodes the amino acid sequence of SEQ ID No: 622. This enzyme is believed to have
  • NADH hydro xymethylfurfural reductase
  • sequence Oxid-313 359_g scaffold00016.pathl .gene305 scaffold00016.G581 is encoded by the nucleotides of SEQ ID No: 625 which encodes the amino acid sequence of SEQ ID No: 626. This enzyme is believed to have 3-dehydroquinate synthase activity, shikimate 5-dehydrogenase activity.
  • Sequence Oxid-314 393_g is encoded by the nucleotides of SEQ ID No: 627 which encodes the amino acid sequence of SEQ ID No: 628. This enzyme is believed to have glycerol-3-phosphate dehydrogenase activity.
  • sequence Oxid-315 398_g scaffold00016.pathl .gene335 scaffold00016.G648 is encoded by the nucleotides of SEQ ID No: 629 which encodes the amino acid sequence of SEQ ID No: 630. This enzyme is believed to have oxoglutarate dehydrogenase succinyl-trans activity.
  • Sequence Oxid-316 438_g scaffold00016.pathl .gene371 scaffold00016.G695 is encoded by the nucleotides of SEQ ID No: 631 which encodes the amino acid sequence of SEQ ID No: 632. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
  • sequence Oxid-317 474_g scaffold00016.pathl .gene402 scaffold00016.G749 is encoded by the nucleotides of SEQ ID No: 633 which encodes the amino acid sequence of SEQ ID No: 634. This enzyme is believed to have alcohol dehydrogenase (NAD) activity.
  • NAD alcohol dehydrogenase
  • the enzyme identified as Sequence Oxid-3118 632_g scaflbld00016.pathl .gene545 scaffold00016.G996 is encoded by the nucleotides of SEQ ID No: 635 which encodes the amino acid sequence of SEQ ID No: 636. This enzyme is believed to have glyceraldehyde-3-phosphate dehydrogenase activity.
  • Sequence Oxid-320 718_g scaffold00016.pathl .gene617 is encoded by the nucleotides of SEQ ID No: 639 which encodes the amino acid sequence of SEQ ID No: 640. This enzyme is believed to have xanthine dehydrogenase activity.
  • sequence Oxid-321 789_g scaffold00016.pathl .gene675 scaffold00016.G1249 is encoded by the nucleotides of SEQ ID No: 641 which encodes the amino acid sequence of SEQ ID No: 642. This enzyme is believed to have aldehyde dehydrogenase (NAD) activity.
  • NAD aldehyde dehydrogenase
  • Sequence Oxid-322 1037_g is encoded by the nucleotides of SEQ ID No: 643 which encodes the amino acid sequence of SEQ ID No: 644.
  • This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
  • the enzyme identified as Sequence Oxid-323 1186_g scaffold00031.pathl .gene222 scaffold00031.G414 is encoded by the nucleotides of SEQ ID No: 645 which encodes the amino acid sequence of SEQ ID No: 646. This enzyme is believed to have L-malate dehydrogenase activity.
  • Sequence Oxid-324 1292_g scaffold00031.pathl .gene320 is encoded by the nucleotides of SEQ ID No: 647 which encodes the amino acid sequence of SEQ ID No: 648. This enzyme is believed to have D-lactate dehydrogenase (Cytochrome) activity.
  • sequence Oxid-325 1294_g scaffold00031.pathl .gene322 scaffold00031.G568 is encoded by the nucleotides of SEQ ID No: 649 which encodes the amino acid sequence of SEQ ID No: 650. This enzyme is believed to have pyruvate dehydrogenase acetyl-transferring activity.
  • Sequence Oxid-326 1412_g scaffold00031.G751 is encoded by the nucleotides of SEQ ID No: 651 which encodes the amino acid sequence of SEQ ID No: 652. This enzyme is believed to have 3-isopropylmalate dehydrogenase activity.
  • Sequence Oxid-327 1474_g scaffold00031.pathl .gene483 is encoded by the nucleotides of SEQ ID No: 653 which encodes the amino acid sequence of SEQ ID No: 654. This enzyme is believed to have NADH
  • ubiquinone dehydrogenase
  • Sequence Oxid-328 1589_g scaffold00031.pathl .gene571 is encoded by the nucleotides of SEQ ID No: 655 which encodes the amino acid sequence of SEQ ID No: 656. This enzyme is believed to have NADH
  • ubiquinone dehydrogenase
  • Sequence Oxid-329 1606_g scaffold00031.pathl .gene587 is encoded by the nucleotides of SEQ ID No: 657 which encodes the amino acid sequence of SEQ ID No: 658. This enzyme is believed to have prephenate dehydrogenase (NADP+) activity.
  • Sequence Oxid-330 161 l_g is encoded by the nucleotides of SEQ ID No: 659 which encodes the amino acid sequence of SEQ ID No: 660.
  • This enzyme is believed to have glutamate dehydrogenase activity.
  • Sequence Oxid-331 1694_g scaffold00031.pathl .gene670 is encoded by the nucleotides of SEQ ID No: 661 which encodes the amino acid sequence of SEQ ID No: 662. This enzyme is believed to have NADPH dehydrogenase activity.
  • Sequence Oxid-332 1753_g scaffold00031.pathl .gene729 scaffold00031.G1281 is encoded by the nucleotides of SEQ ID No: 663 which encodes the amino acid sequence of SEQ ID No: 664. This enzyme is believed to have 3-hydroxyisobutyrate dehydrogenase activity.
  • sequence Oxid-333 1779_g scaffold00031.pathl .gene754 is encoded by the nucleotides of SEQ ID No: 665 which encodes the amino acid sequence of SEQ ID No: 666. This enzyme is believed to have acyl-CoA dehydrogenase activity.
  • Sequence Oxid-334 1822_g scaffold00031.pathl .gene786 is encoded by the nucleotides of SEQ ID No: 667 which encodes the amino acid sequence of SEQ ID No: 668. This enzyme is believed to have dihydroorotate dehydrogenase activity.
  • the enzyme identified as Sequence Oxid-335 1855_g scaflbld00031.pathl .gene813 scaffold00031.G1450 is encoded by the nucleotides of SEQ ID No: 669 which encodes the amino acid sequence of SEQ ID No: 670. This enzyme is believed to have mannitol-1 -phosphate 5-dehydrogenase activity.
  • sequence Oxid-336 2041_g scaffold00031.pathl .gene953 scaffold00031.G1782 is encoded by the nucleotides of SEQ ID No: 671 which encodes the amino acid sequence of SEQ ID No: 672. This enzyme is believed to have L-iditol 2-dehydrogenase activity.
  • sequence Oxid-337 2115_g scaffold00050.pathl .genel2 is encoded by the nucleotides of SEQ ID No: 673 which encodes the amino acid sequence of SEQ ID No: 674. This enzyme is believed to have proline
  • sequence Oxid-339 2678_g scaffold00050.pathl .gene468 scaffold00050.G966 is encoded by the nucleotides of SEQ ID No: 677 which encodes the amino acid sequence of SEQ ID No: 678. This enzyme is believed to have acyl-CoA dehydrogenase activity.
  • Sequence Oxid-340 2682_g scaffold00050.pathl .gene472 is encoded by the nucleotides of SEQ ID No: 679 which encodes the amino acid sequence of SEQ ID No: 680. This enzyme is believed to have acyl-CoA dehydrogenase activity.
  • sequence Oxid-341 2813_g scaffold00050.pathl .gene585 scaffold00050.Gl 184 is encoded by the nucleotides of SEQ ID No: 681 which encodes the amino acid sequence of SEQ ID No: 682. This enzyme is believed to have quinate 5-dehydrogenase activity.
  • Sequence Oxid-342 2879_g scaffold00050.pathl .gene643 is encoded by the nucleotides of SEQ ID No: 683 which encodes the amino acid sequence of SEQ ID No: 684. This enzyme is believed to have dihydrolipoyl dehydrogenase activity.
  • Sequence Oxid-343 3035_g is encoded by the nucleotides of SEQ ID No: 685 which encodes the amino acid sequence of SEQ ID No: 686. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
  • Sequence Oxid-344 3108_g scaffold00050.G1648 is encoded by the nucleotides of SEQ ID No: 687 which encodes the amino acid sequence of SEQ ID No: 688. This enzyme is believed to have NADH
  • ubiquinone dehydrogenase
  • sequence Oxid-345 3228_g scaffold00065.pathl .genel scaffold00065.Gl is encoded by the nucleotides of SEQ ID No: 689 which encodes the amino acid sequence of SEQ ID No: 690. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
  • sequence Oxid-346 3253_g scaffold00071.pathl .genel0 scaffold00071.G21 is encoded by the nucleotides of SEQ ID No: 691 which encodes the amino acid sequence of SEQ ID No: 692. This enzyme is believed to have L-iditol 2-dehydrogenase activity.
  • Sequence Oxid-347 3282_g is encoded by the nucleotides of SEQ ID No: 693 which encodes the amino acid sequence of SEQ ID No: 694. This enzyme is believed to have D-lactate dehydrogenase (Cytochrome) activity.
  • sequence Oxid-348 3303_g scaffold00071.pathl .gene52 scaffold00071.G104 is encoded by the nucleotides of SEQ ID No: 695 which encodes the amino acid sequence of SEQ ID No: 696. This enzyme is believed to have succinate-semialdehyde dehydrogenase [NAD(P activity.
  • the enzyme identified as Sequence Oxid-349 343 l_g scaffold00071.pathl .genel65 scaffold00071.G332 is encoded by the nucleotides of SEQ ID No: 697 which encodes the amino acid sequence of SEQ ID No: 698. This enzyme is believed to have D-arabinitol 2-dehydrogenase activity.
  • sequence Oxid-350 3546_g scaffold00071.pathl .gene254 scaffold00071.G527 is encoded by the nucleotides of SEQ ID No: 699 which encodes the amino acid sequence of 700. This enzyme is believed to have L-iditol 2-dehydrogenase activity.
  • the enzyme identified as Sequence Oxid-351 3585_g scaffold00071.pathl .gene293 scaffold00071.G593 is encoded by the nucleotides of SEQ ID No: 701 which encodes the amino acid sequence of SEQ ID No: 702. This enzyme is believed to have succinate dehydrogenase (ubiquinone) activity.
  • the enzyme identified as Sequence Oxid-352 3624_g scaflbld00071.pathl .gene325 scaffold00071.G644 is encoded by the nucleotides of SEQ ID No: 703 which encodes the amino acid sequence of SEQ ID No: 704. This enzyme is believed to have glucose-6-phosphate dehydrogenase activity.
  • sequence Oxid-353 3725_g scaffold00071.pathl .gene419 scaffold00071.G784 is encoded by the nucleotides of SEQ ID No: 705 which encodes the amino acid sequence of SEQ ID No: 706. This enzyme is believed to have aldehyde dehydrogenase (NADP+) activity.
  • Sequence Oxid-354 3788_g scaffold00071.pathl .gene475 is encoded by the nucleotides of SEQ ID No: 707 which encodes the amino acid sequence of SEQ ID No: 708. This enzyme is believed to have succinate dehydrogenase activity.
  • sequence Oxid-355 3813_g scaffold00071.pathl .gene498 scaffold00071.G905 is encoded by the nucleotides of SEQ ID No: 709 which encodes the amino acid sequence of SEQ ID No: 710. This enzyme is believed to have succinate dehydrogenase (ubiquinone) activity.
  • sequence Oxid-356 3849_g scaffold00071.pathl .gene525 scaffold00071.G953 is encoded by the nucleotides of SEQ ID No : 711 which encodes the amino acid sequence of SEQ ID No: 712. This enzyme is believed to have homoisocitrate dehydrogenase activity.
  • the enzyme identified as Sequence Oxid-357 3893_g scaffold00071.pathl .gene569 scaffold00071.G1018 is encoded by the nucleotides of SEQ ID No: 713 which encodes the amino acid sequence of SEQ ID No: 714. This enzyme is believed to have L-aminoadipate-semialdehyde dehydrogenase activity.
  • Sequence Oxid-358 3904_g scaffold00071.G1033 is encoded by the nucleotides of SEQ ID No: 715 which encodes the amino acid sequence of SEQ ID No: 716. This enzyme is believed to have aldehyde dehydrogenase (NAD) activity.
  • NAD aldehyde dehydrogenase
  • the enzyme identified as Sequence Oxid-359 3907_g scaffold00071.pathl .gene584 scaffold00071.G1037 is encoded by the nucleotides of SEQ ID No: 717 which encodes the amino acid sequence of SEQ ID No: 718. This enzyme is believed to have L-lactate dehydrogenase activity.
  • the enzyme identified as Sequence Oxid-360 3973_g scaflbld00071.pathl .gene627 scaffold00071.Gl 160 is encoded by the nucleotides of SEQ ID No: 719 which encodes the amino acid sequence of SEQ ID No: 720. This enzyme is believed to have iso citrate dehydrogenase (NAD+) activity.
  • sequence Oxid-361 4020_g scaffold00071.pathl .gene663 scaffold00071.G1266 is encoded by the nucleotides of SEQ ID No: 721 which encodes the amino acid sequence of SEQ ID No: 722. This enzyme is believed to have glycerol-3-phosphate dehydrogenase (NAD+) activity.
  • sequence Oxid-362 4078_g scaffold00071.pathl .gene715 scaffold00071.G1360 is encoded by the nucleotides of SEQ ID No: 723 which encodes the amino acid sequence of SEQ ID No: 724. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
  • Sequence Oxid-363 4133_g scaffold00071.pathl .gene764 is encoded by the nucleotides of SEQ ID No: 725 which encodes the amino acid sequence of SEQ ID No: 726. This enzyme is believed to have NADPH dehydrogenase activity.
  • the enzyme identified as Sequence Oxid-364 4146_g scaffold00071.pathl .gene776 scaffold00071.G1457 is encoded by the nucleotides of SEQ ID No: 727 which encodes the amino acid sequence of SEQ ID No: 728. This enzyme is believed to have 3 -beta-hydro xy-delta5 -steroid dehydrogenase activity.
  • sequence Oxid-365 4158_g scaffold00071.pathl .gene786 scaffold00071.G1476 is encoded by the nucleotides of SEQ ID No: 729 which encodes the amino acid sequence of SEQ ID No: 730. This enzyme is believed to have succinate-semialdehyde dehydrogenase activity.
  • sequence Oxid-366 4163_g scaffold00071.pathl .gene791 scaffold00071.G1485 is encoded by the nucleotides of SEQ ID No: 731 which encodes the amino acid sequence of SEQ ID No: 732. This enzyme is believed to have pyridoxine 4-dehydrogenase activity.
  • the enzyme identified as Sequence Oxid-367 4300_g scaffold00071.pathl .gene902 scaffold00071.G1693 is encoded by the nucleotides of SEQ ID No: 733 which encodes the amino acid sequence of SEQ ID No: 734. This enzyme is believed to have histidinol dehydrogenase activity, phosphoribosyl-AMP cyclohydrolase activity.
  • the enzyme identified as Sequence Oxid-368 4326_g scaflbld00071.pathl .gene926 scaffold00071.G1722 is encoded by the nucleotides of SEQ ID No: 735 which encodes the amino acid sequence of SEQ ID No: 736. This enzyme is believed to have saccharopine dehydrogenase (NAD+, L-lysine- activity.
  • the enzyme identified as Sequence Oxid-369 4327_g scaffold00071.pathl .gene927 scaffold00071.G1723 is encoded by the nucleotides of SEQ ID No: 737 which encodes the amino acid sequence of SEQ ID No: 738. This enzyme is believed to have IMP dehydrogenase activity.
  • Sequence Oxid-370 4345_g is encoded by the nucleotides of SEQ ID No: 739 which encodes the amino acid sequence of SEQ ID No: 740. This enzyme is believed to have phospho gluconate dehydrogenase (decarboxylase) activity.
  • sequence Oxid-371 4370_g scaffold00071.pathl .gene967 scaffold00071.G1784 is encoded by the nucleotides of SEQ ID No: 741 which encodes the amino acid sequence of SEQ ID No: 742. This enzyme is believed to have l-pyrroline-5-carboxylate dehydrogenase activity.
  • scaffold00071.pathl .genel l33 scaffold00071.G2097 is encoded by the nucleotides of SEQ ID No: 743 which encodes the amino acid sequence of SEQ ID No: 744.
  • This enzyme is believed to have 3 -beta-hydro xy-delta5 -steroid dehydrogenase, sterol-4-alpha-carboxylate 3-dehydrogenase activity.
  • scaffold00071.pathl .genel l68 scaffold00071.G2157 is encoded by the nucleotides of SEQ ID No: 745 which encodes the amino acid sequence of SEQ ID No: 746. This enzyme is believed to have methylenetetrahydro folate dehydrogenase activity.
  • scaffold00071.pathl .genel276 is encoded by the nucleotides of SEQ ID No: 747 which encodes the amino acid sequence of SEQ ID No: 748. This enzyme is believed to have L-lactate dehydrogenase (Cytochrome) activity.
  • scaffold00071.pathl .genel294 scaffold00071.G2411 is encoded by the nucleotides of SEQ ID No: 749 which encodes the amino acid sequence of SEQ ID No: 750. This enzyme is believed to have 3 -beta-hydro xy-delta5 -steroid dehydrogenase activity.
  • scaffold00071.pathl .genel357 scaffold00071.G2544 is encoded by the nucleotides of SEQ ID No: 751 which encodes the amino acid sequence of SEQ ID No: 752. This enzyme is believed to have pyruvate dehydrogenase (acetyl-transferring) activity.
  • scaffold00071.pathl .genel439 scaffold00071.G2698 is encoded by the nucleotides of SEQ ID No: 753 which encodes the amino acid sequence of SEQ ID No: 754.
  • This enzyme is believed to have aspartate-semialdehyde dehydrogenase activity.
  • Sequence Oxid-378 5088_g scaffold00071.G2977 is encoded by the nucleotides of SEQ ID No: 755 which encodes the amino acid sequence of SEQ ID No: 756. This enzyme is believed to have D-arabinitol 2- dehydrogenase activity.
  • scaffold00071.pathl .genel581 is encoded by the nucleotides of SEQ ID No: 757 which encodes the amino acid sequence of SEQ ID No: 758. This enzyme is believed to have acyl-CoA dehydrogenase activity.
  • Sequence Oxid-380 513 l_g is encoded by the nucleotides of SEQ ID No: 759 which encodes the amino acid sequence of SEQ ID No: 760.
  • This enzyme is believed to have D-lactate dehydrogenase (Cytochrome) activity.
  • scaffold00071.pathl .genel777 scaffold00071.G3328 is encoded by the nucleotides of SEQ ID No: 761 which encodes the amino acid sequence of SEQ ID No: 762.
  • This enzyme is believed to have aldehyde reductase activity, glucose 1- dehydrogenase (NADP+) activity.
  • scaffold00071.pathl .genel843 scaffold00071.G3467 is encoded by the nucleotides of SEQ ID No: 763 which encodes the amino acid sequence of SEQ ID No: 764.
  • This enzyme is believed to have aldehyde dehydrogenase (NAD) activity.
  • scaffold00071.pathl .genel862 scaffold00071.G3501 is encoded by the nucleotides of SEQ ID No: 765 which encodes the amino acid sequence of SEQ ID No: 766. This enzyme is believed to have L-lactate dehydrogenase activity.
  • scaffold00071.pathl .genel869 scaffold00071.G3512 is encoded by the nucleotides of SEQ ID No: 767 which encodes the amino acid sequence of SEQ ID No: 768. This enzyme is believed to have glycine dehydrogenase (decarboxylating) activity.
  • the enzyme identified as Sequence Oxid-385 5625_g scaffold00075.pathl .genel71 scaffold00075.G374 is encoded by the nucleotides of SEQ ID No: 769 which encodes the amino acid sequence of SEQ ID No: 770. This enzyme is believed to have 3-hydroxyisobutyrate dehydrogenase activity, histone-lysine N- methyltransferase activity,phospho gluconate dehydrogenase (decarboxylase) activity.
  • sequence Oxid-386 5768_g scaffold00075.pathl .gene311 is encoded by the nucleotides of SEQ ID No: 771 which encodes the amino acid sequence of SEQ ID No: 772. This enzyme is believed to have isocitrate dehydrogenase (NAD+) activity.
  • sequence Oxid-387 5850_g scaffold00075.pathl .gene393 scaffold00075.G724 is encoded by the nucleotides of SEQ ID No: 773 which encodes the amino acid sequence of SEQ ID No: 774. This enzyme is believed to have phospho gluconate dehydrogenase (decarboxylase) activity.
  • Sequence Oxid-388 5919_g is encoded by the nucleotides of SEQ ID No: 775 which encodes the amino acid sequence of SEQ ID No: 776. This enzyme is believed to have L-lactate dehydrogenase (Cytochrome) activity.
  • the enzyme identified as Sequence Oxid-389 5937_g scaffold00075.pathl .gene469 is encoded by the nucleotides of SEQ ID No: 777 which encodes the amino acid sequence of SEQ ID No: 778. This enzyme is believed to have 3-dehydroquinate dehydratase activity, shikimate 5-dehydrogenase activity, shikimate kinase activity.
  • the enzyme identified as Sequence Oxid-390 613 l_g scaffold00075.pathl .gene641 scaffold00075.Gl 167 is encoded by the nucleotides of SEQ ID No: 779 which encodes the amino acid sequence of SEQ ID No: 780. This enzyme is believed to have betaine-aldehyde dehydrogenase activity.
  • the enzyme identified as Sequence Oxid-391 6269_g scaffold00092.pathl .gene24 scaffold00092.G43 is encoded by the nucleotides of SEQ ID No: 781 which encodes the amino acid sequence of SEQ ID No: 782. This enzyme is believed to have precorrin-2 dehydrogenase activity,F:sirohydrochlorin ferrochelatase activity.
  • the enzyme identified as Sequence Oxid-392 6348_g scaffold00092.pathl .gene81 scaffold00092.G162 is encoded by the nucleotides of SEQ ID No: 783 which encodes the amino acid sequence of SEQ ID No: 784. This enzyme is believed to have L-malate dehydrogenase activity.
  • Sequence Oxid-393 6537_g scaffold00092.pathl .gene235 is encoded by the nucleotides of SEQ ID No: 785 which encodes the amino acid sequence of SEQ ID No: 786. This enzyme is believed to have cellobiose dehydrogenase (acceptor) activity.
  • sequence Oxid-394 6692_g scaffold00092.pathl .gene387 scaffold00092.G738 is encoded by the nucleotides of SEQ ID No: 787 which encodes the amino acid sequence of SEQ ID No: 788. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
  • sequence Oxid-395 6950_g scaffold00122.pathl .genel07 scaffold00122.G197 is encoded by the nucleotides of SEQ ID No: 789 which encodes the amino acid sequence of SEQ ID No: 790. This enzyme is believed to have aldehyde dehydrogenase (NAD) activity.
  • NAD aldehyde dehydrogenase
  • ubiquinone dehydrogenase
  • Sequence Oxid-397 7048_g scaffold00131.pathl .gene70 scaffold00131.G132 is encoded by the nucleotides of SEQ ID No: 793 which encodes the amino acid sequence of SEQ ID No: 794. This enzyme is believed to have alcohol dehydrogenase (NADP+) activity.
  • sequence Oxid-398 7101_g scaffold00131.pathl .genel20 scaffold00131.G220 is encoded by the nucleotides of SEQ ID No: 795 which encodes the amino acid sequence of SEQ ID No: 796. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
  • the enzyme identified as Sequence Oxid-399 7117_g scaffold00131.pathl .genel32 scaffold00131.G239 is encoded by the nucleotides of SEQ ID No: 797 which encodes the amino acid sequence of SEQ ID No: SEQ ID No: 798. This enzyme is believed to have acyl-CoA dehydrogenase activity.
  • the enzyme identified as Sequence Oxid-400 7135_g scaflbld00131.pathl .genel50 scaffold00131.G266 is encoded by the nucleotides of SEQ ID No: 799 which encodes the amino acid sequence of 800. This enzyme is believed to have 3- dehydroquinate synthase activity, 3-phosphoshikimate 1- carboxyvinyltransferas,shikimate 5-dehydrogenase activity, shikimate kinase activity.
  • Sequence Oxid-401 7136_g scaffold00131.pathl .genel52 is encoded by the nucleotides of SEQ ID No: 801 which encodes the amino acid sequence of SEQ ID No: 802. This enzyme is believed to have dihydroorotate dehydrogenase activity.
  • Sequence Oxid-402 7207_g scaffold00131.pathl .gene222 is encoded by the nucleotides of SEQ ID No: 803 which encodes the amino acid sequence of SEQ ID No: 804. This enzyme is believed to have acyl-CoA dehydrogenase activity.
  • sequence Oxid-403 7244_g scaffold00131.pathl .gene256 scaffold00131.G441 is encoded by the nucleotides of SEQ ID No: 805 which encodes the amino acid sequence of SEQ ID No: 806. This enzyme is believed to have malate dehydrogenase (oxaloacetate-decarboxylase) activity.
  • sequence Oxid-404 7344_g scaffold00131.pathl .gene349 scaffold00131.G586 is encoded by the nucleotides of SEQ ID No: 807 which encodes the amino acid sequence of SEQ ID No: 808. This enzyme is believed to have pyruvate dehydrogenase (acetyl-transferring GO:0015976 activity.
  • sequence Oxid-405 7359_g scaffold00131.pathl .gene365 is encoded by the nucleotides of SEQ ID No: 809 which encodes the amino acid sequence of SEQ ID No: 810. This enzyme is believed to have oxidoreductase activity, acting on the CH-0 activity.
  • Sequence Oxid-406 7681_g scaffold00131.Gl 152 is encoded by the nucleotides of SEQ ID No : 811 which encodes the amino acid sequence of SEQ ID No: 812. This enzyme is believed to have succinate dehydrogenase activity.
  • sequence Oxid-407 7688_g scaffold00131.pathl .gene645 scaffold00131.G1161 is encoded by the nucleotides of SEQ ID No: 813 which encodes the amino acid sequence of SEQ ID No: 814. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
  • the enzyme identified as Sequence Oxid-408 7715_g scaflbld00131.pathl .gene672 scaffold00131.G1199 is encoded by the nucleotides of SEQ ID No: 815 which encodes the amino acid sequence of SEQ ID No: 816. This enzyme is believed to have glutamate dehydrogenase (NADP+) activity.
  • sequence Oxid-409 7732_g scaffold00131.pathl .gene687 is encoded by the nucleotides of SEQ ID No: 817 which encodes the amino acid sequence of SEQ ID No: 818. This enzyme is believed to have acyl-CoA dehydrogenase activity.
  • sequence Oxid-410 7808_g scaffold00131.pathl .gene747 scaffold00131.G1330 is encoded by the nucleotides of SEQ ID No: 819 which encodes the amino acid sequence of SEQ ID No: 820. This enzyme is believed to have phosphoglycerate dehydrogenase activity.
  • scaffold00131.pathl .gene895 is encoded by the nucleotides of SEQ ID No: 821 which encodes the amino acid sequence of SEQ ID No: 822. This enzyme is believed to have saccharopine dehydrogenase (NADP+, L-glutamase) activity.
  • scaffold00131.pathl .genel039 scaffold00131.G1851 is encoded by the nucleotides of SEQ ID No: 823 which encodes the amino acid sequence of SEQ ID No: 824. This enzyme is believed to have S-(hydroxymethyl)glutathione dehydrogenase activity.
  • scaffold00131.pathl .genel073 is encoded by the nucleotides of SEQ ID No: 825 which encodes the amino acid sequence of SEQ ID No: 826. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
  • Sequence Oxid-414 8429_g scaffold00137.pathl .gene47 is encoded by the nucleotides of SEQ ID No: 827 which encodes the amino acid sequence of SEQ ID No: 828. This enzyme is believed to have carbohydrate binding, cellobiose dehydrogenase (acceptor) activity.
  • Sequence Oxid-415 8601_g scaffold00142.pathl .gene76 scaffold00142.G177 is encoded by the nucleotides of SEQ ID No: 829 which encodes the amino acid sequence of SEQ ID No: 830. This enzyme is believed to have iso citrate dehydrogenase (NADP+) activity.
  • scaffold00142.pathl .gene91 is encoded by the nucleotides of SEQ ID No: 831 which encodes the amino acid sequence of SEQ ID No: 832. This enzyme is believed to have methylenetetrahydro folate dehydrogenase activity.
  • scaffold00142.G217 scaffold00142.pathl .genel01, scaffold00142.pathl .genel02 is encoded by the nucleotides of SEQ ID No: 833 which encodes the amino acid sequence of SEQ ID No: 834. This enzyme is believed to have NADH
  • ubiquinone dehydrogenase
  • scaffold00142.pathl .genel09 is encoded by the nucleotides of SEQ ID No: 835 which encodes the amino acid sequence of SEQ ID No: 836. This enzyme is believed to have aldehyde dehydrogenase [NAD(P)+] activity.
  • scaffold00142.pathl .genel36 is encoded by the nucleotides of SEQ ID No: 837 which encodes the amino acid sequence of SEQ ID No: 838. This enzyme is believed to have cellobiose dehydrogenase (acceptor) activity.
  • scaffold00142.patnl .genel72 is encoded by the nucleotides of SEQ ID No: 839 which encodes the amino acid sequence of SEQ ID No: 840. This enzyme is believed to have phospho gluconate dehydrogenase (decarboxylase) activity.
  • scaffold00169.pathl .genel43 is encoded by the nucleotides of SEQ ID No: 841 which encodes the amino acid sequence of SEQ ID No: 842. This enzyme is believed to have alcohol dehydrogenase (NADP+) activity, hydroxymethylfurfural reductase (NADH) activity.
  • NADP+ alcohol dehydrogenase
  • NADH hydroxymethylfurfural reductase
  • NADP+ dehydrogenase
  • NADH hydroxymethylfurfural reductase
  • sequence Oxid-423 9103_g scaffold00169.G346 scaffold00169.pathl .genel70 is encoded by the nucleotides of SEQ ID No: 845 which encodes the amino acid sequence of SEQ ID No: 846. This enzyme is believed to have acyl-CoA dehydrogenase activity.
  • scaffold00214.pathl .gene51 is encoded by the nucleotides of SEQ ID No: 847 which encodes the amino acid sequence of SEQ ID No: 848. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
  • scaffold00227.pathl .gene78 is encoded by the nucleotides of SEQ ID No: 849 which encodes the amino acid sequence of SEQ ID No: 850. This enzyme is believed to have phosphoglycerate dehydrogenase activity.
  • scaffold00227.pathl .gene80 is encoded by the nucleotides of SEQ ID No: 851 which encodes the amino acid sequence of SEQ ID No: 852. This enzyme is believed to have phosphoglycerate dehydrogenase activity.
  • scaffold00227.pathl .gene204 is encoded by the nucleotides of SEQ ID No: 853 which encodes the amino acid sequence of SEQ ID No: 854. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
  • scaffold00227.pathl .gene303 is encoded by the nucleotides of SEQ ID No: 855 which encodes the amino acid sequence of SEQ ID No: 856. This enzyme is believed to have homo serine dehydrogenase activity.
  • scaffold00227.pathl .gene360 is encoded by the nucleotides of SEQ ID No: 857 which encodes the amino acid sequence of SEQ ID No: 858. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
  • the enzyme identified as Sequence Oxid-430 8277_g scaffold00131.G2107 scaffold00131.pathl .genel l68 is encoded by the nucleotides of SEQ ID No: 859 which encodes the amino acid sequence of SEQ ID No: 860. This enzyme is believed to have glutamate-5-semialdehyde dehydrogenase activity.
  • scaffold00142.pathl .genel80 is encoded by the nucleotides of SEQ ID No: 861 which encodes the amino acid sequence of SEQ ID No: 862. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-432 8723_g scaffold00142.pathl .genel81 is encoded by the nucleotides of SEQ ID No: 863 which encodes the amino acid sequence of SEQ ID No: 864. This enzyme is believed to have flavin-containing monooxygenase activity.
  • scaffold00142.pathl .gene280 is encoded by the nucleotides of SEQ ID No: 865 which encodes the amino acid sequence of SEQ ID No: 866. This enzyme is believed to have monooxygenase activity.
  • scaffold00142.pathl .gene280, scaffold00142.pathl .gene281 is encoded by the nucleotides of SEQ ID No: 867 which encodes the amino acid sequence of SEQ ID No: 868. This enzyme is believed to have monooxygenase activity.
  • scaffold00142.pathl .gene289 is encoded by the nucleotides of SEQ ID No: 869 which encodes the amino acid sequence of SEQ ID No: 870. This enzyme is believed to have monooxygenase activity.
  • scaffold00169.pathl .genel6 is encoded by the nucleotides of SEQ ID No: 871 which encodes the amino acid sequence of SEQ ID No: 872. This enzyme is believed to have monooxygenase activity.
  • scaffold00169.pathl .gene20 is encoded by the nucleotides of SEQ ID No: 873 which encodes the amino acid sequence of SEQ ID No: 874. This enzyme is believed to have monooxygenase activity.
  • scaffold00169.pathl .genel37 is encoded by the nucleotides of SEQ ID No: 875 which encodes the amino acid sequence of SEQ ID No: 876. This enzyme is believed to have monooxygenase activity.
  • scaffold00169.pathl .genel58 is encoded by the nucleotides of SEQ ID No: 877 which encodes the amino acid sequence of SEQ ID No: 878. This enzyme is believed to have flavin-containing monooxygenase activity.
  • scaffold00169.G318 is encoded by the nucleotides of SEQ ID No: 879 which encodes the amino acid sequence of SEQ ID No: 880. This enzyme is believed to have flavin-containing monooxygenase activity.
  • Sequence Oxid-441 9087_g is encoded by the nucleotides of SEQ ID No: 881 which encodes the amino acid sequence of SEQ ID No: 882.
  • This enzyme is believed to have flavin-containing monooxygenase activity.
  • scaffold00169.pathl .genel61 is encoded by the nucleotides of SEQ ID No: 883 which encodes the amino acid sequence of SEQ ID No: 884. This enzyme is believed to have monooxygenase activity.
  • scaffold00169.pathl .genel62 is encoded by the nucleotides of SEQ ID No: 885 which encodes the amino acid sequence of SEQ ID No: 886. This enzyme is believed to have flavin-containing monooxygenase activity.
  • scaffold00169.pathl .genel95 is encoded by the nucleotides of SEQ ID No: 887 which encodes the amino acid sequence of SEQ ID No: 888. This enzyme is believed to have monooxygenase activity.
  • scaffold00169.pathl .gene209 is encoded by the nucleotides of SEQ ID No: 889 which encodes the amino acid sequence of SEQ ID No: 890. This enzyme is believed to have monooxygenase activity.
  • scaffold00214.G10 scaffold00214.Gl 1 scafGerman00214.pathl .gene7,
  • scaffblg00214.pathl .gene8 is encoded by the nucleotides of SEQ ID No: 893 which encodes the amino acid sequence of SEQ ID No: 894. This enzyme is believed to have monooxygenase activity.
  • the enzyme identified as Sequence Oxid-448 9315_g scaffold00214.G22 scaffold00214.pathl .genel6 is encoded by the nucleotides of SEQ ID No: 895 which encodes the amino acid sequence of SEQ ID No: 896. This enzyme is believed to have monooxygenase activity.
  • scaffold00227.pathl .gene52 is encoded by the nucleotides of SEQ ID No: 897 which encodes the amino acid sequence of SEQ ID No: 898. This enzyme is believed to have monooxygenase activity.
  • scaffold00227.pathl .genel06 is encoded by the nucleotides of SEQ ID No: 899 which encodes the amino acid sequence of 900. This enzyme is believed to have monooxygenase activity.
  • scaffold00227.pathl .gene224 is encoded by the nucleotides of SEQ ID No: 901 which encodes the amino acid sequence of SEQ ID No: 902. This enzyme is believed to have ent-kaurene oxidase activity.
  • scaffold00227.pathl .gene379 is encoded by the nucleotides of SEQ ID No: 903 which encodes the amino acid sequence of SEQ ID No: 904. This enzyme is believed to have monooxygenase activity.
  • scaffold00016.pathl .genel75 is encoded by the nucleotides of SEQ ID No: 905 which encodes the amino acid sequence of SEQ ID No: 906. This enzyme is believed to have phenol 2-monooxygenase activity.
  • Sequence Oxid-454 671_g (CL09554) is encoded by the nucleotides of SEQ ID No: 907 which encodes the amino acid sequence of SEQ ID No: 908. This enzyme is believed to have monooxygenase activity.
  • scaffold00019.pathl .gene7 is encoded by the nucleotides of SEQ ID No: 909 which encodes the amino acid sequence of SEQ ID No: 910. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-456 887_g is encoded by the nucleotides of SEQ ID No: 911 which encodes the amino acid sequence of SEQ ID No: 912. This enzyme is believed to have monooxygenase activity.
  • scaffbld00019.pathl .genel5 is encoded by the nucleotides of SEQ ID No: 913 which encodes the amino acid sequence of SEQ ID No: 914. This enzyme is believed to have monooxygenase activity.
  • scaffold00031.G18, scaffold00031.pathl .genel4, scaffold00031.pathl .genel5 is encoded by the nucleotides of SEQ ID No: 915 which encodes the amino acid sequence of SEQ ID No: 916. This enzyme is believed to have monooxygenase activity.
  • scaffold00031.pathl .gene42, scaffold00031.pathl .gene43 is encoded by the nucleotides of SEQ ID No: 917 which encodes the amino acid sequence of SEQ ID No: 918. This enzyme is believed to have phenol 2-monooxygenase activity.
  • scaffold00031.pathl .gene69 is encoded by the nucleotides of SEQ ID No: 919 which encodes the amino acid sequence of SEQ ID No: 920. This enzyme is believed to have monooxygenase activity.
  • scaffold00031.pathl .genel 15 is encoded by the nucleotides of SEQ ID No: 921 which encodes the amino acid sequence of SEQ ID No: 922. This enzyme is believed to have flavin-containing monooxygenase activity.
  • pathl . gene252 is encoded by the nucleotides of SEQ ID No: 923 which encodes the amino acid sequence of SEQ ID No: 924. This enzyme is believed to have monooxygenase activity.
  • pathl . gene263 is encoded by the nucleotides of SEQ ID No: 925 which encodes the amino acid sequence of SEQ ID No: 926. This enzyme is believed to have monooxygenase activity.
  • pathl . gene521 is encoded by the nucleotides of SEQ ID No: 927 which encodes the amino acid sequence of SEQ ID No: 928. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-465 1643_g scaffold00031.Gl 133 is encoded by the nucleotides of SEQ ID No: 929 which encodes the amino acid sequence of SEQ ID No: 930. This enzyme is believed to have monooxygenase activity.
  • scaffold00031.pathl .gene780 is encoded by the nucleotides of SEQ ID No: 931 which encodes the amino acid sequence of SEQ ID No: 932. This enzyme is believed to have monooxygenase activity.
  • scaffold00031.pathl .gene781 is encoded by the nucleotides of SEQ ID No: 933 which encodes the amino acid sequence of SEQ ID No: 934. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-468 1820_g scaffold00031.pathl .gene783 CL02839 is encoded by the nucleotides of SEQ ID No: 935 which encodes the amino acid sequence of SEQ ID No: 936. This enzyme is believed to have monooxygenase activity.
  • scaffold00031.pathl .gene823 is encoded by the nucleotides of SEQ ID No: 937 which encodes the amino acid sequence of SEQ ID No: 938. This enzyme is believed to have flavin-containing monooxygenase activity.
  • scaffold00050.pathl .genel 16 is encoded by the nucleotides of SEQ ID No: 939 which encodes the amino acid sequence of SEQ ID No: 940. This enzyme is believed to have flavin-containing monooxygenase activity.
  • scaffold00050.pathl .genel29 is encoded by the nucleotides of SEQ ID No: 941 which encodes the amino acid sequence of SEQ ID No: 942. This enzyme is believed to have monooxygenase activity.
  • scaffold00050.pathl .genel30 is encoded by the nucleotides of SEQ ID No: 943 which encodes the amino acid sequence of SEQ ID No: 944. This enzyme is believed to have monooxygenase activity.
  • scaffold00050.pathl .genel45 is encoded by the nucleotides of SEQ ID No: 947 which encodes the amino acid sequence of SEQ ID No: 948. This enzyme is believed to have linoleate diol synthase activity, monooxygenase activity, peroxidase activity.
  • scaffold00050.pathl .genel87 is encoded by the nucleotides of SEQ ID No: 949 which encodes the amino acid sequence of SEQ ID No: 950. This enzyme is believed to have monooxygenase activity.
  • scaffold00050.pathl .gene246 is encoded by the nucleotides of SEQ ID No: 953 which encodes the amino acid sequence of SEQ ID No: 954. This enzyme is believed to have flavin-containing monooxygenase activity.
  • Sequence Oxid-478 2418_g is encoded by the nucleotides of SEQ ID No: 955 which encodes the amino acid sequence of SEQ ID No: 956. This enzyme is believed to have cyclohexanone monooxygenase activity.
  • scaffold00050.pathl .gene325 is encoded by the nucleotides of SEQ ID No: 957 which encodes the amino acid sequence of SEQ ID No: 958. This enzyme is believed to have kynurenine 3 -monooxygenase activity.
  • scaffold00050.G900 scaffold00050.pathl .gene425 is encoded by the nucleotides of SEQ ID No: 959 which encodes the amino acid sequence of SEQ ID No: 960. This enzyme is believed to have flavin-containing monooxygenase activity.
  • sequence Oxid-481 2725_g scaffold00050.G1038 scaffold00050.pathl .gene511 is encoded by the nucleotides of SEQ ID No: 961 which encodes the amino acid sequence of SEQ ID No: 962. This enzyme is believed to have monooxygenase activity.
  • scaffold00050.pathl .gene514 is encoded by the nucleotides of SEQ ID No: 963 which encodes the amino acid sequence of SEQ ID No: 964. This enzyme is believed to have monooxygenase activity.
  • scaffold00050.pathl .gene515 is encoded by the nucleotides of SEQ ID No: 965 which encodes the amino acid sequence of SEQ ID No: 966. This enzyme is believed to have monooxygenase activity.
  • scaffold00050.pathl .gene702 is encoded by the nucleotides of SEQ ID No: 967 which encodes the amino acid sequence of SEQ ID No: 968. This enzyme is believed to have monooxygenase activity.
  • scaffold00050.pathl .gene747 is encoded by the nucleotides of SEQ ID No: 969 which encodes the amino acid sequence of SEQ ID No: 970. This enzyme is believed to have monooxygenase activity.
  • sequence Oxid-486 3022_g scaffold00050.G1491, scaffold00050.G1492 scaffold00050.pathl .gene784 is encoded by the nucleotides of SEQ ID No: 971 which encodes the amino acid sequence of SEQ ID No: 972.
  • This enzyme is believed to have monooxygenase activity.
  • scaffold00050.pathl .gene821 is encoded by the nucleotides of SEQ ID No: 973 which encodes the amino acid sequence of SEQ ID No: 974. This enzyme is believed to have monooxygenase activity.
  • scaffold00050.pathl .gene838 is encoded by the nucleotides of SEQ ID No: 975 which encodes the amino acid sequence of SEQ ID No: 976. This enzyme is believed to have monooxygenase activity.
  • scaffold00050.pathl .gene861 is encoded by the nucleotides of SEQ ID No: 977 which encodes the amino acid sequence of SEQ ID No: 978. This enzyme is believed to have aromatase activity, NADPH-hemoprotein reductase activity.
  • Sequence Oxid-490 3123_g scaffold00050.G1667 is encoded by the nucleotides of SEQ ID No: 979 which encodes the amino acid sequence of SEQ ID No: 980. This enzyme is believed to have monooxygenase activity.
  • scaffold00050.pathl .gene864 is encoded by the nucleotides of SEQ ID No: 981 which encodes the amino acid sequence of SEQ ID No: 982. This enzyme is believed to have monooxygenase activity.
  • scaffold00053.pathl .genel3 is encoded by the nucleotides of SEQ ID No: 983 which encodes the amino acid sequence of SEQ ID No: 984. This enzyme is believed to have monooxygenase activity.
  • scaffold00053.pathl .gene26 is encoded by the nucleotides of SEQ ID No: 985 which encodes the amino acid sequence of SEQ ID No: 986. This enzyme is believed to have monooxygenase activity.
  • scaffold00068.pathl .gene2 is encoded by the nucleotides of SEQ ID No: 987 which encodes the amino acid sequence of SEQ ID No: 988. This enzyme is believed to have monooxygenase activity.
  • scaffold00071.pathl .gene285 is encoded by the nucleotides of SEQ ID No: 989 which encodes the amino acid sequence of SEQ ID No: 990. This enzyme is believed to have sterol 14-demethylase activity.
  • scaffold00071.pathl .gene321 is encoded by the nucleotides of SEQ ID No: 991 which encodes the amino acid sequence of SEQ ID No: 992. This enzyme is believed to have oxidoreductase activity, acting on paired d activity.
  • scaffold00071.pathl .gene427 is encoded by the nucleotides of SEQ ID No: 993 which encodes the amino acid sequence of SEQ ID No: 994. This enzyme is believed to have phenol 2-monooxygenase activity.
  • scaffold00071.pathl .gene427 is encoded by the nucleotides of SEQ ID No: 995 which encodes the amino acid sequence of SEQ ID No: 996. This enzyme is believed to have monooxygenase activity.
  • scaffold00071.pathl .gene459 is encoded by the nucleotides of SEQ ID No: 997 which encodes the amino acid sequence of SEQ ID No: 998. This enzyme is believed to have monophenol monooxygenase activity.
  • Sequence Oxid-500 3805_g scaffold00071.pathl .gene492 is encoded by the nucleotides of SEQ ID No: 999 which encodes the amino acid sequence of SEQ ID No: 1000. This enzyme is believed to have dopamine beta- monooxygenase activity.
  • Sequence Oxid-501 3903_g scaffold00071.pathl .gene580 is encoded by the nucleotides of SEQ ID No: 1001 which encodes the amino acid sequence of SEQ ID No: 1002. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-502 3965_g scaffold00071.pathl .gene621 is encoded by the nucleotides of SEQ ID No: 1003 which encodes the amino acid sequence of SEQ ID No: 1004. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-503 4080_g scaffold00071.pathl .gene716 is encoded by the nucleotides of SEQ ID No: 1005 which encodes the amino acid sequence of SEQ ID No: 1006. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-504 4268_g scaffold00071.pathl .gene875 is encoded by the nucleotides of SEQ ID No: 1007 which encodes the amino acid sequence of SEQ ID No: 1008. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-505 428 l_g scaffold00071.pathl .gene885 is encoded by the nucleotides of SEQ ID No: 1009 which encodes the amino acid sequence of SEQ ID No: 1010. This enzyme is believed to have monooxygenase activity.
  • scaffold00071.pathl .gene 1013 is encoded by the nucleotides of SEQ ID No : 1011 which encodes the amino acid sequence of SEQ ID No: 1012. This enzyme is believed to have monooxygenase activity.
  • scaffold00071. athl . genel020 is encoded by the nucleotides of SEQ ID No: 1013 which encodes the amino acid sequence of SEQ ID No: 1014. This enzyme is believed to have monooxygenase activity.
  • pathl . genel 188 is encoded by the nucleotides of SEQ ID No: 1015 which encodes the amino acid sequence of SEQ ID No: 1016. This enzyme is believed to have monooxygenase activity.
  • pathl . genel246 is encoded by the nucleotides of SEQ ID No: 1017 which encodes the amino acid sequence of SEQ ID No: 1018. This enzyme is believed to have monooxygenase activity.
  • scaffold00071.pathl .genel812 is encoded by the nucleotides of SEQ ID No: 1019 which encodes the amino acid sequence of SEQ ID No: 1020. This enzyme is believed to have monooxygenase activity.
  • sequence Oxid-512 581 l_g scaffold00075. pathl . gene356 is encoded by the nucleotides of SEQ ID No: 1023 which encodes the amino acid sequence of SEQ ID No: 1024. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-513 5910_g is encoded by the nucleotides of SEQ ID No: 1025 which encodes the amino acid sequence of SEQ ID No: 1026. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-514 591 l_g is encoded by the nucleotides of SEQ ID No: 1027 which encodes the amino acid sequence of SEQ ID No: 1028. This enzyme is believed to have monooxygenase activity.
  • sequence Oxid-515 5928_g scaflbld00075.pathl .gene459 is encoded by the nucleotides of SEQ ID No: 1029 which encodes the amino acid sequence of SEQ ID No: 1030. This enzyme is believed to have monooxygenase activity.
  • sequence Oxid-516 5977_g scaffold00075.pathl .gene504 is encoded by the nucleotides of SEQ ID No: 1031 which encodes the amino acid sequence of SEQ ID No: 1032. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-517 6245_g scaffold00092.pathl .gene2 is encoded by the nucleotides of SEQ ID No: 1033 which encodes the amino acid sequence of SEQ ID No: 1034. This enzyme is believed to have monooxygenase activity.
  • the enzyme identified as Sequence Oxid-518 6253_g scaffold00092.pathl .gene9 is encoded by the nucleotides of SEQ ID No: 1035 which encodes the amino acid sequence of SEQ ID No: 1036. This enzyme is believed to have Oxidoreductase activity.
  • sequence Oxid-519 6265_g scaffold00092.pathl .gene20 is encoded by the nucleotides of SEQ ID No: 1037 which encodes the amino acid sequence of SEQ ID No: 1038. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-520 6288_g is encoded by the nucleotides of SEQ ID No: 1039 which encodes the amino acid sequence of SEQ ID No: 1040. This enzyme is believed to have monooxygenase activity.
  • sequence Oxid-521 6289_g scaffold00092.pathl .gene41 is encoded by the nucleotides of SEQ ID No: 1041 which encodes the amino acid sequence of SEQ ID No: 1042. This enzyme is believed to have monooxygenase activity.
  • sequence Oxid-522 629 l_g scaffold00092.pathl .gene42 is encoded by the nucleotides of SEQ ID No: 1043 which encodes the amino acid sequence of SEQ ID No: 1044. This enzyme is believed to have monooxygenase activity.
  • sequence Oxid-523 6302_g scaffold00092.G89 scaffold00092.pathl .gene52 is encoded by the nucleotides of SEQ ID No: 1045 which encodes the amino acid sequence of SEQ ID No: 1046. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-524 6303_g scaffold00092.pathl .gene52 is encoded by the nucleotides of SEQ ID No: 1047 which encodes the amino acid sequence of SEQ ID No: 1048. This enzyme is believed to have monooxygenase activity.
  • scaffold00092.pathl .gene72 is encoded by the nucleotides of SEQ ID No: 1049 which encodes the amino acid sequence of SEQ ID No: 1050. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-526 634 l_g is encoded by the nucleotides of SEQ ID No: 1051 which encodes the amino acid sequence of SEQ ID No: 1052. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-527 6343_g scaffold00092.pathl .gene76 is encoded by the nucleotides of SEQ ID No: 1053 which encodes the amino acid sequence of SEQ ID No: 1054. This enzyme is believed to have monooxygenase activity.
  • the enzyme identified as Sequence Oxid-528 6368_g scaffold00092.pathl .genel03 is encoded by the nucleotides of SEQ ID No: 1055 which encodes the amino acid sequence of SEQ ID No: 1056. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-529 6423_g scaffold00092.pathl .genel47 is encoded by the nucleotides of SEQ ID No: 1057 which encodes the amino acid sequence of SEQ ID No: 1058. This enzyme is believed to have monooxygenase activity.
  • scaffold00092.pathl .genel67 is encoded by the nucleotides of SEQ ID No: 1059 which encodes the amino acid sequence of SEQ ID No: 1060. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-531 6808_g is encoded by the nucleotides of SEQ ID No: 1061 which encodes the amino acid sequence of SEQ ID No: 1062. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-532 6820_g scaflbldOOl 15.pathl .gene2 is encoded by the nucleotides of SEQ ID No: 1063 which encodes the amino acid sequence of SEQ ID No: 1064. This enzyme is believed to have monooxygenase activity.
  • sequence Oxid-533 6828_g scaffold00120.pathl .genel is encoded by the nucleotides of SEQ ID No: 1065 which encodes the amino acid sequence of SEQ ID No: 1066. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-534 6864_g scaffold00122.pathl .gene29 is encoded by the nucleotides of SEQ ID No: 1067 which encodes the amino acid sequence of SEQ ID No: 1068. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-535 687 l_g is encoded by the nucleotides of SEQ ID No: 1069 which encodes the amino acid sequence of SEQ ID No: 1070. This enzyme is believed to have monooxygenase activity.
  • scaffold00122.pathl .genel08 is encoded by the nucleotides of SEQ ID No: 1071 which encodes the amino acid sequence of SEQ ID No: 1072. This enzyme is believed to have monooxygenase activity.
  • sequence Oxid-537 6952_g scaffold00122.pathl .genel09 is encoded by the nucleotides of SEQ ID No: 1073 which encodes the amino acid sequence of SEQ ID No: 1074. This enzyme is believed to have monooxygenase activity.
  • scaffold00122.pathl .genel 11 is encoded by the nucleotides of SEQ ID No: 1075 which encodes the amino acid sequence of SEQ ID No: 1076. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-539 7015_g scaffold00131.pathl .gene39 is encoded by the nucleotides of SEQ ID No: 1077 which encodes the amino acid sequence of SEQ ID No: 1078. This enzyme is believed to have monooxygenase activity.
  • sequence Oxid-541 7247_g scaffold00131.pathl .gene258 is encoded by the nucleotides of SEQ ID No: 1081 which encodes the amino acid sequence of SEQ ID No: 1082. This enzyme is believed to have monooxygenase activity.
  • scaffold00131.pathl .gene445 is encoded by the nucleotides of SEQ ID No: 1083 which encodes the amino acid sequence of SEQ ID No: 1084. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-543 7522_g scaffold00131.pathl .gene518 is encoded by the nucleotides of SEQ ID No: 1085 which encodes the amino acid sequence of SEQ ID No: 1086. This enzyme is believed to have monooxygenase activity.
  • Sequence Oxid-544 7568_g scaffold00131.pathl .gene546 is encoded by the nucleotides of SEQ ID No: 1087 which encodes the amino acid sequence of SEQ ID No: 1088. This enzyme is believed to have monooxygenase activity.
  • sequence Oxid-545 769 l_g scaffold00131.pathl .gene649 is encoded by the nucleotides of SEQ ID No: 1089 which encodes the amino acid sequence of SEQ ID No: 1090. This enzyme is believed to have monooxygenase activity.
  • scaffold00131.pathl .genel016 is encoded by the nucleotides of SEQ ID No: 1091 which encodes the amino acid sequence of SEQ ID No: 1092. This enzyme is believed to have monooxygenase activity.
  • scaffold00131.pathl .gene218 is encoded by the nucleotides of SEQ ID No: 1093 which encodes the amino acid sequence of SEQ ID No: 1094. This enzyme is believed to have monooxygenase activity.
  • sequence Oxid-548 7350_g scaffold00131.pathl .gene355 is encoded by the nucleotides of SEQ ID No: 1095 which encodes the amino acid sequence of SEQ ID No: 1096. This enzyme is believed to have trimethyllysine dioxygenase activity.
  • the enzyme identified as Sequence Oxid-549 735 l_g scaflbld00131.pathl .gene356 is encoded by the nucleotides of SEQ ID No: 1097 which encodes the amino acid sequence of SEQ ID No: 1098. This enzyme is believed to have dioxygenase activity.
  • scaffold00131.pathl .gene479 is encoded by the nucleotides of SEQ ID No: 1099 which encodes the amino acid sequence of SEQ ID NO: 1100. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-551 8028_g is encoded by the nucleotides of SEQ ID No: 1101 which encodes the amino acid sequence of SEQ ID No: 1102. This enzyme is believed to have dioxygenase activity.
  • scaffold00131.pathl .genel l38 is encoded by the nucleotides of SEQ ID No: 1103 which encodes the amino acid sequence of SEQ ID No: 1104. This enzyme is believed to have oxidoreductase activity.
  • sequence Oxid-553 8686_g scaffold00142.pathl .genel49 is encoded by the nucleotides of SEQ ID No: 1105 which encodes the amino acid sequence of SEQ ID No: 1106. This enzyme is believed to have oxidoreductase activity.
  • scaffold00142.pathl .genel94 is encoded by the nucleotides of SEQ ID No: 1107 which encodes the amino acid sequence of SEQ ID No: 1108. This enzyme is believed to have dioxygenase activity.
  • Sequence Oxid-555 8896_g scaffold00169.pathl .gene4 is encoded by the nucleotides of SEQ ID No: 1109 which encodes the amino acid sequence of SEQ ID No: 1110. This enzyme is believed to have oxidoreductase activity.
  • scaffold00227.pathl .gene32 is encoded by the nucleotides of SEQ ID No: 1111 which encodes the amino acid sequence of SEQ ID No: 1112. This enzyme is believed to have dioxygenase activity.
  • the enzyme identified as Sequence Oxid-557 9504_g scaffold00227.G198 scaffold00227.pathl .genel02 is encoded by the nucleotides of SEQ ID No: 1113 which encodes the amino acid sequence of SEQ ID No: 1114. This enzyme is believed to have dioxygenase activity.
  • Sequence Oxid-558 566_g scaffold00016.pathl .gene487 is encoded by the nucleotides of SEQ ID No: 1115 which encodes the amino acid sequence of SEQ ID No: 1116. This enzyme is believed to have dioxygenase activity.
  • scaffold00031.pathl .gene76 is encoded by the nucleotides of SEQ ID No: 1117 which encodes the amino acid sequence of SEQ ID No: 1118. This enzyme is believed to have dioxygenase activity.
  • pathl . genel 17 is encoded by the nucleotides of SEQ ID No: 1119 which encodes the amino acid sequence of SEQ ID No: 1120. This enzyme is believed to have dioxygenase activity.
  • sequence Oxid-561 1426_g scaffold00031. pathl . gene433 is encoded by the nucleotides of SEQ ID No: 1121 which encodes the amino acid sequence of SEQ ID No: 1122. This enzyme is believed to have oxidoreductase activity.
  • pathl . gene891 is encoded by the nucleotides of SEQ ID No: 1123 which encodes the amino acid sequence of SEQ ID No: 1124. This enzyme is believed to have dioxygenase activity.
  • sequence Oxid-563 2265_g scaffold00050.pathl . genel 14 is encoded by the nucleotides of SEQ ID No: 1125 which encodes the amino acid sequence of SEQ ID No: 1126. This enzyme is believed to have dioxygenase activity.
  • scaffold00071.G251 scaffold00071.pathl .genel 14 is encoded by the nucleotides of SEQ ID No: 1127 which encodes the amino acid sequence of SEQ ID No: 1128. This enzyme is believed to have dioxygenase activity.
  • sequence Oxid-565 3432_g scaffold00071. pathl . genel66 is encoded by the nucleotides of SEQ ID No: 1129 which encodes the amino acid sequence of SEQ ID No: 1130. This enzyme is believed to have dioxygenase activity.
  • scaffold00071.pathl .genel225 is encoded by the nucleotides of SEQ ID No: 1131 which encodes the amino acid sequence of SEQ ID No: 1132. This enzyme is believed to have oxidoreductase activity.
  • scaffold00071. athl . genel717 is encoded by the nucleotides of SEQ ID No: 1133 which encodes the amino acid sequence of SEQ ID No: 1134. This enzyme is believed to have dioxygenase activity.
  • Sequence Oxid-568 5645_g is encoded by the nucleotides of SEQ ID No: 1135 which encodes the amino acid sequence of SEQ ID No: 1136.
  • This enzyme is believed to have dioxygenase activity.
  • sequence Oxid-569 6086_g scaffold00075. athl . gene608 is encoded by the nucleotides of SEQ ID No: 1137 which encodes the amino acid sequence of SEQ ID No: 1138. This enzyme is believed to have sulfonate dioxygenase activity.
  • scaffold00016.pathl .gene5 is encoded by the nucleotides of SEQ ID No: 1139 which encodes the amino acid sequence of SEQ ID No: 1140. This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-571 28_g is encoded by the nucleotides of
  • SEQ ID No: 1141 which encodes the amino acid sequence of SEQ ID No: 1142.
  • This enzyme is believed to have oxidoreductase activity.
  • SEQ ID No: 1143 which encodes the amino acid sequence of SEQ ID No: 1144.
  • This enzyme is believed to have oxidoreductase activity.
  • SEQ ID No: 1145 which encodes the amino acid sequence of SEQ ID No: 1146.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-574 105_g is encoded by the nucleotides of SEQ ID No: 1147 which encodes the amino acid sequence of SEQ ID No: 1148.
  • Sequence Oxid-575 174_g is encoded by the nucleotides of SEQ ID No: 1149 which encodes the amino acid sequence of SEQ ID No: 1150.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-576 182_g is encoded by the nucleotides of SEQ ID No: 1151 which encodes the amino acid sequence of SEQ ID No: 1152.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-577 290_g is encoded by the nucleotides of SEQ ID No: 1153 which encodes the amino acid sequence of SEQ ID No: 1154.
  • This enzyme is believed to have glutamate synthase (NADPH) activity.
  • Sequence Oxid-578 308_g is encoded by the nucleotides of SEQ ID No: 1155 which encodes the amino acid sequence of SEQ ID No: 1156.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-579 309_g is encoded by the nucleotides of SEQ ID No: 1157 which encodes the amino acid sequence of SEQ ID No: 1158.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-580 367_g is encoded by the nucleotides of SEQ ID No: 1159 which encodes the amino acid sequence of SEQ ID No: 1160.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-581 394_g is encoded by the nucleotides of SEQ ID No: 1161 which encodes the amino acid sequence of SEQ ID No: 1162.
  • This enzyme is believed to have Oxidase activity.
  • Sequence Oxid-582 429_g is encoded by the nucleotides of SEQ ID No: 1163 which encodes the amino acid sequence of SEQ ID No: 1164.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-583 455_g is encoded by the nucleotides of SEQ ID No: 1165 which encodes the amino acid sequence of SEQ ID No: 1166.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-584 473_g is encoded by the nucleotides of SEQ ID No: 1167 which encodes the amino acid sequence of SEQ ID No: 1168.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-585 541_g is encoded by the nucleotides of SEQ ID No: 1169 which encodes the amino acid sequence of SEQ ID No: 1170.
  • Sequence Oxid-586 645_g is encoded by the nucleotides of SEQ ID No: 1171 which encodes the amino acid sequence of SEQ ID No: 1172.
  • This enzyme is believed to have oxidase activity.
  • Sequence Oxid-587 697_g is encoded by the nucleotides of SEQ ID No: 1173 which encodes the amino acid sequence of SEQ ID No: 1174.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-588 714_g is encoded by the nucleotides of SEQ ID No: 1175 which encodes the amino acid sequence of SEQ ID No: 1176.
  • This enzyme is believed to have carbonyl reductase (NADPH) activity.
  • Sequence Oxid-589 719_g is encoded by the nucleotides of SEQ ID No: 1177 which encodes the amino acid sequence of SEQ ID No: 1178.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-590 730_g is encoded by the nucleotides of SEQ ID No: 1179 which encodes the amino acid sequence of SEQ ID No: 1180.
  • This enzyme is believed to have glutathione-disulfide reductase activity.
  • Sequence Oxid-591 737_g is encoded by the nucleotides of SEQ ID No: 1181 which encodes the amino acid sequence of SEQ ID No: 1182.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-592 829_g is encoded by the nucleotides of SEQ ID No: 1183 which encodes the amino acid sequence of SEQ ID No: 1184.
  • This enzyme is believed to have hydroxylase activity.
  • Sequence Oxid-593 835_g is encoded by the nucleotides of SEQ ID No: 1185 which encodes the amino acid sequence of SEQ ID No: 1186.
  • This enzyme is believed to have ribonucleotide reductase activity.
  • Sequence Oxid-594 940_g is encoded by the nucleotides of SEQ ID No: 1187 which encodes the amino acid sequence of SEQ ID No: 1188.
  • This enzyme is believed to have catalase activity.
  • Sequence Oxid-595 961_g is encoded by the nucleotides of SEQ ID No: 1189 which encodes the amino acid sequence of SEQ ID No: 1190.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-596 987_g is encoded by the nucleotides of SEQ ID No: 1191 which encodes the amino acid sequence of SEQ ID No: 1192.
  • Sequence Oxid-597 999_g is encoded by the nucleotides of SEQ ID No: 1193 which encodes the amino acid sequence of SEQ ID No: 1194.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-598 1025_g is encoded by the nucleotides of SEQ ID No: 1195 which encodes the amino acid sequence of SEQ ID No: 1196.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-599 1040_g is encoded by the nucleotides of SEQ ID No: 1197 which encodes the amino acid sequence of SEQ ID No: 1198.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-600 1087_g is encoded by the nucleotides of SEQ ID No: 1199 which encodes the amino acid sequence of SEQ ID No: 1200.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-601 1115_g is encoded by the nucleotides of SEQ ID No: 1201 which encodes the amino acid sequence of SEQ ID No: 1202.
  • This enzyme is believed to have urate oxidase activity.
  • Sequence Oxid-602 1147_g is encoded by the nucleotides of SEQ ID No: 1203 which encodes the amino acid sequence of SEQ ID No: 1204.
  • This enzyme is believed to have ribonucleoside-diphosphate reductase activity.
  • Sequence Oxid-603 1220_g is encoded by the nucleotides of SEQ ID No: 1205 which encodes the amino acid sequence of SEQ ID No: 1206.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-604 1222_g is encoded by the nucleotides of SEQ ID No: 1207 which encodes the amino acid sequence of SEQ ID No: 1208.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-605 1223_g is encoded by the nucleotides of SEQ ID No: 1209 which encodes the amino acid sequence of SEQ ID No: 1210.
  • This enzyme is believed to have pyrroline-5-carboxylate reductase activity.
  • Sequence Oxid-606 1225_g is encoded by the nucleotides of SEQ ID No: 1211 which encodes the amino acid sequence of SEQ ID No: 1212.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-607 1226_g is encoded by the nucleotides of SEQ ID No: 1213 which encodes the amino acid sequence of SEQ ID No: 1214.
  • Sequence Oxid-608 1232_g is encoded by the nucleotides of SEQ ID No: 1215 which encodes the amino acid sequence of SEQ ID No: 1216.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-609 1250_g is encoded by the nucleotides of SEQ ID No: 1217 which encodes the amino acid sequence of SEQ ID No: 1218.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-610 1272_g is encoded by the nucleotides of SEQ ID No: 1219 which encodes the amino acid sequence of SEQ ID No: 1220.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-611 1273_g is encoded by the nucleotides of SEQ ID No: 1221 which encodes the amino acid sequence of SEQ ID No: 1222.
  • This enzyme is believed to have oxidoreductase activity.
  • Sequence Oxid-612 1298_g is encoded by the nucleotides of SEQ ID No: 1223 which encodes the amino acid sequence of SEQ ID No: 1224.
  • This enzyme is believed to have pyrroline-5-carboxylate reductase activity.
  • Sequence Oxid-613 1306_g is encoded by the nucleotides of SEQ ID No: 1225 which encodes the amino acid sequence of SEQ ID No: 1226.
  • This enzyme is believed to have oxidoreductase activity.

Landscapes

  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Wood Science & Technology (AREA)
  • Zoology (AREA)
  • Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Biochemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Microbiology (AREA)
  • General Engineering & Computer Science (AREA)
  • Biotechnology (AREA)
  • General Chemical & Material Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Molecular Biology (AREA)
  • Medicinal Chemistry (AREA)
  • Biophysics (AREA)
  • Gastroenterology & Hepatology (AREA)
  • Mycology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Biomedical Technology (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)
  • Peptides Or Proteins (AREA)

Abstract

This invention relates to novel enzymes and novel methods for producing the same. More specifically this invention relates to enzymes of fungal origin classified as oxidoreductases and produced by fungi. Nucleic acid molecules encoding such enzymes, compositions, recombinant and genetically modified host cells, and methods of use are described. The invention also relates to methods to use the novel enzymes and compositions of such enzymes in a variety of other processes, including disinfection food, deinking and biobleaching of flour, cotton, paper and pulp, and the treatment of pollution. The invention also relates to a method to aid in the conversion of lignocellulosic biomass to fermentable sugars with enzymes that degrade the lignocellulosic material and novel combinations of enzymes, including those that provide a synergistic release of sugars from plant biomass.

Description

Novel Fungal Oxidoreductases
RELATED APPLICATIONS
[001] This application claims benefit of priority under 35. U.S.C. § 119(e) of United
States Provisional Application number 61/414,137 filed on November 16, 2010.
INCORPORATION BY REFERENCE
[001] The content of all patents, patent applications, publications, articles, or literature cited herein are expressly incorporated by reference.
FIELD OF THE INVENTION
[002] This invention relates to novel enzymes and novel methods for producing the same.
More specifically this invention relates to enzymes of fungal origin classified as oxidoreductases and produced by fungi. Oxidoreductases represent a category of various enzymes including but not limited to oxidases, monooxygenases, Baeyer- Villiger monooxygenases, hydroxylases, peroxidases, dioxygenases, dehydrogenases, and reductases that catalyze an oxidation-reduction reaction. The invention also relates to a method to aid in the conversion of plant biomass to biofuels by degrading lignin to allow enzymes used in the processing of plant biomass to more easily access the cellulose and hemicellulose and to novel combinations of enzymes, including those that provide a combined or synergistic release of sugars from plant biomass. The invention also relates to methods of using the novel enzymes and compositions of such enzymes in a variety of other processes, such as bleaching pulp, cotton and flour; disinfecting food; preserving and increasing shelf life of food and beverages improving baking products; producing sugar alcohols; synthesizing amino acids, steroids, and other fine chemicals; manufacturing of products; and controlling pollution.
BACKGROUND OF THE FNVENTION
[003] Oxidoreductases are enzymes that catalyze the transfer of electrons from one molecule (the reductant or electron donor) to another (the oxidant or electron acceptor). Oxidoreductases can be oxidases or dehydrogenases. Oxidases are enzymes that utilize molecular oxygen as an electron acceptor, while dehydrogenases are enzymes that oxidize a substrate by transferring a hydride to an acceptor that is either an NAD /NADP+ or a flavin-dependent enzyme. Other oxidoreductases include peroxidases, oxygenases, hydroxylases, and reductases. Peroxidases catalyze the reduction of a peroxide.. Oxygenases catalyze the incorporation of oxygen from molecular oxygen into organic substrates. Hydroxylases are a class of oxygenases that catalyze the introduction of hydroxyl groups to organic substrates. Monooxygenases are a class of oxygenases that catalyze the incorporation of one atom of oxygen from molecular oxygen into organic substrates. Dioxygenases are a class of oxygenases that catalyze the incorporation of both atoms of oxygen from molecular oxygen into organic substrates. Baeyer-Villiger monooxygenases are a class of oxygenases that catalyze the insertion of an oxygen atom from molecular oxygen in a ketone, next to the carbonyl carbon atom. Reductases catalyze reductions, in most cases reductases can act like an oxidase. Many pathways of biogenesis and bio degradation require oxidoreductase (dehydrogenase or reductase) activity, coupled to the reduction or oxidation of a donor or acceptor cofactor. Potential cofactors include cytochromes, oxygen, disulfide, iron-sulfur proteins, flavin adenine dinucleotide (FAD), and the nicotinamide adenine dinucleotides NAD and NADP (Newsholme, E. A. and Leech, A. R. (1983) Biochemistry for the Medical Sciences, John Wiley and Sons, Chichester, U. K. pp. 779-793).
[004] Oxidoreductases have found a great number of uses in industry such as aiding in the production of bio fuels; bleaching pulp, cotton and flour; cleansing of food such as vegetables; improving the structure of baked goods; clarification of beer or wine; increasing shelf life of food and beverages; producing xylitol and other sugar alcohols such as sorbitol; synthesizing amino acids, steroids, and other fine chemicals; acting as biosensors; manufacturing adhesives, computer chips, and other products; controlling pollution and soil detoxification; whitening skin/hair, and teeth; various bioremediative processes and textile applications, such as denim treatment, stain removal, treatment of various fibers for textile industry, methods for decolorizing dyes and methods for treating dye house effluents, or use in hair dyeing composition, in hard-surface cleaning or in detergent formulations; and stimulating the immune system to name just a few applications.
[005] Oxidoreductases, such as laccases, have many industrially potential applications, such as delignification of wood pulps, methods for treating lignin containing fibers, methods for treating wood fibers in order to functionalize them, improving of the production of fuel ethanol from renewable raw materials. [006] Plant biomass is being touted as the up-and-coming source for biofuels and chemical building blocks However, biomass, such as corn stover, switchgrass and other feedstocks, is not easily converted to ethanol. Lignin is a complex chemical compound that is an integral part of the secondary cell walls of many plants and some algae. Lignin acts like a kind of glue holding together cellulose and hemicelluose, which are important ingredients in making ethanol or chemical building blocks Oxidoreductases can act upon lignin or as reductases in the degradation of (hemi-) cellulose to allow the enzymes used in the processing of plant biomass to more easily access the cellulose and hemicellulose to create biofuels such as ethanol or chemical intermediates such as succinic acid. There exists a continuing need to develop new and improved oxidoreductases to help meet the demands of the ever changing bio fuel and chemical industry.
[007] Pulp manufactured by the kraft process must be bleached to provide the desired whiteness of fine paper, tissue, and similar products. Traditionally, this was achieved using reactions involving chlorine and sodium hydroxide. More recently, chlorine dioxide has been increasingly substituted for chlorine. Due to environmental concerns over chloroorganic compounds present in the bleaching effluents, non-chlorine bleaching reactions are currently being introduced. These reactions include oxygen delignification followed by chelation and hydrogen peroxide oxidation, and combinations of ozone and other non-chlorine compounds. These processes are presently more costly and less selective for lignin than chlorine bleaching. Thus, there exists the need for more efficient oxidoreductase enzymes to create a more cost effective and environmentally friendly process for whitening paper and tissue products, and the novel enzymes of the present invention fulfil such a need.
[008] The incorporation of bleach into a detergent composition requires a careful balance of good bleaching performance, good bleach stability, and especially good product storage stability. While many different types of bleach have been considered for incorporation into detergent compositions, such as pre-formed peracids, transition metal bleach catalysts, nitrile quaternary amine bleach activators, cationic imine bleach boosting compounds and the like, there remains very few bleach technologies that exhibit sufficient bleach stability, that also provide good bleaching performance and acceptable fabric integrity profile. Oxidoreductases are able to fill that role. However, there exists a need to develop new oxidoreductases to achieve a better bleach for the use in detergents. These novel oxidoreductases may also be used to provide improved whitening benefits due to its effects on the cotton fabric, which make the fabric more resistant to being soiled.
[009] The "stone washed" look has been used by the denim industry to produce a product that appears faded and worn. Because traditional stone washing with pumice stones reduces the strength of fabric and burdens the laundering apparatuses, the industry has turned towards an enzymatic denim finishing processes. A "bleached look" of denim is normally obtained by means of bleaching chemicals, e.g. sodium hypochlorite. However, the hypochlorite process is environmentally very harmful, damages the fabric easily, and is possibly harmful for the user. Furthermore, it cannot be used for Lycra containing products, and antichlor treatment with several rinsing/washing steps is required. In particular, the industry is in need of oxidoreductases that are able to function at low temperatures to accommodate the newer dyes and finishes that must be washed at a lower temperature. Therefore, there exists a need for developing an ecologically less harmful alternative for sodium hypochlorite that can function at lower temperatures, in particular the oxidoreductases of the present invention, (e.g., laccases), can serve that purpose.
[010] Oxidoreductases are useful in the production of cheese. Lactobionic acid can be used as the sole acidulent for direct acidification of cheese, or in conjunction with reduced amounts of lactic acid culture. When the lactobionic acid is generated in situ during cheese manufacture, a lactose oxidase is used in one embodiment to convert lactose intrinsically present in the dairy liquid ingredient(s) into lactobionic acid. It is desirable to manufacture cheeses with reduced lactose content while preserving flavor, texture, and appearance comparable with conventional cheese products. The present invention provides such enzymes to aid in the production of lactobionic acid.
[011] Flavor problems caused by non-specific oxidants due to oxidation of other components of a food system can be eliminated due to the specificity of an enzyme catalyzed reaction. One example of such a use includes a process in which treatment with sulfhydryl oxidase aids in the removal of a burnt flavor from Ultra- High Temperature (UHT) sterilized milk. This is just one example in which the present invention provides enzymes to aid in the reduction of flavor problems of food.
[012] Many beverages (e.g., ready-to-drink beverages) suffer adverse effects from exposure to oxygen. Take ready-to-drink coffee as an example. Ready-to-drink coffee beverages are produced by extracting soluble coffee solids from roasted and ground coffee beans using hot water, and additives are added to the diluted extract. During this process, the coffee is exposed to oxygen several times which can cause an adverse effect on the flavor and aroma of the coffee resulting in a bitter flavor. While various attempts have been made in the past to reduce the influence of oxygen, those methods generally entail preventing the ingress of oxygen or the use of antioxidants. These methods are quite expensive. Thus, there exists a need to develop an antioxidant system (e.g., utilizing oxidoreductases of the present invention) which is inexpensive and potent to remove oxygen from beverages and in which are themselves antioxidants - this need can be satisfied by the enzymes of the present invention.
[013] Many substances (e.g., foods, beverages, tobacco products) stain or decrease the whiteness of teeth. Over many years, these substances tend to accumulate on teeth and permeate the enamel resulting in an observable discoloration of the enamel. The use of toothpaste, gels, powders, containing active oxygen or hydrogen peroxide liberating ingredients such as peroxides, percarbonates and perborates or complex compounds containing hydrogen peroxide generally work very slowly and do not fulfil the needs of individuals who desire rapid whitening of teeth. For rapid whitening of teeth, consumers are required to utilize dental professionals who use 30-35 % hydrogen peroxide in combination with heat and/or light to promote the oxidation reaction. This method, however, is losing favor with the dentists because studies are indicating that high concentrations of peroxide is deleterious to oral tissue. Therefore, there exists a need to develop new oxidoreductase enzymes (e.g., enzymes of the present invention) to create a safer, more efficient process in which the consumer and/or dental professional can administer.
[014] The discovery of new oxidoreductase molecules also satisfies a need in the art by providing new compositions which are useful in the diagnosis, prevention, and treatment of cell proliferative disorders including cancer, endocrine, metabolic, reproductive, neurological, autoimmune/inflammatory, and viral disorders.
[015] Regardless of the type of use, the cost and enzymatic efficiency of enzymes are major factors that restrict the widespread use of oxidoreductases. The production costs of microbial produced enzymes are tightly connected with the productivity of the enzyme-producing strain and the final activity yield in the fermentation broth. The enzymatic efficiency of a multi-enzyme cocktail depends on properties of individual enzymes, the synergies between them, and their ratio in the multi-enzyme cocktail.
[016] Filamentous fungi are a rich source of oxidoreductases, such as but not limited to oxidases, monooxygenases, Baeyer-Villiger monooxygenases, hydroxylases, peroxidases, dioxygenases, dehydrogenases, and reductases that catalyze an oxidation-reduction reaction. It is desirable to produce inexpensive enzymes and enzyme mixtures that efficiently aid in the conversion of (plant) biomass for use in a variety of industrial applications.
[017] In spite of the continued research of the last few decades to understand oxidoreductases, it remains desirable to discover or to engineer new highly active oxidoreductase. It would also be highly desirable to construct highly efficient enzyme compositions capable of performing under varied environmental conditions.
[018] SUMMARY OF THE INVENTION
[019] In one embodiment, the present invention comprises an isolated nucleic acid sequence selected from the group consisting of:
a) a nucleic acid sequence encoding a protein comprising an amino acid sequence selected from SEQ ID NO: 2, SEQ ID No: 4, SEQ ID No: 6, SEQ ID No: 8, SEQ ID No: 10, SEQ ID No: 12, SEQ ID No: 14, SEQ ID No: 16, SEQ ID No: 18, SEQ ID No: 20, SEQ ID No: 22, SEQ ID No: 24, SEQ ID No: 26, SEQ ID No: 28, SEQ ID No: 30, SEQ ID No: 32, SEQ ID No: 34, SEQ ID No: 36, SEQ ID No: 38, SEQ ID No: 40, SEQ ID No: 42, SEQ ID No: 44, SEQ ID No: 46, SEQ ID No: 48, SEQ ID No: 50, SEQ ID No: 52, SEQ ID No: 54, SEQ ID No: 56, SEQ ID No: 58, SEQ ID No: 60, SEQ ID No: 62, SEQ ID No: 64, SEQ ID No: 66, SEQ ID No: 68, SEQ ID No: 70, SEQ ID No: 72, SEQ ID No: 74, SEQ ID No: 76, SEQ ID No: 78, SEQ ID No: 80, SEQ ID No: 82, SEQ ID No: 84, SEQ ID No: 86, SEQ ID No: 88, SEQ ID No: 90, SEQ ID No: 92, SEQ ID No: 94, SEQ ID No: 96, SEQ ID No: 98, SEQ ID No: 100, SEQ ID No: 102, SEQ ID No: 104, SEQ ID No: 106, SEQ ID No: 108, SEQ ID No: 110, SEQ ID No: 1 12, SEQ ID No: 1 14, SEQ ID No: 1 16, SEQ ID No: 1 18, SEQ ID No: 120, SEQ ID No: 122, SEQ ID No: 124, SEQ ID No: 126, SEQ ID No: 128, SEQ ID No: 130, SEQ ID No: 132, SEQ ID No: 134, SEQ ID No: 136, SEQ ID No: 138, SEQ ID No: 140, SEQ ID No: 142, SEQ ID No: 144, SEQ ID No: 146, SEQ ID No: 148, SEQ ID No: 150, SEQ ID No: 152, SEQ ID No: 154, SEQ ID No: 156, SEQ ID No: 158, SEQ ID No: 160, SEQ ID No: 162, SEQ ID No: 164, SEQ ID No: 166, SEQ ID No: 168, SEQ ID No: 170, SEQ ID No: 172, SEQ ID No: 174, SEQ ID No: 176, SEQ ID No: 178, SEQ ID No: 180, SEQ ID No: 182, SEQ ID No: 184, SEQ ID No: 186, SEQ ID No: 188, SEQ ID No: 190, SEQ ID No: 192, SEQ ID No: 194, SEQ ID No: 196, SEQ ID No: 198, SEQ ID No: 200, SEQ ID No: 202, SEQ ID No: 204, SEQ ID No: 206, SEQ ID No: 208, SEQ ID No: 210, SEQ ID No: 212, SEQ ID No: 214, SEQ ID No: 216, SEQ ID No: 218, SEQ ID No: 220, SEQ ID No: 222, SEQ ID No: 224, SEQ ID No: 226, SEQ ID No: 228, SEQ ID No: 230, SEQ ID No: 232, SEQ ID No: 234, SEQ ID No: 236, SEQ ID No: 238, SEQ ID No: 240, SEQ ID No: 242, SEQ ID No: 244, SEQ ID No: 246, SEQ ID No: 248, SEQ ID No: 250, SEQ ID No: 252, SEQ ID No: 254, SEQ ID No: 256, SEQ ID No: 258, SEQ ID No: 260, SEQ ID No: 262, SEQ ID No: 264, SEQ ID No: 266, SEQ ID No: 268, SEQ ID No: 270, SEQ ID No: 272, SEQ ID No: 274, SEQ ID No: 276, SEQ ID No: 278, SEQ ID No: 280, SEQ ID No: 282, SEQ ID No: 284, SEQ ID No: 286, SEQ ID No: 288, SEQ ID No: 290, SEQ ID No: 292, SEQ ID No: 294, SEQ ID No: 296, SEQ ID No: 298, SEQ ID No: 300, SEQ ID No: 302, SEQ ID No: 304, SEQ ID No: 306, SEQ ID No: 308, SEQ ID No: 310, SEQ ID No: 312, SEQ ID No: 314, SEQ ID No: 316, SEQ ID No: 318, SEQ ID No: 320, SEQ ID No: 322, SEQ ID No: 324, SEQ ID No: 326, SEQ ID No: 328, SEQ ID No: 330, SEQ ID No: 332, SEQ ID No: 334, SEQ ID No: 336, SEQ ID No: 338, SEQ ID No: 340, SEQ ID No: 342, SEQ ID No: 344, SEQ ID No: 346, SEQ ID No: 348, SEQ ID No: 350, SEQ ID No: 352, SEQ ID No: 354, SEQ ID No: 356, SEQ ID No: 358, SEQ ID No: 360, SEQ ID No: 362, SEQ ID No: 364, SEQ ID No: 366, SEQ ID No: 368, SEQ ID No: 370, SEQ ID No: 372, SEQ ID No: 374, SEQ ID No: 376, SEQ ID No: 378, SEQ ID No: 380, SEQ ID No: 382, SEQ ID No: 384, SEQ ID No: 386, SEQ ID No: 388, SEQ ID No: 390, SEQ ID No: 392, SEQ ID No: 394, SEQ ID No: 396, SEQ ID No: 398, SEQ ID No: 400, SEQ ID No: 402, SEQ ID No: 404, SEQ ID No: 406, SEQ ID No: 408, SEQ ID No: 410, SEQ ID No: 412, SEQ ID No: 414, SEQ ID No: 416, SEQ ID No: 418, SEQ ID No: 420, SEQ ID No: 422, SEQ ID No: 424, SEQ ID No: 426, SEQ ID No: 428, SEQ ID No: 430, SEQ ID No: 432, SEQ ID No: 434, SEQ ID No: 436, SEQ ID No: 438, SEQ ID No: 440, SEQ ID No: 442, SEQ ID No: 444, SEQ ID No: 446, SEQ ID No: 448, SEQ ID No: 450, SEQ ID No: 452, SEQ ID No: 454, SEQ ID No: 456, SEQ ID No: 458, SEQ ID No: 460, SEQ ID No: 462, SEQ ID No: 464, SEQ ID No: 466, SEQ ID No: 468, SEQ ID No: 470, SEQ ID No: 472, SEQ ID No: 474, SEQ ID No: 476, SEQ ID No: 478, SEQ ID No: 480, SEQ ID No: 482, SEQ ID No: 484, SEQ ID No: 486, SEQ ID No: 488, SEQ ID No: 490, SEQ ID No: 492, SEQ ID No: 494, SEQ ID No: 496, SEQ ID No: 498, SEQ ID No: 500, SEQ ID No: 502, SEQ ID No: 504, SEQ ID No: 506, SEQ ID No: 508, SEQ ID No: 510, SEQ ID No: 512, SEQ ID No: 514, SEQ ID No: 516, SEQ ID No: 518, SEQ ID No: 520, SEQ ID No: 522, SEQ ID No: 524, SEQ ID No: 526, SEQ ID No: 528, SEQ ID No: 530, SEQ ID No: 532, SEQ ID No: 534, SEQ ID No: 536, SEQ ID No: 538, SEQ ID No: 540, SEQ ID No: 542, SEQ ID No: 544, SEQ ID No: 546, SEQ ID No: 548, SEQ ID No: 550, SEQ ID No: 552, SEQ ID No: 554, SEQ ID No: 556, SEQ ID No: 558, SEQ ID No: 560, SEQ ID No: 562, SEQ ID No: 564, SEQ ID No: 566, SEQ ID No: 568, SEQ ID No: 570, SEQ ID No: 572, SEQ ID No: 574, SEQ ID No: 576, SEQ ID No: 578, SEQ ID No: 580, SEQ ID No: 582, SEQ ID No: 584, SEQ ID No: 586, SEQ ID No: 588, SEQ ID No: 590, SEQ ID No: 592, SEQ ID No: 594, SEQ ID No: 596, SEQ ID No: 598, SEQ ID No: 600, SEQ ID No: 602, SEQ ID No: 604, SEQ ID No: 606, SEQ ID No: 608, SEQ ID No: 610, SEQ ID No: 612, SEQ ID No: 614, SEQ ID No: 616, SEQ ID No: 618, SEQ ID No: 620, SEQ ID No: 622, SEQ ID No: 624, SEQ ID No: 626, SEQ ID No: 628, SEQ ID No: 630, SEQ ID No: 632, SEQ ID No: 634, SEQ ID No: 636, SEQ ID No: 638, SEQ ID No: 640, SEQ ID No: 642, SEQ ID No: 644, SEQ ID No: 646, SEQ ID No: 648, SEQ ID No: 650, SEQ ID No: 652, SEQ ID No: 654, SEQ ID No: 656, SEQ ID No: 658, SEQ ID No: 660, SEQ ID No: 662, SEQ ID No: 664, SEQ ID No: 666, SEQ ID No: 668, SEQ ID No: 670, SEQ ID No: 672, SEQ ID No: 674, SEQ ID No: 676, SEQ ID No: 678, SEQ ID No: 680, SEQ ID No: 682, SEQ ID No: 684, SEQ ID No: 686, SEQ ID No: 688, SEQ ID No: 690, SEQ ID No: 692, SEQ ID No: 694, SEQ ID No: 696, SEQ ID No: 698, SEQ ID No: 700, SEQ ID No: 702, SEQ ID No: 704, SEQ ID No: 706, SEQ ID No: 708, SEQ ID No: 710, SEQ ID No: 712, SEQ ID No: 714, SEQ ID No: 716, SEQ ID No: 718, SEQ ID No: 720, SEQ ID No: 722, SEQ ID No: 724, SEQ ID No: 726, SEQ ID No: 728, SEQ ID No: 730, SEQ ID No: 732, SEQ ID No: 734, SEQ ID No: 736, SEQ ID No: 738, SEQ ID No: 740, SEQ ID No: 742, SEQ ID No: 744, SEQ ID No: 746, SEQ ID No: 748, SEQ ID No: 750, SEQ ID No: 752, SEQ ID No: 754, SEQ ID No: 756, SEQ ID No: 758, SEQ ID No: 760, SEQ ID No: 762, SEQ ID No: 764, SEQ ID No: 766, SEQ ID No: 768, SEQ ID No: 770, SEQ ID No: 772, SEQ ID No: 774, SEQ ID No: 776, SEQ ID No: 778, SEQ ID No: 780, SEQ ID No: 782, SEQ ID No: 784, SEQ ID No: 786, SEQ ID No: 788, SEQ ID No: 790, SEQ ID No: 792, SEQ ID No: 794, SEQ ID No: 796, SEQ ID No: SEQ ID No: 798, SEQ ID No: 800, SEQ ID No: 802, SEQ ID No: 804, SEQ ID No: 806, SEQ ID No: 808, SEQ ID No: 810, SEQ ID No: 812, SEQ ID No: 814, SEQ ID No: 816, SEQ ID No: 818, SEQ ID No: 820, SEQ ID No: 822, SEQ ID No: 824, SEQ ID No: 826, SEQ ID No: 828, SEQ ID No: 830, SEQ ID No: 832, SEQ ID No: 834, SEQ ID No: 836, SEQ ID No: 838, SEQ ID No: 840, SEQ ID No: 842, SEQ ID No: 844, SEQ ID No: 846, SEQ ID No: 848, SEQ ID No: 850, SEQ ID No: 852, SEQ ID No: 854, SEQ ID No: 856, SEQ ID No: 858, SEQ ID No: 860, SEQ ID No: 862, SEQ ID No: 864, SEQ ID No: 866, SEQ ID No: 868, SEQ ID No: 870, SEQ ID No: 872, SEQ ID No: 874, SEQ ID No: 876, SEQ ID No: 878, SEQ ID No: 880, SEQ ID No: 882, SEQ ID No: 884, SEQ ID No: 886, SEQ ID No: 888, SEQ ID No: 890, SEQ ID No: 892, SEQ ID No: 894, SEQ ID No: 896, SEQ ID No: 898, SEQ ID No: 900, SEQ ID No: 902, SEQ ID No: 904, SEQ ID No: 906, SEQ ID No: 908, SEQ ID No: 910, SEQ ID No: 912, SEQ ID No: 914, SEQ ID No: 916, SEQ ID No: 918, SEQ ID No: 920, SEQ ID No: 922, SEQ ID No: 924, SEQ ID No: 926, SEQ ID No: 928, SEQ ID No: 930, SEQ ID No: 932, SEQ ID No: 934, SEQ ID No: 936, SEQ ID No: 938, SEQ ID No: 940, SEQ ID No: 942, SEQ ID No: 944, SEQ ID No: 946, SEQ ID No: 948, SEQ ID No: 950, SEQ ID No: 952, SEQ ID No: 954, SEQ ID No: 956, SEQ ID No: 958, SEQ ID No: 960, SEQ ID No: 962, SEQ ID No: 964, SEQ ID No: 966, SEQ ID No: 968, SEQ ID No: 970, SEQ ID No: 972, SEQ ID No: 974, SEQ ID No: 976, SEQ ID No: 978, SEQ ID No: 980, SEQ ID No: 982, SEQ ID No: 984, SEQ ID No: 986, SEQ ID No: 988, SEQ ID No: 990, SEQ ID No: 992, SEQ ID No: 994, SEQ ID No: 996, SEQ ID No: 998, SEQ ID No: 1000, SEQ ID No: 1002, SEQ ID No: 1004, SEQ ID No: 1006, SEQ ID No: 1008, SEQ ID No: 1010, SEQ ID No: 1012, SEQ ID No: 1014, SEQ ID No: 1016, SEQ ID No: 1018, SEQ ID No: 1020, SEQ ID No: 1022, SEQ ID No: 1024, SEQ ID No: 1026, SEQ ID No: 1028, SEQ ID No: 1030, SEQ ID No: 1032, SEQ ID No: 1034, SEQ ID No: 1036, SEQ ID No: 1038, SEQ ID No: 1040, SEQ ID No: 1042, SEQ ID No: 1044, SEQ ID No: 1046, SEQ ID No: 1048, SEQ ID No: 1050, SEQ ID No: 1052, SEQ ID No: 1054, SEQ ID No: 1056, SEQ ID No: 1058, SEQ ID No: 1060, SEQ ID No: 1062, SEQ ID No: 1064, SEQ ID No: 1066, SEQ ID No: 1068, SEQ ID No: 1070, SEQ ID No: 1072, SEQ ID No: 1074, SEQ ID No: 1076, SEQ ID No: 1078, SEQ ID No: 1080, SEQ ID No: 1082, SEQ ID No: 1084, SEQ ID No: 1086, SEQ ID No: 1088, SEQ ID No: 1090, SEQ ID No: 1092, SEQ ID No: 1094, SEQ ID No: 1096, SEQ ID No: 1098, SEQ ID NO: 1100, SEQ ID No: 1102, SEQ ID No: 1104, SEQ ID No: 1106, SEQ ID No: 1108, SEQ ID No: 1110, SEQ ID No: 1112, SEQ ID No: 1114, SEQ ID No: 1116, SEQ ID No: 1118, SEQ ID No: 1120, SEQ ID No: 1122, SEQ ID No: 1124, SEQ ID No: 1126, SEQ ID No: 1128, SEQ ID No: 1130, SEQ ID No: 1132, SEQ ID No: 1134, SEQ ID No: 1136, SEQ ID No: 1138, SEQ ID No: 1140, SEQ ID No: 1142, SEQ ID No: 1144, SEQ ID No: 1146, SEQ ID No: 1148, SEQ ID No: 1150, SEQ ID No: 1152, SEQ ID No: 1154, SEQ ID No: 1156, SEQ ID No: 1158, SEQ ID No: 1160, SEQ ID No: 1162, SEQ ID No: 1164, SEQ ID No: 1166, SEQ ID No: 1168, SEQ ID No: 1170, SEQ ID No: 1172, SEQ ID No: 1174, SEQ ID No: 1176, SEQ ID No: 1178, SEQ ID No: 1180, SEQ ID No: 1182, SEQ ID No: 1184, SEQ ID No: 1186, SEQ ID No: 1188, SEQ ID No: 1190, SEQ ID No: 1192, SEQ ID No: 1194, SEQ ID No: 1196, SEQ ID No: 1198, SEQ ID No: 1200, SEQ ID No: 1202, SEQ ID No: 1204, SEQ ID No: 1206, SEQ ID No: 1208, SEQ ID No: 1210, SEQ ID No: 1212, SEQ ID No: 1214, SEQ ID No: 1216, SEQ ID No: 1218, SEQ ID No: 1220, SEQ ID No: 1222, SEQ ID No: 1224, SEQ ID No: 1226, SEQ ID No: 1228, SEQ ID No: 1230, SEQ ID No: 1232, SEQ ID No: 1234, SEQ ID No: 1236, SEQ ID No: 1238, SEQ ID No: 1240, SEQ ID No: 1242, SEQ ID No: 1244, SEQ ID No: 1246, SEQ ID No: 1248, SEQ ID No: 1250, SEQ ID No: 1252, SEQ ID No: 1254, SEQ ID No: 1256, SEQ ID No: 1258, SEQ ID No: 1260, SEQ ID No: 1262, SEQ ID No: 1264, SEQ ID No: 1266, SEQ ID No: 1268, SEQ ID No: 1270, SEQ ID No: 1272, SEQ ID No: 1274, SEQ ID No: 1276, SEQ ID No: 1278, SEQ ID No: 1280, SEQ ID No: 1282, SEQ ID No: 1284, SEQ ID No: 1286, SEQ ID No: 1288, SEQ ID No: 1290, SEQ ID No: 1292, SEQ ID No: 1294, SEQ ID No: 1296, SEQ ID No: 1298, SEQ ID No: 1300, SEQ ID No: 1302, SEQ ID No: 1304, SEQ ID No: 1306, SEQ ID No: 1308, SEQ ID No: 1310, SEQ ID No: 1312, SEQ ID No: 1314, SEQ ID No: 1316, SEQ ID No: 1318, SEQ ID No: 1320, SEQ ID No: 1322, SEQ ID No: 1324, SEQ ID No: 1326, SEQ ID No: 1328, SEQ ID No: 1330, SEQ ID No: 1332, SEQ ID No: 1334, SEQ ID No: 1336, SEQ ID No: 1338, SEQ ID No: 1340, SEQ ID No: 1342, SEQ ID No: 1344, SEQ ID No: 1346, SEQ ID No: 1348, SEQ ID No: 1350, SEQ ID No: 1352, SEQ ID No: 1354, SEQ ID No: 1356, SEQ ID No: 1358, SEQ ID No: 1360, SEQ ID No: 1362, SEQ ID No: 1364, SEQ ID No: 1366, SEQ ID No: 1368, SEQ ID No: 1370, SEQ ID No: 1372, SEQ ID No: 1374, SEQ ID No: 1376, SEQ ID No: 1378, SEQ ID No: 1380, SEQ ID No: 1382, SEQ ID No: 1384, SEQ ID No: 1386, SEQ ID No: 1388, SEQ ID No: 1390, SEQ ID No: 1392, SEQ ID No: 1394, SEQ ID No: 1396, SEQ ID No: 1398, SEQ ID No: 1400, SEQ ID No: 1402, SEQ ID No: 1404, SEQ ID No: 1406, SEQ ID No: 1408, SEQ ID No: 1410, SEQ ID No: 1412, SEQ ID No: 1414, SEQ ID No: 1416, SEQ ID No: 1418, SEQ ID No: 1420, SEQ ID No: 1422, SEQ ID No: 1424, SEQ ID No: 1426, SEQ ID No: 1428, SEQ ID No: 1430, SEQ ID No: 1432, SEQ ID No: 1434, SEQ ID No: 1436, SEQ ID No: 1438, SEQ ID No: 1440, SEQ ID No: 1442, SEQ ID No: 1444, SEQ ID No: 1446, SEQ ID No: 1448, SEQ ID No: 1450, SEQ ID No: 1452, SEQ ID No: 1454, SEQ ID No: 1456, SEQ ID No: 1458, SEQ ID No: 1460, SEQ ID No: 1462, SEQ ID No: 1464, SEQ ID No: 1466, SEQ ID No: 1468, SEQ ID No: 1470, SEQ ID No: 1472, SEQ ID No: 1474, SEQ ID No: 1476, SEQ ID No: 1478, SEQ ID No: 1480, SEQ ID No: 1482, SEQ ID No: 1484, SEQ ID No: 1486, SEQ ID No: 1488, SEQ ID No: 1490, SEQ ID No: 1492, SEQ ID No: 1494, SEQ ID No: 1496, SEQ ID No: 1498, SEQ ID No: 1500, SEQ ID No: 1502, SEQ ID No: 1504, SEQ ID No: 1506, SEQ ID No: 1508, SEQ ID No: 1510, SEQ ID No: 1512, SEQ ID No: 1514, SEQ ID No: 1516, SEQ ID No: 1518, SEQ ID No: 1520, SEQ ID No: 1522, SEQ ID No: 1524, SEQ ID No: 1526, SEQ ID No: 1528, SEQ ID No: 1530, SEQ ID No: 1532, SEQ ID No: 1534, SEQ ID No: 1536, SEQ ID No: 1538, SEQ ID No: 1540, SEQ ID No: 1542, SEQ ID No: 1544, SEQ ID No: 1546, SEQ ID No: 1548, SEQ ID No: 1550, SEQ ID No: 1552, SEQ ID No: 1554, SEQ ID No: 1556, SEQ ID No: 1558, SEQ ID No: 1560, SEQ ID No: 1562, SEQ ID No: 1564, SEQ ID No: 1566, SEQ ID No: 1568, SEQ ID No: 1570, SEQ ID No: 1572, SEQ ID No: 1574, SEQ ID No: 1576, SEQ ID No: 1578, SEQ ID No: 1580, SEQ ID No: 1582, SEQ ID No: 1584, SEQ ID No: 1586, SEQ ID No: 1588, SEQ ID No: 1590, SEQ ID No: 1592, SEQ ID No: 1594, SEQ ID No: 1596, SEQ ID No: 1598, SEQ ID No: 1600, SEQ ID No: 1602, SEQ ID No: 1604, SEQ ID No: 1606, SEQ ID No: 1608, SEQ ID No: 1610, SEQ ID No: 1612, SEQ ID No: 1614, SEQ ID No: 1616, SEQ ID No: 1618, SEQ ID No: 1620, SEQ ID No: 1622, SEQ ID No: 1624, SEQ ID No: 1626, SEQ ID No: 1628, SEQ ID No: 1630, SEQ ID No: 1632, SEQ ID No: 1634, SEQ ID No: 1636, SEQ ID No: 1638, SEQ ID No: 1640, SEQ ID No: 1642, SEQ ID No: 1644, SEQ ID No: 1646, SEQ ID No: 1648, SEQ ID No: 1650, SEQ ID No: 1652, SEQ ID No: 1654, SEQ ID No: 1656, SEQ ID No: 1658, SEQ ID No: 1660, SEQ ID No: 1662, SEQ ID No: 1664, SEQ ID No: 1666, SEQ ID No: 1668, SEQ ID No: 1670, SEQ ID No: 1672, SEQ ID No: 1674, SEQ ID No: 1676, SEQ ID No: 1678, SEQ ID No: 1680, SEQ ID No: 1682, SEQ ID No: 1684, SEQ ID No: 1686, SEQ ID No: 1688, SEQ ID No: 1690, SEQ ID No: 1692, SEQ ID No: 1694, SEQ ID No: 1696, SEQ ID No: 1698, SEQ ID No: 1700, SEQ ID No: 1702, SEQ ID No: 1704, SEQ ID No: 1706, SEQ ID No: 1708, SEQ ID No: 1710, SEQ ID No: 1712, SEQ ID No: 1714, SEQ ID No: 1716, SEQ ID No: 1718, SEQ ID No: 1720, SEQ ID No: 1722, SEQ ID No: 1724, SEQ ID No: 1726, SEQ ID No: 1728, SEQ ID No: 1730, SEQ ID No: 1732, SEQ ID No: 1734, SEQ ID No: 1736, SEQ ID No: 1738, SEQ ID No: 1740, SEQ ID No: 1742, SEQ ID No: 1744, SEQ ID No: 1746, SEQ ID No: 1748, SEQ ID No: 1750, SEQ ID No: 1752, SEQ ID No: 1754, SEQ ID No: 1756, SEQ ID No: 1758, SEQ ID No: 1760, SEQ ID No: 1762, SEQ ID No: 1764, SEQ ID No: 1766, SEQ ID No: 1768, SEQ ID No: 1770, SEQ ID No: 1772, SEQ ID No: 1774, SEQ ID No: 1776, SEQ ID No: 1778, SEQ ID No: 1780, SEQ ID No: 1782, SEQ ID No: 1784, SEQ ID No: 1786, SEQ ID No: 1788, SEQ ID No: 1790, SEQ ID No: 1792, SEQ ID No: 1794, SEQ ID No: 1796, SEQ ID No: 1798, SEQ ID No: 1800, SEQ ID No: 1802, SEQ ID No: 1804, SEQ ID No: 1806, SEQ ID No: 1808, SEQ ID No: 1810, SEQ ID No: 1812, SEQ ID No: 1814, SEQ ID No: 1816, SEQ ID No: 1818, SEQ ID No: 1820, SEQ ID No: 1822, SEQ ID No: 1824, SEQ ID No: 1826, SEQ ID No: 1828, SEQ ID No: 1830, SEQ ID No: 1832, SEQ ID No: 1834, SEQ ID No: 1836, SEQ ID No: 1838, SEQ ID No: 1840, SEQ ID No: 1842, SEQ ID No: 1844, SEQ ID No: 1846, SEQ ID No: 1848, SEQ ID No: 1850, SEQ ID No: 1852, SEQ ID No: 1854, SEQ ID No: 1856, SEQ ID No: 1858, SEQ ID No: 1860, SEQ ID No: 1862, SEQ ID No: 1864, SEQ ID No: 1866, SEQ ID No: 1868, SEQ ID No: 1870, SEQ ID No: 1872, SEQ ID No: 1874, SEQ ID No: 1876, SEQ ID No: 1878, SEQ ID No: 1880, SEQ ID No: 1882, SEQ ID No: 1884, SEQ ID No: 1886, SEQ ID No: 1888, SEQ ID No: 1890, SEQ ID No: 1892, SEQ ID No: 1894, SEQ ID No: 1896, SEQ ID No: 1898, SEQ ID No: 1900, SEQ ID No: 1902, SEQ ID No: 1904, SEQ ID No: 1906, SEQ ID No: 1908, SEQ ID No: 1910, SEQ ID No: 1912, SEQ ID No: 1914, SEQ ID No: 1916, SEQ ID No: 1918, SEQ ID No: 1920, SEQ ID No: 1922, SEQ ID No: 1924, SEQ ID No: 1926, SEQ ID No: 1928, SEQ ID No: 1930, SEQ ID No: 1932, SEQ ID No: 1934, SEQ ID No: 1936, SEQ ID No: 1938, SEQ ID No: 1940, SEQ ID No: 1942, SEQ ID No: 1944, SEQ ID No: 1946, SEQ ID No: 1948, SEQ ID No: 1950, SEQ ID No: 1952, SEQ ID No: 1954, SEQ ID No: 1956, SEQ ID No: 1958, SEQ ID No: 1960, SEQ ID No: 1962, SEQ ID No: 1964, SEQ ID No: 1966, SEQ ID No: 1968, SEQ ID No: 1970, SEQ ID No: 1972, SEQ ID No: 19742.
b) a nucleic acid sequence encoding a fragment of the protein of (a), wherein the fragment has a biological activity of the protein of (a); and
c) a nucleic acid sequence encoding an amino acid sequence that is at least about 70% identical to an amino acid sequence of (a) and has a biological activity of the protein comprising the amino acid sequence.
[020] In some embodiments, the nucleic acid sequence encodes an amino acid sequence that is at least about 90%, at least about 95%, at least about 97% or at least about 99% identical to the amino acid sequence of (a) and has a biological activity of the protein comprising the amino acid sequence.
[021] In some embodiments, the nucleic acid sequence encodes a protein comprising an amino acid sequence selected from SEQ ID NO: 2, SEQ ID No: 4, SEQ ID No: 6, SEQ ID No: 8, SEQ ID No: 10, SEQ ID No: 12, SEQ ID No: 14, SEQ ID No: 16, SEQ ID No: 18, SEQ ID No: 20, SEQ ID No: 22, SEQ ID No: 24, SEQ ID No: 26, SEQ ID No: 28, SEQ ID No: 30, SEQ ID No: 32, SEQ ID No: 34, SEQ ID No: 36, SEQ ID No: 38, SEQ ID No: 40, SEQ ID No: 42, SEQ ID No: 44, SEQ ID No: 46, SEQ ID No: 48, SEQ ID No: 50, SEQ ID No: 52, SEQ ID No: 54, SEQ ID No: 56, SEQ ID No: 58, SEQ ID No: 60, SEQ ID No: 62, SEQ ID No: 64, SEQ ID No: 66, SEQ ID No: 68, SEQ ID No: 70, SEQ ID No: 72, SEQ ID No: 74, SEQ ID No: 76, SEQ ID No: 78, SEQ ID No: 80, SEQ ID No: 82, SEQ ID No: 84, SEQ ID No: 86, SEQ ID No: 88, SEQ ID No: 90, SEQ ID No: 92, SEQ ID No: 94, SEQ ID No: 96, SEQ ID No: 98, SEQ ID No: 100, SEQ ID No: 102, SEQ ID No: 104, SEQ ID No: 106, SEQ ID No: 108, SEQ ID No: 110, SEQ ID No: 112, SEQ ID No: 114, SEQ ID No: 116, SEQ ID No: 118, SEQ ID No: 120, SEQ ID No: 122, SEQ ID No: 124, SEQ ID No: 126, SEQ ID No: 128, SEQ ID No: 130, SEQ ID No: 132, SEQ ID No: 134, SEQ ID No: 136, SEQ ID No: 138, SEQ ID No: 140, SEQ ID No: 142, SEQ ID No: 144, SEQ ID No: 146, SEQ ID No: 148, SEQ ID No: 150, SEQ ID No: 152, SEQ ID No: 154, SEQ ID No: 156, SEQ ID No: 158, SEQ ID No: 160, SEQ ID No: 162, SEQ ID No: 164, SEQ ID No: 166, SEQ ID No: 168, SEQ ID No: 170, SEQ ID No: 172, SEQ ID No: 174, SEQ ID No: 176, SEQ ID No: 178, SEQ ID No: 180, SEQ ID No: 182, SEQ ID No: 184, SEQ ID No: 186, SEQ ID No: 188, SEQ ID No: 190, SEQ ID No: 192, SEQ ID No: 194, SEQ ID No: 196, SEQ ID No: 198, SEQ ID No: 200, SEQ ID No: 202, SEQ ID No: 204, SEQ ID No: 206, SEQ ID No: 208, SEQ ID No: 210, SEQ ID No: 212, SEQ ID No: 214, SEQ ID No: 216, SEQ ID No: 218, SEQ ID No: 220, SEQ ID No: 222, SEQ ID No: 224, SEQ ID No: 226, SEQ ID No: 228, SEQ ID No: 230, SEQ ID No: 232, SEQ ID No: 234, SEQ ID No: 236, SEQ ID No: 238, SEQ ID No: 240, SEQ ID No: 242, SEQ ID No: 244, SEQ ID No: 246, SEQ ID No: 248, SEQ ID No: 250, SEQ ID No: 252, SEQ ID No: 254, SEQ ID No: 256, SEQ ID No: 258, SEQ ID No: 260, SEQ ID No: 262, SEQ ID No: 264, SEQ ID No: 266, SEQ ID No: 268, SEQ ID No: 270, SEQ ID No: 272, SEQ ID No: 274, SEQ ID No: 276, SEQ ID No: 278, SEQ ID No: 280, SEQ ID No: 282, SEQ ID No: 284, SEQ ID No: 286, SEQ ID No: 288, SEQ ID No: 290, SEQ ID No: 292, SEQ ID No: 294, SEQ ID No: 296, SEQ ID No: 298, SEQ ID No: 300, SEQ ID No: 302, SEQ ID No: 304, SEQ ID No: 306, SEQ ID No: 308, SEQ ID No: 310, SEQ ID No: 312, SEQ ID No: 314, SEQ ID No: 316, SEQ ID No: 318, SEQ ID No: 320, SEQ ID No: 322, SEQ ID No: 324, SEQ ID No: 326, SEQ ID No: 328, SEQ ID No: 330, SEQ ID No: 332, SEQ ID No: 334, SEQ ID No: 336, SEQ ID No: 338, SEQ ID No: 340, SEQ ID No: 342, SEQ ID No: 344, SEQ ID No: 346, SEQ ID No: 348, SEQ ID No: 350, SEQ ID No: 352, SEQ ID No: 354, SEQ ID No: 356, SEQ ID No: 358, SEQ ID No: 360, SEQ ID No: 362, SEQ ID No: 364, SEQ ID No: 366, SEQ ID No: 368, SEQ ID No: 370, SEQ ID No: 372, SEQ ID No: 374, SEQ ID No: 376, SEQ ID No: 378, SEQ ID No: 380, SEQ ID No: 382, SEQ ID No: 384, SEQ ID No: 386, SEQ ID No: 388, SEQ ID No: 390, SEQ ID No: 392, SEQ ID No: 394, SEQ ID No: 396, SEQ ID No: 398, SEQ ID No: 400, SEQ ID No: 402, SEQ ID No: 404, SEQ ID No: 406, SEQ ID No: 408, SEQ ID No: 410, SEQ ID No: 412, SEQ ID No: 414, SEQ ID No: 416, SEQ ID No: 418, SEQ ID No: 420, SEQ ID No: 422, SEQ ID No: 424, SEQ ID No: 426, SEQ ID No: 428, SEQ ID No: 430, SEQ ID No: 432, SEQ ID No: 434, SEQ ID No: 436, SEQ ID No: 438, SEQ ID No: 440, SEQ ID No: 442, SEQ ID No: 444, SEQ ID No: 446, SEQ ID No: 448, SEQ ID No: 450, SEQ ID No: 452, SEQ ID No: 454, SEQ ID No: 456, SEQ ID No: 458, SEQ ID No: 460, SEQ ID No: 462, SEQ ID No: 464, SEQ ID No: 466, SEQ ID No: 468, SEQ ID No: 470, SEQ ID No: 472, SEQ ID No: 474, SEQ ID No: 476, SEQ ID No: 478, SEQ ID No: 480, SEQ ID No: 482, SEQ ID No: 484, SEQ ID No: 486, SEQ ID No: 488, SEQ ID No: 490, SEQ ID No: 492, SEQ ID No: 494, SEQ ID No: 496, SEQ ID No: 498, SEQ ID No: 500, SEQ ID No: 502, SEQ ID No: 504, SEQ ID No: 506, SEQ ID No: 508, SEQ ID No: 510, SEQ ID No: 512, SEQ ID No: 514, SEQ ID No: 516, SEQ ID No: 518, SEQ ID No: 520, SEQ ID No: 522, SEQ ID No: 524, SEQ ID No: 526, SEQ ID No: 528, SEQ ID No: 530, SEQ ID No: 532, SEQ ID No: 534, SEQ ID No: 536, SEQ ID No: 538, SEQ ID No: 540, SEQ ID No: 542, SEQ ID No: 544, SEQ ID No: 546, SEQ ID No: 548, SEQ ID No: 550, SEQ ID No: 552, SEQ ID No: 554, SEQ ID No: 556, SEQ ID No: 558, SEQ ID No: 560, SEQ ID No: 562, SEQ ID No: 564, SEQ ID No: 566, SEQ ID No: 568, SEQ ID No: 570, SEQ ID No: 572, SEQ ID No: 574, SEQ ID No: 576, SEQ ID No: 578, SEQ ID No: 580, SEQ ID No: 582, SEQ ID No: 584, SEQ ID No: 586, SEQ ID No: 588, SEQ ID No: 590, SEQ ID No: 592, SEQ ID No: 594, SEQ ID No: 596, SEQ ID No: 598, SEQ ID No: 600, SEQ ID No: 602, SEQ ID No: 604, SEQ ID No: 606, SEQ ID No: 608, SEQ ID No: 610, SEQ ID No: 612, SEQ ID No: 614, SEQ ID No: 616, SEQ ID No: 618, SEQ ID No: 620, SEQ ID No: 622, SEQ ID No: 624, SEQ ID No: 626, SEQ ID No: 628, SEQ ID No: 630, SEQ ID No: 632, SEQ ID No: 634, SEQ ID No: 636, SEQ ID No: 638, SEQ ID No: 640, SEQ ID No: 642, SEQ ID No: 644, SEQ ID No: 646, SEQ ID No: 648, SEQ ID No: 650, SEQ ID No: 652, SEQ ID No: 654, SEQ ID No: 656, SEQ ID No: 658, SEQ ID No: 660, SEQ ID No: 662, SEQ ID No: 664, SEQ ID No: 666, SEQ ID No: 668, SEQ ID No: 670, SEQ ID No: 672, SEQ ID No: 674, SEQ ID No: 676, SEQ ID No: 678, SEQ ID No: 680, SEQ ID No: 682, SEQ ID No: 684, SEQ ID No: 686, SEQ ID No: 688, SEQ ID No: 690, SEQ ID No: 692, SEQ ID No: 694, SEQ ID No: 696, SEQ ID No: 698, SEQ ID No: 700, SEQ ID No: 702, SEQ ID No: 704, SEQ ID No: 706, SEQ ID No: 708, SEQ ID No: 710, SEQ ID No: 712, SEQ ID No: 714, SEQ ID No: 716, SEQ ID No: 718, SEQ ID No: 720, SEQ ID No: 722, SEQ ID No: 724, SEQ ID No: 726, SEQ ID No: 728, SEQ ID No: 730, SEQ ID No: 732, SEQ ID No: 734, SEQ ID No: 736, SEQ ID No: 738, SEQ ID No: 740, SEQ ID No: 742, SEQ ID No: 744, SEQ ID No: 746, SEQ ID No: 748, SEQ ID No: 750, SEQ ID No: 752, SEQ ID No: 754, SEQ ID No: 756, SEQ ID No: 758, SEQ ID No: 760, SEQ ID No: 762, SEQ ID No: 764, SEQ ID No: 766, SEQ ID No: 768, SEQ ID No: 770, SEQ ID No: 772, SEQ ID No: 774, SEQ ID No: 776, SEQ ID No: 778, SEQ ID No: 780, SEQ ID No: 782, SEQ ID No: 784, SEQ ID No: 786, SEQ ID No: 788, SEQ ID No: 790, SEQ ID No: 792, SEQ ID No: 794, SEQ ID No: 796, SEQ ID No: SEQ ID No: 798, SEQ ID No: 800, SEQ ID No: 802, SEQ ID No: 804, SEQ ID No: 806, SEQ ID No: 808, SEQ ID No: 810, SEQ ID No: 812, SEQ ID No: 814, SEQ ID No: 816, SEQ ID No: 818, SEQ ID No: 820, SEQ ID No: 822, SEQ ID No: 824, SEQ ID No: 826, SEQ ID No: 828, SEQ ID No: 830, SEQ ID No: 832, SEQ ID No: 834, SEQ ID No: 836, SEQ ID No: 838, SEQ ID No: 840, SEQ ID No: 842, SEQ ID No: 844, SEQ ID No: 846, SEQ ID No: 848, SEQ ID No: 850, SEQ ID No: 852, SEQ ID No: 854, SEQ ID No: 856, SEQ ID No: 858, SEQ ID No: 860, SEQ ID No: 862, SEQ ID No: 864, SEQ ID No: 866, SEQ ID No: 868, SEQ ID No: 870, SEQ ID No: 872, SEQ ID No: 874, SEQ ID No: 876, SEQ ID No: 878, SEQ ID No: 880, SEQ ID No: 882, SEQ ID No: 884, SEQ ID No: 886, SEQ ID No: 888, SEQ ID No: 890, SEQ ID No: 892, SEQ ID No: 894, SEQ ID No: 896, SEQ ID No: 898, SEQ ID No: 900, SEQ ID No: 902, SEQ ID No: 904, SEQ ID No: 906, SEQ ID No: 908, SEQ ID No: 910, SEQ ID No: 912, SEQ ID No: 914, SEQ ID No: 916, SEQ ID No: 918, SEQ ID No: 920, SEQ ID No: 922, SEQ ID No: 924, SEQ ID No: 926, SEQ ID No: 928, SEQ ID No: 930, SEQ ID No: 932, SEQ ID No: 934, SEQ ID No: 936, SEQ ID No: 938, SEQ ID No: 940, SEQ ID No: 942, SEQ ID No: 944, SEQ ID No: 946, SEQ ID No: 948, SEQ ID No: 950, SEQ ID No: 952, SEQ ID No: 954, SEQ ID No: 956, SEQ ID No: 958, SEQ ID No: 960, SEQ ID No: 962, SEQ ID No: 964, SEQ ID No: 966, SEQ ID No: 968, SEQ ID No: 970, SEQ ID No: 972, SEQ ID No: 974, SEQ ID No: 976, SEQ ID No: 978, SEQ ID No: 980, SEQ ID No: 982, SEQ ID No: 984, SEQ ID No: 986, SEQ ID No: 988, SEQ ID No: 990, SEQ ID No: 992, SEQ ID No: 994, SEQ ID No: 996, SEQ ID No: 998, SEQ ID No: 1000, SEQ ID No: 1002, SEQ ID No: 1004, SEQ ID No: 1006, SEQ ID No: 1008, SEQ ID No: 1010, SEQ ID No: 1012, SEQ ID No: 1014, SEQ ID No: 1016, SEQ ID No: 1018, SEQ ID No: 1020, SEQ ID No: 1022, SEQ ID No: 1024, SEQ ID No: 1026, SEQ ID No: 1028, SEQ ID No: 1030, SEQ ID No: 1032, SEQ ID No: 1034, SEQ ID No: 1036, SEQ ID No: 1038, SEQ ID No: 1040, SEQ ID No: 1042, SEQ ID No: 1044, SEQ ID No: 1046, SEQ ID No: 1048, SEQ ID No: 1050, SEQ ID No: 1052, SEQ ID No: 1054, SEQ ID No: 1056, SEQ ID No: 1058, SEQ ID No: 1060, SEQ ID No: 1062, SEQ ID No: 1064, SEQ ID No: 1066, SEQ ID No: 1068, SEQ ID No: 1070, SEQ ID No: 1072, SEQ ID No: 1074, SEQ ID No: 1076, SEQ ID No: 1078, SEQ ID No: 1080, SEQ ID No: 1082, SEQ ID No: 1084, SEQ ID No: 1086, SEQ ID No: 1088, SEQ ID No: 1090, SEQ ID No: 1092, SEQ ID No: 1094, SEQ ID No: 1096, SEQ ID No: 1098, SEQ ID NO: 1100, SEQ ID No: 1102, SEQ ID No: 1104, SEQ ID No: 1106, SEQ ID No: 1108, SEQ ID No: 1110, SEQ ID No: 1112, SEQ ID No: 1114, SEQ ID No: 1116, SEQ ID No: 1118, SEQ ID No: 1120, SEQ ID No: 1122, SEQ ID No: 1124, SEQ ID No: 1126, SEQ ID No: 1128, SEQ ID No: 1130, SEQ ID No: 1132, SEQ ID No: 1134, SEQ ID No: 1136, SEQ ID No: 1138, SEQ ID No: 1140, SEQ ID No: 1142, SEQ ID No: 1144, SEQ ID No: 1146, SEQ ID No: 1148, SEQ ID No: 1150, SEQ ID No: 1152, SEQ ID No: 1154, SEQ ID No: 1156, SEQ ID No: 1158, SEQ ID No: 1160, SEQ ID No: 1162, SEQ ID No: 1164, SEQ ID No: 1166, SEQ ID No: 1168, SEQ ID No: 1170, SEQ ID No: 1172, SEQ ID No: 1174, SEQ ID No: 1176, SEQ ID No: 1178, SEQ ID No: 1180, SEQ ID No: 1182, SEQ ID No: 1184, SEQ ID No: 1186, SEQ ID No: 1188, SEQ ID No: 1190, SEQ ID No: 1192, SEQ ID No: 1194, SEQ ID No: 1196, SEQ ID No: 1198, SEQ ID No: 1200, SEQ ID No: 1202, SEQ ID No: 1204, SEQ ID No: 1206, SEQ ID No: 1208, SEQ ID No: 1210, SEQ ID No: 1212, SEQ ID No: 1214, SEQ ID No: 1216, SEQ ID No: 1218, SEQ ID No: 1220, SEQ ID No: 1222, SEQ ID No: 1224, SEQ ID No: 1226, SEQ ID No: 1228, SEQ ID No: 1230, SEQ ID No: 1232, SEQ ID No: 1234, SEQ ID No: 1236, SEQ ID No: 1238, SEQ ID No: 1240, SEQ ID No: 1242, SEQ ID No: 1244, SEQ ID No: 1246, SEQ ID No: 1248, SEQ ID No: 1250, SEQ ID No: 1252, SEQ ID No: 1254, SEQ ID No: 1256, SEQ ID No: 1258, SEQ ID No: 1260, SEQ ID No: 1262, SEQ ID No: 1264, SEQ ID No: 1266, SEQ ID No: 1268, SEQ ID No: 1270, SEQ ID No: 1272, SEQ ID No: 1274, SEQ ID No: 1276, SEQ ID No: 1278, SEQ ID No: 1280, SEQ ID No: 1282, SEQ ID No: 1284, SEQ ID No: 1286, SEQ ID No: 1288, SEQ ID No: 1290, SEQ ID No: 1292, SEQ ID No: 1294, SEQ ID No: 1296, SEQ ID No: 1298, SEQ ID No: 1300, SEQ ID No: 1302, SEQ ID No: 1304, SEQ ID No: 1306, SEQ ID No: 1308, SEQ ID No: 1310, SEQ ID No: 1312, SEQ ID No: 1314, SEQ ID No: 1316, SEQ ID No: 1318, SEQ ID No: 1320, SEQ ID No: 1322, SEQ ID No: 1324, SEQ ID No: 1326, SEQ ID No: 1328, SEQ ID No: 1330, SEQ ID No: 1332, SEQ ID No: 1334, SEQ ID No: 1336, SEQ ID No: 1338, SEQ ID No: 1340, SEQ ID No: 1342, SEQ ID No: 1344, SEQ ID No: 1346, SEQ ID No: 1348, SEQ ID No: 1350, SEQ ID No: 1352, SEQ ID No: 1354, SEQ ID No: 1356, SEQ ID No: 1358, SEQ ID No: 1360, SEQ ID No: 1362, SEQ ID No: 1364, SEQ ID No: 1366, SEQ ID No: 1368, SEQ ID No: 1370, SEQ ID No: 1372, SEQ ID No: 1374, SEQ ID No: 1376, SEQ ID No: 1378, SEQ ID No: 1380, SEQ ID No: 1382, SEQ ID No: 1384, SEQ ID No: 1386, SEQ ID No: 1388, SEQ ID No: 1390, SEQ ID No: 1392, SEQ ID No: 1394, SEQ ID No: 1396, SEQ ID No: 1398, SEQ ID No: 1400, SEQ ID No: 1402, SEQ ID No: 1404, SEQ ID No: 1406, SEQ ID No: 1408, SEQ ID No: 1410, SEQ ID No: 1412, SEQ ID No: 1414, SEQ ID No: 1416, SEQ ID No: 1418, SEQ ID No: 1420, SEQ ID No: 1422, SEQ ID No: 1424, SEQ ID No: 1426, SEQ ID No: 1428, SEQ ID No: 1430, SEQ ID No: 1432, SEQ ID No: 1434, SEQ ID No: 1436, SEQ ID No: 1438, SEQ ID No: 1440, SEQ ID No: 1442, SEQ ID No: 1444, SEQ ID No: 1446, SEQ ID No: 1448, SEQ ID No: 1450, SEQ ID No: 1452, SEQ ID No: 1454, SEQ ID No: 1456, SEQ ID No: 1458, SEQ ID No: 1460, SEQ ID No: 1462, SEQ ID No: 1464, SEQ ID No: 1466, SEQ ID No: 1468, SEQ ID No: 1470, SEQ ID No: 1472, SEQ ID No: 1474, SEQ ID No: 1476, SEQ ID No: 1478, SEQ ID No: 1480, SEQ ID No: 1482, SEQ ID No: 1484, SEQ ID No: 1486, SEQ ID No: 1488, SEQ ID No: 1490, SEQ ID No: 1492, SEQ ID No: 1494, SEQ ID No: 1496, SEQ ID No: 1498, SEQ ID No: 1500, SEQ ID No: 1502, SEQ ID No: 1504, SEQ ID No: 1506, SEQ ID No: 1508, SEQ ID No: 1510, SEQ ID No: 1512, SEQ ID No: 1514, SEQ ID No: 1516, SEQ ID No: 1518, SEQ ID No: 1520, SEQ ID No: 1522, SEQ ID No: 1524, SEQ ID No: 1526, SEQ ID No: 1528, SEQ ID No: 1530, SEQ ID No: 1532, SEQ ID No: 1534, SEQ ID No: 1536, SEQ ID No: 1538, SEQ ID No: 1540, SEQ ID No: 1542, SEQ ID No: 1544, SEQ ID No: 1546, SEQ ID No: 1548, SEQ ID No: 1550, SEQ ID No: 1552, SEQ ID No: 1554, SEQ ID No: 1556, SEQ ID No: 1558, SEQ ID No: 1560, SEQ ID No: 1562, SEQ ID No: 1564, SEQ ID No: 1566, SEQ ID No: 1568, SEQ ID No: 1570, SEQ ID No: 1572, SEQ ID No: 1574, SEQ ID No: 1576, SEQ ID No: 1578, SEQ ID No: 1580, SEQ ID No: 1582, SEQ ID No: 1584, SEQ ID No: 1586, SEQ ID No: 1588, SEQ ID No: 1590, SEQ ID No: 1592, SEQ ID No: 1594, SEQ ID No: 1596, SEQ ID No: 1598, SEQ ID No: 1600, SEQ ID No: 1602, SEQ ID No: 1604, SEQ ID No: 1606, SEQ ID No: 1608, SEQ ID No: 1610, SEQ ID No: 1612, SEQ ID No: 1614, SEQ ID No: 1616, SEQ ID No: 1618, SEQ ID No: 1620, SEQ ID No: 1622, SEQ ID No: 1624, SEQ ID No: 1626, SEQ ID No: 1628, SEQ ID No: 1630, SEQ ID No: 1632, SEQ ID No: 1634, SEQ ID No: 1636, SEQ ID No: 1638, SEQ ID No: 1640, SEQ ID No: 1642, SEQ ID No: 1644, SEQ ID No: 1646, SEQ ID No: 1648, SEQ ID No: 1650, SEQ ID No: 1652, SEQ ID No: 1654, SEQ ID No: 1656, SEQ ID No: 1658, SEQ ID No: 1660, SEQ ID No: 1662, SEQ ID No: 1664, SEQ ID No: 1666, SEQ ID No: 1668, SEQ ID No: 1670, SEQ ID No: 1672, SEQ ID No: 1674, SEQ ID No: 1676, SEQ ID No: 1678, SEQ ID No: 1680, SEQ ID No: 1682, SEQ ID No: 1684, SEQ ID No: 1686, SEQ ID No: 1688, SEQ ID No: 1690, SEQ ID No: 1692, SEQ ID No: 1694, SEQ ID No: 1696, SEQ ID No: 1698, SEQ ID No: 1700, SEQ ID No: 1702, SEQ ID No: 1704, SEQ ID No: 1706, SEQ ID No: 1708, SEQ ID No: 1710, SEQ ID No: 1712, SEQ ID No: 1714, SEQ ID No: 1716, SEQ ID No: 1718, SEQ ID No: 1720, SEQ ID No: 1722, SEQ ID No: 1724, SEQ ID No: 1726, SEQ ID No: 1728, SEQ ID No: 1730, SEQ ID No: 1732, SEQ ID No: 1734, SEQ ID No: 1736, SEQ ID No: 1738, SEQ ID No: 1740, SEQ ID No: 1742, SEQ ID No: 1744, SEQ ID No: 1746, SEQ ID No: 1748, SEQ ID No: 1750, SEQ ID No: 1752, SEQ ID No: 1754, SEQ ID No: 1756, SEQ ID No: 1758, SEQ ID No: 1760, SEQ ID No: 1762, SEQ ID No: 1764, SEQ ID No: 1766, SEQ ID No: 1768, SEQ ID No: 1770, SEQ ID No: 1772, SEQ ID No: 1774, SEQ ID No: 1776, SEQ ID No: 1778, SEQ ID No: 1780, SEQ ID No: 1782, SEQ ID No: 1784, SEQ ID No: 1786, SEQ ID No: 1788, SEQ ID No: 1790, SEQ ID No: 1792, SEQ ID No: 1794, SEQ ID No: 1796, SEQ ID No: 1798, SEQ ID No: 1800, SEQ ID No: 1802, SEQ ID No: 1804, SEQ ID No: 1806, SEQ ID No: 1808, SEQ ID No: 1810, SEQ ID No: 1812, SEQ ID No: 1814, SEQ ID No: 1816, SEQ ID No: 1818, SEQ ID No: 1820, SEQ ID No: 1822, SEQ ID No: 1824, SEQ ID No: 1826, SEQ ID No: 1828, SEQ ID No: 1830, SEQ ID No: 1832, SEQ ID No: 1834, SEQ ID No: 1836, SEQ ID No: 1838, SEQ ID No: 1840, SEQ ID No: 1842, SEQ ID No: 1844, SEQ ID No: 1846, SEQ ID No: 1848, SEQ ID No: 1850, SEQ ID No: 1852, SEQ ID No: 1854, SEQ ID No: 1856, SEQ ID No: 1858, SEQ ID No: 1860, SEQ ID No: 1862, SEQ ID No: 1864, SEQ ID No: 1866, SEQ ID No: 1868, SEQ ID No: 1870, SEQ ID No: 1872, SEQ ID No: 1874, SEQ ID No: 1876, SEQ ID No: 1878, SEQ ID No: 1880, SEQ ID No: 1882, SEQ ID No: 1884, SEQ ID No: 1886, SEQ ID No: 1888, SEQ ID No: 1890, SEQ ID No: 1892, SEQ ID No: 1894, SEQ ID No: 1896, SEQ ID No: 1898, SEQ ID No: 1900, SEQ ID No: 1902, SEQ ID No: 1904, SEQ ID No: 1906, SEQ ID No: 1908, SEQ ID No: 1910, SEQ ID No: 1912, SEQ ID No: 1914, SEQ ID No: 1916, SEQ ID No: 1918, SEQ ID No: 1920, SEQ ID No: 1922, SEQ ID No: 1924, SEQ ID No: 1926, SEQ ID No: 1928, SEQ ID No: 1930, SEQ ID No: 1932, SEQ ID No: 1934, SEQ ID No: 1936, SEQ ID No: 1938, SEQ ID No: 1940, SEQ ID No: 1942, SEQ ID No: 1944, SEQ ID No: 1946, SEQ ID No: 1948, SEQ ID No: 1950, SEQ ID No: 1952, SEQ ID No: 1954, SEQ ID No: 1956, SEQ ID No: 1958, SEQ ID No: 1960, SEQ ID No: 1962, SEQ ID No: 1964, SEQ ID No: 1966, SEQ ID No: 1968, SEQ ID No: 1970, SEQ ID No: 1972, SEQ ID No: 1974.
In some embodiments, the nucleic acid sequence comprises a nucleic acid sequence selected from SEQ ID No: 1, SEQ ID No: 3, SEQ ID No: 5, SEQ ID No: 7, SEQ ID No: 9, SEQ ID No: 11, SEQ ID No: 13, SEQ ID No: 15, SEQ ID No: 17, SEQ ID No: 19, SEQ ID No: 21, SEQ ID No: 23, SEQ ID No: 25, SEQ ID No: 27, SEQ ID No: 29, SEQ ID No: 31, SEQ ID No: 33, SEQ ID No: 35, SEQ ID No: 37, SEQ ID No: 39, SEQ ID No: 41, SEQ ID No: 43, SEQ ID No: 45, SEQ ID No: 47, SEQ ID No: 49, SEQ ID No: 51, SEQ ID No: 53, SEQ ID No: 55, SEQ ID No: 56, SEQ ID No: 57, SEQ ID No: 59, SEQ ID No: 61, SEQ ID No: 63, SEQ ID No: 65, SEQ ID No: 67, SEQ ID No: 69, SEQ ID No: 71, SEQ ID No: 73, SEQ ID No: 75, SEQ ID No: 77, SEQ ID No: 79, SEQ ID No: 81, SEQ ID No: 83, SEQ ID No: 85, SEQ ID No: 87, SEQ ID No: 89, SEQ ID No: 91, SEQ ID No: 93, SEQ ID No: 95, SEQ ID No: 97, SEQ ID No: 99, SEQ ID No: 101, SEQ ID No: 103, SEQ ID No: 105, SEQ ID No: 107, SEQ ID No: 109, SEQ ID No: 111, SEQ ID No: 113, SEQ ID No: 115, SEQ ID No: 117, SEQ ID No: 119, SEQ ID No: 121, SEQ ID No: 123, SEQ ID No: 125, SEQ ID No: 127, SEQ ID No: 129, SEQ ID No: 131, SEQ ID No: 133, SEQ ID No: 135, SEQ ID No: 137, SEQ ID No: 139, SEQ ID No: 141, SEQ ID No: 143, SEQ ID No: 145, SEQ ID No: 147, SEQ ID No: 149, SEQ ID No: 151, SEQ ID No: 153, SEQ ID No: 155, SEQ ID No: 157, SEQ ID No: 159, SEQ ID No: 161, SEQ ID No: 163, SEQ ID No: 165, SEQ ID No: 167, SEQ ID No: 169, SEQ ID No: 171, SEQ ID No: 173, SEQ ID No: 175, SEQ ID No: 177, SEQ ID No: 179, SEQ ID No: 181, SEQ ID No: 183, SEQ ID No: 185, SEQ ID No: 187, SEQ ID No: 189, SEQ ID No: 191, SEQ ID No: 193, SEQ ID No: 195, SEQ ID No: 197, SEQ ID No: 199, SEQ ID No: 201, SEQ ID No: 203, SEQ ID No: 205, SEQ ID No: 207, SEQ ID No: 209, SEQ ID No: 211, SEQ ID No: 213, SEQ ID No: 215, SEQ ID No: 217, SEQ ID No: 219, SEQ ID No: 221, SEQ ID No: 223, SEQ ID No: 225, SEQ ID No: 227, SEQ ID No: 229, SEQ ID No: 231, SEQ ID No: 233, SEQ ID No: 235. SEQ ID No: 237, SEQ ID No: 239, SEQ ID No: 241, SEQ ID No: 243, SEQ ID No: 245, SEQ ID No: 247, SEQ ID No: 249, SEQ ID No: 251, SEQ ID No: 253, SEQ ID No: 255, SEQ ID No: 257, SEQ ID No: 259, SEQ ID No: 261, SEQ ID No: 263, SEQ ID No: 265, SEQ ID No: 267, SEQ ID No: 269, SEQ ID No: 271, SEQ ID No: 273, SEQ ID No: 275, SEQ ID No: 277, SEQ ID No: 279, SEQ ID No: 281, SEQ ID No: 283, SEQ ID No: 285, SEQ ID No: 287, SEQ ID No: 289, SEQ ID No: 291, SEQ ID No: 293, SEQ ID No: 295, SEQ ID No: 297, SEQ ID No: 299, SEQ ID No: 301, SEQ ID No: 303, SEQ ID No: 305, SEQ ID No: 307, SEQ ID No: 309, SEQ ID No: 311, SEQ ID No: 313, SEQ ID No: 315, SEQ ID No: 317, SEQ ID No: 319, SEQ ID No: 321, SEQ ID No: 323, SEQ ID No: 325, SEQ ID No: 327, SEQ ID No: 329, SEQ ID No: 331, SEQ ID No: 333, SEQ ID No: 335, SEQ ID No: 337, SEQ ID No: 339, SEQ ID No: 341, SEQ ID No: 343, SEQ ID No: 345, SEQ ID No: 347, SEQ ID No: 349, SEQ ID No: 351, SEQ ID No: 353, SEQ ID No: 355, SEQ ID No: 357, SEQ ID No: 359, SEQ ID No: 361, SEQ ID No: 363, SEQ ID No: 365, SEQ ID No: 367, SEQ ID No: 369, SEQ ID No: 371, SEQ ID No: 373, SEQ ID No: 375, SEQ ID No: 377, SEQ ID No: 379, SEQ ID No: 381, SEQ ID No: 383, SEQ ID No: 385, SEQ ID No: 387, SEQ ID No: 389, SEQ ID No: 391, SEQ ID No: 393, SEQ ID No: 395, SEQ ID No: 397, SEQ ID No: 399, SEQ ID No: 401, SEQ ID No: 403, SEQ ID No: 405, SEQ ID No: 407, SEQ ID No: 409, SEQ ID No: 411, SEQ ID No: 413, SEQ ID No: 415, SEQ ID No: 417, SEQ ID No: 419, SEQ ID No: 421, SEQ ID No: 423, SEQ ID No: 425, SEQ ID No: 427, SEQ ID No: 429, SEQ ID No: 431, SEQ ID No: 433, SEQ ID No: 435, SEQ ID No: 437, SEQ ID No: 439, SEQ ID No: 441, SEQ ID No: 443, SEQ ID No: 445, SEQ ID No: 447, SEQ ID No: 449, SEQ ID No: 451, SEQ ID No: 453, SEQ ID No: 455, SEQ ID No: 457, SEQ ID No: 459, SEQ ID No: 461, SEQ ID No: 463, SEQ ID No: 465, SEQ ID No: 467, SEQ ID No: 469, SEQ ID No: 471, SEQ ID No: 473, SEQ ID No: 475, SEQ ID No: 477, SEQ ID No: 479, SEQ ID No: 481, SEQ ID No: 483, SEQ ID No: 485, SEQ ID No: 487, SEQ ID No: 489, SEQ ID No: 491, SEQ ID No: 493, SEQ ID No: 495, SEQ ID No: 497, SEQ ID No: 499, SEQ ID No: 501, SEQ ID No: 503, SEQ ID No: 505, SEQ ID No: 507, SEQ ID No: 509, SEQ ID No: 511, SEQ ID No: 513, SEQ ID No: 515, SEQ ID No: 517, SEQ ID No: 519, SEQ ID No: 521, SEQ ID No: 523, SEQ ID No: 525, SEQ ID No: 527, SEQ ID No: 529, SEQ ID No: 531, SEQ ID No: 533, SEQ ID No: 535, SEQ ID No: 537, SEQ ID No: 539, SEQ ID No: 541, SEQ ID No: 543, SEQ ID No: 545, SEQ ID No: 547, SEQ ID No: 549, SEQ ID No: 551, SEQ ID No: 553, SEQ ID No: 555, SEQ ID No: 557, SEQ ID No: 559, SEQ ID No: 561, SEQ ID No: 563, SEQ ID No: 565, SEQ ID No: 567, SEQ ID No: 569, SEQ ID No: 571, SEQ ID No: 573, SEQ ID No: 575, SEQ ID No: 577, SEQ ID No: 579, SEQ ID No: 581, SEQ ID No: 583, SEQ ID No: 585, SEQ ID No: 587, SEQ ID No: 589, SEQ ID No: 591, SEQ ID No: 593, SEQ ID No: 595, SEQ ID No: 597, SEQ ID No: 599, SEQ ID No: 601, SEQ ID No: 603, SEQ ID No: 605, SEQ ID No: 607, SEQ ID No: 609, SEQ ID No: 611, SEQ ID No: 613, SEQ ID No: 615, SEQ ID No: 617, SEQ ID No: 619, SEQ ID No: 621, SEQ ID No: 623, SEQ ID No: 625, SEQ ID No: 627, SEQ ID No: 629, SEQ ID No: 631, SEQ ID No: 633, SEQ ID No: 635, SEQ ID No: 637, SEQ ID No: 639, SEQ ID No: 641, SEQ ID No: 643, SEQ ID No: 645, SEQ ID No: 647, SEQ ID No: 649, SEQ ID No: 651, SEQ ID No: 653, SEQ ID No: 655, SEQ ID No: 657, SEQ ID No: 659, SEQ ID No: 661, SEQ ID No: 663, SEQ ID No: 665, SEQ ID No: 667, SEQ ID No: 669, SEQ ID No: 671, SEQ ID No: 673, SEQ ID No: 675, SEQ ID No: 677, SEQ ID No: 679, SEQ ID No: 681, SEQ ID No: 683, SEQ ID No: 685, SEQ ID No: 687, SEQ ID No: 689, SEQ ID No: 691, SEQ ID No: 693, SEQ ID No: 695, SEQ ID No: 697, SEQ ID No: 699, SEQ ID No: 701, SEQ ID No: 703, SEQ ID No: 705, SEQ ID No: 707, SEQ ID No: 709, SEQ ID No: 711, SEQ ID No: 713, SEQ ID No: 715, SEQ ID No: 717, SEQ ID No: 719, SEQ ID No: 721, SEQ ID No: 723, SEQ ID No: 725, SEQ ID No: 727, SEQ ID No: 729, SEQ ID No: 731, SEQ ID No: 733, SEQ ID No: 735, SEQ ID No: 737, SEQ ID No: 739, SEQ ID No: 741, SEQ ID No: 743, SEQ ID No: 745, SEQ ID No: 747, SEQ ID No: 749, SEQ ID No: 751, SEQ ID No: 753, SEQ ID No: 755, SEQ ID No: 757, SEQ ID No: 759, SEQ ID No: 761, SEQ ID No: 763, SEQ ID No: 765, SEQ ID No: 767, SEQ ID No: 769, SEQ ID No: 771, SEQ ID No: 773, SEQ ID No: 775, SEQ ID No: 777, SEQ ID No: 779, SEQ ID No: 781, SEQ ID No: 783, SEQ ID No: 785, SEQ ID No: 787, SEQ ID No: 789, SEQ ID No: 791, SEQ ID No: 793, SEQ ID No: 795, SEQ ID No: 797, SEQ ID No: 799, SEQ ID No: 801, SEQ ID No: 803, SEQ ID No: 805, SEQ ID No: 807, SEQ ID No: 809, SEQ ID No: 811, SEQ ID No: 813, SEQ ID No: 815, SEQ ID No: 817, SEQ ID No: 819, SEQ ID No: 821, SEQ ID No: 823, SEQ ID No: 825, SEQ ID No: 827, SEQ ID No: 829, SEQ ID No: 831, SEQ ID No: 833, SEQ ID No: 835, SEQ ID No: 837, SEQ ID No: 839, SEQ ID No: 841, SEQ ID No: 843, SEQ ID No: 845, SEQ ID No: 847, SEQ ID No: 849, SEQ ID No: 851, SEQ ID No: 853, SEQ ID No: 855, SEQ ID No: 857, SEQ ID No: 859, SEQ ID No: 861, SEQ ID No: 863, SEQ ID No: 865, SEQ ID No: 867, SEQ ID No: 869, SEQ ID No: 871, SEQ ID No: 873, SEQ ID No: 875, SEQ ID No: 877, SEQ ID No: 879, SEQ ID No: 881, SEQ ID No: 883, SEQ ID No: 885, SEQ ID No: 887, SEQ ID No: 889, SEQ ID No: 891, SEQ ID No: 893, SEQ ID No: 895, SEQ ID No: 897, SEQ ID No: 899, SEQ ID No: 901, SEQ ID No: 903, SEQ ID No: 905, SEQ ID No: 907, SEQ ID No: 909, SEQ ID No: 911, SEQ ID No: 913, SEQ ID No: 915, SEQ ID No: 917, SEQ ID No: 919, SEQ ID No: 921, SEQ ID No: 923, SEQ ID No: 925, SEQ ID No: 927, SEQ ID No: 929, SEQ ID No: 931, SEQ ID No: 933, SEQ ID No: 935, SEQ ID No: 937, SEQ ID No: 939, SEQ ID No: 941, SEQ ID No: 943, SEQ ID No: 945, SEQ ID No: 947, SEQ ID No: 949, SEQ ID No: 951, SEQ ID No: 953, SEQ ID No: 955, SEQ ID No: 957, SEQ ID No: 959, SEQ ID No: 961, SEQ ID No: 963, SEQ ID No: 965, SEQ ID No: 967, SEQ ID No: 969, SEQ ID No: 971, SEQ ID No: 973, SEQ ID No: 975, SEQ ID No: 977, SEQ ID No: 979, SEQ ID No: 981, SEQ ID No: 983, SEQ ID No: 985, SEQ ID No: 987, SEQ ID No: 989, SEQ ID No: 991, SEQ ID No: 993, SEQ ID No: 995, SEQ ID No: 997, SEQ ID No: 999, SEQ ID No: 1001, SEQ ID No: 1003, SEQ ID No: 1005, SEQ ID No: 1007, SEQ ID No: 1009, SEQ ID No: 1011, SEQ ID No: 1013, SEQ ID No: 1015, SEQ ID No: 1017, SEQ ID No: 1019, SEQ ID No: 1021, SEQ ID No: 1023, SEQ ID No: 1025, SEQ ID No: 1027, SEQ ID No: 1029, SEQ ID No: 1031, SEQ ID No: 1033, SEQ ID No: 1035, SEQ ID No: 1037, SEQ ID No: 1039, SEQ ID No: 1041, SEQ ID No: 1043, SEQ ID No: 1045, SEQ ID No: 1047, SEQ ID No: 1049, SEQ ID No: 1051, SEQ ID No: 1053, SEQ ID No: 1055, SEQ ID No: 1057, SEQ ID No: 1059, SEQ ID No: 1061, SEQ ID No: 1063, SEQ ID No: 1065, SEQ ID No: 1067, SEQ ID No: 1069, SEQ ID No: 1071, SEQ ID No: 1073, SEQ ID No: 1075, SEQ ID No: 1077, SEQ ID No: 1079, SEQ ID No: 1081, SEQ ID No: 1083, SEQ ID No: 1085, SEQ ID No: 1087, SEQ ID No: 1089, SEQ ID No: 1091, SEQ ID No: 1093, SEQ ID No: 1095, SEQ ID No: 1097, SEQ ID No: 1099, SEQ ID No: 1101, SEQ ID No: 1103, SEQ ID No: 1105, SEQ ID No: 1107, SEQ ID No: 1109, SEQ ID No: 1111, SEQ ID No: 1113, SEQ ID No: 1115, SEQ ID No: 1117, SEQ ID No: 1119, SEQ ID No: 1121, SEQ ID No: 1123, SEQ ID No: 1125, SEQ ID No: 1127, SEQ ID No: 1129, SEQ ID No: 1131, SEQ ID No: 1133, SEQ ID No: 1135, SEQ ID No: 1137, SEQ ID No: 1139, SEQ ID No: 1141, SEQ ID No: 1143, SEQ ID No: 1145, SEQ ID No: 1147, SEQ ID No: 1149, SEQ ID No: 1151, SEQ ID No: 1153, SEQ ID No: 1155, SEQ ID No: 1157, SEQ ID No: 1159, SEQ ID No: 1161, SEQ ID No: 1163, SEQ ID No: 1165, SEQ ID No: 1167, SEQ ID No: 1169, SEQ ID No: 1171, SEQ ID No: 1173, SEQ ID No: 1175, SEQ ID No: 1177, SEQ ID No: 1179, SEQ ID No: 1181, SEQ ID No: 1183, SEQ ID No: 1185, SEQ ID No: 1187, SEQ ID No: 1189, SEQ ID No: 1191, SEQ ID No: 1193, SEQ ID No: 1195, SEQ ID No: 1197, SEQ ID No: 1199, SEQ ID No: 1201, SEQ ID No: 1203, SEQ ID No: 1205, SEQ ID No: 1207, SEQ ID No: 1209, SEQ ID No: 1211, SEQ ID No: 1213, SEQ ID No: 1215, SEQ ID No: 1217, SEQ ID No: 1219, SEQ ID No: 1221, SEQ ID No: 1223, SEQ ID No: 1225, SEQ ID No: 1227, SEQ ID No: 1229, SEQ ID No: 1231, SEQ ID No: 1233, SEQ ID No: 1235, SEQ ID No: 1237, SEQ ID No: 1239, SEQ ID No: 1241, SEQ ID No: 1243, SEQ ID No: 1245, SEQ ID No: 1247, SEQ ID No: 1249, SEQ ID No: 1251, SEQ ID No: 1253, SEQ ID No: 1255, SEQ ID No: 1257, SEQ ID No: 1259, SEQ ID No: 1261, SEQ ID No: 1263, SEQ ID No: 1265, SEQ ID No: 1267, SEQ ID No: 1269, SEQ ID No: 1271, SEQ ID No: 1273, SEQ ID No: 1275, SEQ ID No: 1277, SEQ ID No: 1279, SEQ ID No: 1281, SEQ ID No: 1283, SEQ ID No: 1285, SEQ ID No: 1287, SEQ ID No: 1289, SEQ ID No: 1291, SEQ ID No: 1293, SEQ ID No: 1295, SEQ ID No: 1297, SEQ ID No: 1299, SEQ ID No: 1301, SEQ ID No: 1303, SEQ ID No: 1305, SEQ ID No: 1307, SEQ ID No: 1309, SEQ ID No: 1311, SEQ ID No: 1313, SEQ ID No: 1315, SEQ ID No: 1317, SEQ ID No: 1319, SEQ ID No: 1321, SEQ ID No: 1323, SEQ ID No: 1325, SEQ ID No: 1327, SEQ ID No: 1329, SEQ ID No: 1331, SEQ ID No: 1333, SEQ ID No: 1335, SEQ ID No: 1337, SEQ ID No: 1339, SEQ ID No: 1341, SEQ ID No: 1343, SEQ ID No: 1345, SEQ ID No: 1347, SEQ ID No: 1349, SEQ ID No: 1351, SEQ ID No: 1353, SEQ ID No: 1355, SEQ ID No: 1357, SEQ ID No: 1359, SEQ ID No: 1361, SEQ ID No: 1363, SEQ ID No: 1365, SEQ ID No: 1367, SEQ ID No: 1369, SEQ ID No: 1371, SEQ ID No: 1373, SEQ ID No: 1375, SEQ ID No: 1377, SEQ ID No: 1379, SEQ ID No: 1381, SEQ ID No: 1383, SEQ ID No: 1385, SEQ ID No: 1387, SEQ ID No: 1389, SEQ ID No: 1391, SEQ ID No: 1393, SEQ ID No: 1395, SEQ ID No: 1397, SEQ ID No: 1399, SEQ ID No: 1401, SEQ ID No: 1403, SEQ ID No: 1405, SEQ ID No: 1407, SEQ ID No: 1409, SEQ ID No: 1411, SEQ ID No: 1413, SEQ ID No: 1415, SEQ ID No: 1417, SEQ ID No: 1419, SEQ ID No: 1421, SEQ ID No: 1423, SEQ ID No: 1425, SEQ ID No: 1427, SEQ ID No: 1429, SEQ ID No: 1431, SEQ ID No: 1433, SEQ ID No: 1435, SEQ ID No: 1437, SEQ ID No: 1439, SEQ ID No: 1441, SEQ ID No: 1443, SEQ ID No: 1445, SEQ ID No: 1447, SEQ ID No: 1449, SEQ ID No: 1451, SEQ ID No: 1453, SEQ ID No: 1455, SEQ ID No: 1457, SEQ ID No: 1459, SEQ ID No: 1461, SEQ ID No: 1463, SEQ ID No: 1465, SEQ ID No: 1467, SEQ ID No: 1469, SEQ ID No: 1471, SEQ ID No: 1473, SEQ ID No: 1475, SEQ ID No: 1477, SEQ ID No: 1479, SEQ ID No: 1481, SEQ ID No: 1483, SEQ ID No: 1485, SEQ ID No: 1487, SEQ ID No: 1489, SEQ ID No: 1491, SEQ ID No: 1493, SEQ ID No: 1495, SEQ ID No: 1497, SEQ ID No: 1499, SEQ ID No: 1501, SEQ ID No: 1503, SEQ ID No: 1505, SEQ ID No: 1507, SEQ ID No: 1509, SEQ ID No: 1511, SEQ ID No: 1513, SEQ ID No: 1515, SEQ ID No: 1517, SEQ ID No: 1519, SEQ ID No: 1521, SEQ ID No: 1523, SEQ ID No: 1525, SEQ ID No: 1527, SEQ ID No: 1529, SEQ ID No: 1531, SEQ ID No: 1533, SEQ ID No: 1535, SEQ ID No: 1537, SEQ ID No: 1539, SEQ ID No: 1541, SEQ ID No: 1543, SEQ ID No: 1545, SEQ ID No: 1547, SEQ ID No: 1549, SEQ ID No: 1551, SEQ ID No: 1553, SEQ ID No: 1555, SEQ ID No: 1557, SEQ ID No: 1559, SEQ ID No: 1561, SEQ ID No: 1563, SEQ ID No: 1565, SEQ ID No: 1567, SEQ ID No: 1569, SEQ ID No: 1571, SEQ ID No: 1573, SEQ ID No: 1575, SEQ ID No: 1577, SEQ ID No: 1579, SEQ ID No: 1581, SEQ ID No: 1583, SEQ ID No: 1585, SEQ ID No: 1587, SEQ ID No: 1589, SEQ ID No: 1591, SEQ ID No: 1593, SEQ ID No: 1595, SEQ ID No: 1597, SEQ ID No: 1599, SEQ ID No: 1601, SEQ ID No: 1603, SEQ ID No: 1605, SEQ ID No: 1607, SEQ ID No: 1609, SEQ ID No: 1611, SEQ ID No: 1613, SEQ ID No: 1615, SEQ ID No: 1617, SEQ ID No: 1619, SEQ ID No: 1621, SEQ ID No: 1623, SEQ ID No: 1625, SEQ ID No: 1627, SEQ ID No: 1629, SEQ ID No: 1631, SEQ ID No: 1633, SEQ ID No: 1635, SEQ ID No: 1637, SEQ ID No: 1639, SEQ ID No: 1641, SEQ ID No: 1643, SEQ ID No: 1645, SEQ ID No: 1647, SEQ ID No: 1649, SEQ ID No: 1651, SEQ ID No: 1653, SEQ ID No: 1655, SEQ ID No: 1657, SEQ ID No: 1659, SEQ ID No: 1661, SEQ ID No: 1663, SEQ ID No: 1665, SEQ ID No: 1667, SEQ ID No: 1669, SEQ ID No: 1671, SEQ ID No: 1673, SEQ ID No: 1675, SEQ ID No: 1677, SEQ ID No: 1679, SEQ ID No: 1681, SEQ ID No: 1683, SEQ ID No: 1685, SEQ ID No: 1687, SEQ ID No: 1689, SEQ ID No: 1691, SEQ ID No: 1693, SEQ ID No: 1695, SEQ ID No: 1697, SEQ ID No: 1699, SEQ ID No: 1701, SEQ ID No: 1703, SEQ ID No: 1705, SEQ ID No: 1707, SEQ ID No: 1709, SEQ ID No: 1711, SEQ ID No: 1713, SEQ ID No: 1715, SEQ ID No: 1717, SEQ ID No: 1719, SEQ ID No: 1721, SEQ ID No: 1723, SEQ ID No: 1725, SEQ ID No: 1727, SEQ ID No: 1729, SEQ ID No: 1731, SEQ ID No: 1733, SEQ ID No: 1735, SEQ ID No: 1737, SEQ ID No: 1739, SEQ ID No: 1741, SEQ ID No: 1743, SEQ ID No: 1745, SEQ ID No: 1747, SEQ ID No: 1749, SEQ ID No: 1751, SEQ ID No: 1753, SEQ ID No: 1755, SEQ ID No: 1757, SEQ ID No: 1759, SEQ ID No: 1761, SEQ ID No: 1763, SEQ ID No: 1765, SEQ ID No: 1767, SEQ ID No: 1769, SEQ ID No: 1771, SEQ ID No: 1773, SEQ ID No: 1775, SEQ ID No: 1777, SEQ ID No: 1779, SEQ ID No: 1781, SEQ ID No: 1783, SEQ ID No: 1785, SEQ ID No: 1787, SEQ ID No: 1789, SEQ ID No: 1791, SEQ ID No: 1793, SEQ ID No: 1795, SEQ ID No: 1797, SEQ ID No: 1799, SEQ ID No: 1801, SEQ ID No: 1803, SEQ ID No: 1805, SEQ ID No: 1807, SEQ ID No: 1809, SEQ ID No: 1811, SEQ ID No: 1813, SEQ ID No: 1815, SEQ ID No: 1817, SEQ ID No: 1819, SEQ ID No: 1821, SEQ ID No: 1823, SEQ ID No: 1825, SEQ ID No: 1827, SEQ ID No: 1829, SEQ ID No: 1831, SEQ ID No: 1833, SEQ ID No: 1835, SEQ ID No: 1837, SEQ ID No: 1839, SEQ ID No: 1841, SEQ ID No: 1843, SEQ ID No: 1845, SEQ ID No: 1847, SEQ ID No: 1849, SEQ ID No: 1851, SEQ ID No: 1853, SEQ ID No: 1855, SEQ ID No: 1857, SEQ ID No: 1859, SEQ ID No: 1861, SEQ ID No: 1863, SEQ ID No: 1865, SEQ ID No: 1867, SEQ ID No: 1869, SEQ ID No: 1871, SEQ ID No: 1873, SEQ ID No: 1875, SEQ ID No: 1877, SEQ ID No: 1879, SEQ ID No: 1881, SEQ ID No: 1883, SEQ ID No: 1885, SEQ ID No: 1887, SEQ ID No: 1889, SEQ ID No: 1891, SEQ ID No: 1893, SEQ ID No: 1895, SEQ ID No: 1897, SEQ ID No: 1899, SEQ ID No: 1901, SEQ ID No: 1903, SEQ ID No: 1905, SEQ ID No: 1907, SEQ ID No: 1909, SEQ ID No: 1911, SEQ ID No: 1913, SEQ ID No: 1915, SEQ ID No: 1917, SEQ ID No: 1919, SEQ ID No: 1921, SEQ ID No: 1923, SEQ ID No: 1925, SEQ ID No: 1927, SEQ ID No: 1929, SEQ ID No: 1931, SEQ ID No: 1933, SEQ ID No: 1935, SEQ ID No: 1937, SEQ ID No: 1939, SEQ ID No: 1941, SEQ ID No: 1943, SEQ ID No: 1945, SEQ ID No: 1947, SEQ ID No: 1949, SEQ ID No: 1951, SEQ ID No: 1953, SEQ ID No: 1955, SEQ ID No: 1957, SEQ ID No: 1959, SEQ ID No: 1961, SEQ ID No: 1963, SEQ ID No: 1965, SEQ ID No: 1967, SEQ ID No: 1969, SEQ ID No: 1971, SEQ ID No: 1973.
[023] In some embodiments, the present invention comprises nucleic acid sequences that are fully complementary to any of the nucleic acid sequences described above.
[024] In some embodiments, the present invention comprises an isolated protein comprising an amino acid sequence encoded by any of the nucleic acid molecules described above.
[025] In some embodiments, the present invention comprises an isolated fusion protein comprising an isolated protein of the present invention fused to a protein comprising an amino acid sequence that is heterologous to the isolated protein.
[026] In some embodiments, the present invention comprises a kit for degrading a plant biomass to comprising at least one isolated protein of the present invention.
[027] In some embodiments, the present invention comprises a bleach comprising at least one isolated protein of the present invention.
[028] In some embodiments, the present invention comprises a composition for the degradation of lignin comprising at least one isolated protein of the present invention.
[029] In some embodiments, the present invention comprises a recombinant nucleic acid molecule comprising an isolated nucleic acid molecule of the present invention, operatively linked to at least one expression control sequence. In some embodiments, the recombinant nucleic acid molecule comprises an expression vector. In some embodiments, the recombinant nucleic acid molecule comprises a targeting vector.
[030] In some embodiments, the present invention comprises an isolated host cell transfected with a nucleic acid molecule of the present invention. In some embodiments, the host cell is a fungus. In some embodiments, the host cell is a filamentous fungus. In some embodiments, the filamentous fungus is from a genus selected from the group consisting of: Chrysosporium, Thielavia, Talaromyces, Neurospora, Aureobasidium, Filibasidium, Piromyces, Corynascus, Cryptococcus, Acremonium, Tolypocladium, Scytalidium, Schizophyllum, Sporotrichum, Penicillium, Gibberella, Myceliophthora, Mucor, Aspergillus, Fusarium, Humicola, and Trichoderma, and anamorphs and teleomorphs thereof. In some embodiments, the host cell is a bacterium.
[031] In some embodiments, the present invention comprises an oligonucleotide consisting essentially of at least 12 consecutive nucleotides of a nucleic acid sequence selected from SEQ ID No: 1, SEQ ID No: 3, SEQ ID No: 5, SEQ ID No: 7, SEQ ID No: 9, SEQ ID No: 11, SEQ ID No: 13, SEQ ID No: 15, SEQ ID No: 17, SEQ ID No: 19, SEQ ID No: 21, SEQ ID No: 23, SEQ ID No: 25, SEQ ID No: 27, SEQ ID No: 29, SEQ ID No: 31, SEQ ID No: 33, SEQ ID No: 35, SEQ ID No: 37, SEQ ID No: 39, SEQ ID No: 41, SEQ ID No: 43, SEQ ID No: 45, SEQ ID No: 47, SEQ ID No: 49, SEQ ID No: 51, SEQ ID No: 53, SEQ ID No: 55, SEQ ID No: 56, SEQ ID No: 57, SEQ ID No: 59, SEQ ID No: 61, SEQ ID No: 63, SEQ ID No: 65, SEQ ID No: 67, SEQ ID No: 69, SEQ ID No: 71, SEQ ID No: 73, SEQ ID No: 75, SEQ ID No: 77, SEQ ID No: 79, SEQ ID No: 81, SEQ ID No: 83, SEQ ID No: 85, SEQ ID No: 87, SEQ ID No: 89, SEQ ID No: 91, SEQ ID No: 93, SEQ ID No: 95, SEQ ID No: 97, SEQ ID No: 99, SEQ ID No: 101, SEQ ID No: 103, SEQ ID No: 105, SEQ ID No: 107, SEQ ID No: 109, SEQ ID No: 111, SEQ ID No: 113, SEQ ID No: 115, SEQ ID No: 117, SEQ ID No: 119, SEQ ID No: 121, SEQ ID No: 123, SEQ ID No: 125, SEQ ID No: 127, SEQ ID No: 129, SEQ ID No: 131, SEQ ID No: 133, SEQ ID No: 135, SEQ ID No: 137, SEQ ID No: 139, SEQ ID No: 141, SEQ ID No: 143, SEQ ID No: 145, SEQ ID No: 147, SEQ ID No: 149, SEQ ID No: 151, SEQ ID No: 153, SEQ ID No: 155, SEQ ID No: 157, SEQ ID No: 159, SEQ ID No: 161, SEQ ID No: 163, SEQ ID No: 165, SEQ ID No: 167, SEQ ID No: 169, SEQ ID No: 171, SEQ ID No: 173, SEQ ID No: 175, SEQ ID No: 177, SEQ ID No: 179, SEQ ID No: 181, SEQ ID No: 183, SEQ ID No: 185, SEQ ID No: 187, SEQ ID No: 189, SEQ ID No: 191, SEQ ID No: 193, SEQ ID No: 195, SEQ ID No: 197, SEQ ID No: 199, SEQ ID No: 201, SEQ ID No: 203, SEQ ID No: 205, SEQ ID No: 207, SEQ ID No: 209, SEQ ID No: 211, SEQ ID No: 213, SEQ ID No: 215, SEQ ID No: 217, SEQ ID No: 219, SEQ ID No: 221, SEQ ID No: 223, SEQ ID No: 225, SEQ ID No: 227, SEQ ID No: 229, SEQ ID No: 231, SEQ ID No: 233, SEQ ID No: 235. SEQ ID No: 237, SEQ ID No: 239, SEQ ID No: 241, SEQ ID No: 243, SEQ ID No: 245, SEQ ID No: 247, SEQ ID No: 249, SEQ ID No: 251, SEQ ID No: 253, SEQ ID No: 255, SEQ ID No: 257, SEQ ID No: 259, SEQ ID No: 261, SEQ ID No: 263, SEQ ID No: 265, SEQ ID No: 267, SEQ ID No: 269, SEQ ID No: 271, SEQ ID No: 273, SEQ ID No: 275, SEQ ID No: 277, SEQ ID No: 279, SEQ ID No: 281, SEQ ID No: 283, SEQ ID No: 285, SEQ ID No: 287, SEQ ID No: 289, SEQ ID No: 291, SEQ ID No: 293, SEQ ID No: 295, SEQ ID No: 297, SEQ ID No: 299, SEQ ID No: 301, SEQ ID No: 303, SEQ ID No: 305, SEQ ID No: 307, SEQ ID No: 309, SEQ ID No: 311, SEQ ID No: 313, SEQ ID No: 315, SEQ ID No: 317, SEQ ID No: 319, SEQ ID No: 321, SEQ ID No: 323, SEQ ID No: 325, SEQ ID No: 327, SEQ ID No: 329, SEQ ID No: 331, SEQ ID No: 333, SEQ ID No: 335, SEQ ID No: 337, SEQ ID No: 339, SEQ ID No: 341, SEQ ID No: 343, SEQ ID No: 345, SEQ ID No: 347, SEQ ID No: 349, SEQ ID No: 351, SEQ ID No: 353, SEQ ID No: 355, SEQ ID No: 357, SEQ ID No: 359, SEQ ID No: 361, SEQ ID No: 363, SEQ ID No: 365, SEQ ID No: 367, SEQ ID No: 369, SEQ ID No: 371, SEQ ID No: 373, SEQ ID No: 375, SEQ ID No: 377, SEQ ID No: 379, SEQ ID No: 381, SEQ ID No: 383, SEQ ID No: 385, SEQ ID No: 387, SEQ ID No: 389, SEQ ID No: 391, SEQ ID No: 393, SEQ ID No: 395, SEQ ID No: 397, SEQ ID No: 399, SEQ ID No: 401, SEQ ID No: 403, SEQ ID No: 405, SEQ ID No: 407, SEQ ID No: 409, SEQ ID No: 411, SEQ ID No: 413, SEQ ID No: 415, SEQ ID No: 417, SEQ ID No: 419, SEQ ID No: 421, SEQ ID No: 423, SEQ ID No: 425, SEQ ID No: 427, SEQ ID No: 429, SEQ ID No: 431, SEQ ID No: 433, SEQ ID No: 435, SEQ ID No: 437, SEQ ID No: 439, SEQ ID No: 441, SEQ ID No: 443, SEQ ID No: 445, SEQ ID No: 447, SEQ ID No: 449, SEQ ID No: 451, SEQ ID No: 453, SEQ ID No: 455, SEQ ID No: 457, SEQ ID No: 459, SEQ ID No: 461, SEQ ID No: 463, SEQ ID No: 465, SEQ ID No: 467, SEQ ID No: 469, SEQ ID No: 471, SEQ ID No: 473, SEQ ID No: 475, SEQ ID No: 477, SEQ ID No: 479, SEQ ID No: 481, SEQ ID No: 483, SEQ ID No: 485, SEQ ID No: 487, SEQ ID No: 489, SEQ ID No: 491, SEQ ID No: 493, SEQ ID No: 495, SEQ ID No: 497, SEQ ID No: 499, SEQ ID No: 501, SEQ ID No: 503, SEQ ID No: 505, SEQ ID No: 507, SEQ ID No: 509, SEQ ID No: 511, SEQ ID No: 513, SEQ ID No: 515, SEQ ID No: 517, SEQ ID No: 519, SEQ ID No: 521, SEQ ID No: 523, SEQ ID No: 525, SEQ ID No: 527, SEQ ID No: 529, SEQ ID No: 531, SEQ ID No: 533, SEQ ID No: 535, SEQ ID No: 537, SEQ ID No: 539, SEQ ID No: 541, SEQ ID No: 543, SEQ ID No: 545, SEQ ID No: 547, SEQ ID No: 549, SEQ ID No: 551, SEQ ID No: 553, SEQ ID No: 555, SEQ ID No: 557, SEQ ID No: 559, SEQ ID No: 561, SEQ ID No: 563, SEQ ID No: 565, SEQ ID No: 567, SEQ ID No: 569, SEQ ID No: 571, SEQ ID No: 573, SEQ ID No: 575, SEQ ID No: 577, SEQ ID No: 579, SEQ ID No: 581, SEQ ID No: 583, SEQ ID No: 585, SEQ ID No: 587, SEQ ID No: 589, SEQ ID No: 591, SEQ ID No: 593, SEQ ID No: 595, SEQ ID No: 597, SEQ ID No: 599, SEQ ID No: 601, SEQ ID No: 603, SEQ ID No: 605, SEQ ID No: 607, SEQ ID No: 609, SEQ ID No: 611, SEQ ID No: 613, SEQ ID No: 615, SEQ ID No: 617, SEQ ID No: 619, SEQ ID No: 621, SEQ ID No: 623, SEQ ID No: 625, SEQ ID No: 627, SEQ ID No: 629, SEQ ID No: 631, SEQ ID No: 633, SEQ ID No: 635, SEQ ID No: 637, SEQ ID No: 639, SEQ ID No: 641, SEQ ID No: 643, SEQ ID No: 645, SEQ ID No: 647, SEQ ID No: 649, SEQ ID No: 651, SEQ ID No: 653, SEQ ID No: 655, SEQ ID No: 657, SEQ ID No: 659, SEQ ID No: 661, SEQ ID No: 663, SEQ ID No: 665, SEQ ID No: 667, SEQ ID No: 669, SEQ ID No: 671, SEQ ID No: 673, SEQ ID No: 675, SEQ ID No: 677, SEQ ID No: 679, SEQ ID No: 681, SEQ ID No: 683, SEQ ID No: 685, SEQ ID No: 687, SEQ ID No: 689, SEQ ID No: 691, SEQ ID No: 693, SEQ ID No: 695, SEQ ID No: 697, SEQ ID No: 699, SEQ ID No: 701, SEQ ID No: 703, SEQ ID No: 705, SEQ ID No: 707, SEQ ID No: 709, SEQ ID No: 711, SEQ ID No: 713, SEQ ID No: 715, SEQ ID No: 717, SEQ ID No: 719, SEQ ID No: 721, SEQ ID No: 723, SEQ ID No: 725, SEQ ID No: 727, SEQ ID No: 729, SEQ ID No: 731, SEQ ID No: 733, SEQ ID No: 735, SEQ ID No: 737, SEQ ID No: 739, SEQ ID No: 741, SEQ ID No: 743, SEQ ID No: 745, SEQ ID No: 747, SEQ ID No: 749, SEQ ID No: 751, SEQ ID No: 753, SEQ ID No: 755, SEQ ID No: 757, SEQ ID No: 759, SEQ ID No: 761, SEQ ID No: 763, SEQ ID No: 765, SEQ ID No: 767, SEQ ID No: 769, SEQ ID No: 771, SEQ ID No: 773, SEQ ID No: 775, SEQ ID No: 777, SEQ ID No: 779, SEQ ID No: 781, SEQ ID No: 783, SEQ ID No: 785, SEQ ID No: 787, SEQ ID No: 789, SEQ ID No: 791, SEQ ID No: 793, SEQ ID No: 795, SEQ ID No: 797, SEQ ID No: 799, SEQ ID No: 801, SEQ ID No: 803, SEQ ID No: 805, SEQ ID No: 807, SEQ ID No: 809, SEQ ID No: 811, SEQ ID No: 813, SEQ ID No: 815, SEQ ID No: 817, SEQ ID No: 819, SEQ ID No: 821, SEQ ID No: 823, SEQ ID No: 825, SEQ ID No: 827, SEQ ID No: 829, SEQ ID No: 831, SEQ ID No: 833, SEQ ID No: 835, SEQ ID No: 837, SEQ ID No: 839, SEQ ID No: 841, SEQ ID No: 843, SEQ ID No: 845, SEQ ID No: 847, SEQ ID No: 849, SEQ ID No: 851, SEQ ID No: 853, SEQ ID No: 855, SEQ ID No: 857, SEQ ID No: 859, SEQ ID No: 861, SEQ ID No: 863, SEQ ID No: 865, SEQ ID No: 867, SEQ ID No: 869, SEQ ID No: 871, SEQ ID No: 873, SEQ ID No: 875, SEQ ID No: 877, SEQ ID No: 879, SEQ ID No: 881, SEQ ID No: 883, SEQ ID No: 885, SEQ ID No: 887, SEQ ID No: 889, SEQ ID No: 891, SEQ ID No: 893, SEQ ID No: 895, SEQ ID No: 897, SEQ ID No: 899, SEQ ID No: 901, SEQ ID No: 903, SEQ ID No: 905, SEQ ID No: 907, SEQ ID No: 909, SEQ ID No: 911, SEQ ID No: 913, SEQ ID No: 915, SEQ ID No: 917, SEQ ID No: 919, SEQ ID No: 921, SEQ ID No: 923, SEQ ID No: 925, SEQ ID No: 927, SEQ ID No: 929, SEQ ID No: 931, SEQ ID No: 933, SEQ ID No: 935, SEQ ID No: 937, SEQ ID No: 939, SEQ ID No: 941, SEQ ID No: 943, SEQ ID No: 945, SEQ ID No: 947, SEQ ID No: 949, SEQ ID No: 951, SEQ ID No: 953, SEQ ID No: 955, SEQ ID No: 957, SEQ ID No: 959, SEQ ID No: 961, SEQ ID No: 963, SEQ ID No: 965, SEQ ID No: 967, SEQ ID No: 969, SEQ ID No: 971, SEQ ID No: 973, SEQ ID No: 975, SEQ ID No: 977, SEQ ID No: 979, SEQ ID No: 981, SEQ ID No: 983, SEQ ID No: 985, SEQ ID No: 987, SEQ ID No: 989, SEQ ID No: 991, SEQ ID No: 993, SEQ ID No: 995, SEQ ID No: 997, SEQ ID No: 999, SEQ ID No: 1001, SEQ ID No: 1003, SEQ ID No: 1005, SEQ ID No: 1007, SEQ ID No: 1009, SEQ ID No: 1011, SEQ ID No: 1013, SEQ ID No: 1015, SEQ ID No: 1017, SEQ ID No: 1019, SEQ ID No: 1021, SEQ ID No: 1023, SEQ ID No: 1025, SEQ ID No: 1027, SEQ ID No: 1029, SEQ ID No: 1031, SEQ ID No: 1033, SEQ ID No: 1035, SEQ ID No: 1037, SEQ ID No: 1039, SEQ ID No: 1041, SEQ ID No: 1043, SEQ ID No: 1045, SEQ ID No: 1047, SEQ ID No: 1049, SEQ ID No: 1051, SEQ ID No: 1053, SEQ ID No: 1055, SEQ ID No: 1057, SEQ ID No: 1059, SEQ ID No: 1061, SEQ ID No: 1063, SEQ ID No: 1065, SEQ ID No: 1067, SEQ ID No: 1069, SEQ ID No: 1071, SEQ ID No: 1073, SEQ ID No: 1075, SEQ ID No: 1077, SEQ ID No: 1079, SEQ ID No: 1081, SEQ ID No: 1083, SEQ ID No: 1085, SEQ ID No: 1087, SEQ ID No: 1089, SEQ ID No: 1091, SEQ ID No: 1093, SEQ ID No: 1095, SEQ ID No: 1097, SEQ ID No: 1099, SEQ ID No: 1101, SEQ ID No: 1103, SEQ ID No: 1105, SEQ ID No: 1107, SEQ ID No: 1109, SEQ ID No: 1111, SEQ ID No: 1113, SEQ ID No: 1115, SEQ ID No: 1117, SEQ ID No: 1119, SEQ ID No: 1121, SEQ ID No: 1123, SEQ ID No: 1125, SEQ ID No: 1127, SEQ ID No: 1129, SEQ ID No: 1131, SEQ ID No: 1133, SEQ ID No: 1135, SEQ ID No: 1137, SEQ ID No: 1139, SEQ ID No: 1141, SEQ ID No: 1143, SEQ ID No: 1145, SEQ ID No: 1147, SEQ ID No: 1149, SEQ ID No: 1151, SEQ ID No: 1153, SEQ ID No: 1155, SEQ ID No: 1157, SEQ ID No: 1159, SEQ ID No: 1161, SEQ ID No: 1163, SEQ ID No: 1165, SEQ ID No: 1167, SEQ ID No: 1169, SEQ ID No: 1171, SEQ ID No: 1173, SEQ ID No: 1175, SEQ ID No: 1177, SEQ ID No: 1179, SEQ ID No: 1181, SEQ ID No: 1183, SEQ ID No: 1185, SEQ ID No: 1187, SEQ ID No: 1189, SEQ ID No: 1191, SEQ ID No: 1193, SEQ ID No: 1195, SEQ ID No: 1197, SEQ ID No: 1199, SEQ ID No: 1201, SEQ ID No: 1203, SEQ ID No: 1205, SEQ ID No: 1207, SEQ ID No: 1209, SEQ ID No: 1211, SEQ ID No: 1213, SEQ ID No: 1215, SEQ ID No: 1217, SEQ ID No: 1219, SEQ ID No: 1221, SEQ ID No: 1223, SEQ ID No: 1225, SEQ ID No: 1227, SEQ ID No: 1229, SEQ ID No: 1231, SEQ ID No: 1233, SEQ ID No: 1235, SEQ ID No: 1237, SEQ ID No: 1239, SEQ ID No: 1241, SEQ ID No: 1243, SEQ ID No: 1245, SEQ ID No: 1247, SEQ ID No: 1249, SEQ ID No: 1251, SEQ ID No: 1253, SEQ ID No: 1255, SEQ ID No: 1257, SEQ ID No: 1259, SEQ ID No: 1261, SEQ ID No: 1263, SEQ ID No: 1265, SEQ ID No: 1267, SEQ ID No: 1269, SEQ ID No: 1271, SEQ ID No: 1273, SEQ ID No: 1275, SEQ ID No: 1277, SEQ ID No: 1279, SEQ ID No: 1281, SEQ ID No: 1283, SEQ ID No: 1285, SEQ ID No: 1287, SEQ ID No: 1289, SEQ ID No: 1291, SEQ ID No: 1293, SEQ ID No: 1295, SEQ ID No: 1297, SEQ ID No: 1299, SEQ ID No: 1301, SEQ ID No: 1303, SEQ ID No: 1305, SEQ ID No: 1307, SEQ ID No: 1309, SEQ ID No: 1311, SEQ ID No: 1313, SEQ ID No: 1315, SEQ ID No: 1317, SEQ ID No: 1319, SEQ ID No: 1321, SEQ ID No: 1323, SEQ ID No: 1325, SEQ ID No: 1327, SEQ ID No: 1329, SEQ ID No: 1331, SEQ ID No: 1333, SEQ ID No: 1335, SEQ ID No: 1337, SEQ ID No: 1339, SEQ ID No: 1341, SEQ ID No: 1343, SEQ ID No: 1345, SEQ ID No: 1347, SEQ ID No: 1349, SEQ ID No: 1351, SEQ ID No: 1353, SEQ ID No: 1355, SEQ ID No: 1357, SEQ ID No: 1359, SEQ ID No: 1361, SEQ ID No: 1363, SEQ ID No: 1365, SEQ ID No: 1367, SEQ ID No: 1369, SEQ ID No: 1371, SEQ ID No: 1373, SEQ ID No: 1375, SEQ ID No: 1377, SEQ ID No: 1379, SEQ ID No: 1381, SEQ ID No: 1383, SEQ ID No: 1385, SEQ ID No: 1387, SEQ ID No: 1389, SEQ ID No: 1391, SEQ ID No: 1393, SEQ ID No: 1395, SEQ ID No: 1397, SEQ ID No: 1399, SEQ ID No: 1401, SEQ ID No: 1403, SEQ ID No: 1405, SEQ ID No: 1407, SEQ ID No: 1409, SEQ ID No: 1411, SEQ ID No: 1413, SEQ ID No: 1415, SEQ ID No: 1417, SEQ ID No: 1419, SEQ ID No: 1421, SEQ ID No: 1423, SEQ ID No: 1425, SEQ ID No: 1427, SEQ ID No: 1429, SEQ ID No: 1431, SEQ ID No: 1433, SEQ ID No: 1435, SEQ ID No: 1437, SEQ ID No: 1439, SEQ ID No: 1441, SEQ ID No: 1443, SEQ ID No: 1445, SEQ ID No: 1447, SEQ ID No: 1449, SEQ ID No: 1451, SEQ ID No: 1453, SEQ ID No: 1455, SEQ ID No: 1457, SEQ ID No: 1459, SEQ ID No: 1461, SEQ ID No: 1463, SEQ ID No: 1465, SEQ ID No: 1467, SEQ ID No: 1469, SEQ ID No: 1471, SEQ ID No: 1473, SEQ ID No: 1475, SEQ ID No: 1477, SEQ ID No: 1479, SEQ ID No: 1481, SEQ ID No: 1483, SEQ ID No: 1485, SEQ ID No: 1487, SEQ ID No: 1489, SEQ ID No: 1491, SEQ ID No: 1493, SEQ ID No: 1495, SEQ ID No: 1497, SEQ ID No: 1499, SEQ ID No: 1501, SEQ ID No: 1503, SEQ ID No: 1505, SEQ ID No: 1507, SEQ ID No: 1509, SEQ ID No: 1511, SEQ ID No: 1513, SEQ ID No: 1515, SEQ ID No: 1517, SEQ ID No: 1519, SEQ ID No: 1521, SEQ ID No: 1523, SEQ ID No: 1525, SEQ ID No: 1527, SEQ ID No: 1529, SEQ ID No: 1531, SEQ ID No: 1533, SEQ ID No: 1535, SEQ ID No: 1537, SEQ ID No: 1539, SEQ ID No: 1541, SEQ ID No: 1543, SEQ ID No: 1545, SEQ ID No: 1547, SEQ ID No: 1549, SEQ ID No: 1551, SEQ ID No: 1553, SEQ ID No: 1555, SEQ ID No: 1557, SEQ ID No: 1559, SEQ ID No: 1561, SEQ ID No: 1563, SEQ ID No: 1565, SEQ ID No: 1567, SEQ ID No: 1569, SEQ ID No: 1571, SEQ ID No: 1573, SEQ ID No: 1575, SEQ ID No: 1577, SEQ ID No: 1579, SEQ ID No: 1581, SEQ ID No: 1583, SEQ ID No: 1585, SEQ ID No: 1587, SEQ ID No: 1589, SEQ ID No: 1591, SEQ ID No: 1593, SEQ ID No: 1595, SEQ ID No: 1597, SEQ ID No: 1599, SEQ ID No: 1601, SEQ ID No: 1603, SEQ ID No: 1605, SEQ ID No: 1607, SEQ ID No: 1609, SEQ ID No: 1611, SEQ ID No: 1613, SEQ ID No: 1615, SEQ ID No: 1617, SEQ ID No: 1619, SEQ ID No: 1621, SEQ ID No: 1623, SEQ ID No: 1625, SEQ ID No: 1627, SEQ ID No: 1629, SEQ ID No: 1631, SEQ ID No: 1633, SEQ ID No: 1635, SEQ ID No: 1637, SEQ ID No: 1639, SEQ ID No: 1641, SEQ ID No: 1643, SEQ ID No: 1645, SEQ ID No: 1647, SEQ ID No: 1649, SEQ ID No: 1651, SEQ ID No: 1653, SEQ ID No: 1655, SEQ ID No: 1657, SEQ ID No: 1659, SEQ ID No: 1661, SEQ ID No: 1663, SEQ ID No: 1665, SEQ ID No: 1667, SEQ ID No: 1669, SEQ ID No: 1671, SEQ ID No: 1673, SEQ ID No: 1675, SEQ ID No: 1677, SEQ ID No: 1679, SEQ ID No: 1681, SEQ ID No: 1683, SEQ ID No: 1685, SEQ ID No: 1687, SEQ ID No: 1689, SEQ ID No: 1691, SEQ ID No: 1693, SEQ ID No: 1695, SEQ ID No: 1697, SEQ ID No: 1699, SEQ ID No: 1701, SEQ ID No: 1703, SEQ ID No: 1705, SEQ ID No: 1707, SEQ ID No: 1709, SEQ ID No: 1711, SEQ ID No: 1713, SEQ ID No: 1715, SEQ ID No: 1717, SEQ ID No: 1719, SEQ ID No: 1721, SEQ ID No: 1723, SEQ ID No: 1725, SEQ ID No: 1727, SEQ ID No: 1729, SEQ ID No: 1731, SEQ ID No: 1733, SEQ ID No: 1735, SEQ ID No: 1737, SEQ ID No: 1739, SEQ ID No: 1741, SEQ ID No: 1743, SEQ ID No: 1745, SEQ ID No: 1747, SEQ ID No: 1749, SEQ ID No: 1751, SEQ ID No: 1753, SEQ ID No: 1755, SEQ ID No: 1757, SEQ ID No: 1759, SEQ ID No: 1761, SEQ ID No: 1763, SEQ ID No: 1765, SEQ ID No: 1767, SEQ ID No: 1769, SEQ ID No: 1771, SEQ ID No: 1773, SEQ ID No: 1775, SEQ ID No: 1777, SEQ ID No: 1779, SEQ ID No: 1781, SEQ ID No: 1783, SEQ ID No: 1785, SEQ ID No: 1787, SEQ ID No: 1789, SEQ ID No: 1791, SEQ ID No: 1793, SEQ ID No: 1795, SEQ ID No: 1797, SEQ ID No: 1799, SEQ ID No: 1801, SEQ ID No: 1803, SEQ ID No: 1805, SEQ ID No: 1807, SEQ ID No: 1809, SEQ ID No: 1811, SEQ ID No: 1813, SEQ ID No: 1815, SEQ ID No: 1817, SEQ ID No: 1819, SEQ ID No: 1821, SEQ ID No: 1823, SEQ ID No: 1825, SEQ ID No: 1827, SEQ ID No: 1829, SEQ ID No: 1831, SEQ ID No: 1833, SEQ ID No: 1835, SEQ ID No: 1837, SEQ ID No: 1839, SEQ ID No: 1841, SEQ ID No: 1843, SEQ ID No: 1845, SEQ ID No: 1847, SEQ ID No: 1849, SEQ ID No: 1851, SEQ ID No: 1853, SEQ ID No: 1855, SEQ ID No: 1857, SEQ ID No: 1859, SEQ ID No: 1861, SEQ ID No: 1863, SEQ ID No: 1865, SEQ ID No: 1867, SEQ ID No: 1869, SEQ ID No: 1871, SEQ ID No: 1873, SEQ ID No: 1875, SEQ ID No: 1877, SEQ ID No: 1879, SEQ ID No: 1881, SEQ ID No: 1883, SEQ ID No: 1885, SEQ ID No: 1887, SEQ ID No: 1889, SEQ ID No: 1891, SEQ ID No: 1893, SEQ ID No: 1895, SEQ ID No: 1897, SEQ ID No: 1899, SEQ ID No: 1901, SEQ ID No: 1903, SEQ ID No: 1905, SEQ ID No: 1907, SEQ ID No: 1909, SEQ ID No: 1911, SEQ ID No: 1913, SEQ ID No: 1915, SEQ ID No: 1917, SEQ ID No: 1919, SEQ ID No: 1921, SEQ ID No: 1923, SEQ ID No: 1925, SEQ ID No: 1927, SEQ ID No: 1929, SEQ ID No: 1931, SEQ ID No: 1933, SEQ ID No: 1935, SEQ ID No: 1937, SEQ ID No: 1939, SEQ ID No: 1941, SEQ ID No: 1943, SEQ ID No: 1945, SEQ ID No: 1947, SEQ ID No: 1949, SEQ ID No: 1951, SEQ ID No: 1953, SEQ ID No: 1955, SEQ ID No: 1957, SEQ ID No: 1959, SEQ ID No: 1961, SEQ ID No: 1963, SEQ ID No: 1965, SEQ ID No: 1967, SEQ ID No: 1969, SEQ ID No: 1971, SEQ ID No: 1973 or the complement thereof.
[032] In some embodiments, the present invention comprises a kit comprising at least one oligonucleotide of the present invention.
[033] In some embodiments, the present invention comprises methods for producing a protein of the present invention, comprising culturing a cell that has been transfected with a nucleic acid molecule comprising a nucleic acid sequence encoding the protein, and expressing the protein with the transfected cell. In some embodiments, the present invention further comprises recovering the protein from the cell or from a culture comprising the cell.
[034] In some embodiments, the present invention comprises a genetically modified organism comprising components suitable for degrading lignin, wherein the organism has been genetically modified to express at least one protein of the present invention.
[035] In some embodiments, the genetically modified organism is a plant, alga, fungus or bacterium. In some embodiments, the fungus is yeast, mushroom or filamentous fungus. In some embodiments, the filamentous fungus is from a genus selected from the group consisting of: Chrysosporium, Thielavia, Neurospora, Aureobasidium, Filibasidium, Piromyces, Corynascus, Cryptococcus, Acremonium, Tolypocladium, Scytalidium, Schizophyllum, Sporotrichum, Penicillium, Talaromyces, Gibberella, Myceliophthora, Mucor, Aspergillus, Fusarium, Humicola, and Trichoderma. In some embodiments, the filamentous fungus is selected from the group consisting of: Trichoderma reesei, Trichoderma harzanium, Myceliophthora thermophila, Aspergillus niger, Aspergillus oryzae, Aspergillus japonicus, Aspergillus niger Penicillium canescens, Penicillium solitum, Penicillium funiculosum, Talaromyces emersonii, Talaromyces flavus, Talaromyces emersonii and Myceliophthora thermophila.
[036] In some embodiments, the genetically modified organism has been genetically modified to express at least one additional enzyme. In some embodiments, the additional enzyme is an enzyme selected from the group consisting of: cellulase, glucosidase, xylanase, xylosidase, ligninase, glucuronidase, arabinofuranosidase, arabinase, arabinogalactanase, esterase, lipase, pectinase, glucomannanase, amylase, laminarinase, xyloglucanase, galactanase, galactosidase, glucoamylase, pectate and pectin lyase, chitosanases, exo-P-D-glucosaminidase, and cellobiose dehydrogenase.
[037] In some embodiments, the genetically modified organism is a plant.
[038] In some embodiments, the present invention comprises a recombinant enzyme isolated from a genetically modified microorganism of the present invention. In some embodiments the recombinant enzyme has been subjected to a purification step.
[039] In some embodiments, the present invention comprises a crude fermentation product produced by culturing the cells from the genetically modified organism of the present invention, wherein the crude fermentation product contains at least one protein of the present invention.
[040] In some embodiments, the present invention comprises a multi-enzyme composition comprising enzymes produced by a genetically modified organism of the present invention , and recovered therefrom.
[041] In some embodiments, the present invention comprises a multi-enzyme composition comprising at least one protein of the present inventions, and at least one additional protein for degrading a biomass material or a fragment thereof that has biological activity.
[042] In some embodiments, the present invention comprises a multi-enzyme composition comprising at least one protein selected from SEQ ID No: 1892, SEQ ID No: 1894, SEQ ID No: 1896, SEQ ID No: 1898, SEQ ID No: 1900, SEQ ID No: 1902, SEQ ID No: 1904, SEQ ID No: 1906, SEQ ID No: 1908, SEQ ID No: 1910, SEQ ID No: 1912, SEQ ID No: 1914, SEQ ID No: 1916, SEQ ID No: 1918, SEQ ID No: 1920, SEQ ID No: 1922, SEQ ID No: 1924, SEQ ID No: 1926, SEQ ID No: 1928, SEQ ID No: 1930, SEQ ID No: 1932, SEQ ID No: 1934, SEQ ID No: 1936, SEQ ID No: 1938, SEQ ID No: 1940, SEQ ID No: 1942, SEQ ID No: 1944, SEQ ID No: 1946, SEQ ID No: 1948, SEQ ID No: 1950, SEQ ID No: 1952, SEQ ID No: 1954, SEQ ID No: 1956, SEQ ID No: 1958, SEQ ID No: 1960, SEQ ID No: 1962, SEQ ID No: 1964, SEQ ID No: 1966, SEQ ID No: 1968, SEQ ID No: 1970, SEQ ID No: 1972, or SEQ ID No: 1974, at least one protein selected from SEQ ID NO: 234, SEQ ID NO: 1000, SEQ ID NO: 1774, SEQ ID NO: 1884 and SEQ ID NO: 1890-, and at least one additional protein for degrading a biomass material or a fragment thereof that has biological activity.
[043] In some embodiments, the present invention comprises a multi-enzyme composition comprising at least one protein selected from SEQ ID No: 1892, SEQ ID No: 1894, SEQ ID No: 1896, SEQ ID No: 1898, SEQ ID No: 1900, SEQ ID No: 1902, SEQ ID No: 1904, SEQ ID No: 1906, SEQ ID No: 1908, SEQ ID No: 1910, SEQ ID No: 1912, SEQ ID No: 1914, SEQ ID No: 1916, SEQ ID No: 1918, SEQ ID No: 1920, SEQ ID No: 1922, SEQ ID No: 1924, SEQ ID No: 1926, SEQ ID No: 1928, SEQ ID No: 1930, SEQ ID No: 1932, SEQ ID No: 1934, SEQ ID No: 1936, SEQ ID No: 1938, SEQ ID No: 1940, SEQ ID No: 1942, SEQ ID No: 1944, SEQ ID No: 1946, SEQ ID No: 1948, SEQ ID No: 1950, SEQ ID No: 1952, SEQ ID No: 1954, SEQ ID No: 1956, SEQ ID No: 1958, SEQ ID No: 1960, SEQ ID No: 1962, SEQ ID No: 1964, SEQ ID No: 1966, SEQ ID No: 1968, SEQ ID No: 1970, SEQ ID No: 1972, or SEQ ID No: 1974., and at least one additional protein for degrading a biomass material or a fragment thereof that has biological activity.
[044] In some embodiments, the present invention comprises a multi-enzyme composition comprising at least one protein selected from SEQ ID NO: 234, SEQ ID NO: 786, SEQ ID NO: 828, SEQ ID NO: 836, SEQ ID NO: 1000, SEQ ID NO: 1774, SEQ ID NO: 1884, SEQ ID NO: 1886, SEQ ID NO: 1888 and SEQ ID NO: 1990, and at least one additional protein for degrading a biomass material or a fragment thereof that has biological activity.
[045] DETAILED DESCRIPTION OF THE INVENTION
[046] The present invention relates generally to proteins that play a role in reduction- oxidation reactions. In particular, the present invention relates to enzymes isolated from a filamentous fungal strain denoted herein as CI (Accession No. VKM F- 3500-D), nucleic acids encoding the enzymes, and methods of producing and using the enzymes. The invention also provides compositions that include at least one of the enzymes described herein for uses including, but not limited to, the degradation/modification of lignin or (hemi-) cellulose. The invention stems, in part, from the discovery of a variety of novel oxidoreductases produced by the CI fungus that exhibit high activity toward plant biomass.
[047] The present invention also provides methods and compositions for aiding in the conversion of plant biomass to fermentable sugars that can, in turn, be converted to useful products. Such products may include, without limitation, metabolites, and bio fuels. The methods include methods for degrading lignin and lignocellulosic material using enzyme mixtures to liberate sugars. The compositions of the invention include enzyme combinations that break down lignin and ligno cellulose.
[048] As used herein the terms "lignin" or "lignen" refers to complex polymers, the chief noncarbohydrate constituent of wood, that binds to cellulose fibers and hardens and strengthens the cell walls of plants. Lignin is an integral part of the secondary cell walls of many plants and some algae. Lignin acts to hold together cellulose and hemicelluose, which are important ingredients in making ethanol.
[049] As used herein the terms "biomass" or "lignocellulosic material" includes materials containing cellulose and/or hemicellulose. Generally, these materials also contain pectin, lignin, protein, carbohydrates (such as starch and sugar) and ash. Ligno cellulose is generally found, for example, in the stems, leaves, hulls, husks, and cobs of plants or leaves, branches, and wood of trees.
[050] The process of converting less or more complex carbohydrates (such as starch, cellulose or hemicellulose) into fermentable sugars is also referred to herein as "saccharification. "
[051] Fermentable sugars, as used herein, refers to simple sugars, such as glucose, xylose, arabinose, galactose, mannose, rhamnose, sucrose and fructose.
[052] Biomass can include virgin biomass and/or non-virgin biomass such as agricultural biomass, commercial organics, construction and demolition debris, municipal solid waste, waste paper and yard waste. Common forms of biomass include trees, shrubs and grasses, wheat, wheat straw, sugar cane bagasse, sugar beet, soybean, corn, corn husks, corn kernel including fiber from kernels, products and byproducts from milling of grains such as corn, tobacco, wheat and barley (including wet milling and dry milling) as well as municipal solid waste, waste paper and yard waste. The biomass can also be, but is not limited to, herbaceous material, agricultural residues, forestry residues, municipal solid wastes, waste paper, and pulp and paper mill residues. "Agricultural biomass" includes branches, bushes, canes, corn and corn husks, energy crops, algae, fruits, flowers, grains, grasses, herbaceous crops, leaves, bark, needles, logs, roots, saplings, short rotation woody crops, shrubs, switch grasses, trees, vegetables, fruit peels, vines, sugar beet pulp, wheat midlings, oat hulls, peat moss, mushroom compost and hard and soft woods (not including woods with deleterious materials). In addition, agricultural biomass includes organic waste materials generated from agricultural processes including farming and forestry activities, specifically including forestry wood waste. Agricultural biomass may be any of the aforestated singularly or in any combination or mixture thereof.
[053] Energy crops are fast-growing crops that are grown for the specific purpose of producing energy, including without limitation, biofuels, from all or part of the plant. Energy crops can include crops that are grown (or are designed to grow) for their increased cellulose, xylose and sugar contents. Examples of such plants include, without limitation, switchgrass, willow and poplar. Energy crops may also include algae, for example, designer algae that are genetically engineered for enhanced production of hydrogen, alcohols, and oils, which can be further processed into diesel and jet fuels, as well as other bio-based products.
[054] Biomass high in starch, sugar, or protein such as corn, grains, fruits and vegetables are usually consumed as food. Conversely, biomass high in cellulose, hemicellulose and lignin are not readily digestible and are primarily utilized for wood and paper products, animal feed, fuel, or are typically disposed. Generally, the substrate is of high ligno cellulose content, including distillers' dried grains corn stover, corn cobs, rice straw, wheat straw, hay, sugarcane bagasse, sugar cane pulp, citrus peels and other agricultural biomass, switchgrass, forestry wastes, poplar wood chips, pine wood chips, sawdust, yard waste, and the like, including any combination thereof.
[055] Due in part to the many components that comprise biomass and lignocellulosic materials, enzymes or a mixture of enzymes capable of degrading xylan, lignin, protein, and carbohydrates are needed to achieve saccharification. The present invention includes enzymes or compositions thereof with, for example, oxidoreductases, cellobiohydrolase, endoglucanase, xylanase, β-glucosidase, and hemicellulase activities.
[056] Fermentable sugars can be converted to useful value-added fermentation products, non-limiting examples of which include amino acids, vitamins, pharmaceuticals, animal feed supplements, specialty chemicals, chemical feedstocks, plastics, solvents, fuels, or other organic polymers, lactic acid, and ethanol, including fuel ethanol. Specific value-added products that may be produced by the methods of the invention include, but not limited to, biofuels (including ethanol and butanol); lactic acid; plastics; specialty chemicals; organic acids, including citric acid, succinic acid and maleic acid; solvents; animal feed supplements; pharmaceuticals; vitamins; amino acids, such as lysine, methionine, tryptophan, threonine, and aspartic acid; industrial enzymes, such as proteases, cellulases, amylases, glucanases, xylanases, arabinanases, lactases, lipases, esterases, lyases, oxidoreductases, transferases ; and chemical feedstocks.
[057] The enzymes of the present invention may be used alone, or in combination with other enzymes, chemicals or biological materials. The enzymes of the present invention may be used for in vitro applications in which the enzymes or mixtures thereof are added to or mixed with the appropriate substrates to catalyze the desired reactions. Additionally, the enzymes of the present invention may be used for in vivo applications in which nucleic acid molecules encoding the enzymes are introduced into cells and are expressed therein to produce the enzymes and catalyze the desired reactions within the cells. For example, in some embodiments, enzymes capable of promoting cell wall degradation may be added to algal cells suspended in solutions to degrade the algal cell walls and release their content, whereas in some embodiments, nucleic acid molecules encoding such enzymes may be introduced into the algal cells to express the enzymes therein, so that these enzymes can degrade the algal cell walls from within. Some embodiments may combine the in vitro applications with the in vivo applications. In some embodiments, the enzymes used for in vitro applications may be different from the enzymes used for in vivo applications.
[058] In one aspect, the present invention includes proteins isolated from, or derived from the knowledge of enzymes from, a fungus such as Myceliophthora thermophila or a mutant or other derivative thereof, and more particularly, from the fungal strain denoted herein as CI (Accession No. VKM F-3500-D). M. thermophila has previously appeared in patent applications and in the literature as Myceliophthora thermophila or Sporotrichum thermophile. Preferably, the proteins of the invention possess enzymatic activity. As described in U.S. Patent No. 6,015,707 or U.S. Patent No. 6,573,086 a strain called CI (Accession No. VKM F-3500-D), was isolated from samples of forest alkaline soil from Sola Lake, Far East of the Russian Federation. This strain was deposited at the All-Russian Collection of Microorganisms of Russian Academy of Sciences (VKM), Bakhurhina St. 8, Moscow, Russia, 113184, under the terms of the Budapest Treaty on the International Regulation of the Deposit of Microorganisms for the Purposes of Patent Procedure on August 29, 1996, as Myceliophthora thermophila Garg 27K, VKM-F 3500 D. Various mutant strains of M. thermophila (C. lucknowense) CI have been produced and these strains have also been deposited at the All-Russian Collection of Microorganisms of Russian Academy of Sciences (VKM), Bakhurhina St. 8, Moscow, Russia, 113184, under the terms of the Budapest Treaty on the International Regulation of the Deposit of Microorganisms for the Purposes of Patent Procedure on September 2, 1998 or at the Centraal Bureau voor Schimmelcultures (CBS), Uppsalalaan 8, 3584 CT Utrecht, The Netherlands for the purposes of Patent Procedure on December 5, 2007. For example, Strain CI was mutagenised by subjecting it to ultraviolet light to generate strain UV13-6 (Accession No. VKM F-3632 D). This strain was subsequently further mutated with N-methyl-N- nitro-N-nitrosoguanidine to generate strain NG7C-19 (Accession No. VKM F-3633 D). This latter strain in turn was subjected to mutation by ultraviolet light, resulting in strain UV18-25 (Accession No. VKM F-3631 D). This strain in turn was again subjected to mutation by ultraviolet light, resulting in strain W1L (Accession No. CBS 122189), which was subsequently subjected to mutation by ultraviolet light, resulting in strain W1L#100L (Accession No. CBS122190). Strain CI was initially classified as a Myceliophthora thermophila based on morphological and growth characteristics of the microorganism, as discussed in detail in U.S. Patent No. 6,015,707, U.S. Patent No. 6,573,086 and patent PCT/NL2010/000045. The CI strain was subsequently reclassified as M. thermophila based on genetic tests.
In certain embodiments of the present invention, a protein of the invention comprises, consists essentially of, or consists of an amino acid sequence selected from SEQ ID NO: 2, SEQ ID No: 4, SEQ ID No: 6, SEQ ID No: 8, SEQ ID No: 10, SEQ ID No: 12, SEQ ID No: 14, SEQ ID No: 16, SEQ ID No: 18, SEQ ID No: 20, SEQ ID No: 22, SEQ ID No: 24, SEQ ID No: 26, SEQ ID No: 28, SEQ ID No: 30, SEQ ID No: 32, SEQ ID No: 34, SEQ ID No: 36, SEQ ID No: 38, SEQ ID No: 40, SEQ ID No: 42, SEQ ID No: 44, SEQ ID No: 46, SEQ ID No: 48, SEQ ID No: 50, SEQ ID No: 52, SEQ ID No: 54, SEQ ID No: 56, SEQ ID No: 58, SEQ ID No: 60, SEQ ID No: 62, SEQ ID No: 64, SEQ ID No: 66, SEQ ID No: 68, SEQ ID No: 70, SEQ ID No: 72, SEQ ID No: 74, SEQ ID No: 76, SEQ ID No: 78, SEQ ID No: 80, SEQ ID No: 82, SEQ ID No: 84, SEQ ID No: 86, SEQ ID No: 88, SEQ ID No: 90, SEQ ID No: 92, SEQ ID No: 94, SEQ ID No: 96, SEQ ID No: 98, SEQ ID No: 100, SEQ ID No: 102, SEQ ID No: 104, SEQ ID No: 106, SEQ ID No: 108, SEQ ID No: 110, SEQ ID No: 112, SEQ ID No: 114, SEQ ID No: 116, SEQ ID No: 118, SEQ ID No: 120, SEQ ID No: 122, SEQ ID No: 124, SEQ ID No: 126, SEQ ID No: 128, SEQ ID No: 130, SEQ ID No: 132, SEQ ID No: 134, SEQ ID No: 136, SEQ ID No: 138, SEQ ID No: 140, SEQ ID No: 142, SEQ ID No: 144, SEQ ID No: 146, SEQ ID No: 148, SEQ ID No: 150, SEQ ID No: 152, SEQ ID No: 154, SEQ ID No: 156, SEQ ID No: 158, SEQ ID No: 160, SEQ ID No: 162, SEQ ID No: 164, SEQ ID No: 166, SEQ ID No: 168, SEQ ID No: 170, SEQ ID No: 172, SEQ ID No: 174, SEQ ID No: 176, SEQ ID No: 178, SEQ ID No: 180, SEQ ID No: 182, SEQ ID No: 184, SEQ ID No: 186, SEQ ID No: 188, SEQ ID No: 190, SEQ ID No: 192, SEQ ID No: 194, SEQ ID No: 196, SEQ ID No: 198, SEQ ID No: 200, SEQ ID No: 202, SEQ ID No: 204, SEQ ID No: 206, SEQ ID No: 208, SEQ ID No: 210, SEQ ID No: 212, SEQ ID No: 214, SEQ ID No: 216, SEQ ID No: 218, SEQ ID No: 220, SEQ ID No: 222, SEQ ID No: 224, SEQ ID No: 226, SEQ ID No: 228, SEQ ID No: 230, SEQ ID No: 232, SEQ ID No: 234, SEQ ID No: 236, SEQ ID No: 238, SEQ ID No: 240, SEQ ID No: 242, SEQ ID No: 244, SEQ ID No: 246, SEQ ID No: 248, SEQ ID No: 250, SEQ ID No: 252, SEQ ID No: 254, SEQ ID No: 256, SEQ ID No: 258, SEQ ID No: 260, SEQ ID No: 262, SEQ ID No: 264, SEQ ID No: 266, SEQ ID No: 268, SEQ ID No: 270, SEQ ID No: 272, SEQ ID No: 274, SEQ ID No: 276, SEQ ID No: 278, SEQ ID No: 280, SEQ ID No: 282, SEQ ID No: 284, SEQ ID No: 286, SEQ ID No: 288, SEQ ID No: 290, SEQ ID No: 292, SEQ ID No: 294, SEQ ID No: 296, SEQ ID No: 298, SEQ ID No: 300, SEQ ID No: 302, SEQ ID No: 304, SEQ ID No: 306, SEQ ID No: 308, SEQ ID No: 310, SEQ ID No: 312, SEQ ID No: 314, SEQ ID No: 316, SEQ ID No: 318, SEQ ID No: 320, SEQ ID No: 322, SEQ ID No: 324, SEQ ID No: 326, SEQ ID No: 328, SEQ ID No: 330, SEQ ID No: 332, SEQ ID No: 334, SEQ ID No: 336, SEQ ID No: 338, SEQ ID No: 340, SEQ ID No: 342, SEQ ID No: 344, SEQ ID No: 346, SEQ ID No: 348, SEQ ID No: 350, SEQ ID No: 352, SEQ ID No: 354, SEQ ID No: 356, SEQ ID No: 358, SEQ ID No: 360, SEQ ID No: 362, SEQ ID No: 364, SEQ ID No: 366, SEQ ID No: 368, SEQ ID No: 370, SEQ ID No: 372, SEQ ID No: 374, SEQ ID No: 376, SEQ ID No: 378, SEQ ID No: 380, SEQ ID No: 382, SEQ ID No: 384, SEQ ID No: 386, SEQ ID No: 388, SEQ ID No: 390, SEQ ID No: 392, SEQ ID No: 394, SEQ ID No: 396, SEQ ID No: 398, SEQ ID No: 400, SEQ ID No: 402, SEQ ID No: 404, SEQ ID No: 406, SEQ ID No: 408, SEQ ID No: 410, SEQ ID No: 412, SEQ ID No: 414, SEQ ID No: 416, SEQ ID No: 418, SEQ ID No: 420, SEQ ID No: 422, SEQ ID No: 424, SEQ ID No: 426, SEQ ID No: 428, SEQ ID No: 430, SEQ ID No: 432, SEQ ID No: 434, SEQ ID No: 436, SEQ ID No: 438, SEQ ID No: 440, SEQ ID No: 442, SEQ ID No: 444, SEQ ID No: 446, SEQ ID No: 448, SEQ ID No: 450, SEQ ID No: 452, SEQ ID No: 454, SEQ ID No: 456, SEQ ID No: 458, SEQ ID No: 460, SEQ ID No: 462, SEQ ID No: 464, SEQ ID No: 466, SEQ ID No: 468, SEQ ID No: 470, SEQ ID No: 472, SEQ ID No: 474, SEQ ID No: 476, SEQ ID No: 478, SEQ ID No: 480, SEQ ID No: 482, SEQ ID No: 484, SEQ ID No: 486, SEQ ID No: 488, SEQ ID No: 490, SEQ ID No: 492, SEQ ID No: 494, SEQ ID No: 496, SEQ ID No: 498, SEQ ID No: 500, SEQ ID No: 502, SEQ ID No: 504, SEQ ID No: 506, SEQ ID No: 508, SEQ ID No: 510, SEQ ID No: 512, SEQ ID No: 514, SEQ ID No: 516, SEQ ID No: 518, SEQ ID No: 520, SEQ ID No: 522, SEQ ID No: 524, SEQ ID No: 526, SEQ ID No: 528, SEQ ID No: 530, SEQ ID No: 532, SEQ ID No: 534, SEQ ID No: 536, SEQ ID No: 538, SEQ ID No: 540, SEQ ID No: 542, SEQ ID No: 544, SEQ ID No: 546, SEQ ID No: 548, SEQ ID No: 550, SEQ ID No: 552, SEQ ID No: 554, SEQ ID No: 556, SEQ ID No: 558, SEQ ID No: 560, SEQ ID No: 562, SEQ ID No: 564, SEQ ID No: 566, SEQ ID No: 568, SEQ ID No: 570, SEQ ID No: 572, SEQ ID No: 574, SEQ ID No: 576, SEQ ID No: 578, SEQ ID No: 580, SEQ ID No: 582, SEQ ID No: 584, SEQ ID No: 586, SEQ ID No: 588, SEQ ID No: 590, SEQ ID No: 592, SEQ ID No: 594, SEQ ID No: 596, SEQ ID No: 598, SEQ ID No: 600, SEQ ID No: 602, SEQ ID No: 604, SEQ ID No: 606, SEQ ID No: 608, SEQ ID No: 610, SEQ ID No: 612, SEQ ID No: 614, SEQ ID No: 616, SEQ ID No: 618, SEQ ID No: 620, SEQ ID No: 622, SEQ ID No: 624, SEQ ID No: 626, SEQ ID No: 628, SEQ ID No: 630, SEQ ID No: 632, SEQ ID No: 634, SEQ ID No: 636, SEQ ID No: 638, SEQ ID No: 640, SEQ ID No: 642, SEQ ID No: 644, SEQ ID No: 646, SEQ ID No: 648, SEQ ID No: 650, SEQ ID No: 652, SEQ ID No: 654, SEQ ID No: 656, SEQ ID No: 658, SEQ ID No: 660, SEQ ID No: 662, SEQ ID No: 664, SEQ ID No: 666, SEQ ID No: 668, SEQ ID No: 670, SEQ ID No: 672, SEQ ID No: 674, SEQ ID No: 676, SEQ ID No: 678, SEQ ID No: 680, SEQ ID No: 682, SEQ ID No: 684, SEQ ID No: 686, SEQ ID No: 688, SEQ ID No: 690, SEQ ID No: 692, SEQ ID No: 694, SEQ ID No: 696, SEQ ID No: 698, SEQ ID No: 700, SEQ ID No: 702, SEQ ID No: 704, SEQ ID No: 706, SEQ ID No: 708, SEQ ID No: 710, SEQ ID No: 712, SEQ ID No: 714, SEQ ID No: 716, SEQ ID No: 718, SEQ ID No: 720, SEQ ID No: 722, SEQ ID No: 724, SEQ ID No: 726, SEQ ID No: 728, SEQ ID No: 730, SEQ ID No: 732, SEQ ID No: 734, SEQ ID No: 736, SEQ ID No: 738, SEQ ID No: 740, SEQ ID No: 742, SEQ ID No: 744, SEQ ID No: 746, SEQ ID No: 748, SEQ ID No: 750, SEQ ID No: 752, SEQ ID No: 754, SEQ ID No: 756, SEQ ID No: 758, SEQ ID No: 760, SEQ ID No: 762, SEQ ID No: 764, SEQ ID No: 766, SEQ ID No: 768, SEQ ID No: 770, SEQ ID No: 772, SEQ ID No: 774, SEQ ID No: 776, SEQ ID No: 778, SEQ ID No: 780, SEQ ID No: 782, SEQ ID No: 784, SEQ ID No: 786, SEQ ID No: 788, SEQ ID No: 790, SEQ ID No: 792, SEQ ID No: 794, SEQ ID No: 796, SEQ ID No: SEQ ID No: 798, SEQ ID No: 800, SEQ ID No: 802, SEQ ID No: 804, SEQ ID No: 806, SEQ ID No: 808, SEQ ID No: 810, SEQ ID No: 812, SEQ ID No: 814, SEQ ID No: 816, SEQ ID No: 818, SEQ ID No: 820, SEQ ID No: 822, SEQ ID No: 824, SEQ ID No: 826, SEQ ID No: 828, SEQ ID No: 830, SEQ ID No: 832, SEQ ID No: 834, SEQ ID No: 836, SEQ ID No: 838, SEQ ID No: 840, SEQ ID No: 842, SEQ ID No: 844, SEQ ID No: 846, SEQ ID No: 848, SEQ ID No: 850, SEQ ID No: 852, SEQ ID No: 854, SEQ ID No: 856, SEQ ID No: 858, SEQ ID No: 860, SEQ ID No: 862, SEQ ID No: 864, SEQ ID No: 866, SEQ ID No: 868, SEQ ID No: 870, SEQ ID No: 872, SEQ ID No: 874, SEQ ID No: 876, SEQ ID No: 878, SEQ ID No: 880, SEQ ID No: 882, SEQ ID No: 884, SEQ ID No: 886, SEQ ID No: 888, SEQ ID No: 890, SEQ ID No: 892, SEQ ID No: 894, SEQ ID No: 896, SEQ ID No: 898, SEQ ID No: 900, SEQ ID No: 902, SEQ ID No: 904, SEQ ID No: 906, SEQ ID No: 908, SEQ ID No: 910, SEQ ID No: 912, SEQ ID No: 914, SEQ ID No: 916, SEQ ID No: 918, SEQ ID No: 920, SEQ ID No: 922, SEQ ID No: 924, SEQ ID No: 926, SEQ ID No: 928, SEQ ID No: 930, SEQ ID No: 932, SEQ ID No: 934, SEQ ID No: 936, SEQ ID No: 938, SEQ ID No: 940, SEQ ID No: 942, SEQ ID No: 944, SEQ ID No: 946, SEQ ID No: 948, SEQ ID No: 950, SEQ ID No: 952, SEQ ID No: 954, SEQ ID No: 956, SEQ ID No: 958, SEQ ID No: 960, SEQ ID No: 962, SEQ ID No: 964, SEQ ID No: 966, SEQ ID No: 968, SEQ ID No: 970, SEQ ID No: 972, SEQ ID No: 974, SEQ ID No: 976, SEQ ID No: 978, SEQ ID No: 980, SEQ ID No: 982, SEQ ID No: 984, SEQ ID No: 986, SEQ ID No: 988, SEQ ID No: 990, SEQ ID No: 992, SEQ ID No: 994, SEQ ID No: 996, SEQ ID No: 998, SEQ ID No: 1000, SEQ ID No: 1002, SEQ ID No: 1004, SEQ ID No: 1006, SEQ ID No: 1008, SEQ ID No: 1010, SEQ ID No: 1012, SEQ ID No: 1014, SEQ ID No: 1016, SEQ ID No: 1018, SEQ ID No: 1020, SEQ ID No: 1022, SEQ ID No: 1024, SEQ ID No: 1026, SEQ ID No: 1028, SEQ ID No: 1030, SEQ ID No: 1032, SEQ ID No: 1034, SEQ ID No: 1036, SEQ ID No: 1038, SEQ ID No: 1040, SEQ ID No: 1042, SEQ ID No: 1044, SEQ ID No: 1046, SEQ ID No: 1048, SEQ ID No: 1050, SEQ ID No: 1052, SEQ ID No: 1054, SEQ ID No: 1056, SEQ ID No: 1058, SEQ ID No: 1060, SEQ ID No: 1062, SEQ ID No: 1064, SEQ ID No: 1066, SEQ ID No: 1068, SEQ ID No: 1070, SEQ ID No: 1072, SEQ ID No: 1074, SEQ ID No: 1076, SEQ ID No: 1078, SEQ ID No: 1080, SEQ ID No: 1082, SEQ ID No: 1084, SEQ ID No: 1086, SEQ ID No: 1088, SEQ ID No: 1090, SEQ ID No: 1092, SEQ ID No: 1094, SEQ ID No: 1096, SEQ ID No: 1098, SEQ ID NO: 1100, SEQ ID No: 1102, SEQ ID No: 1104, SEQ ID No: 1106, SEQ ID No: 1108, SEQ ID No: 1110, SEQ ID No: 1112, SEQ ID No: 1114, SEQ ID No: 1116, SEQ ID No: 1118, SEQ ID No: 1120, SEQ ID No: 1122, SEQ ID No: 1124, SEQ ID No: 1126, SEQ ID No: 1128, SEQ ID No: 1130, SEQ ID No: 1132, SEQ ID No: 1134, SEQ ID No: 1136, SEQ ID No: 1138, SEQ ID No: 1140, SEQ ID No: 1142, SEQ ID No: 1144, SEQ ID No: 1146, SEQ ID No: 1148, SEQ ID No: 1150, SEQ ID No: 1152, SEQ ID No: 1154, SEQ ID No: 1156, SEQ ID No: 1158, SEQ ID No: 1160, SEQ ID No: 1162, SEQ ID No: 1164, SEQ ID No: 1166, SEQ ID No: 1168, SEQ ID No: 1170, SEQ ID No: 1172, SEQ ID No: 1174, SEQ ID No: 1176, SEQ ID No: 1178, SEQ ID No: 1180, SEQ ID No: 1182, SEQ ID No: 1184, SEQ ID No: 1186, SEQ ID No: 1188, SEQ ID No: 1190, SEQ ID No: 1192, SEQ ID No: 1194, SEQ ID No: 1196, SEQ ID No: 1198, SEQ ID No: 1200, SEQ ID No: 1202, SEQ ID No: 1204, SEQ ID No: 1206, SEQ ID No: 1208, SEQ ID No: 1210, SEQ ID No: 1212, SEQ ID No: 1214, SEQ ID No: 1216, SEQ ID No: 1218, SEQ ID No: 1220, SEQ ID No: 1222, SEQ ID No: 1224, SEQ ID No: 1226, SEQ ID No: 1228, SEQ ID No: 1230, SEQ ID No: 1232, SEQ ID No: 1234, SEQ ID No: 1236, SEQ ID No: 1238, SEQ ID No: 1240, SEQ ID No: 1242, SEQ ID No: 1244, SEQ ID No: 1246, SEQ ID No: 1248, SEQ ID No: 1250, SEQ ID No: 1252, SEQ ID No: 1254, SEQ ID No: 1256, SEQ ID No: 1258, SEQ ID No: 1260, SEQ ID No: 1262, SEQ ID No: 1264, SEQ ID No: 1266, SEQ ID No: 1268, SEQ ID No: 1270, SEQ ID No: 1272, SEQ ID No: 1274, SEQ ID No: 1276, SEQ ID No: 1278, SEQ ID No: 1280, SEQ ID No: 1282, SEQ ID No: 1284, SEQ ID No: 1286, SEQ ID No: 1288, SEQ ID No: 1290, SEQ ID No: 1292, SEQ ID No: 1294, SEQ ID No: 1296, SEQ ID No: 1298, SEQ ID No: 1300, SEQ ID No: 1302, SEQ ID No: 1304, SEQ ID No: 1306, SEQ ID No: 1308, SEQ ID No: 1310, SEQ ID No: 1312, SEQ ID No: 1314, SEQ ID No: 1316, SEQ ID No: 1318, SEQ ID No: 1320, SEQ ID No: 1322, SEQ ID No: 1324, SEQ ID No: 1326, SEQ ID No: 1328, SEQ ID No: 1330, SEQ ID No: 1332, SEQ ID No: 1334, SEQ ID No: 1336, SEQ ID No: 1338, SEQ ID No: 1340, SEQ ID No: 1342, SEQ ID No: 1344, SEQ ID No: 1346, SEQ ID No: 1348, SEQ ID No: 1350, SEQ ID No: 1352, SEQ ID No: 1354, SEQ ID No: 1356, SEQ ID No: 1358, SEQ ID No: 1360, SEQ ID No: 1362, SEQ ID No: 1364, SEQ ID No: 1366, SEQ ID No: 1368, SEQ ID No: 1370, SEQ ID No: 1372, SEQ ID No: 1374, SEQ ID No: 1376, SEQ ID No: 1378, SEQ ID No: 1380, SEQ ID No: 1382, SEQ ID No: 1384, SEQ ID No: 1386, SEQ ID No: 1388, SEQ ID No: 1390, SEQ ID No: 1392, SEQ ID No: 1394, SEQ ID No: 1396, SEQ ID No: 1398, SEQ ID No: 1400, SEQ ID No: 1402, SEQ ID No: 1404, SEQ ID No: 1406, SEQ ID No: 1408, SEQ ID No: 1410, SEQ ID No: 1412, SEQ ID No: 1414, SEQ ID No: 1416, SEQ ID No: 1418, SEQ ID No: 1420, SEQ ID No: 1422, SEQ ID No: 1424, SEQ ID No: 1426, SEQ ID No: 1428, SEQ ID No: 1430, SEQ ID No: 1432, SEQ ID No: 1434, SEQ ID No: 1436, SEQ ID No: 1438, SEQ ID No: 1440, SEQ ID No: 1442, SEQ ID No: 1444, SEQ ID No: 1446, SEQ ID No: 1448, SEQ ID No: 1450, SEQ ID No: 1452, SEQ ID No: 1454, SEQ ID No: 1456, SEQ ID No: 1458, SEQ ID No: 1460, SEQ ID No: 1462, SEQ ID No: 1464, SEQ ID No: 1466, SEQ ID No: 1468, SEQ ID No: 1470, SEQ ID No: 1472, SEQ ID No: 1474, SEQ ID No: 1476, SEQ ID No: 1478, SEQ ID No: 1480, SEQ ID No: 1482, SEQ ID No: 1484, SEQ ID No: 1486, SEQ ID No: 1488, SEQ ID No: 1490, SEQ ID No: 1492, SEQ ID No: 1494, SEQ ID No: 1496, SEQ ID No: 1498, SEQ ID No: 1500, SEQ ID No: 1502, SEQ ID No: 1504, SEQ ID No: 1506, SEQ ID No: 1508, SEQ ID No: 1510, SEQ ID No: 1512, SEQ ID No: 1514, SEQ ID No: 1516, SEQ ID No: 1518, SEQ ID No: 1520, SEQ ID No: 1522, SEQ ID No: 1524, SEQ ID No: 1526, SEQ ID No: 1528, SEQ ID No: 1530, SEQ ID No: 1532, SEQ ID No: 1534, SEQ ID No: 1536, SEQ ID No: 1538, SEQ ID No: 1540, SEQ ID No: 1542, SEQ ID No: 1544, SEQ ID No: 1546, SEQ ID No: 1548, SEQ ID No: 1550, SEQ ID No: 1552, SEQ ID No: 1554, SEQ ID No: 1556, SEQ ID No: 1558, SEQ ID No: 1560, SEQ ID No: 1562, SEQ ID No: 1564, SEQ ID No: 1566, SEQ ID No: 1568, SEQ ID No: 1570, SEQ ID No: 1572, SEQ ID No: 1574, SEQ ID No: 1576, SEQ ID No: 1578, SEQ ID No: 1580, SEQ ID No: 1582, SEQ ID No: 1584, SEQ ID No: 1586, SEQ ID No: 1588, SEQ ID No: 1590, SEQ ID No: 1592, SEQ ID No: 1594, SEQ ID No: 1596, SEQ ID No: 1598, SEQ ID No: 1600, SEQ ID No: 1602, SEQ ID No: 1604, SEQ ID No: 1606, SEQ ID No: 1608, SEQ ID No: 1610, SEQ ID No: 1612, SEQ ID No: 1614, SEQ ID No: 1616, SEQ ID No: 1618, SEQ ID No: 1620, SEQ ID No: 1622, SEQ ID No: 1624, SEQ ID No: 1626, SEQ ID No: 1628, SEQ ID No: 1630, SEQ ID No: 1632, SEQ ID No: 1634, SEQ ID No: 1636, SEQ ID No: 1638, SEQ ID No: 1640, SEQ ID No: 1642, SEQ ID No: 1644, SEQ ID No: 1646, SEQ ID No: 1648, SEQ ID No: 1650, SEQ ID No: 1652, SEQ ID No: 1654, SEQ ID No: 1656, SEQ ID No: 1658, SEQ ID No: 1660, SEQ ID No: 1662, SEQ ID No: 1664, SEQ ID No: 1666, SEQ ID No: 1668, SEQ ID No: 1670, SEQ ID No: 1672, SEQ ID No: 1674, SEQ ID No: 1676, SEQ ID No: 1678, SEQ ID No: 1680, SEQ ID No: 1682, SEQ ID No: 1684, SEQ ID No: 1686, SEQ ID No: 1688, SEQ ID No: 1690, SEQ ID No: 1692, SEQ ID No: 1694, SEQ ID No: 1696, SEQ ID No: 1698, SEQ ID No: 1700, SEQ ID No: 1702, SEQ ID No: 1704, SEQ ID No: 1706, SEQ ID No: 1708, SEQ ID No: 1710, SEQ ID No: 1712, SEQ ID No: 1714, SEQ ID No: 1716, SEQ ID No: 1718, SEQ ID No: 1720, SEQ ID No: 1722, SEQ ID No: 1724, SEQ ID No: 1726, SEQ ID No: 1728, SEQ ID No: 1730, SEQ ID No: 1732, SEQ ID No: 1734, SEQ ID No: 1736, SEQ ID No: 1738, SEQ ID No: 1740, SEQ ID No: 1742, SEQ ID No: 1744, SEQ ID No: 1746, SEQ ID No: 1748, SEQ ID No: 1750, SEQ ID No: 1752, SEQ ID No: 1754, SEQ ID No: 1756, SEQ ID No: 1758, SEQ ID No: 1760, SEQ ID No: 1762, SEQ ID No: 1764, SEQ ID No: 1766, SEQ ID No: 1768, SEQ ID No: 1770, SEQ ID No: 1772, SEQ ID No: 1774, SEQ ID No: 1776, SEQ ID No: 1778, SEQ ID No: 1780, SEQ ID No: 1782, SEQ ID No: 1784, SEQ ID No: 1786, SEQ ID No: 1788, SEQ ID No: 1790, SEQ ID No: 1792, SEQ ID No: 1794, SEQ ID No: 1796, SEQ ID No: 1798, SEQ ID No: 1800, SEQ ID No: 1802, SEQ ID No: 1804, SEQ ID No: 1806, SEQ ID No: 1808, SEQ ID No: 1810, SEQ ID No: 1812, SEQ ID No: 1814, SEQ ID No: 1816, SEQ ID No: 1818, SEQ ID No: 1820, SEQ ID No: 1822, SEQ ID No: 1824, SEQ ID No: 1826, SEQ ID No: 1828, SEQ ID No: 1830, SEQ ID No: 1832, SEQ ID No: 1834, SEQ ID No: 1836, SEQ ID No: 1838, SEQ ID No: 1840, SEQ ID No: 1842, SEQ ID No: 1844, SEQ ID No: 1846, SEQ ID No: 1848, SEQ ID No: 1850, SEQ ID No: 1852, SEQ ID No: 1854, SEQ ID No: 1856, SEQ ID No: 1858, SEQ ID No: 1860, SEQ ID No: 1862, SEQ ID No: 1864, SEQ ID No: 1866, SEQ ID No: 1868, SEQ ID No: 1870, SEQ ID No: 1872, SEQ ID No: 1874, SEQ ID No: 1876, SEQ ID No: 1878, SEQ ID No: 1880, SEQ ID No: 1882, SEQ ID No: 1884, SEQ ID No: 1886, SEQ ID No: 1888, SEQ ID No: 1890, SEQ ID No: 1892, SEQ ID No: 1894, SEQ ID No: 1896, SEQ ID No: 1898, SEQ ID No: 1900, SEQ ID No: 1902, SEQ ID No: 1904, SEQ ID No: 1906, SEQ ID No: 1908, SEQ ID No: 1910, SEQ ID No: 1912, SEQ ID No: 1914, SEQ ID No: 1916, SEQ ID No: 1918, SEQ ID No: 1920, SEQ ID No: 1922, SEQ ID No: 1924, SEQ ID No: 1926, SEQ ID No: 1928, SEQ ID No: 1930, SEQ ID No: 1932, SEQ ID No: 1934, SEQ ID No: 1936, SEQ ID No: 1938, SEQ ID No: 1940, SEQ ID No: 1942, SEQ ID No: 1944, SEQ ID No: 1946, SEQ ID No: 1948, SEQ ID No: 1950, SEQ ID No: 1952, SEQ ID No: 1954, SEQ ID No: 1956, SEQ ID No: 1958, SEQ ID No: 1960, SEQ ID No: 1962, SEQ ID No: 1964, SEQ ID No: 1966, SEQ ID No: 1968, SEQ ID No: 1970, SEQ ID No: 1972, or SEQ ID No: 1974. The present invention also includes homologues or variants of any of the above sequences, including fragments and sequences having a given identity to any of the above sequences, wherein the homologue, variant, or fragment has at least one biological activity of the wild-type protein, as described herein.
As used herein, "oxidoreductase" refers to an enzyme that catalyzes the transfer of electrons from one molecule (the reductant, also called the hydride or electron donor) to another (the oxidant, also called the idem or electron acceptor). A few of the oxidoreductase enzymes are listed below. This list is not exhaustive. Other oxidoreductase and their activity are well known to those skilled in the art.
[061] "Oxidase" refers to any enzyme that catalyzes an oxidation-reduction reaction involving molecular oxygen (O2) as the electron acceptor.
[062] "Monooxygenases" are oxidoreductases that induce the incorporation of one atom of oxygen from 02 into the substance being oxidized.
[063] "Baeyer-Villiger Monooxygenases" are oxidoreductases that induce the incorporation of one atom of oxygen from O2 next to the carbonyl goup of the ketone substance being oxidized.
[064] "Peroxidases" are enzymes that typically catalyze a reaction of the form: ROOR' + electron donor (2 e") + 2H+→ ROH + R'OH.
[065] "Hydroxylases" are oxidoreductases that induce the introduction of a hydroxyl group in the substance being oxidized.
[066] "Dioxygenases" are enzymes that incorporate both atoms of O2 into one substrate.
[067] "Dehydrogenases" refer to enzymes that catalyze the removal of hydrogen from organic compounds.
[068] "Reductases" refers to any enzyme that catalyzes the reduction of a substrate.
[069] "Cytochrome-c oxidase" is an enzyme that receives an electron from each of four cytochrome c molecules, and transfers them to one oxygen molecule, converting molecular oxygen to two molecules of water. "Xanthine oxidoreductase" is an enzyme that generates reactive oxygen species. "Xanthine oxidase" is an enzyme that catalyzes the oxidation of hypoxanthine to xanthine and can further catalyze the oxidation of xanthine to uric acid.
[070] "Cellobiose dehydrogenase" refers to a protein that oxidizes cellobiose to cellobiono lactone .
[071] "Sulfhydryl oxidases" or SOX are enzymes known to catalyze the conversion of thio compounds to the corresponding disulfides. Sulfhydryl oxidases are therefore of interest in applications where oxidation of free sulfhydryl groups to disulfide linkages is sought.
[072] Other examples of oxidases are those catalyzing the oxidation of sugars such as glucose oxidase, galactose oxidase and hexose oxidase .
[073] Laccases" belong to a family of multi-copper oxidases. Laccases are characterized by low substrate specificity, oxidizing various substrate, including diphenols, polyphenols, different substituted phenols, diamines, aromatic amines, and even inorganic compounds like iodine. Laccases oxidize their substrates by a one- electron oxidation mechanism, and they use molecular oxygen as an electron acceptor. Among laccases the primary sequence, induction mechanism, physico- chemical (e.g. isoelectric point and carbohydrate content) and biochemical characteristics are variable. The copper binding sites of laccases are, however, strictly conserved.
[074] In general, the proteins disclosed herein possess oxidoreductase activity. The proteins of the present invention can be combined with various enzymes as discussed below to aid in the production of bio fuels.
[075] As used herein, "carbohydrase" refers to any protein that catalyzes the hydrolysis of carbohydrates. "Glycoside hydrolase", "glycosyl hydrolase" or "glycosidase" refers to a protein that catalyzes the hydrolysis of the glycosidic bonds between carbohydrates or between a carbohydrate and a non-carbohydrate residue. Endoglucanases, cellobiohydrolases, β-glucosidases, a-glucosidases, xylanases, β- xylosidases, alpha- xylosidases, galactanases, a-galactosidases, β-galactosidases, a- amylases, glucoamylases, endo-arabinases, arabinofuranosidases, mannanases, β- mannosidases, pectinases, acetyl xylan esterases, acetyl mannan esterases, ferulic acid esterases, coumaric acid esterases, pectin methyl esterases, and chitosanases are examples of glycosidases.
[076] "Cellulose" is a linear beta-(l-4) glucan consisting of anhydrocellobiose units.
Cellulases include endoglucanases, cellobiohydrolases, and β-glucosidases. "Cellulase" refers to a protein that catalyzes the hydrolysis of l,4^-D-glycosidic linkages in cellulose; cellulose derivatives (such as carboxymethylcellulose and hydroxyethylcellulose); plant lignocellulosic materials, beta-D-glucans or xyloglucans.
[077] "Endoglucanase" refers to a protein that catalyzes the hydrolysis of cellulose to oligosaccharide chains at random locations by means of an endoglucanase activity.
[078] "Cellobiohydrolase" refers to a protein that catalyzes the hydrolysis of cellulose to cellobiose via an exoglucanase activity, sequentially releasing molecules of cellobiose from the reducing or non-reducing ends of cellulose or cello - oligosaccharides. [079] "β-glucosidase" refers to an enzyme that catalyzes the conversion of cellobiose and oligosaccharides to glucose.
[080] "Hemicellulase" refers to a protein that catalyzes the hydrolysis of hemicellulose, such as that found in lignocellulosic materials. Hemicelluloses are complex polymers, and their composition often varies widely from organism to organism, and from one tissue type to another. Hemicelluloses include a variety of compounds, such as xylans, arabinoxylans, xyloglucans, mannans, glucomannans, pectins, polygalacturonan, rhamnogalacturonan, xylogalacturonan and galacto(gluco)mannans. Hemicellulose can also contain glucan, which is a general term for beta-linked glucose residues. In general, a main component of hemicellulose is beta-l,4-linked xylose, a five carbon sugar. However, this xylose is often branched as beta- 1,3 linkages or beta- 1,2 linkages, and can be substituted with linkages to arabinose, galactose, mannose, glucuronic acid, or by esterification to acetic acid. The composition, nature of substitution, and degree of branching of hemicellulose is very different in dicotyledonous plants (dicots, i.e., plant whose seeds have two cotyledons or seed leaves such as lima beans, peanuts, almonds, peas, kidney beans) as compared to monocotyledonous plants (monocots; i.e., plants having a single cotyledon or seed leaf such as corn, wheat, rice, grasses, barley). In dicots, hemicellulose is comprised mainly of xyloglucans that are 1,4- beta-linked glucose chains with 1,6-alpha-linked xylosyl side chains. In monocots, including most grain crops, the principal components of hemicellulose are hetero xylans. These are primarily comprised of 1 ,4-beta- linked xylose backbone polymers with 1,2- or 1,3-alpha linkages to arabinose, linkage of galactose and mannose to arabinose or xylose in side chains, as well as xylose modified by ester- linked acetic acids. Also present are branched beta glucans comprised of 1,3- and 1 ,4-beta- linked glucosyl chains. In monocots, cellulose, hetero xylans and beta glucans are present in roughly equal amounts, each comprising about 15-25% of the dry matter of cell walls. Hemicellulo lytic enzymes, i.e. Hemicellulases, include both endo-acting and exo-acting enzymes, such as xylanases, β-xylosidases. alpha- xylosidases, galactanases, a-galactosidases, β-galactosidases, endo-arabinases, arabinofuranosidases, mannanases, β-mannosidases. Hemicellulases also include the accessory enzymes, such as acetylesterases, ferulic acid esterases, and coumaric acid esterases. Among these, xylanases and acetyl xylan esterases cleave the xylan and acetyl side chains of xylan and the remaining xylo -oligomers are unsubstituted and can thus be hydro lysed with β-xylosidase only. In addition, several less known side activities have been found in enzyme preparations which hydrolyze hemicellulose. Accordingly, xylanases, acetylesterases and β-xylosidases are examples of hemicellulases.
[081] "Xylanase" specifically refers to an enzyme that hydro lyzes the β-1,4 bond in the xylan backbone, producing short xylooligosaccharides.
[082] "β-Mannanase" or "endo-l,4^-mannosidase" refers to a protein that hydro lyzes mannan-based hemicelluloses (mannan, glucomannan, galacto(gluco)mannan) and produces short β-l,4-mannooligosaccharides.
[083] "Mannan endo-l,6-a-mannosidase" refers to a protein that hydro lyzes 1,6-a- mannosidic linkages in unbranched 1,6-mannans.
[084] "β-Mannosidase" (β-l,4-mannoside mannohydrolase; EC 3.2.1.25) refers to a protein that catalyzes the removal of β-D-mannose residues from the nonreducing ends of oligosaccharides.
[085] "Galactanase", "endo^-l,6-galactanse" or "arabinogalactan εηάο-1,4-β- galactosidase" refers to a protein that catalyzes the hydrolysis of εηάο-1,4-β-Ό- galactosidic linkages in arabinogalactans.
[086] "Gluco amylase" refers to a protein that catalyzes the hydrolysis of terminal 1,4- linked a-D-glucose residues successively from non-reducing ends of the glycosyl chains in starch with the release of β-D-glucose.
[087] "β -hexosaminidase" or "β-Ν-acetylglucosaminidase" refers to a protein that catalyzes the hydrolysis of terminal N-acetyl-D-hexosamine residues in N-acetyl-β-
D-hexosamines.
[088] "a-L-arabinofuranosidase", "a-N-arabinofuranosidase", "a-arabinofuranosidase", "arabinosidase" or "arabinofuranosidase" refers to a protein that hydro lyzes arabinofuranosyl-containing hemicelluloses. Some of these enzymes remove arabino fur ano side residues from 0-2 or 0-3 single substituted xylose residues, as well as from 0-2 and/or 0-3 double substituted xylose residues.
[089] "Endo-arabinase" refers to a protein that catalyzes the hydrolysis of 1,5-a- arabinofuranosidic linkages in 1,5-arabinans.
[090] "Exo-arabinase" refers to a protein that catalyzes the hydrolysis of 1,5-a-linkages in 1,5-arabinans or 1,5-a-L arabino-oligosaccharides, releasing mainly arabinobiose, although a small amount of arabinotriose can also be liberated.
[091] "β-xylosidase" refers to a protein that hydro lyzes short l,4-P-D-xylooligomers into xylose.
[092] "Cellobiose dehydrogenase" refers to a protein that oxidizes cellobiose to cellobiono lactone .
[093] "Chitosanase" refers to a protein that catalyzes the endohydro lysis of P-l,4-linkages between D-glucosamine residues in acetylated chitosan (i.e., deacetylated chitin).
[094] "Exo -polygalacturonase" refers to a protein that catalyzes the hydrolysis of terminal alpha 1 ,4-linked galacturonic acid residues from non-reducing ends thus converting polygalacturonides to galacturonic acid.
[095] "Acetyl xylan esterase" refers to a protein that catalyzes the removal of the acetyl groups from xylose residues. "Acetyl mannan esterase" refers to a protein that catalyzes the removal of the acetyl groups from mannose residues, "ferulic esterase" or "ferulic acid esterase" refers to a protein that hydro lyzes the ester bond between the arabinose substituent group and ferulic acid. "Coumaric acid esterase" refers to a protein that hydro lyzes the ester bond between the arabinose substituent group and coumaric acid. Acetyl xylan esterases, ferulic acid esterases and pectin methyl esterases are examples of carbohydrate esterases.
[096] "Pectate lyase" and "pectin lyases" refer to proteins that catalyze the cleavage of 1 ,4-a-D-galacturonan by beta-elimination acting on polymeric and/or oligosaccharide substrates (pectates and pectins, respectively).
[097] "Endo-l,3- -glucanase" or "laminarinase" refers to a protein that catalyzes the cleavage of 1,3-linkages in β-D-glucans such as laminarin or lichenin. Laminarin is a linear polysaccharide made up of β-1 -glucan with -l,6-linkages.
[098] "Lichenase" refers to a protein that catalyzes the hydrolysis of lichenan, a linear, 1,3-1,4-β-ϋ glucan.
[099] Rhamnogalacturonan is composed of alternating a-l,4-rhamnose and a-l,2-linked galacturonic acid, with side chains linked 1,4 to rhamnose. The side chains include Type I galactan, which is -l,4-linked galactose with a-l,3-linked arabinose substituents; Type II galactan, which is -l,3-l,6-linked galactoses (very branched) with arabinose substituents; and arabinan, which is a-l,5-linked arabinose with a- 1,3-linked arabinose branches. The galacturonic acid substituents may be acetylated and/or methylated. [0100] "Exo-rhamnogalacturonanase" refers to a protein that catalyzes the degradation of the rhamnogalacturonan backbone of pectin from the nonreducing end.
[0101] "Rhamnogalacturonan acetylesterase" refers to a protein that catalyzes the removal of the acetyl groups ester-linked to the highly branched rhamnogalacturonan (hairy) regions of pectin.
[0102] "Rhamnogalacturonan lyase" refers to a protein that catalyzes the degradation of the rhamnogalacturonan backbone of pectin via a β-elimination mechanism (see, e.g., Pages et al, J. Bacteriol. 185:4727-4733 (2003)).
[0103] "Alpha-rhamnosidase" refers to a protein that catalyzes the hydrolysis of terminal non-reducing a-L-rhamnose residues in a-L-rhamno sides.
[0104] Glycosidases (glycoside hydrolases; GH), a large family of enzymes that includes cellulases and hemicellulases, catalyze the hydrolysis of glycosidic linkages, predominantly in carbohydrates. Glycosidases such as the proteins of the present invention may be assigned to families on the basis of sequence similarities, and there are now over 100 different such families defined (see the CAZy (Carbohydrate Active EnZymes database) website, maintained by the Architecture of Fonction de Macromolecules Biologiques of the Centre National de la Recherche Scientifique, which describes the families of structurally-related catalytic and carbohydrate- binding modules (or functional domains) of enzymes that degrade, modify, or create glycosidic bonds; Coutinho, P.M. & Henrissat, B. (1999) Carbohydrate-active enzymes: an integrated database approach. In "Recent Advances in Carbohydrate Bioengineering", H.J. Gilbert, G. Davies, B. Henrissat and B. Svensson eds., The Royal Society of Chemistry, Cambridge, pp. 3-12). Because there is a direct relationship between the amino acid sequence of a protein and its folding similarities, such a classification reflects the structural features of these enzymes and their substrate specificity. Such a classification system can help to reveal the evolutionary relationships between these enzymes and provide a convenient tool to detemiine information such as an enzyme's activity and function. Thus, enzymes assigned to a particular family based on sequence homology with other members of the family are expected to have similar enzymatic activities and related substrate specificities. CAZy family classifications also exist for glycosyltransferases (GT), polysaccharide lyases (PL), and carbohydrate esterases (CE). Likewise, sequence homology may be used to identify particular domains within proteins, such as carbohydrate binding modules (CBMs; also known as carbohydrate binding domains (CBDs), sometimes called cellulose binding domains). The CAZy homologies of proteins of the present invention are disclosed below. An enzyme assigned to a particular CAZy family may exhibit one or more of the enzymatic activities or substrate specificities associated with the CAZy family. In other embodiments, the enzymes of the present invention may exhibit one or more of the enzyme activities discussed above.
[0105] Certain proteins used in the multi-enzyme compositions of the present invention may be classified as "Family 61 glycosidases" based on homology of the polypeptides to CAZy Family GH61. Family 61 glycosidases may exhibit oxidative activity towards biopolymers including, but not limited to, cellulose, hemicellulose, chitin, chitosan, amylose, amylopectin, pectin and lignin. The oxidative activity towards the biopolymers may results in an enhancing effect on the degradation of the corresponding biopolymer. Polynuceo tides encoding "Family 61 glycosidases" and polypetides thereof are provided as SEQ ID NO: 1892 through SEQ ID NO: 1944. Additional information on the properties of Family 61 glycosidases may be found in U.S. Patent Application Publication Nos. 2005/0191736, 2006/0005279, 2007/0077630, and in PCT Publication No. WO 2004/031378.
[0106] "Cellulo lytic enhancing activity" refers to a biological activity that enhances the hydrolysis of a cellulo sic material by proteins having cellulo lytic activity. This enhancing activity is expected to be related by the cellulose oxidizing activity of the GH61 enzyme.
[0107] "Hemicellulo lytic enhancing activity" refers to a biological activity that enhances the hydrolysis of a hemicellulo sic material by proteins having hemicellulo lytic activity. This enhancing activity is expected to be related by the hemicellulose oxidizing activity of the GH61 enzyme. As used herein, "hemicellulo stic materials" include, but are not limited to, xylan, glucuronoxylan, arabinoxylan, glucomannan, and xyloglucan
[0108] "Chitino lytic enhancing activity" refers to a biological activity that enhances the hydrolysis of a chitinoic material by proteins having chitinase activity. This enhancing activity is expected to be related by the chitin oxidizing activity of the GH61 enzyme.
[0109] "Amylo lytic enhancing activity" refers to a biological activity that enhances the hydrolysis of a amylosic material by proteins having amylase activity. This enhancing activity is expected to be related by the amylose oxidizing activity of the GH61 enzyme.
[0110] "Amylopectino lytic enhancing activity" refers to a biological activity that enhances the hydrolysis of a amylopectinoic materials by proteins having amylopectinase activity. This enhancing activity is expected to be related by the amylopectin oxidizing activity of the GH61 enzyme.
[0111] "Pectino lytic enhancing activity" refers to a biological activity that enhances the hydrolysis of a pectinoic materials by proteins having pectinase activity. This enhancing activity is expected to be related by the pectin oxidizing activity of the GH61 enzyme.
[0112] "Lignino lytic enhancing activity" refers to a biological activity that enhances the hydrolysis of a ligno lytic materials by proteins having ligninase activity. This enhancing activity is expected to be related by the lignin oxidizing activity of the GH61 enzyme.
[0113] "Cellobiose dehydrogenases" and "cellobiose oxidases" are oxidoreductases that oxidize cellobiose to cellobiono-l,5-lactone and can utilize electron acceptors including, but not limited to, molecular oxygen, CDH-like reductases, GH61 enzymes, cytochrome c and Felll
[0114] "CDH-like reductases" are oxidoreductases that can be reduced by an oxidoreductase such as, but not limited to, Cellobiose dehydrogenase, and that can be oxidized by "CDH-like reductases" and GH61 enzymes. The polynucelo tides encoding the CDH-like reductases and the polypeptides thereoff are provided as sequences SEQ ID NO: 234, SEQ ID NO: 1000, SEQ ID NO: 1774, SEQ ID NO: 1884, SEQ ID NO: 1886, SEQ ID NO: 1888 and SEQ ID NO: 1890.
[0115] This enhancing activity observed for the GH61 enzymes is expected to be related to the reduction of the GH61 enzyme by oxidoreductases such as, but not limited to, cellobiose dehydrogenases and CDH-like reductases. Reduced GH61 in combination hydrogen peroxide can oxidize biopolymers. The oxidation of biopolymers by the GH61 enzyme enhances the degradation of the biopolymer.
[0116] The enhancing activity of the degradation of polysaccharide containing materials can be determined by measuring the increase in sugars from the hydrolysis of the material by polysaccharide degrading protein. [0117] Proteins used in the multi-enzyme compositions of the present invention may also include homologues, variants, and fragments of the proteins disclosed herein. The protein fragments include, but are not limited to, fragments comprising a catalytic domain (CD) and/or a carbohydrate binding module (CBM) ( also known as a cellulose-binding domain; both can be referred to herein as CBM). The identity and location of domains within proteins of the present invention are disclosed in detail below. The present invention encompasses all combinations of the disclosed domains. For example, a protein fragment may comprise a CD of a protein but not a CBM of the protein or a CBM of a protein but not a CD. Similarly, domains from different proteins may be combined. Protein fragments comprising a CD, CBM or combinations thereof for each protein disclosed herein can be readily produced using standard techniques known in the art. In some embodiments, a protein fragment comprises a domain of a protein that has at least one biological activity of the full-length protein. Homologues or variants of proteins of the invention that have at least one biological activity of the full-length protein are described in detail below. As used herein, the phrase "biological activity" of a protein refers to any function(s) exhibited or performed by the protein that is ascribed to the naturally occurring form of the protein as measured or observed in vitro or in vivo. In certain embodiments, a protein fragment comprises a domain of a protein that has the catalytic activity of the full-length enzyme.
[0118] Descriptions of the enzymes of the present invention are provided below, along with activities and homologies. Although each enzyme is expected to exhibit the activity exemplified below, enzymes of the present invention may also exhibit any of the enzyme activities or substrate specificities discussed throughout this disclosure.
Oxidoreductases of the Present Invention
[0119] Oxidoreductases represent a category of various enzymes including but not limited to oxidases, oxygenases, monoxygenases, Baeyer-Villiger monooxygenases, dioxygenases, peroxidases, dehydrogenases, reductases that catalyze an oxidation- reduction reaction.
[0120] The following is a listing of the nucleic acid and amino acid sequences of the oxidoreductases of the present invention along with their expected acitivity.
[0121] The enzyme identified as Sequence Oxid-1 scaffold00008.G4 is encoded by the nucleotides of SEQ ID No: 1 which encodes the amino acid sequence of SEQ ID NO: 2. This enzyme is believed to have cytochrome-c oxidase activity.
[0122] The enzyme identified as Sequence Oxid-2 scaflbld00016.G278 is encoded by the nucleotides of SEQ ID No: 3 which encodes the amino acid sequence of SEQ ID No: 4. This enzyme is believed to have cytochrome-c oxidase activity.
[0123] The enzyme identified as Sequence Oxid-3 scaffold00016.G284 is encoded by the nucleotides of SEQ ID No: 5 which encodes the amino acid sequence of SEQ ID No: 6. This enzyme is believed to have ent-kaurene oxidase activity.
[0124] The enzyme identified as Sequence Oxid-4 scaffold00016.G642 is encoded by the nucleotides of SEQ ID No: 7 which encodes the amino acid sequence of SEQ ID No: 8. This enzyme is believed to have cytochrome-c oxidase activity.
[0125] The enzyme identified as Sequence Oxid-5 scaffold00016.G1015 is encoded by the nucleotides of SEQ ID No: 9 which encodes the amino acid sequence of SEQ ID No: 10. This enzyme is believed to have coproporphyrinogen oxidase activity.
[0126] The enzyme identified as Sequence Oxid-6 scaffold00016.Gl 147 is encoded by the nucleotides of SEQ ID No: 11 which encodes the amino acid sequence of SEQ ID No: 12. This enzyme is believed to have xanthine oxidase activity.
[0127] The enzyme identified as Sequence Oxid-7 scaffold00031.G10 is encoded by the nucleotides of SEQ ID No: 13 which encodes the amino acid sequence of SEQ ID No: 14. This enzyme is believed to have catalase activity.
[0128] The enzyme identified as Sequence Oxid-8 scaffold00031.G81 is encoded by the nucleotides of SEQ ID No: 15 which encodes the amino acid sequence of SEQ ID No: 16. This enzyme is believed to have glutathione peroxidase activity.
[0129] The enzyme identified as Sequence Oxid-9 scaffold00031.G109 is encoded by the nucleotides of SEQ ID No: 17 which encodes the amino acid sequence of SEQ ID No: 18. This enzyme is believed to have cytochrome-c oxidase activity.
[0130] The enzyme identified as Sequence Oxid-10 scaffold00031.G306 is encoded by the nucleotides of SEQ ID No: 19 which encodes the amino acid sequence of SEQ ID No: 20. This enzyme is believed to have urate oxidase activity.
[0131] The enzyme identified as Sequence Oxid-11 scaffold00031.G894 is encoded by the nucleotides of SEQ ID No: 21 which encodes the amino acid sequence of SEQ ID No: 22. This enzyme is believed to have glutathione peroxidase activity.
[0132] The enzyme identified as Sequence Oxid-12 scaffold00031.G1329 is encoded by the nucleotides of SEQ ID No: 23 which encodes the amino acid sequence of SEQ ID No: 24. This enzyme is believed to have D-amino-acid oxidase activity.
[0133] The enzyme identified as Sequence Oxid-13 scaflbld00031.G1386 is encoded by the nucleotides of SEQ ID No: 25 which encodes the amino acid sequence of SEQ ID No: 26. This enzyme is believed to have dihydroorotate oxidase activity.
[0134] The enzyme identified as Sequence Oxid-14 scaffold00050.G316 is encoded by the nucleotides of SEQ ID No: 27 which encodes the amino acid sequence of SEQ ID No: 28. This enzyme is believed to have linoleate diol synthase activity.
[0135] The enzyme identified as Sequence Oxid-15 scaffold00050.G973 is encoded by the nucleotides of SEQ ID No: 29 which encodes the amino acid sequence of SEQ ID No: 30. This enzyme is believed to have cytochrome-c oxidase activity.
[0136] The enzyme identified as Sequence Oxid-16 scaffold00050.G992 is encoded by the nucleotides of SEQ ID No: 31 which encodes the amino acid sequence of SEQ ID No: 32. This enzyme is believed to have amine oxidase activity.
[0137] The enzyme identified as Sequence Oxid-17 scaffold00050.Gl 115 is encoded by the nucleotides of SEQ ID No: 33 which encodes the amino acid sequence of SEQ ID No: 34. This enzyme is believed to have thiol oxidase activity.
[0138] The enzyme identified as Sequence Oxid-18 scaffold00050.Gl 138 is encoded by the nucleotides of SEQ ID No: 35 which encodes the amino acid sequence of SEQ ID No: 36. This enzyme is believed to have thioredoxin peroxidase activity.
[0139] The enzyme identified as Sequence Oxid-19 scaffold00050.Gl 145 is encoded by the nucleotides of SEQ ID No: 37 which encodes the amino acid sequence of SEQ ID No: 38. This enzyme is believed to have glucose oxidase - alcohol oxidase activity.
[0140] The enzyme identified as Sequence Oxid-20 scaffold00050.G1403 is encoded by the nucleotides of SEQ ID No: 39 which encodes the amino acid sequence of SEQ ID No: 40. This enzyme is believed to have Peroxidase activity.
[0141] The enzyme identified as Sequence Oxid-21 scaffold00050.G1668 is encoded by the nucleotides of SEQ ID No: 41 which encodes the amino acid sequence of SEQ ID No: 42. This enzyme is believed to have ent-kaurene oxidase activity.
[0142] The enzyme identified as Sequence Oxid-22 scaffold00071.G641 is encoded by the nucleotides of SEQ ID No: 43 which encodes the amino acid sequence of SEQ ID No: 44. This enzyme is believed to have oxygen-dependent protoporphyrinogen oxidase activity.
[0143] The enzyme identified as Sequence Oxid-23 scaffold00071.G707 is encoded by the nucleotides of SEQ ID No: 45 which encodes the amino acid sequence of SEQ ID No: 46. This enzyme is believed to have cytochrome-c peroxidase activity.
[0144] The enzyme identified as Sequence Oxid-24 scaffold00071.G1701 is encoded by the nucleotides of SEQ ID No: 47 which encodes the amino acid sequence of SEQ ID No: 48. This enzyme is believed to have D-amino-acid oxidase activity.
[0145] The enzyme identified as Sequence Oxid-25 scaffold00071.G2756 is encoded by the nucleotides of SEQ ID No: 49 which encodes the amino acid sequence of SEQ ID No: 50. This enzyme is believed to have peroxiredoxin activity.
[0146] The enzyme identified as Sequence Oxid-26 scaffold00071.G2771 is encoded by the nucleotides of SEQ ID No: 51 which encodes the amino acid sequence of SEQ ID No: 52. This enzyme is believed to have D-arabinono-l,4-lactone oxidase activity.
[0147] The enzyme identified as Sequence Oxid-27 scaffold00071.G2849 is encoded by the nucleotides of SEQ ID No: 53 which encodes the amino acid sequence of SEQ ID No: 54. This enzyme is believed to have D-arabinono-l,4-lactone oxidase activity.
[0148] The enzyme identified as Sequence Oxid-28 scaffold00071.G3230 is encoded by the nucleotides of SEQ ID No: 55 which encodes the amino acid sequence of SEQ ID No: 56. This enzyme is believed to have cytochrome-c oxidase activity.
[0149] The enzyme identified as Sequence Oxid-29 scaffold00071.G3441 is encoded by the nucleotides of SEQ ID No: 56 which encodes the amino acid sequence of SEQ ID No: 58. This enzyme is believed to have alcohol oxidase activity.
[0150] The enzyme identified as Sequence Oxid-30 scaffold00071.G3442 is encoded by the nucleotides of SEQ ID No: 57 which encodes the amino acid sequence of SEQ ID No: 60. This enzyme is believed to have alcohol oxidase activity.
[0151] The enzyme identified as Sequence Oxid-31 scaffold00071.G3476 is encoded by the nucleotides of SEQ ID No: 59 which encodes the amino acid sequence of SEQ ID No: 62. This enzyme is believed to have amine oxidase activity.
[0152] The enzyme identified as Sequence Oxid-32 scaffold00075.G779 is encoded by the nucleotides of SEQ ID No: 61 which encodes the amino acid sequence of SEQ ID No: 64. This enzyme is believed to have C-4 methylsterol oxidase activity.
[0153] The enzyme identified as Sequence Oxid-33 scaffold00092.G21 is encoded by the nucleotides of SEQ ID No: 63 which encodes the amino acid sequence of SEQ ID No: 66. This enzyme is believed to have glucose oxidase activity.
[0154] The enzyme identified as Sequence Oxid-34 scaffold00122.G43 is encoded by the nucleotides of SEQ ID No: 65 which encodes the amino acid sequence of SEQ ID No: 68. This enzyme is believed to have catalase activity.
[0155] The enzyme identified as Sequence Oxid-35 scaffold00122.G57 is encoded by the nucleotides of SEQ ID No: 67 which encodes the amino acid sequence of SEQ ID No: 70. This enzyme is believed to have glucose oxidase - alcohol oxidase activity.
[0156] The enzyme identified as Sequence Oxid-36 scaffold00131.G269 is encoded by the nucleotides of SEQ ID No: 69 which encodes the amino acid sequence of SEQ ID No: 72. This enzyme is believed to have dihydroorotate oxidase activity.
[0157] The enzyme identified as Sequence Oxid-37 scaffold00131.G1286 is encoded by the nucleotides of SEQ ID No: 71 which encodes the amino acid sequence of SEQ ID No: 74. This enzyme is believed to have cytochrome-c oxidase activity.
[0158] The enzyme identified as Sequence Oxid-38 scaffold00131.G1420 is encoded by the nucleotides of SEQ ID No: 73 which encodes the amino acid sequence of SEQ ID No: 76. This enzyme is believed to have phospholipid-hydroperoxide glutathione peroxidase activity.
[0159] The enzyme identified as Sequence Oxid-39 scaffold00137.G197 is encoded by the nucleotides of SEQ ID No: 75 which encodes the amino acid sequence of SEQ ID No: 78. This enzyme is believed to have alcohol oxidase activity.
[0160] The enzyme identified as Sequence Oxid-40 scaffold00142.G451 is encoded by the nucleotides of SEQ ID No: 77 which encodes the amino acid sequence of SEQ ID No: 80. This enzyme is believed to have cytochrome-c oxidase activity.
[0161] The enzyme identified as Sequence Oxid-41 scaffold00169.G174 is encoded by the nucleotides of SEQ ID No: 79 which encodes the amino acid sequence of SEQ ID No: 82. This enzyme is believed to have alcohol oxidase activity.
[0162] The enzyme identified as Sequence Oxid-42 scaffold00227.G212 is encoded by the nucleotides of SEQ ID No: 81 which encodes the amino acid sequence of SEQ ID No: 84. This enzyme is believed to have versatile peroxidase activity.
[0163] The enzyme identified as Sequence Oxid-43 scaffold00227.G247 is encoded by the nucleotides of SEQ ID No: 83 which encodes the amino acid sequence of SEQ ID No: 86. This enzyme is believed to have L-pipecolate oxidase - proline oxidase activity.
[0164] The enzyme identified as Sequence Oxid-44 scaffold00227.G400 is encoded by the nucleotides of SEQ ID No: 85 which encodes the amino acid sequence of SEQ ID No: 88. This enzyme is believed to have ent-kaurene oxidase activity.
[0165] The enzyme identified as Sequence Oxid-45 scaffold00050.G1500 is encoded by the nucleotides of SEQ ID No: 87 which encodes the amino acid sequence of SEQ ID
No: 90. This enzyme is believed to have catalase activity.
[0166] The enzyme identified as Sequence Oxid-46 177_g is encoded by the nucleotides of
SEQ ID No: 89 which encodes the amino acid sequence of SEQ ID No: 92. This enzyme is believed to have ent-kaurene oxidase activity.
[0167] The enzyme identified as Sequence Oxid-47 578_g is encoded by the nucleotides of
SEQ ID No: 91 which encodes the amino acid sequence of SEQ ID No: 94. This enzyme is believed to have cytochrome-c oxidase activity.
[0168] The enzyme identified as Sequence Oxid-48 941_g is encoded by the nucleotides of
SEQ ID No: 93 which encodes the amino acid sequence of SEQ ID No: 96. This enzyme is believed to have catalase activity.
[0169] The enzyme identified as Sequence Oxid-49 1538_g is encoded by the nucleotides of SEQ ID No: 95 which encodes the amino acid sequence of SEQ ID No: 98.
This enzyme is believed to have catalase activity.
[0170] The enzyme identified as Sequence Oxid-50 1787_g is encoded by the nucleotides of SEQ ID No: 97 which encodes the amino acid sequence of SEQ ID No: 100.
This enzyme is believed to have D-amino-acid oxidase activity.
[0171] The enzyme identified as Sequence Oxid-51 2870_g is encoded by the nucleotides of SEQ ID No: 99 which encodes the amino acid sequence of SEQ ID No: 102.
This enzyme is believed to have flavin-linked sulfhydryl oxidase activity.
[0172] The enzyme identified as Sequence Oxid-52 362 l_g is encoded by the nucleotides of SEQ ID No: 101 which encodes the amino acid sequence of SEQ ID No: 104.
This enzyme is believed to have oxygen-dependent protoporphyrinogen oxidase activity.
[0173] The enzyme identified as Sequence Oxid-53 5878_g is encoded by the nucleotides of SEQ ID No: 103 which encodes the amino acid sequence of SEQ ID No: 106.
This enzyme is believed to have pyridoxamine-phosphate oxidase activity.
[0174] The enzyme identified as Sequence Oxid-54 6852_g is encoded by the nucleotides of SEQ ID No: 105 which encodes the amino acid sequence of SEQ ID No: 108.
This enzyme is believed to have catalase activity.
[0175] The enzyme identified as Sequence Oxid-55 7956_g is encoded by the nucleotides of SEQ ID No: 107 which encodes the amino acid sequence of SEQ ID No: 110.
This enzyme is believed to have peroxidase activity.
[0176] The enzyme identified as Sequence Oxid-56 8774_g is encoded by the nucleotides of SEQ ID No: 109 which encodes the amino acid sequence of SEQ ID No: 112.
This enzyme is believed to have cytochrome-c oxidase activity.
[0177] The enzyme identified as Sequence Oxid-57 scaffold00050.pathl .gene349 is
encoded by the nucleotides of SEQ ID No: 111 which encodes the amino acid sequence of SEQ ID No: 114. This enzyme is believed to have peroxidase - peroxiredoxin activity.
[0178] The enzyme identified as Sequence Oxid-58 scaffold00122.pathl .genel6 is encoded by the nucleotides of SEQ ID No: 113 which encodes the amino acid sequence of SEQ ID No: 116. This enzyme is believed to have catalase activity.
[0179] The enzyme identified as Sequence Oxid-59 scaffold00131.pathl .genel 19 is
encoded by the nucleotides of SEQ ID No: 115 which encodes the amino acid sequence of SEQ ID No: 118. This enzyme is believed to have thioredoxin peroxidase activity.
[0180] The enzyme identified as Sequence Oxid-60 scaffold00131.pathl .gene510 is
encoded by the nucleotides of SEQ ID No: 117 which encodes the amino acid sequence of SEQ ID No: 120. This enzyme is believed to have glutathione peroxidase - Protein disulfide oxidoreductase activity.
[0181] The enzyme identified as Sequence Oxid-61 scaffold00050.G998 is encoded by the nucleotides of SEQ ID No: 119 which encodes the amino acid sequence of SEQ ID
No: 122. This enzyme is believed to have laccase activity.
[0182] The enzyme identified as Sequence Oxid-62 scaffold00071.G2587 is encoded by the nucleotides of SEQ ID No: 121 which encodes the amino acid sequence of SEQ ID
No: 124. This enzyme is believed to have laccase activity.
[0183] The enzyme identified as Sequence Oxid-63 scaffold00169.G454 is encoded by the nucleotides of SEQ ID No: 123 which encodes the amino acid sequence of SEQ ID
No: 126. This enzyme is believed to have laccase activity.
[0184] The enzyme identified as Sequence Oxid-64 scaffold00169.G455 is encoded by the nucleotides of SEQ ID No: 125 which encodes the amino acid sequence of SEQ ID
No: 128. This enzyme is believed to have laccase activity.
[0185] The enzyme identified as Sequence Oxid-65 scaffold00071.G416 is encoded by the nucleotides of SEQ ID No: 127 which encodes the amino acid sequence of SEQ ID No: 130. This enzyme is believed to have thioredoxin-disulfide reductase activity.
[0186] The enzyme identified as Sequence Oxid-66 scaffold00071.G1899 is encoded by the nucleotides of SEQ ID No: 129 which encodes the amino acid sequence of SEQ ID No: 132. This enzyme is believed to have arsenate reductase (glutaredoxin) activity.
[0187] The enzyme identified as Sequence Oxid-67 scaffold00075.G497 is encoded by the nucleotides of SEQ ID No: 131 which encodes the amino acid sequence of SEQ ID No: 134. This enzyme is believed to have ferredoxin-NADP+ reductase activity.
[0188] The enzyme identified as Sequence Oxid-68 scaffold00031.G158 is encoded by the nucleotides of SEQ ID No: 133 which encodes the amino acid sequence of SEQ ID No: 136. This enzyme is believed to have tryptophan 2,3-dioxygenase activity.
[0189] The enzyme identified as Sequence Oxid-69 scaffold00031.G227 is encoded by the nucleotides of SEQ ID No: 135 which encodes the amino acid sequence of SEQ ID No: 138. This enzyme is believed to have sulfonate dioxygenase activity.
[0190] The enzyme identified as Sequence Oxid-70 scaffold00031.G625 is encoded by the nucleotides of SEQ ID No: 137 which encodes the amino acid sequence of SEQ ID No: 140. This enzyme is believed to have catechol 1 ,2-dioxygenase activity.
[0191] The enzyme identified as Sequence Oxid-71 scaffold00031.G776 is encoded by the nucleotides of SEQ ID No: 139 which encodes the amino acid sequence of SEQ ID No: 142. This enzyme is believed to have oxidoreductase activity.
[0192] The enzyme identified as Sequence Oxid-72 scaffold00031.G1607 is encoded by the nucleotides of SEQ ID No: 141 which encodes the amino acid sequence of SEQ ID No: 144. This enzyme is believed to have 2-nitropropane dioxygenase activity.
[0193] The enzyme identified as Sequence Oxid-73 scaffold00050.G277 is encoded by the nucleotides of SEQ ID No: 143 which encodes the amino acid sequence of SEQ ID No: 146. This enzyme is believed to have nitric oxide dioxygenase activity.
[0194] The enzyme identified as Sequence Oxid-74 scaffold00071.G251 is encoded by the nucleotides of SEQ ID No: 145 which encodes the amino acid sequence of SEQ ID No: 148. This enzyme is believed to have 3-hydroxyanthranilate 3,4-dioxygenase activity.
[0195] The enzyme identified as Sequence Oxid-75 scaffold00071.G335 is encoded by the nucleotides of SEQ ID No: 147 which encodes the amino acid sequence of SEQ ID No: 150. This enzyme is believed to have nitric oxide dioxygenase activity.
[0196] The enzyme identified as Sequence Oxid-76 scaflbld00071.G2259 is encoded by the nucleotides of SEQ ID No: 149 which encodes the amino acid sequence of SEQ ID No: 152. This enzyme is believed to have oxidoreductase activity.
[0197] The enzyme identified as Sequence Oxid-77 scaffold00071.G3208 is encoded by the nucleotides of SEQ ID No: 151 which encodes the amino acid sequence of SEQ ID No: 154. This enzyme is believed to have catechol 1 ,2-dioxygenase activity.
[0198] The enzyme identified as Sequence Oxid-78 scaffold00075.G417 is encoded by the nucleotides of SEQ ID No: 153 which encodes the amino acid sequence of SEQ ID No: 156. This enzyme is believed to have cysteine dioxygenase activity.
[0199] The enzyme identified as Sequence Oxid-79 scaffold00075.G1075 is encoded by the nucleotides of SEQ ID No: 155 which encodes the amino acid sequence of SEQ ID No: 158. This enzyme is believed to have sulfonate dioxygenase activity.
[0200] The enzyme identified as Sequence Oxid-80 scaffold00075.G1251 is encoded by the nucleotides of SEQ ID No: 157 which encodes the amino acid sequence of SEQ ID No: 160. This enzyme is believed to have sulfonate dioxygenase activity.
[0201] The enzyme identified as Sequence Oxid-81 scaffold00131.G595 is encoded by the nucleotides of SEQ ID No: 159 which encodes the amino acid sequence of SEQ ID No: 162. This enzyme is believed to have trimethyllysine dioxygenase activity.
[0202] The enzyme identified as Sequence Oxid-82 scaffold00131.G596 is encoded by the nucleotides of SEQ ID No: 161 which encodes the amino acid sequence of SEQ ID No: 164. This enzyme is believed to have trimethyllysine dioxygenase activity.
[0203] The enzyme identified as Sequence Oxid-83 scaffold00131.G810 is encoded by the nucleotides of SEQ ID No: 163 which encodes the amino acid sequence of SEQ ID No: 166. This enzyme is believed to have oxidoreductase activity.
[0204] The enzyme identified as Sequence Oxid-84 scaffold00131.G1675 is encoded by the nucleotides of SEQ ID No: 165 which encodes the amino acid sequence of SEQ ID No: 168. This enzyme is believed to have 2-nitropropane dioxygenase activity.
[0205] The enzyme identified as Sequence Oxid-85 scaffold00131.G2052 is encoded by the nucleotides of SEQ ID No: 167 which encodes the amino acid sequence of SEQ ID No: 170. This enzyme is believed to have oxidoreductase activity.
[0206] The enzyme identified as Sequence Oxid-86 scaffold00131.G2141 is encoded by the nucleotides of SEQ ID No: 169 which encodes the amino acid sequence of SEQ ID No: 172. This enzyme is believed to have oxidoreductase activity.
[0207] The enzyme identified as Sequence Oxid-87 scaflbld00142.G307 is encoded by the nucleotides of SEQ ID No: 171 which encodes the amino acid sequence of SEQ ID No: 174. This enzyme is believed to have oxidoreductase activity.
[0208] The enzyme identified as Sequence Oxid-88 scaffold00142.G386 is encoded by the nucleotides of SEQ ID No: 173 which encodes the amino acid sequence of SEQ ID No: 176. This enzyme is believed to have tryptophan 2,3-dioxygenase activity.
[0209] The enzyme identified as Sequence Oxid-89 scaffold00169.G8 is encoded by the nucleotides of SEQ ID No: 175 which encodes the amino acid sequence of SEQ ID No: 178. This enzyme is believed to have oxidoreductase activity.
[0210] The enzyme identified as Sequence Oxid-90 scaffold00169.G77 is encoded by the nucleotides of SEQ ID No: 177 which encodes the amino acid sequence of SEQ ID No: 180. This enzyme is believed to have sulfonate dioxygenase activity.
[0211] The enzyme identified as Sequence Oxid-91 scaffold00169.G407 is encoded by the nucleotides of SEQ ID No: 179 which encodes the amino acid sequence of SEQ ID No: 182. This enzyme is believed to have oxidoreductase activity.
[0212] The enzyme identified as Sequence Oxid-92 scaffold00227.G198 is encoded by the nucleotides of SEQ ID No: 181 which encodes the amino acid sequence of SEQ ID No: 184. This enzyme is believed to have 2-nitropropane dioxygenase activity.
[0213] The enzyme identified as Sequence Oxid-93 scaffold00227.G634 is encoded by the nucleotides of SEQ ID No: 183 which encodes the amino acid sequence of SEQ ID No: 186. This enzyme is believed to have catechol 1 ,2-dioxygenase activity.
[0214] The enzyme identified as Sequence Oxid-94 2107_g is encoded by the nucleotides of SEQ ID No: 185 which encodes the amino acid sequence of SEQ ID No: 188. This enzyme is believed to have 2-nitropropane dioxygenase activity.
[0215] The enzyme identified as Sequence Oxid-95 977 l_g is encoded by the nucleotides of SEQ ID No: 187 which encodes the amino acid sequence of SEQ ID No: 190. This enzyme is believed to have catechol 1 ,2-dioxygenase activity.
[0216] The enzyme identified as Sequence Oxid-96 scaffold00031.G1073 is encoded by the nucleotides of SEQ ID No: 189 which encodes the amino acid sequence of SEQ ID No: 192. This enzyme is believed to have prephenate dehydrogenase (NADP+) activity.
[0217] The enzyme identified as Sequence Oxid-97 scaffold00227.G60 is encoded by the nucleotides of SEQ ID No: 191 which encodes the amino acid sequence of SEQ ID No: 194. This enzyme is believed to have homogentisate 1 ,2-dioxygenase activity.
[0218] The enzyme identified as Sequence Oxid-98 scaffold00016.G898 is encoded by the nucleotides of SEQ ID No: 193 which encodes the amino acid sequence of SEQ ID No: 196. This enzyme is believed to have 4-hydroxyphenylpyruvate dioxygenase activity.
[0219] The enzyme identified as Sequence Oxid-99 scaffold00071.G470 is encoded by the nucleotides of SEQ ID No: 195 which encodes the amino acid sequence of SEQ ID No: 198. This enzyme is believed to have oxidoreductase activity.
[0220] The enzyme identified as Sequence Oxid-100 scaffold00071.G607 is encoded by the nucleotides of SEQ ID No: 197 which encodes the amino acid sequence of SEQ ID No: 200. This enzyme is believed to have Protein disulfide oxidoreductase activity.
[0221] The enzyme identified as Sequence Oxid-101 scaffold00071.G1052 is encoded by the nucleotides of SEQ ID No: 199 which encodes the amino acid sequence of SEQ ID No: 202. This enzyme is believed to have Protein disulfide isomerase activity.
[0222] The enzyme identified as Sequence Oxid-102 scaffold00071.G1584 is encoded by the nucleotides of SEQ ID No: 201 which encodes the amino acid sequence of SEQ ID No: 204. This enzyme is believed to have Protein disulfide isomerase activity.
[0223] The enzyme identified as Sequence Oxid-103 scaffold00071.G2169 is encoded by the nucleotides of SEQ ID No: 203 which encodes the amino acid sequence of SEQ ID No: 206. This enzyme is believed to have Protein disulfide oxidoreductase activity.
[0224] The enzyme identified as Sequence Oxid-104 scaffold00131.G1597 is encoded by the nucleotides of SEQ ID No: 205 which encodes the amino acid sequence of SEQ ID No: 208. This enzyme is believed to have Protein disulfide isomerase activity.
[0225] The enzyme identified as Sequence Oxid-105 scaffold00227.G519 is encoded by the nucleotides of SEQ ID No: 207 which encodes the amino acid sequence of SEQ ID No: 210. This enzyme is believed to have Protein disulfide oxidoreductase activity.
[0226] The enzyme identified as Sequence Oxid-106 scaffold00016.G594 is encoded by the nucleotides of SEQ ID No: 209 which encodes the amino acid sequence of SEQ ID No: 212. This enzyme is believed to have Protein disulfide oxidoreductase activity.
[0227] The enzyme identified as Sequence Oxid-107 scaffold00016.Gl 163 is encoded by the nucleotides of SEQ ID No: 211 which encodes the amino acid sequence of SEQ ID No: 214. This enzyme is believed to have glutathione-disulfide reductase activity.
[0228] The enzyme identified as Sequence Oxid-108 scaflbld00031.G1301 is encoded by the nucleotides of SEQ ID No: 213 which encodes the amino acid sequence of SEQ ID No: 216. This enzyme is believed to have Protein disulfide oxidoreductase activity.
[0229] The enzyme identified as Sequence Oxid-109 scaffold00050.G952 is encoded by the nucleotides of SEQ ID No: 215 which encodes the amino acid sequence of SEQ ID No: 218. This enzyme is believed to have Protein disulfide oxidoreductase activity.
[0230] The enzyme identified as Sequence Oxid-110 scaffold00031.G37 is encoded by the nucleotides of SEQ ID No: 217 which encodes the amino acid sequence of SEQ ID No: 220. This enzyme is believed to have Redox-active center Protein activity.
[0231] The enzyme identified as Sequence Oxid-111 scaffold00031.G200 is encoded by the nucleotides of SEQ ID No: 219 which encodes the amino acid sequence of SEQ ID No: 222. This enzyme is believed to have Redox-active center Protein activity.
[0232] The enzyme identified as Sequence Oxid-112 scaffold00031.G1677 is encoded by the nucleotides of SEQ ID No: 221 which encodes the amino acid sequence of SEQ ID No: 224. This enzyme is believed to have Redox-active center Protein activity.
[0233] The enzyme identified as Sequence Oxid-113 scaffold00071.G1335 is encoded by the nucleotides of SEQ ID No: 223 which encodes the amino acid sequence of SEQ ID No: 226. This enzyme is believed to have Redox-active center Protein activity.
[0234] The enzyme identified as Sequence Oxid-114 scaffold00071.G3221 is encoded by the nucleotides of SEQ ID No: 225 which encodes the amino acid sequence of SEQ ID No: 228. This enzyme is believed to have Redox-active center Protein activity.
[0235] The enzyme identified as Sequence Oxid-115 scaffold00129.Gl is encoded by the nucleotides of SEQ ID No: 227 which encodes the amino acid sequence of SEQ ID No: 230. This enzyme is believed to have Redox-active center Protein activity.
[0236] The enzyme identified as Sequence Oxid-116 scaffold00142.G269 is encoded by the nucleotides of SEQ ID No: 229 which encodes the amino acid sequence of SEQ ID No: 232. This enzyme is believed to have Redox-active center Protein activity.
[0237] The enzyme identified as Sequence Oxid-117 scaffold00071.G3389 is encoded by the nucleotides of SEQ ID No: 231 which encodes the amino acid sequence of SEQ ID No: 234. This enzyme is believed to have cellobiose dehydrogenase (acceptor) activity.
[0238] The enzyme identified as Sequence Oxid-118 scaflbld00092.G499 is encoded by the nucleotides of SEQ ID No: 233 which encodes the amino acid sequence of SEQ ID No: 236. This enzyme is believed to have cellobiose dehydrogenase (acceptor) activity.
[0239] The enzyme identified as Sequence Oxid-119 scaffold00137.G80 is encoded by the nucleotides of SEQ ID No: 235. SEQ ID No: 237 which encodes the amino acid sequence of SEQ ID No: 238. This enzyme is believed to have cellobiose dehydrogenase (acceptor) activity.
[0240] The enzyme identified as Sequence Oxid-120 scaffold00142.G279 is encoded by the nucleotides of SEQ ID No: 239 which encodes the amino acid sequence of SEQ ID No: 240. This enzyme is believed to have cellobiose dehydrogenase (acceptor) activity.
[0241] The enzyme identified as Sequence Oxid-121 scaffold00142.G282 is encoded by the nucleotides of SEQ ID No: 241 which encodes the amino acid sequence of SEQ ID No: 242. This enzyme is believed to have cellobiose dehydrogenase (acceptor) activity.
[0242] The enzyme identified as Sequence Oxid-122 scaffold00050.G528 is encoded by the nucleotides of SEQ ID No: 243 which encodes the amino acid sequence of SEQ ID No: 244. This enzyme is believed to have oxidoreductase activity.
[0243] The enzyme identified as Sequence Oxid-123 scaffold00050.Gl 147 is encoded by the nucleotides of SEQ ID No: 245 which encodes the amino acid sequence of SEQ ID No: 246. This enzyme is believed to have oxidoreductase activity.
[0244] The enzyme identified as Sequence Oxid-124 scaffold00071.G1252 is encoded by the nucleotides of SEQ ID No: 247 which encodes the amino acid sequence of SEQ ID No: 248. This enzyme is believed to have oxidoreductase activity.
[0245] The enzyme identified as Sequence Oxid-125 scaffold00092.G8 is encoded by the nucleotides of SEQ ID No: 249 which encodes the amino acid sequence of SEQ ID No: 250. This enzyme is believed to have oxidoreductase activity.
[0246] The enzyme identified as Sequence Oxid-126 scaffold00092.G500 is encoded by the nucleotides of SEQ ID No: 251 which encodes the amino acid sequence of SEQ ID No: 252. This enzyme is believed to have cellobiose dehydrogenase (acceptor) activity. [0247] The enzyme identified as Sequence Oxid-127 scaflbld00122.G120 is encoded by the nucleotides of SEQ ID No: 253 which encodes the amino acid sequence of SEQ ID No: 254. This enzyme is believed to have oxidoreductase activity.
[0248] The enzyme identified as Sequence Oxid-128 scaffold00131.G1200 is encoded by the nucleotides of SEQ ID No: 255 which encodes the amino acid sequence of SEQ ID No: 256. This enzyme is believed to have oxidoreductase activity.
[0249] The enzyme identified as Sequence Oxid-129 scaffold00169.G243 is encoded by the nucleotides of SEQ ID No: 257 which encodes the amino acid sequence of SEQ ID No: 258. This enzyme is believed to have oxidoreductase activity.
[0250] The enzyme identified as Sequence Oxid-130 scaffold00169.G244 is encoded by the nucleotides of SEQ ID No: 259 which encodes the amino acid sequence of SEQ ID No: 260. This enzyme is believed to have oxidoreductase activity.
[0251] The enzyme identified as Sequence Oxid-131 scaffold00131.G1201 is encoded by the nucleotides of SEQ ID No: 261 which encodes the amino acid sequence of SEQ ID No: 262. This enzyme is believed to have oxidoreductase activity.
[0252] The enzyme identified as Sequence Oxid-132 scaffold00050.G593 is encoded by the nucleotides of SEQ ID No: 263 which encodes the amino acid sequence of SEQ ID No: 264. This enzyme is believed to have nitrate reductase (NADPH) activity.
[0253] The enzyme identified as Sequence Oxid-133 scaffold00075.G929 is encoded by the nucleotides of SEQ ID No: 265 which encodes the amino acid sequence of SEQ ID No: 266. This enzyme is believed to have nitrate reductase (NADPH) activity.
[0254] The enzyme identified as Sequence Oxid-134 scaffold00227.G302 is encoded by the nucleotides of SEQ ID No: 267 which encodes the amino acid sequence of SEQ ID No: 268. This enzyme is believed to have nitrite reductase [NAD(P)H] activity.
[0255] The enzyme identified as Sequence Oxid-135 scaffold00131.G1207 is encoded by the nucleotides of SEQ ID No: 269 which encodes the amino acid sequence of SEQ ID No: 270. This enzyme is believed to have nitrite reductase (NO-forming) activity.
[0256] The enzyme identified as Sequence Oxid-136 scaffold00016.G461 is encoded by the nucleotides of SEQ ID No: 271 which encodes the amino acid sequence of SEQ ID No: 272. This enzyme is believed to have glutamate synthase (NADPH) activity.
[0257] The enzyme identified as Sequence Oxid-137 scaffold00031.G1084 is encoded by the nucleotides of SEQ ID No: 273 which encodes the amino acid sequence of SEQ ID No: 274. This enzyme is believed to have glutamate dehydrogenase activity.
[0258] The enzyme identified as Sequence Oxid-138 scaffold00050.G21 is encoded by the nucleotides of SEQ ID No: 275 which encodes the amino acid sequence of SEQ ID No: 276. This enzyme is believed to have proline dehydrogenase activity.
[0259] The enzyme identified as Sequence Oxid-139 scaffold00075.G589 is encoded by the nucleotides of SEQ ID No: 277 which encodes the amino acid sequence of SEQ ID No: 278. This enzyme is believed to have isocitrate dehydrogenase (NAD+) activity.
[0260] The enzyme identified as Sequence Oxid-140 scaffold00016.G283
[0261] (CL09102) is encoded by the nucleotides of SEQ ID No: 279 which encodes the amino acid sequence of SEQ ID No: 280. This enzyme is believed to have monooxygenase activity.
[0262] The enzyme identified as Sequence Oxid-141 scaffold00016.G359
220_gscaffold00016.pathl .gene 175
[0263] (CL09141) is encoded by the nucleotides of SEQ ID No: 281 which encodes the amino acid sequence of SEQ ID No: 282. This enzyme is believed to have phenol
2-monooxygenase activity.
[0264] The enzyme identified as Sequence Oxid-142 scaffold00016.G1047 (CL09554) is encoded by the nucleotides of SEQ ID No: 283 which encodes the amino acid sequence of SEQ ID No: 284. This enzyme is believed to have monooxygenase activity.
[0265] The enzyme identified as Sequence Oxid-143 scaffold00019.G30 882_g
scaffold00019.pathl .gene7 (CL05569) is encoded by the nucleotides of SEQ ID No: 285 which encodes the amino acid sequence of SEQ ID No: 286. This enzyme is believed to have oxidation reduction activity.
[0266] The enzyme identified as Sequence Oxid-144 scaffold00022.Gl 923_g
scaffold00022.pathl .genel (CL08704) is encoded by the nucleotides of SEQ ID No: 287 which encodes the amino acid sequence of SEQ ID No: 288. This enzyme is believed to have oxidation reduction activity.
[0267] The enzyme identified as Sequence Oxid-145 scaffold00031.G17 946_g,
scaffold00031.pathl .genel4 (CL07195) is encoded by the nucleotides of SEQ ID No: 289 which encodes the amino acid sequence of SEQ ID No: 290. This enzyme is believed to have oxidation reduction activity. [0268] The enzyme identified as Sequence Oxid-146 scaffold00031.G86 976_g
scafFold00031.pathl .gene42 (CL07149) is encoded by the nucleotides of SEQ ID No: 291 which encodes the amino acid sequence of SEQ ID No: 292. This enzyme is believed to have oxidation reduction activity.
[0269] The enzyme identified as Sequence Oxid-147 scaffold00031.G144 1007_g,
scaffold00031.pathl .gene69 (CL07117) is encoded by the nucleotides of SEQ ID No: 293 which encodes the amino acid sequence of SEQ ID No: 294. This enzyme is believed to have oxidation reduction activity.
[0270] The enzyme identified as Sequence Oxid-148 scaffold00031.G225 1063 9 (partly), scaffold00031. pathl . genel 15 (CL07057) is encoded by the nucleotides of SEQ ID No: 295 which encodes the amino acid sequence of SEQ ID No: 296. This enzyme is believed to have oxidation reduction activity.
[0271] The enzyme identified as Sequence Oxid-149 scaffold00031.G454 1216_g,
scaffold00031. pathl . gene252 (CL06915) is encoded by the nucleotides of SEQ ID No: 297 which encodes the amino acid sequence of SEQ ID No: 298. This enzyme is believed to have regulation of transcription, DNA-dependent activity.
[0272] The enzyme identified as Sequence Oxid-150 scaffold00031.G472 1227_g,
scaffold00031. pathl . gene263 (CL06904) is encoded by the nucleotides of SEQ ID No: 299 which encodes the amino acid sequence of SEQ ID No: 300. This enzyme is believed to have oxidation reduction activity.
[0273] The enzyme identified as Sequence Oxid-151 scaffold00031.G951 1526_g,
scaffold00031. pathl . gene521 (CL06630) is encoded by the nucleotides of SEQ ID No: 301 which encodes the amino acid sequence of SEQ ID No: 302. This enzyme is believed to have oxidation reduction activity.
[0274] The enzyme identified as Sequence Oxid-152 scaffold00031.G1375 1815_g,
scaffold00031. pathl . gene780 (CL02845) is encoded by the nucleotides of SEQ ID No: 303 which encodes the amino acid sequence of SEQ ID No: 304. This enzyme is believed to have oxidation reduction activity.
[0275] The enzyme identified as Sequence Oxid-153 scaffold00031.G1384 1820_g,
scaffold00031. pathl . gene783 (CL02839) is encoded by the nucleotides of SEQ ID No: 305 which encodes the amino acid sequence of SEQ ID No: 306. This enzyme is believed to have oxidation reduction activity.
[0276] The enzyme identified as Sequence Oxid-154 scaffold00050.G279 1167_g, 2268_g, 2269_g, scaffold00050.pathl .genel l6, scaffold00050.pathl .genel l7 (CL10139 CL10141 CL10140) is encoded by the nucleotides of SEQ ID No: 307 which encodes the amino acid sequence of SEQ ID No: 308. This enzyme is believed to have oxidation reduction activity.
[0277] The enzyme identified as Sequence Oxid-155 scaffold00050.G298 2280_g, 228 l_g, scaffold00050.pathl .genel29, scaffold00050.pathl .genel30 (CL10151) is encoded by the nucleotides of SEQ ID No: 309 which encodes the amino acid sequence of SEQ ID No: 310. This enzyme is believed to have oxidation reduction activity.
[0278] The enzyme identified as Sequence Oxid-156 scaffold00050.G308 (CL10159) is encoded by the nucleotides of SEQ ID No: 311 which encodes the amino acid sequence of SEQ ID No: 312. This enzyme is believed to have monooxygenase activity.
[0279] The enzyme identified as Sequence Oxid-157 scaffold00050.G397 234 l_g, 2342_g, scaffold00050.pathl .genel87 (CL10213) is encoded by the nucleotides of SEQ ID No: 313 which encodes the amino acid sequence of SEQ ID No: 314. This enzyme is believed to have oxidation reduction activity.
[0280] The enzyme identified as Sequence Oxid-158 scaffold00050.G524 2417_g,
scaffold00050.pathl .gene246 (CL10291) is encoded by the nucleotides of SEQ ID No: 315 which encodes the amino acid sequence of SEQ ID No: 316. This enzyme is believed to have flavin-containing monooxygenase activity.
[0281] The enzyme identified as Sequence Oxid-159 scaffold00050.G695 2516_g,
scaffold00050.pathl .gene325 (CL10405) is encoded by the nucleotides of SEQ ID No: 317 which encodes the amino acid sequence of SEQ ID No: 318. This enzyme is believed to have kynurenine 3 -monooxygenase activity.
[0282] The enzyme identified as Sequence Oxid-160 scaffold00050.G900 2632_g,
scaffold00050.pathl .gene425 (CL10527) is encoded by the nucleotides of SEQ ID No: 319 which encodes the amino acid sequence of SEQ ID No: 320. This enzyme is believed to have flavin-containing monooxygenase activity.
[0283] The enzyme identified as Sequence Oxid-161 scaffold00050.G1038 2725_g,
scaffold00050.pathl .gene511 (CL10614) is encoded by the nucleotides of SEQ ID No: 321 which encodes the amino acid sequence of SEQ ID No: 322. This enzyme is believed to have monooxygenase activity.
[0284] The enzyme identified as Sequence Oxid-162 scaffold00050.G1041 2727_g scaffold00050.pathl .gene514 is encoded by the nucleotides of SEQ ID No: 323 which encodes the amino acid sequence of SEQ ID No: 324. This enzyme is believed to have monooxygenase activity.
[0285] The enzyme identified as Sequence Oxid-163 scaffold00050.G1042 2729_g
scaffold00050.pathl .gene515 (CL10617) is encoded by the nucleotides of SEQ ID
No: 325 which encodes the amino acid sequence of SEQ ID No: 326. This enzyme is believed to have monooxygenase activity.
[0286] The enzyme identified as Sequence Oxid-164 scaffold00050.G1359 2937_g
scaffold00050.pathl .gene702 (CL10825) is encoded by the nucleotides of SEQ ID
No: 327 which encodes the amino acid sequence of SEQ ID No: 328. This enzyme is believed to have monooxygenase activity.
[0287] The enzyme identified as Sequence Oxid-165 scaffold00050.G1435 2987_g
scaffold00050.pathl .gene747 (CL10883) is encoded by the nucleotides of SEQ ID
No: 329 which encodes the amino acid sequence of SEQ ID No: 330. This enzyme is believed to have monooxygenase activity.
[0288] The enzyme identified as Sequence Oxid-166 scaffold00050.G1590 3068_g
scaffold00050.pathl .gene821 (CL10975) is encoded by the nucleotides of SEQ ID
No: 331 which encodes the amino acid sequence of SEQ ID No: 332. This enzyme is believed to have monooxygenase activity.
[0289] The enzyme identified as Sequence Oxid-167 scaffold00050.G1619 3091_g
scaffold00050.pathl .gene838 (CL10989) is encoded by the nucleotides of SEQ ID
No: 333 which encodes the amino acid sequence of SEQ ID No: 334. This enzyme is believed to have monooxygenase activity.
[0290] The enzyme identified as Sequence Oxid-168 scaffold00053.G27 3152_g
scaffold00053.pathl .genel3 (CL11584) is encoded by the nucleotides of SEQ ID
No: 335 which encodes the amino acid sequence of SEQ ID No: 336. This enzyme is believed to have monooxygenase activity.
[0291] The enzyme identified as Sequence Oxid-169 scaffold00053.G67 3168_g
scaffold00053.pathl .gene26 (CL11558) is encoded by the nucleotides of SEQ ID
No: 337 which encodes the amino acid sequence of SEQ ID No: 338. This enzyme is believed to have monooxygenase activity.
[0292] The enzyme identified as Sequence Oxid-170 scaffold00071.G796 3733_g
scaffold00071.pathl .gene427 (CL00475 CL00476) is encoded by the nucleotides of SEQ ID No: 339 which encodes the amino acid sequence of SEQ ID No: 340. This enzyme is believed to have phenol 2-monooxygenase activity.
[0293] The enzyme identified as Sequence Oxid-171 scaffold00071.G797 3734_g
scaffold00071.pathl .gene427 is encoded by the nucleotides of SEQ ID No: 341 which encodes the amino acid sequence of SEQ ID No: 342. This enzyme is believed to have monooxygenase activity.
[0294] The enzyme identified as Sequence Oxid-172 scaffold00071.G852 3775_g
scaffold00071.pathl .gene459 (CL00510) is encoded by the nucleotides of SEQ ID No: 343 which encodes the amino acid sequence of SEQ ID No: 344. This enzyme is believed to have monophenol monooxygenase activity.
[0295] The enzyme identified as Sequence Oxid-173 scaffold00071.G897 3805_g
scaffold00071.pathl .gene492 (CL00537) is encoded by the nucleotides of SEQ ID No: 345 which encodes the amino acid sequence of SEQ ID No: 346. This enzyme is believed to have dopamine beta-monooxygenase activity.
[0296] The enzyme identified as Sequence Oxid-174 scaffold00071.G1032 3903_g
scaffold00071.pathl .gene580 (CL00621) is encoded by the nucleotides of SEQ ID No: 347 which encodes the amino acid sequence of SEQ ID No: 348. This enzyme is believed to have monooxygenase activity.
[0297] The enzyme identified as Sequence Oxid-175 scaffold00071.Gl 138 3965_g
scaffold00071.pathl .gene621 (CL00688 CL08353 CL01496 CL03246) is encoded by the nucleotides of SEQ ID No: 349 which encodes the amino acid sequence of SEQ ID No: 350. This enzyme is believed to have flavin-containing
monooxygenase activity.
[0298] The enzyme identified as Sequence Oxid-176 scaffold00071.G1646 4268_g
scaffold00071.pathl .gene875 (CL08558 CL00981) is encoded by the nucleotides of SEQ ID No: 351 which encodes the amino acid sequence of SEQ ID No: 352. This enzyme is believed to have flavin-containing monooxygenase activity.
[0299] The enzyme identified as Sequence Oxid-177 scaffold00071.G1884 4431_g
scaffold00071.pathl .genel020 (CL01129) is encoded by the nucleotides of SEQ ID No: 353 which encodes the amino acid sequence of SEQ ID No: 354. This enzyme is believed to have lactate 2-monooxygenase activity.
[0300] The enzyme identified as Sequence Oxid-178 scaffold00071.G2181 4623_g
scaffold00071.pathl .genel 187, scaffold00071.pathl .genel 188 (CL07578 CL01313) is encoded by the nucleotides of SEQ ID No: 355 which encodes the amino acid sequence of SEQ ID No: 356. This enzyme is believed to have monooxygenase activity.
[0301] The enzyme identified as Sequence Oxid-179 scaffold00071.G2310 4698_g
scaffold00071.pathl .genel245, scaffold00071.pathl .genel246 (CL01384) is encoded by the nucleotides of SEQ ID No: 357 which encodes the amino acid sequence of SEQ ID No: 358. This enzyme is believed to have flavin-containing monooxygenase activity.
[0302] The enzyme identified as Sequence Oxid-180 scaffold00071.G3395 5346_g
scaffold00071.pathl .genel812 (CL11406) is encoded by the nucleotides of SEQ ID No: 359 which encodes the amino acid sequence of SEQ ID No: 360. This enzyme is believed to have monooxygenase activity.
[0303] The enzyme identified as Sequence Oxid-181 scaffold00075.G661 581 l_g
scaffold00075.pathl .gene356 (CL03408) is encoded by the nucleotides of SEQ ID No: 361 which encodes the amino acid sequence of SEQ ID No: 362. This enzyme is believed to have monooxygenase activity.
[0304] The enzyme identified as Sequence Oxid-182 scaffold00075.G806 5910_g
scaffold00075.pathl .gene444 (CL03483) is encoded by the nucleotides of SEQ ID No: 363 which encodes the amino acid sequence of SEQ ID No: 364. This enzyme is believed to have squalene monooxygenase activity.
[0305] The enzyme identified as Sequence Oxid-183 scaffold00075.G834 5928_g
scaffold00075.pathl .gene459 (CL03497) is encoded by the nucleotides of SEQ ID No: 365 which encodes the amino acid sequence of SEQ ID No: 366. This enzyme is believed to have deoxyhypusine monooxygenase activity.
[0306] The enzyme identified as Sequence Oxid-184 scaffold00092.G3 (CL05970) is encoded by the nucleotides of SEQ ID No: 367 which encodes the amino acid sequence of SEQ ID No: 368. This enzyme is believed to have monooxygenase activity.
[0307] The enzyme identified as Sequence Oxid-185 scaffold00092.G38 6265_g
scaffold00092.pathl .gene20 (CL05985) is encoded by the nucleotides of SEQ ID No: 369 which encodes the amino acid sequence of SEQ ID No: 370. This enzyme is believed to have monooxygenase activity.
[0308] The enzyme identified as Sequence Oxid-186 scaffold00092.G71 6289_g scaffold00092.pathl .gene41 (CL06010) is encoded by the nucleotides of SEQ ID No: 371 which encodes the amino acid sequence of SEQ ID No: 372. This enzyme is believed to have monooxygenase activity.
[0309] The enzyme identified as Sequence Oxid-187 scaffold00092.G73 629 l_g
scaffold00092.pathl .gene42 (CL06011 CL06012) is encoded by the nucleotides of SEQ ID No: 373 which encodes the amino acid sequence of SEQ ID No: 374. This enzyme is believed to have monooxygenase activity.
[0310] The enzyme identified as Sequence Oxid-188 scaffold00092.G89 (CL06022) is encoded by the nucleotides of SEQ ID No: 375 which encodes the amino acid sequence of SEQ ID No: 376. This enzyme is believed to have monooxygenase activity.
[0311] The enzyme identified as Sequence Oxid-189 scaffold00092.G158 (CL06068) is encoded by the nucleotides of SEQ ID No: 377 which encodes the amino acid sequence of SEQ ID No: 378. This enzyme is believed to have monooxygenase activity.
[0312] The enzyme identified as Sequence Oxid-190 scaffold00092.G332 (CL06172) is encoded by the nucleotides of SEQ ID No: 379 which encodes the amino acid sequence of SEQ ID No: 380. This enzyme is believed to have monooxygenase activity.
[0313] The enzyme identified as Sequence Oxid-191 scaffold00105.G2 is encoded by the nucleotides of SEQ ID No: 381 which encodes the amino acid sequence of SEQ ID No: 382. This enzyme is believed to have flavin-containing monooxygenase activity.
[0314] The enzyme identified as Sequence Oxid-192 scaffoldOOl 15.G2 (CL08560) is
encoded by the nucleotides of SEQ ID No: 383 which encodes the amino acid sequence of SEQ ID No: 384. This enzyme is believed to have monooxygenase activity.
[0315] The enzyme identified as Sequence Oxid-193 scaffold00120.Gl is encoded by the nucleotides of SEQ ID No: 385 which encodes the amino acid sequence of SEQ ID No: 386. This enzyme is believed to have monooxygenase activity.
[0316] The enzyme identified as Sequence Oxid-194 scaffold00120.G2 (CL04452) is
encoded by the nucleotides of SEQ ID No: 387 which encodes the amino acid sequence of SEQ ID No: 388. This enzyme is believed to have monooxygenase activity.
[0317] The enzyme identified as Sequence Oxid-195 scaffold00122.G64 (CL03833
CL03832) is encoded by the nucleotides of SEQ ID No: 389 which encodes the amino acid sequence of SEQ ID No: 390. This enzyme is believed to have monooxygenase activity.
[0318] The enzyme identified as Sequence Oxid-196 scaffold00122.G80 (CL03841) is encoded by the nucleotides of SEQ ID No: 391 which encodes the amino acid sequence of SEQ ID No: 392. This enzyme is believed to have monooxygenase activity.
[0319] The enzyme identified as Sequence Oxid-197 scaffold00122.G198 (CL03918) is encoded by the nucleotides of SEQ ID No: 393 which encodes the amino acid sequence of SEQ ID No: 394. This enzyme is believed to have monooxygenase activity.
[0320] The enzyme identified as Sequence Oxid-198 scaffold00122.G199 (CL03919) is encoded by the nucleotides of SEQ ID No: 395 which encodes the amino acid sequence of SEQ ID No: 396. This enzyme is believed to have monooxygenase activity.
[0321] The enzyme identified as Sequence Oxid-199 scaffold00122.G202 (CL03922) is encoded by the nucleotides of SEQ ID No: 397 which encodes the amino acid sequence of SEQ ID No: 398. This enzyme is believed to have monooxygenase activity.
[0322] The enzyme identified as Sequence Oxid-200 scaffold00131.G83 (CL06009
CL04267) is encoded by the nucleotides of SEQ ID No: 399 which encodes the amino acid sequence of 400. This enzyme is believed to have monooxygenase activity.
[0323] The enzyme identified as Sequence Oxid-201 scaffold00131.G363 is encoded by the nucleotides of SEQ ID No: 401 which encodes the amino acid sequence of SEQ ID No: 402. This enzyme is believed to have monooxygenase activity.
[0324] The enzyme identified as Sequence Oxid-202 scaffold00131.G364 (CL04453) is encoded by the nucleotides of SEQ ID No: 403 which encodes the amino acid sequence of SEQ ID No: 404. This enzyme is believed to have monooxygenase activity.
[0325] The enzyme identified as Sequence Oxid-203 scaffold00131.G446 is encoded by the nucleotides of SEQ ID No: 405 which encodes the amino acid sequence of SEQ ID No: 406. This enzyme is believed to have flavin-containing monooxygenase activity CL04492 activity.
[0326] The enzyme identified as Sequence Oxid-204 scaffold00131.G752 (CL04674) is encoded by the nucleotides of SEQ ID No: 407 which encodes the amino acid sequence of SEQ ID No: 408. This enzyme is believed to have phenol 2- monooxygenase activity.
[0327] The enzyme identified as Sequence Oxid-205 scaffold00131.G875 (CL04745) is encoded by the nucleotides of SEQ ID No: 409 which encodes the amino acid sequence of SEQ ID No: 410. This enzyme is believed to have flavin-containing monooxygenase activity.
[0328] The enzyme identified as Sequence Oxid-206 scaffold00131.G941 (CL04795
CL04796) is encoded by the nucleotides of SEQ ID No: 411 which encodes the amino acid sequence of SEQ ID No: 412. This enzyme is believed to have benzoate 4-monooxygenase activity.
[0329] The enzyme identified as Sequence Oxid-207 scaffold00131.Gl 166 (CL04936) is encoded by the nucleotides of SEQ ID No: 413 which encodes the amino acid sequence of SEQ ID No: 414. This enzyme is believed to have monooxygenase activity.
[0330] The enzyme identified as Sequence Oxid-208 scaffold00131.G1265 is encoded by the nucleotides of SEQ ID No: 415 which encodes the amino acid sequence of SEQ ID No: 416. This enzyme is believed to have monooxygenase activity.
[0331] The enzyme identified as Sequence Oxid-209 scaffold00131.G1806 (CL05310) is encoded by the nucleotides of SEQ ID No: 417 which encodes the amino acid sequence of SEQ ID No: 418. This enzyme is believed to have monooxygenase activity.
[0332] The enzyme identified as Sequence Oxid-210 scaffold00142.G365 (CL08556
CL05012 CL08560 CL08557) is encoded by the nucleotides of SEQ ID No: 419 which encodes the amino acid sequence of SEQ ID No: 420. This enzyme is believed to have monooxygenase activity.
[0333] The enzyme identified as Sequence Oxid-211 scaffold00142.G368 is encoded by the nucleotides of SEQ ID No: 421 which encodes the amino acid sequence of SEQ ID No: 422. This enzyme is believed to have flavin-containing monooxygenase activity.
[0334] The enzyme identified as Sequence Oxid-212 scaflbld00142.G370 is encoded by the nucleotides of SEQ ID No: 423 which encodes the amino acid sequence of SEQ ID No: 424. This enzyme is believed to have monooxygenase activity.
[0335] The enzyme identified as Sequence Oxid-213 scaffold00142.G465 (CL08624) is encoded by the nucleotides of SEQ ID No: 425 which encodes the amino acid sequence of SEQ ID No: 426. This enzyme is believed to have monooxygenase activity.
[0336] The enzyme identified as Sequence Oxid-214 scaffold00142.G579 (CL08695
CL05970) is encoded by the nucleotides of SEQ ID No: 427 which encodes the amino acid sequence of SEQ ID No: 428. This enzyme is believed to have monooxygenase activity.
[0337] The enzyme identified as Sequence Oxid-215 scaffold00142.G589 is encoded by the nucleotides of SEQ ID No: 429 which encodes the amino acid sequence of SEQ ID No: 430. This enzyme is believed to have monooxygenase activity.
[0338] The enzyme identified as Sequence Oxid-216 scaffold00169.G30 (CL07907) is encoded by the nucleotides of SEQ ID No: 431 which encodes the amino acid sequence of SEQ ID No: 432. This enzyme is believed to have monooxygenase activity.
[0339] The enzyme identified as Sequence Oxid-217 scaffold00169.G35 (CL07903
CL11558 CL07902) is encoded by the nucleotides of SEQ ID No: 433 which encodes the amino acid sequence of SEQ ID No: 434. This enzyme is believed to have monooxygenase activity.
[0340] The enzyme identified as Sequence Oxid-218 scaffold00169.G288 (CL07724) is encoded by the nucleotides of SEQ ID No: 435 which encodes the amino acid sequence of SEQ ID No: 436. This enzyme is believed to have monooxygenase activity.
[0341] The enzyme identified as Sequence Oxid-219 scaffold00169.G316 (CL07703) is encoded by the nucleotides of SEQ ID No: 437 which encodes the amino acid sequence of SEQ ID No: 438. This enzyme is believed to have flavin-containing monooxygenase activity.
[0342] The enzyme identified as Sequence Oxid-220 scaffold00169.G318 (CL07702) is encoded by the nucleotides of SEQ ID No: 439 which encodes the amino acid sequence of SEQ ID No: 440. This enzyme is believed to have flavin-containing monooxygenase activity.
[0343] The enzyme identified as Sequence Oxid-221 scaffold00169.G321 (CL07700) is encoded by the nucleotides of SEQ ID No: 441 which encodes the amino acid sequence of SEQ ID No: 442. This enzyme is believed to have monooxygenase activity.
[0344] The enzyme identified as Sequence Oxid-222 scaffold00169.G325 (CL07697) is encoded by the nucleotides of SEQ ID No: 443 which encodes the amino acid sequence of SEQ ID No: 444. This enzyme is believed to have flavin-containing monooxygenase activity.
[0345] The enzyme identified as Sequence Oxid-223 scaffold00169.G402 (CL07634) is encoded by the nucleotides of SEQ ID No: 445 which encodes the amino acid sequence of SEQ ID No: 446. This enzyme is believed to have monooxygenase activity.
[0346] The enzyme identified as Sequence Oxid-224 scaffold00169.G442 (CL07610) is encoded by the nucleotides of SEQ ID No: 447 which encodes the amino acid sequence of SEQ ID No: 448. This enzyme is believed to have monooxygenase activity.
[0347] The enzyme identified as Sequence Oxid-225 scaffold00214.G9 (CL02472) is encoded by the nucleotides of SEQ ID No: 449 which encodes the amino acid sequence of SEQ ID No: 450. This enzyme is believed to have monooxygenase activity.
[0348] The enzyme identified as Sequence Oxid-226 scaffold00214.G10 is encoded by the nucleotides of SEQ ID No: 451 which encodes the amino acid sequence of SEQ ID No: 452. This enzyme is believed to have monooxygenase activity.
[0349] The enzyme identified as Sequence Oxid-227 scaffold00214.G22 (CL02480
CL02481) is encoded by the nucleotides of SEQ ID No: 453 which encodes the amino acid sequence of SEQ ID No: 454. This enzyme is believed to have monooxygenase activity.
[0350] The enzyme identified as Sequence Oxid-228 scaffold00227.G204 (CL08208) is encoded by the nucleotides of SEQ ID No: 455 which encodes the amino acid sequence of SEQ ID No: 456. This enzyme is believed to have monooxygenase activity. [0351] The enzyme identified as Sequence Oxid-229 scaffold00227.G683 (CL08810
CL07938) is encoded by the nucleotides of SEQ ID No: 457 which encodes the amino acid sequence of SEQ ID No: 458. This enzyme is believed to have monooxygenase activity.
[0352] The enzyme identified as Sequence Oxid-230 scaffold00050.G1657 (CL11016) is encoded by the nucleotides of SEQ ID No: 459 which encodes the amino acid sequence of SEQ ID No: 460. This enzyme is believed to have NADPH-hemo Protein reductase activity.
[0353] The enzyme identified as Sequence Oxid-231 scaffold00068.Gl is encoded by the nucleotides of SEQ ID No: 461 which encodes the amino acid sequence of SEQ ID No: 462. This enzyme is believed to have oxidoreductase activity, acting on paired activity.
[0354] The enzyme identified as Sequence Oxid-232 scaffold00071.G571 (CL00326) is encoded by the nucleotides of SEQ ID No: 463 which encodes the amino acid sequence of SEQ ID No: 464. This enzyme is believed to have sterol 14- demethylase activity.
[0355] The enzyme identified as Sequence Oxid-233 scaffold00071.G633 is encoded by the nucleotides of SEQ ID No: 465 which encodes the amino acid sequence of SEQ ID No: 466. This enzyme is believed to have oxidoreductase activity, acting on paired d activity.
[0356] The enzyme identified as Sequence Oxid-234 scaffold00071.G634 (CL00365) is encoded by the nucleotides of SEQ ID No: 467 which encodes the amino acid sequence of SEQ ID No: 468. This enzyme is believed to have oxidoreductase activity, acting on paired d activity.
[0357] The enzyme identified as Sequence Oxid-235 scaffold00071.G1361 (CL00816) is encoded by the nucleotides of SEQ ID No: 469 which encodes the amino acid sequence of SEQ ID No: 470. This enzyme is believed to have oxidoreductase activity, acting on paired d activity.
[0358] The enzyme identified as Sequence Oxid-236 scaffold00071.G1662 (CL00992) is encoded by the nucleotides of SEQ ID No: 471 which encodes the amino acid sequence of SEQ ID No: 472. This enzyme is believed to have oxidoreductase activity, acting on paired d activity.
[0359] The enzyme identified as Sequence Oxid-237 scaffold00071.G1865 (CLOU 14) is encoded by the nucleotides of SEQ ID No: 473 which encodes the amino acid sequence of SEQ ID No: 474. This enzyme is believed to have oxidoreductase activity, acting on paired d activity.
[0360] The enzyme identified as Sequence Oxid-238 scaffold00092.G20 (CL05975) is encoded by the nucleotides of SEQ ID No: 475 which encodes the amino acid sequence of SEQ ID No: 476. This enzyme is believed to have NADPH-hemo Protein reductase activity.
[0361] The enzyme identified as Sequence Oxid-239 scaffold00092.G200 (CL06088
CL06087) is encoded by the nucleotides of SEQ ID No: 477 which encodes the amino acid sequence of SEQ ID No: 478. This enzyme is believed to have oxidoreductase activity, acting on paired d activity.
[0362] The enzyme identified as Sequence Oxid-240 scaffold00227.G102 (CL08261) is encoded by the nucleotides of SEQ ID No: 479 which encodes the amino acid sequence of SEQ ID No: 480. This enzyme is believed to have oxidoreductase activity, acting on paired d activity.
[0363] The enzyme identified as Sequence Oxid-241 scaffold00071.G592 (CL00336) is encoded by the nucleotides of SEQ ID No: 481 which encodes the amino acid sequence of SEQ ID No: 482. This enzyme is believed to have succinate dehydrogenase (ubiquinone) activity
[0364] The enzyme identified as Sequence Oxid-242 scaffold00142.G540 (CL08666) is encoded by the nucleotides of SEQ ID No: 483 which encodes the amino acid sequence of SEQ ID No: 484. This enzyme is believed to have activity.
[0365] The enzyme identified as Sequence Oxid-243 scaffold00031.G1485 (CL02772) is encoded by the nucleotides of SEQ ID No: 485 which encodes the amino acid sequence of SEQ ID No: 486. This enzyme is believed to have chitin binding activity.
[0366] The enzyme identified as Sequence Oxid-244 scaffold00071.G1644 (CL00980) is encoded by the nucleotides of SEQ ID No: 487 which encodes the amino acid sequence of SEQ ID No: 488. This enzyme is believed to have ATP-binding Hydrolase Lipid degradation activity.
[0367] The enzyme identified as Sequence Oxid-245 scaffold00131.G793 (CL04696) is encoded by the nucleotides of SEQ ID No: 489 which encodes the amino acid sequence of SEQ ID No: 490. This enzyme is believed to have oxidoreductase activity, Glucooligosaccharide oxidase putative activity.
[0368] The enzyme identified as Sequence Oxid-246 scaffold00131.G1570 (CL05186) is encoded by the nucleotides of SEQ ID No: 491 which encodes the amino acid sequence of SEQ ID No: 492. This enzyme is believed to have defense response to fungus and seems to be a combination between manganese peroxidase (MnP) and a (number of) carbohydrate binding domain(s). activity.
[0369] The enzyme identified as Sequence Oxid-247 scaffold00169.G412 (CL07628) is encoded by the nucleotides of SEQ ID No: 493 which encodes the amino acid sequence of SEQ ID No: 494. This enzyme is believed to have oxidoreductase activity, lactose oxidase activity.
[0370] The enzyme identified as Sequence Oxid-248iiscaffold00131.pathl .gene468
(CL04696) is encoded by the nucleotides of SEQ ID No: 495 which encodes the amino acid sequence of SEQ ID No: 496. This enzyme is believed to have oxidoreductase activity.
[0371] The enzyme identified as Sequence Oxid-249 scaffold00092.G538 (CL06304) is encoded by the nucleotides of SEQ ID No: 497 which encodes the amino acid sequence of SEQ ID No: 498. This enzyme is believed to have cytochrome-b5 reductase activity.
[0372] The enzyme identified as Sequence Oxid-250 scaffold00050.G497 (CL02826
CL 10276) is encoded by the nucleotides of SEQ ID No: 499 which encodes the amino acid sequence of 500. This enzyme is believed to have oxidoreductase activity.
[0373] The enzyme identified as Sequence Oxid-251 scaffold00050.pathl .gene232
(CL10276) is encoded by the nucleotides of SEQ ID No: 501 which encodes the amino acid sequence of SEQ ID No: 502. This enzyme is believed to have oxidoreductase activity.
[0374] The enzyme identified as Sequence Oxid-252 scaffold00071.G2538 (CL01543) is encoded by the nucleotides of SEQ ID No: 503 which encodes the amino acid sequence of SEQ ID No: 504. This enzyme is believed to have oxidoreductase activity.
[0375] The enzyme identified as Sequence Oxid-253 scaffold00131.G2158 (CL05501) is encoded by the nucleotides of SEQ ID No: 505 which encodes the amino acid sequence of SEQ ID No: 506. This enzyme is believed to have copper ion binding, oxidoreductase activity, Laccase activity.
[0376] The enzyme identified as Sequence Oxid-254 scaffold00142.G37 (CL08347) is encoded by the nucleotides of SEQ ID No: 507 which encodes the amino acid sequence of SEQ ID No: 508. This enzyme is believed to have copper ion binding, oxidoreductase activity.
[0377] The enzyme identified as Sequence Oxid-255 scaffold00016.G641 (CL09304) is encoded by the nucleotides of SEQ ID No: 509 which encodes the amino acid sequence of SEQ ID No: 510. This enzyme is believed to have glycerol-3- phosphate dehydrogenase activity.
[0378] The enzyme identified as Sequence Oxid-256 scaffold00031.G565 (CL06842
CL06843) (Cytochrome) is encoded by the nucleotides of SEQ ID No: 511 which encodes the amino acid sequence of SEQ ID No: 512. This enzyme is believed to have D-lactate dehydrogenase activity.
[0379] The enzyme identified as Sequence Oxid-257 scaffold00031.G638 (CL06798
CL06797) is encoded by the nucleotides of SEQ ID No: 513 which encodes the amino acid sequence of SEQ ID No: 514. This enzyme is believed to have FAD
Flavo Protein, tRNA dihydrouridine synthase activity.
[0380] The enzyme identified as Sequence Oxid-258 scaffold00031.G851 (CL06688)
activity is encoded by the nucleotides of SEQ ID No: 515 which encodes the amino acid sequence of SEQ ID No: 516. This enzyme is believed to have FAD Flavo
Protein, NADH dehydrogenase (ubiquinone) activity.
[0381] The enzyme identified as Sequence Oxid-259 scaffold00031.G1052 (CL06572) activity is encoded by the nucleotides of SEQ ID No: 517 which encodes the amino acid sequence of SEQ ID No: 518. This enzyme is believed to have FAD Flavo
Protein, NADH dehydrogenase (ubiquinone) activity.
[0382] The enzyme identified as Sequence Oxid-260 scaffold00031.Gl 199 (CL02964) is encoded by the nucleotides of SEQ ID No: 519 which encodes the amino acid sequence of SEQ ID No: 520. This enzyme is believed to have FMN Flavo Protein,
NADPH dehydrogenase activity.
[0383] The enzyme identified as Sequence Oxid-261 scaffold00031.G1320 (CL02890) is encoded by the nucleotides of SEQ ID No: 521 which encodes the amino acid sequence of SEQ ID No: 522. This enzyme is believed to have FAD flavo protein, acyl-CoA dehydrogenase activity. [0384] The enzyme identified as Sequence Oxid-262 scaffold00050.G972 (CL10574) is encoded by the nucleotides of SEQ ID No: 523 which encodes the amino acid sequence of SEQ ID No: 524. This enzyme is believed to have FAD flavo protein, acyl-CoA dehydrogenase activity.
[0385] The enzyme identified as Sequence Oxid-263 scaffold00050.G1269 (CL10770) is encoded by the nucleotides of SEQ ID No: 525 which encodes the amino acid sequence of SEQ ID No: 526. This enzyme is believed to have disulfide bond FAD Flavo Protein, dihydrolipoyl dehydrogenase activity.
[0386] The enzyme identified as Sequence Oxid-264 scaffold00050.G1295 (CL10786) is encoded by the nucleotides of SEQ ID No: 527 which encodes the amino acid sequence of SEQ ID No: 528. This enzyme is believed to have electron transport FAD flavo protein mitochondrion respiratory chain transit peptide transport activity.
[0387] The enzyme identified as Sequence Oxid-265 scaffold00050.G1321 (CL10801) is encoded by the nucleotides of SEQ ID No: 529 which encodes the amino acid sequence of SEQ ID No: 530. This enzyme is believed to have FMN Flavo Protein, photoreceptor activity, transcription factor activity.
[0388] The enzyme identified as Sequence Oxid-266 scaffold00050.G1429 (CL10879) is encoded by the nucleotides of SEQ ID No: 531 which encodes the amino acid sequence of SEQ ID No: 532. This enzyme is believed to have Cadmium Disulfide bond FAD Flavo Protein, oxidoreductase activity, acting on sulfur g activity.
[0389] The enzyme identified as Sequence Oxid-267 scaffold00071.G59 (CL00036) is encoded by the nucleotides of SEQ ID No: 533 which encodes the amino acid sequence of SEQ ID No: 534. This enzyme is believed to have FAD Flavo Protein, D-lactate dehydrogenase (Cytochrome) activity.
[0390] The enzyme identified as Sequence Oxid-268 scaffold00071.G556 (CL00318) is encoded by the nucleotides of SEQ ID No: 535 which encodes the amino acid sequence of SEQ ID No: 536. This enzyme is believed to have Cytoplasm FAD Flavo Protein, tRNA dihydrouridine synthase activity.
[0391] The enzyme identified as Sequence Oxid-269 scaffold00071.G744 (CL00443) is encoded by the nucleotides of SEQ ID No: 537 which encodes the amino acid sequence of SEQ ID No: 538. This enzyme is believed to have Cytoplasm FAD Flavo Protein, tRNA dihydrouridine synthase activity. [0392] The enzyme identified as Sequence Oxid-270 scaffold00071.G1440 (CL00865) is encoded by the nucleotides of SEQ ID No: 539 which encodes the amino acid sequence of SEQ ID No: 540. This enzyme is believed to have FMN Flavo Protein, NADPH dehydrogenase activity.
[0393] The enzyme identified as Sequence Oxid-271 scaffold00071.G2386 (CL01424) is encoded by the nucleotides of SEQ ID No: 541 which encodes the amino acid sequence of SEQ ID No: 542. This enzyme is believed to have heme binding, L- lactate dehydrogenase (Cytochrome) activity.
[0394] The enzyme identified as Sequence Oxid-272 scaffold00071.G2604 (CL01584) is encoded by the nucleotides of SEQ ID No: 543 which encodes the amino acid sequence of SEQ ID No: 544. This enzyme is believed to have FMN binding activity.
[0395] The enzyme identified as Sequence Oxid-273 scaffold00075.G430 (CL03269) is encoded by the nucleotides of SEQ ID No: 545 which encodes the amino acid sequence of SEQ ID No: 546. This enzyme is believed to have oxidoreductase activity.
[0396] The enzyme identified as Sequence Oxid-274 scaffold00075.G449 (CL03284) is encoded by the nucleotides of SEQ ID No: 547 which encodes the amino acid sequence of SEQ ID No: 548. This enzyme is believed to have FAD FMN Flavo Protein, oxidoreductase activity TAH18 GIBZE | FAD FMN Flavo Protein NADP Oxidoreductase PF00667 PF00258 PF00175 GO:0010181 F:FMN binding
GO:0005506 F: iron ion binding GO:0016491 F:oxidoreductase activity
GO:0055114 P:oxidation reduction activity.
[0397] The enzyme identified as Sequence Oxid-275 scaffold00075.G652 (CL03401) is encoded by the nucleotides of SEQ ID No: 549 which encodes the amino acid sequence of SEQ ID No: 550. This enzyme is believed to have NADPH-hemo Protein reductase activity.
[0398] The enzyme identified as Sequence Oxid-276 scaffold00075.G818 (Cytochrome) is encoded by the nucleotides of SEQ ID No: 551 which encodes the amino acid sequence of SEQ ID No: 552. This enzyme is believed to have L-lactate dehydrogenase (Cytochrome) activity.
[0399] The enzyme identified as Sequence Oxid-277 scaffold00092.G461 (CL06252) is encoded by the nucleotides of SEQ ID No: 553 which encodes the amino acid sequence of SEQ ID No: 554. This enzyme is believed to have FMN binding activity.
[0400] The enzyme identified as Sequence Oxid-278 scaffold00131.G685 (CL04637) is encoded by the nucleotides of SEQ ID No: 555 which encodes the amino acid sequence of SEQ ID No: 556. This enzyme is believed to have oxidoreductase activity.
[0401] The enzyme identified as Sequence Oxid-279 scaffold00131.G729 (CL04661) is encoded by the nucleotides of SEQ ID No: 557 which encodes the amino acid sequence of SEQ ID No: 558. This enzyme is believed to have FMN binding activity.
[0402] The enzyme identified as Sequence Oxid-280 scaffold00131.G1632 (CL05218) is encoded by the nucleotides of SEQ ID No: 559 which encodes the amino acid sequence of SEQ ID No: 560. This enzyme is believed to have heme binding, L- lactate dehydrogenase (Cytochrome) activity.
[0403] The enzyme identified as Sequence Oxid-281 scaffold00214.G35 (CL02491) is encoded by the nucleotides of SEQ ID No: 561 which encodes the amino acid sequence of SEQ ID No: 562. This enzyme is believed to have FMN binding activity.
[0404] The enzyme identified as Sequence Oxid-282 scaffold00214.G73 (CL02521) is encoded by the nucleotides of SEQ ID No: 563 which encodes the amino acid sequence of SEQ ID No: 564. This enzyme is believed to have heme binding, sulfite reductase (NADPH)
[0405] The enzyme identified as Sequence Oxid-283 scaffold00227.G366 (CL08117) is encoded by the nucleotides of SEQ ID No: 565 which encodes the amino acid sequence of SEQ ID No: 566. This enzyme is believed to have NAD or NADH binding, NADH dehydrogenase (ubiquinone)
[0406] The enzyme identified as Sequence Oxid-284 scaffold00227.G646 (CL07959) is encoded by the nucleotides of SEQ ID No: 567 which encodes the amino acid sequence of SEQ ID No: 568. This enzyme is believed to have sulfite reductase (NADPH)
[0407] The enzyme identified as Sequence Oxid-285 scaffold00227.G647 (CL07958) is encoded by the nucleotides of SEQ ID No: 569 which encodes the amino acid sequence of SEQ ID No: 570. This enzyme is believed to have Metal-binding Mitochondrion NAD Oxidoreductase, alcohol dehydrogenase activity.
[0408] The enzyme identified as Sequence Oxid-286 scaffbld00071.G964 (CL00580) is encoded by the nucleotides of SEQ ID No: 571 which encodes the amino acid sequence of SEQ ID No: 572. This enzyme is believed to have FMN binding, oxidoreductase activity.
[0409] The enzyme identified as Sequence Oxid-287 scaffold00071.G874 (CL00522) is encoded by the nucleotides of SEQ ID No: 573 which encodes the amino acid sequence of SEQ ID No: 574. This enzyme is believed to have fumarate reductase
(NADH) activity, succinate dehydrogenase activity
[0410] The enzyme identified as Sequence Oxid-288 scaffold00071.G901 (CL00541) is encoded by the nucleotides of SEQ ID No: 575 which encodes the amino acid sequence of SEQ ID No: 576. This enzyme is believed to have FAD binding, tRNA dihydrouridine synthase activity.
[0411] The enzyme identified as Sequence Oxid-289 scaffold00071.G1736 (CL01038) is encoded by the nucleotides of SEQ ID No: 577 which encodes the amino acid sequence of SEQ ID No: 578. This enzyme is believed to have cytochrome-b5 reductase activity.
[0412] The enzyme identified as Sequence Oxid-290 scaffold00071.G2980 (CL01805) is encoded by the nucleotides of SEQ ID No: 579 which encodes the amino acid sequence of SEQ ID No: 580. This enzyme is believed to have acyl-CoA dehydrogenase activity, FAD binding activity.
[0413] The enzyme identified as Sequence Oxid-291 scaffold00071.G3041 (Cytochrome) is encoded by the nucleotides of SEQ ID No: 581 which encodes the amino acid sequence of SEQ ID No: 582. This enzyme is believed to have D-lactate dehydrogenase activityFAD binding (CL01846) activity.
[0414] The enzyme identified as Sequence Oxid-292 scaffold00075.G444 (CL03281) is encoded by the nucleotides of SEQ ID No: 583 which encodes the amino acid sequence of SEQ ID No: 584. This enzyme is believed to have FAD Flavo Protein, electron carrier activity.
[0415] The enzyme identified as Sequence Oxid-293 scaffold00075.G498 (CL03310) is encoded by the nucleotides of SEQ ID No: 585 which encodes the amino acid sequence of SEQ ID No: 586. This enzyme is believed to have FAD Flavo Protein, electron carrier activity. [0416] The enzyme identified as Sequence Oxid-294 scaffold00075.G582 (CL03364
CL05169) DNA scaffold00075.G582 | CL03364 CL05169 | MTHR1 SCHPO | CL03364 CL05169 is encoded by the nucleotides of SEQ ID No: 587 which encodes the amino acid sequence of SEQ ID No: 588. This enzyme is believed to have methylenetetrahydro folate reductase (NADPH) and FAD FlavoProtein NADP Oxidoreductase PhosphoProtein PF02219 1 5 1 20 GO:0005829 GO:0005634 GO:0004489 F:methylenetetrahydrofolate reductase (NADPH) GO:0009086 P:methionine biosynthetic process GO:0055114 P:oxidation reduction activity.
[0417] The enzyme identified as Sequence Oxid-295 scaffold00075.G1087 (CL03644) is encoded by the nucleotides of SEQ ID No: 589 which encodes the amino acid sequence of SEQ ID No: 590. This enzyme is believed to have cytochrome-b5 reductase activity.
[0418] The enzyme identified as Sequence Oxid-296 scaffold00122.G187 (CL03910) is encoded by the nucleotides of SEQ ID No: 591 which encodes the amino acid sequence of SEQ ID No: 592. This enzyme is believed to have FAD Flavo Protein, oxidoreductase activity.
[0419] The enzyme identified as Sequence Oxid-297 scaffold00131.G377 (CL04457) is encoded by the nucleotides of SEQ ID No: 593 which encodes the amino acid sequence of SEQ ID No: 594. This enzyme is believed to have acyl-CoA dehydrogenase activity.
[0420] The enzyme identified as Sequence Oxid-298 scaffold00131.G684 (CL04636) is encoded by the nucleotides of SEQ ID No: 595 which encodes the amino acid sequence of SEQ ID No: 596. This enzyme is believed to have FAD FlavoProtein, oxidoreductase activity.
[0421] The enzyme identified as Sequence Oxid-299 scaffold00131.G1217 (CL04976) is encoded by the nucleotides of SEQ ID No: 597 which encodes the amino acid sequence of SEQ ID No: 598. This enzyme is believed to have acyl-CoA dehydrogenase activity, FAD binding activity.
[0422] The enzyme identified as Sequence Oxid-300 scaffold00142.G588 (CL08704) is encoded by the nucleotides of SEQ ID No: 599 which encodes the amino acid sequence of 600. This enzyme is believed to have 2 iron, 2 sulfur cluster binding, FAD binding, oxidoreductase activity.
[0423] The enzyme identified as Sequence Oxid-301 scaffold00214.G90 (CL02529) is encoded by the nucleotides of SEQ ID No: 601 which encodes the amino acid sequence of SEQ ID No: 602. This enzyme is believed to have FAD binding, NADH dehydrogenase (ubiquinone) activity.
[0424] The enzyme identified as Sequence Oxid-302 scaffold00227.G251 (CL08179) is encoded by the nucleotides of SEQ ID No: 603 which encodes the amino acid sequence of SEQ ID No: 604. This enzyme is believed to have 4 iron, 4 sulfur cluster binding, electron-transferring-flavoprotein dehydrogenase activity.
[0425] The enzyme identified as Sequence Oxid-303 scaffold00008.Gl (CL11660) is encoded by the nucleotides of SEQ ID No: 605 which encodes the amino acid sequence of SEQ ID No: 606. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity GO: 0042773 activity.
[0426] The enzyme identified as Sequence Oxid-304 scaffold00016.G15 (CL08920) is encoded by the nucleotides of SEQ ID No: 607 which encodes the amino acid sequence of SEQ ID No: 608. This enzyme is believed to have FAD binding, oxidoreductase activity.
[0427] The enzyme identified as Sequence Oxid-305 scaffold00016.G18 (CL08922) is encoded by the nucleotides of SEQ ID No: 609 which encodes the amino acid sequence of SEQ ID No: 610. This enzyme is believed to have alcohol dehydrogenase (NADP+) activity, hydroxymethylfurfural reductase (NADH) activity.
[0428] The enzyme identified as Sequence Oxid-306 scaffold00016.G58 (CL08949) is encoded by the nucleotides of SEQ ID No: 611 which encodes the amino acid sequence of SEQ ID No: 612. This enzyme is believed to have oxidoreductase activity.
[0429] The enzyme identified as Sequence Oxid-307 scaffold00016.Gl 17 (CL08986) is encoded by the nucleotides of SEQ ID No: 613 which encodes the amino acid sequence of SEQ ID No: 614. This enzyme is believed to have oxidoreductase activity.
[0430] The enzyme identified as Sequence Oxid-308 scaffold00016.G162 (CL09014) is encoded by the nucleotides of SEQ ID No: 615 which encodes the amino acid sequence of SEQ ID No: 616. This enzyme is believed to have oxidoreductase activity.
[0431] The enzyme identified as Sequence Oxid-309 scaffold00016.G280 (CL09100) is encoded by the nucleotides of SEQ ID No: 617 which encodes the amino acid sequence of SEQ ID No: 618. This enzyme is believed to have L-xylulose reductase (NADP+) activity.
[0432] The enzyme identified as Sequence Oxid-310 scaffold00016.G288 (CL09105) is encoded by the nucleotides of SEQ ID No: 619 which encodes the amino acid sequence of SEQ ID No: 620. This enzyme is believed to have chorismate synthase activity, oxidoreductase activity.
[0433] The enzyme identified as Sequence Oxid-311 30_g scaffold00016.pathl .gene8 is encoded by the nucleotides of SEQ ID No: 621 which encodes the amino acid sequence of SEQ ID No: 622. This enzyme is believed to have
hydro xymethylfurfural reductase (NADH) activity.
[0434] The enzyme identified as Sequence Oxid-312 252_g scaffold00016.G402 is
encoded by the nucleotides of SEQ ID No: 623 which encodes the amino acid sequence of SEQ ID No: 624. This enzyme is believed to have pyruvate dehydrogenase acetyl-transferring activity.
[0435] The enzyme identified as Sequence Oxid-313 359_g scaffold00016.pathl .gene305 scaffold00016.G581 is encoded by the nucleotides of SEQ ID No: 625 which encodes the amino acid sequence of SEQ ID No: 626. This enzyme is believed to have 3-dehydroquinate synthase activity, shikimate 5-dehydrogenase activity.
[0436] The enzyme identified as Sequence Oxid-314 393_g is encoded by the nucleotides of SEQ ID No: 627 which encodes the amino acid sequence of SEQ ID No: 628. This enzyme is believed to have glycerol-3-phosphate dehydrogenase activity.
[0437] The enzyme identified as Sequence Oxid-315 398_g scaffold00016.pathl .gene335 scaffold00016.G648 is encoded by the nucleotides of SEQ ID No: 629 which encodes the amino acid sequence of SEQ ID No: 630. This enzyme is believed to have oxoglutarate dehydrogenase succinyl-trans activity.
[0438] The enzyme identified as Sequence Oxid-316 438_g scaffold00016.pathl .gene371 scaffold00016.G695 is encoded by the nucleotides of SEQ ID No: 631 which encodes the amino acid sequence of SEQ ID No: 632. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
[0439] The enzyme identified as Sequence Oxid-317 474_g scaffold00016.pathl .gene402 scaffold00016.G749 is encoded by the nucleotides of SEQ ID No: 633 which encodes the amino acid sequence of SEQ ID No: 634. This enzyme is believed to have alcohol dehydrogenase (NAD) activity.
[0440] The enzyme identified as Sequence Oxid-3118 632_g scaflbld00016.pathl .gene545 scaffold00016.G996 is encoded by the nucleotides of SEQ ID No: 635 which encodes the amino acid sequence of SEQ ID No: 636. This enzyme is believed to have glyceraldehyde-3-phosphate dehydrogenase activity.
[0441] The enzyme identified as Sequence Oxid-319 711_g scaffold00016.Gl 136 is
encoded by the nucleotides of SEQ ID No: 637 which encodes the amino acid sequence of SEQ ID No: 638. This enzyme is believed to have 3-oxo-5-alpha- steroid 4-dehydrogenase activity.
[0442] The enzyme identified as Sequence Oxid-320 718_g scaffold00016.pathl .gene617 is encoded by the nucleotides of SEQ ID No: 639 which encodes the amino acid sequence of SEQ ID No: 640. This enzyme is believed to have xanthine dehydrogenase activity.
[0443] The enzyme identified as Sequence Oxid-321 789_g scaffold00016.pathl .gene675 scaffold00016.G1249 is encoded by the nucleotides of SEQ ID No: 641 which encodes the amino acid sequence of SEQ ID No: 642. This enzyme is believed to have aldehyde dehydrogenase (NAD) activity.
[0444] The enzyme identified as Sequence Oxid-322 1037_g is encoded by the nucleotides of SEQ ID No: 643 which encodes the amino acid sequence of SEQ ID No: 644.
This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
[0445] The enzyme identified as Sequence Oxid-323 1186_g scaffold00031.pathl .gene222 scaffold00031.G414 is encoded by the nucleotides of SEQ ID No: 645 which encodes the amino acid sequence of SEQ ID No: 646. This enzyme is believed to have L-malate dehydrogenase activity.
[0446] The enzyme identified as Sequence Oxid-324 1292_g scaffold00031.pathl .gene320 is encoded by the nucleotides of SEQ ID No: 647 which encodes the amino acid sequence of SEQ ID No: 648. This enzyme is believed to have D-lactate dehydrogenase (Cytochrome) activity.
[0447] The enzyme identified as Sequence Oxid-325 1294_g scaffold00031.pathl .gene322 scaffold00031.G568 is encoded by the nucleotides of SEQ ID No: 649 which encodes the amino acid sequence of SEQ ID No: 650. This enzyme is believed to have pyruvate dehydrogenase acetyl-transferring activity.
[0448] The enzyme identified as Sequence Oxid-326 1412_g scaffold00031.G751 is encoded by the nucleotides of SEQ ID No: 651 which encodes the amino acid sequence of SEQ ID No: 652. This enzyme is believed to have 3-isopropylmalate dehydrogenase activity.
[0449] The enzyme identified as Sequence Oxid-327 1474_g scaffold00031.pathl .gene483 is encoded by the nucleotides of SEQ ID No: 653 which encodes the amino acid sequence of SEQ ID No: 654. This enzyme is believed to have NADH
dehydrogenase (ubiquinone) activity.
[0450] The enzyme identified as Sequence Oxid-328 1589_g scaffold00031.pathl .gene571 is encoded by the nucleotides of SEQ ID No: 655 which encodes the amino acid sequence of SEQ ID No: 656. This enzyme is believed to have NADH
dehydrogenase (ubiquinone) activity.
[0451] The enzyme identified as Sequence Oxid-329 1606_g scaffold00031.pathl .gene587 is encoded by the nucleotides of SEQ ID No: 657 which encodes the amino acid sequence of SEQ ID No: 658. This enzyme is believed to have prephenate dehydrogenase (NADP+) activity.
[0452] The enzyme identified as Sequence Oxid-330 161 l_g is encoded by the nucleotides of SEQ ID No: 659 which encodes the amino acid sequence of SEQ ID No: 660.
This enzyme is believed to have glutamate dehydrogenase activity.
[0453] The enzyme identified as Sequence Oxid-331 1694_g scaffold00031.pathl .gene670 is encoded by the nucleotides of SEQ ID No: 661 which encodes the amino acid sequence of SEQ ID No: 662. This enzyme is believed to have NADPH dehydrogenase activity.
[0454] The enzyme identified as Sequence Oxid-332 1753_g scaffold00031.pathl .gene729 scaffold00031.G1281 is encoded by the nucleotides of SEQ ID No: 663 which encodes the amino acid sequence of SEQ ID No: 664. This enzyme is believed to have 3-hydroxyisobutyrate dehydrogenase activity.
[0455] The enzyme identified as Sequence Oxid-333 1779_g scaffold00031.pathl .gene754 is encoded by the nucleotides of SEQ ID No: 665 which encodes the amino acid sequence of SEQ ID No: 666. This enzyme is believed to have acyl-CoA dehydrogenase activity.
[0456] The enzyme identified as Sequence Oxid-334 1822_g scaffold00031.pathl .gene786 is encoded by the nucleotides of SEQ ID No: 667 which encodes the amino acid sequence of SEQ ID No: 668. This enzyme is believed to have dihydroorotate dehydrogenase activity.
[0457] The enzyme identified as Sequence Oxid-335 1855_g scaflbld00031.pathl .gene813 scaffold00031.G1450 is encoded by the nucleotides of SEQ ID No: 669 which encodes the amino acid sequence of SEQ ID No: 670. This enzyme is believed to have mannitol-1 -phosphate 5-dehydrogenase activity.
[0458] The enzyme identified as Sequence Oxid-336 2041_g scaffold00031.pathl .gene953 scaffold00031.G1782 is encoded by the nucleotides of SEQ ID No: 671 which encodes the amino acid sequence of SEQ ID No: 672. This enzyme is believed to have L-iditol 2-dehydrogenase activity.
[0459] The enzyme identified as Sequence Oxid-337 2115_g scaffold00050.pathl .genel2 is encoded by the nucleotides of SEQ ID No: 673 which encodes the amino acid sequence of SEQ ID No: 674. This enzyme is believed to have proline
dehydrogenase activity.
[0460] The enzyme identified as Sequence Oxid-338 2148_g scaffold00050.G73 is
encoded by the nucleotides of SEQ ID No: 675 which encodes the amino acid sequence of SEQ ID No: 676. This enzyme is believed to have malate
dehydrogenase (oxaloacetate-decarbox activity.
[0461] The enzyme identified as Sequence Oxid-339 2678_g scaffold00050.pathl .gene468 scaffold00050.G966 is encoded by the nucleotides of SEQ ID No: 677 which encodes the amino acid sequence of SEQ ID No: 678. This enzyme is believed to have acyl-CoA dehydrogenase activity.
[0462] The enzyme identified as Sequence Oxid-340 2682_g scaffold00050.pathl .gene472 is encoded by the nucleotides of SEQ ID No: 679 which encodes the amino acid sequence of SEQ ID No: 680. This enzyme is believed to have acyl-CoA dehydrogenase activity.
[0463] The enzyme identified as Sequence Oxid-341 2813_g scaffold00050.pathl .gene585 scaffold00050.Gl 184 is encoded by the nucleotides of SEQ ID No: 681 which encodes the amino acid sequence of SEQ ID No: 682. This enzyme is believed to have quinate 5-dehydrogenase activity.
[0464] The enzyme identified as Sequence Oxid-342 2879_g scaffold00050.pathl .gene643 is encoded by the nucleotides of SEQ ID No: 683 which encodes the amino acid sequence of SEQ ID No: 684. This enzyme is believed to have dihydrolipoyl dehydrogenase activity. [0465] The enzyme identified as Sequence Oxid-343 3035_g is encoded by the nucleotides of SEQ ID No: 685 which encodes the amino acid sequence of SEQ ID No: 686. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
[0466] The enzyme identified as Sequence Oxid-344 3108_g scaffold00050.G1648 is encoded by the nucleotides of SEQ ID No: 687 which encodes the amino acid sequence of SEQ ID No: 688. This enzyme is believed to have NADH
dehydrogenase (ubiquinone) activity.
[0467] The enzyme identified as Sequence Oxid-345 3228_g scaffold00065.pathl .genel scaffold00065.Gl is encoded by the nucleotides of SEQ ID No: 689 which encodes the amino acid sequence of SEQ ID No: 690. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
[0468] The enzyme identified as Sequence Oxid-346 3253_g scaffold00071.pathl .genel0 scaffold00071.G21 is encoded by the nucleotides of SEQ ID No: 691 which encodes the amino acid sequence of SEQ ID No: 692. This enzyme is believed to have L-iditol 2-dehydrogenase activity.
[0469] The enzyme identified as Sequence Oxid-347 3282_g is encoded by the nucleotides of SEQ ID No: 693 which encodes the amino acid sequence of SEQ ID No: 694. This enzyme is believed to have D-lactate dehydrogenase (Cytochrome) activity.
[0470] The enzyme identified as Sequence Oxid-348 3303_g scaffold00071.pathl .gene52 scaffold00071.G104 is encoded by the nucleotides of SEQ ID No: 695 which encodes the amino acid sequence of SEQ ID No: 696. This enzyme is believed to have succinate-semialdehyde dehydrogenase [NAD(P activity.
[0471] The enzyme identified as Sequence Oxid-349 343 l_g scaffold00071.pathl .genel65 scaffold00071.G332 is encoded by the nucleotides of SEQ ID No: 697 which encodes the amino acid sequence of SEQ ID No: 698. This enzyme is believed to have D-arabinitol 2-dehydrogenase activity.
[0472] The enzyme identified as Sequence Oxid-350 3546_g scaffold00071.pathl .gene254 scaffold00071.G527 is encoded by the nucleotides of SEQ ID No: 699 which encodes the amino acid sequence of 700. This enzyme is believed to have L-iditol 2-dehydrogenase activity.
[0473] The enzyme identified as Sequence Oxid-351 3585_g scaffold00071.pathl .gene293 scaffold00071.G593 is encoded by the nucleotides of SEQ ID No: 701 which encodes the amino acid sequence of SEQ ID No: 702. This enzyme is believed to have succinate dehydrogenase (ubiquinone) activity.
[0474] The enzyme identified as Sequence Oxid-352 3624_g scaflbld00071.pathl .gene325 scaffold00071.G644 is encoded by the nucleotides of SEQ ID No: 703 which encodes the amino acid sequence of SEQ ID No: 704. This enzyme is believed to have glucose-6-phosphate dehydrogenase activity.
[0475] The enzyme identified as Sequence Oxid-353 3725_g scaffold00071.pathl .gene419 scaffold00071.G784 is encoded by the nucleotides of SEQ ID No: 705 which encodes the amino acid sequence of SEQ ID No: 706. This enzyme is believed to have aldehyde dehydrogenase (NADP+) activity.
[0476] The enzyme identified as Sequence Oxid-354 3788_g scaffold00071.pathl .gene475 is encoded by the nucleotides of SEQ ID No: 707 which encodes the amino acid sequence of SEQ ID No: 708. This enzyme is believed to have succinate dehydrogenase activity.
[0477] The enzyme identified as Sequence Oxid-355 3813_g scaffold00071.pathl .gene498 scaffold00071.G905 is encoded by the nucleotides of SEQ ID No: 709 which encodes the amino acid sequence of SEQ ID No: 710. This enzyme is believed to have succinate dehydrogenase (ubiquinone) activity.
[0478] The enzyme identified as Sequence Oxid-356 3849_g scaffold00071.pathl .gene525 scaffold00071.G953 is encoded by the nucleotides of SEQ ID No : 711 which encodes the amino acid sequence of SEQ ID No: 712. This enzyme is believed to have homoisocitrate dehydrogenase activity.
[0479] The enzyme identified as Sequence Oxid-357 3893_g scaffold00071.pathl .gene569 scaffold00071.G1018 is encoded by the nucleotides of SEQ ID No: 713 which encodes the amino acid sequence of SEQ ID No: 714. This enzyme is believed to have L-aminoadipate-semialdehyde dehydrogenase activity.
[0480] The enzyme identified as Sequence Oxid-358 3904_g scaffold00071.G1033 is encoded by the nucleotides of SEQ ID No: 715 which encodes the amino acid sequence of SEQ ID No: 716. This enzyme is believed to have aldehyde dehydrogenase (NAD) activity.
[0481] The enzyme identified as Sequence Oxid-359 3907_g scaffold00071.pathl .gene584 scaffold00071.G1037 is encoded by the nucleotides of SEQ ID No: 717 which encodes the amino acid sequence of SEQ ID No: 718. This enzyme is believed to have L-lactate dehydrogenase activity. [0482] The enzyme identified as Sequence Oxid-360 3973_g scaflbld00071.pathl .gene627 scaffold00071.Gl 160 is encoded by the nucleotides of SEQ ID No: 719 which encodes the amino acid sequence of SEQ ID No: 720. This enzyme is believed to have iso citrate dehydrogenase (NAD+) activity.
[0483] The enzyme identified as Sequence Oxid-361 4020_g scaffold00071.pathl .gene663 scaffold00071.G1266 is encoded by the nucleotides of SEQ ID No: 721 which encodes the amino acid sequence of SEQ ID No: 722. This enzyme is believed to have glycerol-3-phosphate dehydrogenase (NAD+) activity.
[0484] The enzyme identified as Sequence Oxid-362 4078_g scaffold00071.pathl .gene715 scaffold00071.G1360 is encoded by the nucleotides of SEQ ID No: 723 which encodes the amino acid sequence of SEQ ID No: 724. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
[0485] The enzyme identified as Sequence Oxid-363 4133_g scaffold00071.pathl .gene764 is encoded by the nucleotides of SEQ ID No: 725 which encodes the amino acid sequence of SEQ ID No: 726. This enzyme is believed to have NADPH dehydrogenase activity.
[0486] The enzyme identified as Sequence Oxid-364 4146_g scaffold00071.pathl .gene776 scaffold00071.G1457 is encoded by the nucleotides of SEQ ID No: 727 which encodes the amino acid sequence of SEQ ID No: 728. This enzyme is believed to have 3 -beta-hydro xy-delta5 -steroid dehydrogenase activity.
[0487] The enzyme identified as Sequence Oxid-365 4158_g scaffold00071.pathl .gene786 scaffold00071.G1476 is encoded by the nucleotides of SEQ ID No: 729 which encodes the amino acid sequence of SEQ ID No: 730. This enzyme is believed to have succinate-semialdehyde dehydrogenase activity.
[0488] The enzyme identified as Sequence Oxid-366 4163_g scaffold00071.pathl .gene791 scaffold00071.G1485 is encoded by the nucleotides of SEQ ID No: 731 which encodes the amino acid sequence of SEQ ID No: 732. This enzyme is believed to have pyridoxine 4-dehydrogenase activity.
[0489] The enzyme identified as Sequence Oxid-367 4300_g scaffold00071.pathl .gene902 scaffold00071.G1693 is encoded by the nucleotides of SEQ ID No: 733 which encodes the amino acid sequence of SEQ ID No: 734. This enzyme is believed to have histidinol dehydrogenase activity, phosphoribosyl-AMP cyclohydrolase activity. [0490] The enzyme identified as Sequence Oxid-368 4326_g scaflbld00071.pathl .gene926 scaffold00071.G1722 is encoded by the nucleotides of SEQ ID No: 735 which encodes the amino acid sequence of SEQ ID No: 736. This enzyme is believed to have saccharopine dehydrogenase (NAD+, L-lysine- activity.
[0491] The enzyme identified as Sequence Oxid-369 4327_g scaffold00071.pathl .gene927 scaffold00071.G1723 is encoded by the nucleotides of SEQ ID No: 737 which encodes the amino acid sequence of SEQ ID No: 738. This enzyme is believed to have IMP dehydrogenase activity.
[0492] The enzyme identified as Sequence Oxid-370 4345_g is encoded by the nucleotides of SEQ ID No: 739 which encodes the amino acid sequence of SEQ ID No: 740. This enzyme is believed to have phospho gluconate dehydrogenase (decarboxylase) activity.
[0493] The enzyme identified as Sequence Oxid-371 4370_g scaffold00071.pathl .gene967 scaffold00071.G1784 is encoded by the nucleotides of SEQ ID No: 741 which encodes the amino acid sequence of SEQ ID No: 742. This enzyme is believed to have l-pyrroline-5-carboxylate dehydrogenase activity.
[0494] The enzyme identified as Sequence Oxid-372 4568_g
scaffold00071.pathl .genel l33 scaffold00071.G2097 is encoded by the nucleotides of SEQ ID No: 743 which encodes the amino acid sequence of SEQ ID No: 744. This enzyme is believed to have 3 -beta-hydro xy-delta5 -steroid dehydrogenase, sterol-4-alpha-carboxylate 3-dehydrogenase activity.
[0495] The enzyme identified as Sequence Oxid-373 4602_g
scaffold00071.pathl .genel l68 scaffold00071.G2157 is encoded by the nucleotides of SEQ ID No: 745 which encodes the amino acid sequence of SEQ ID No: 746. This enzyme is believed to have methylenetetrahydro folate dehydrogenase activity.
[0496] The enzyme identified as Sequence Oxid-374 4737_g
scaffold00071.pathl .genel276 is encoded by the nucleotides of SEQ ID No: 747 which encodes the amino acid sequence of SEQ ID No: 748. This enzyme is believed to have L-lactate dehydrogenase (Cytochrome) activity.
[0497] The enzyme identified as Sequence Oxid-375 4754_g
scaffold00071.pathl .genel294 scaffold00071.G2411 is encoded by the nucleotides of SEQ ID No: 749 which encodes the amino acid sequence of SEQ ID No: 750. This enzyme is believed to have 3 -beta-hydro xy-delta5 -steroid dehydrogenase activity.
[0498] The enzyme identified as Sequence Oxid-376 4835_g
scaffold00071.pathl .genel357 scaffold00071.G2544 is encoded by the nucleotides of SEQ ID No: 751 which encodes the amino acid sequence of SEQ ID No: 752. This enzyme is believed to have pyruvate dehydrogenase (acetyl-transferring) activity.
[0499] The enzyme identified as Sequence Oxid-377 4925_g
scaffold00071.pathl .genel439 scaffold00071.G2698 is encoded by the nucleotides of SEQ ID No: 753 which encodes the amino acid sequence of SEQ ID No: 754.
This enzyme is believed to have aspartate-semialdehyde dehydrogenase activity.
[0500] The enzyme identified as Sequence Oxid-378 5088_g scaffold00071.G2977 is encoded by the nucleotides of SEQ ID No: 755 which encodes the amino acid sequence of SEQ ID No: 756. This enzyme is believed to have D-arabinitol 2- dehydrogenase activity.
[0501] The enzyme identified as Sequence Oxid-379 5090_g
scaffold00071.pathl .genel581 is encoded by the nucleotides of SEQ ID No: 757 which encodes the amino acid sequence of SEQ ID No: 758. This enzyme is believed to have acyl-CoA dehydrogenase activity.
[0502] The enzyme identified as Sequence Oxid-380 513 l_g is encoded by the nucleotides of SEQ ID No: 759 which encodes the amino acid sequence of SEQ ID No: 760.
This enzyme is believed to have D-lactate dehydrogenase (Cytochrome) activity.
[0503] The enzyme identified as Sequence Oxid-381 5305_g
scaffold00071.pathl .genel777 scaffold00071.G3328 is encoded by the nucleotides of SEQ ID No: 761 which encodes the amino acid sequence of SEQ ID No: 762.
This enzyme is believed to have aldehyde reductase activity, glucose 1- dehydrogenase (NADP+) activity.
[0504] The enzyme identified as Sequence Oxid-382 5384_g
scaffold00071.pathl .genel843 scaffold00071.G3467 is encoded by the nucleotides of SEQ ID No: 763 which encodes the amino acid sequence of SEQ ID No: 764.
This enzyme is believed to have aldehyde dehydrogenase (NAD) activity.
[0505] The enzyme identified as Sequence Oxid-383 5408_g
scaffold00071.pathl .genel862 scaffold00071.G3501 is encoded by the nucleotides of SEQ ID No: 765 which encodes the amino acid sequence of SEQ ID No: 766. This enzyme is believed to have L-lactate dehydrogenase activity.
[0506] The enzyme identified as Sequence Oxid-384 5415_g
scaffold00071.pathl .genel869 scaffold00071.G3512 is encoded by the nucleotides of SEQ ID No: 767 which encodes the amino acid sequence of SEQ ID No: 768. This enzyme is believed to have glycine dehydrogenase (decarboxylating) activity.
[0507] The enzyme identified as Sequence Oxid-385 5625_g scaffold00075.pathl .genel71 scaffold00075.G374 is encoded by the nucleotides of SEQ ID No: 769 which encodes the amino acid sequence of SEQ ID No: 770. This enzyme is believed to have 3-hydroxyisobutyrate dehydrogenase activity, histone-lysine N- methyltransferase activity,phospho gluconate dehydrogenase (decarboxylase) activity.
[0508] The enzyme identified as Sequence Oxid-386 5768_g scaffold00075.pathl .gene311 is encoded by the nucleotides of SEQ ID No: 771 which encodes the amino acid sequence of SEQ ID No: 772. This enzyme is believed to have isocitrate dehydrogenase (NAD+) activity.
[0509] The enzyme identified as Sequence Oxid-387 5850_g scaffold00075.pathl .gene393 scaffold00075.G724 is encoded by the nucleotides of SEQ ID No: 773 which encodes the amino acid sequence of SEQ ID No: 774. This enzyme is believed to have phospho gluconate dehydrogenase (decarboxylase) activity.
[0510] The enzyme identified as Sequence Oxid-388 5919_g is encoded by the nucleotides of SEQ ID No: 775 which encodes the amino acid sequence of SEQ ID No: 776. This enzyme is believed to have L-lactate dehydrogenase (Cytochrome) activity.
[0511] The enzyme identified as Sequence Oxid-389 5937_g scaffold00075.pathl .gene469 is encoded by the nucleotides of SEQ ID No: 777 which encodes the amino acid sequence of SEQ ID No: 778. This enzyme is believed to have 3-dehydroquinate dehydratase activity, shikimate 5-dehydrogenase activity, shikimate kinase activity.
[0512] The enzyme identified as Sequence Oxid-390 613 l_g scaffold00075.pathl .gene641 scaffold00075.Gl 167 is encoded by the nucleotides of SEQ ID No: 779 which encodes the amino acid sequence of SEQ ID No: 780. This enzyme is believed to have betaine-aldehyde dehydrogenase activity.
[0513] The enzyme identified as Sequence Oxid-391 6269_g scaffold00092.pathl .gene24 scaffold00092.G43 is encoded by the nucleotides of SEQ ID No: 781 which encodes the amino acid sequence of SEQ ID No: 782. This enzyme is believed to have precorrin-2 dehydrogenase activity,F:sirohydrochlorin ferrochelatase activity.
[0514] The enzyme identified as Sequence Oxid-392 6348_g scaffold00092.pathl .gene81 scaffold00092.G162 is encoded by the nucleotides of SEQ ID No: 783 which encodes the amino acid sequence of SEQ ID No: 784. This enzyme is believed to have L-malate dehydrogenase activity.
[0515] The enzyme identified as Sequence Oxid-393 6537_g scaffold00092.pathl .gene235 is encoded by the nucleotides of SEQ ID No: 785 which encodes the amino acid sequence of SEQ ID No: 786. This enzyme is believed to have cellobiose dehydrogenase (acceptor) activity.
[0516] The enzyme identified as Sequence Oxid-394 6692_g scaffold00092.pathl .gene387 scaffold00092.G738 is encoded by the nucleotides of SEQ ID No: 787 which encodes the amino acid sequence of SEQ ID No: 788. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
[0517] The enzyme identified as Sequence Oxid-395 6950_g scaffold00122.pathl .genel07 scaffold00122.G197 is encoded by the nucleotides of SEQ ID No: 789 which encodes the amino acid sequence of SEQ ID No: 790. This enzyme is believed to have aldehyde dehydrogenase (NAD) activity.
[0518] The enzyme identified as Sequence Oxid-396 7026_g scaffold00131.G97 is
encoded by the nucleotides of SEQ ID No: 791 which encodes the amino acid sequence of SEQ ID No: 792. This enzyme is believed to have NADH
dehydrogenase (ubiquinone) activity.
[0519] The enzyme identified as Sequence Oxid-397 7048_g scaffold00131.pathl .gene70 scaffold00131.G132 is encoded by the nucleotides of SEQ ID No: 793 which encodes the amino acid sequence of SEQ ID No: 794. This enzyme is believed to have alcohol dehydrogenase (NADP+) activity.
[0520] The enzyme identified as Sequence Oxid-398 7101_g scaffold00131.pathl .genel20 scaffold00131.G220 is encoded by the nucleotides of SEQ ID No: 795 which encodes the amino acid sequence of SEQ ID No: 796. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
[0521] The enzyme identified as Sequence Oxid-399 7117_g scaffold00131.pathl .genel32 scaffold00131.G239 is encoded by the nucleotides of SEQ ID No: 797 which encodes the amino acid sequence of SEQ ID No: SEQ ID No: 798. This enzyme is believed to have acyl-CoA dehydrogenase activity. [0522] The enzyme identified as Sequence Oxid-400 7135_g scaflbld00131.pathl .genel50 scaffold00131.G266 is encoded by the nucleotides of SEQ ID No: 799 which encodes the amino acid sequence of 800. This enzyme is believed to have 3- dehydroquinate synthase activity, 3-phosphoshikimate 1- carboxyvinyltransferas,shikimate 5-dehydrogenase activity, shikimate kinase activity.
[0523] The enzyme identified as Sequence Oxid-401 7136_g scaffold00131.pathl .genel52 is encoded by the nucleotides of SEQ ID No: 801 which encodes the amino acid sequence of SEQ ID No: 802. This enzyme is believed to have dihydroorotate dehydrogenase activity.
[0524] The enzyme identified as Sequence Oxid-402 7207_g scaffold00131.pathl .gene222 is encoded by the nucleotides of SEQ ID No: 803 which encodes the amino acid sequence of SEQ ID No: 804. This enzyme is believed to have acyl-CoA dehydrogenase activity.
[0525] The enzyme identified as Sequence Oxid-403 7244_g scaffold00131.pathl .gene256 scaffold00131.G441 is encoded by the nucleotides of SEQ ID No: 805 which encodes the amino acid sequence of SEQ ID No: 806. This enzyme is believed to have malate dehydrogenase (oxaloacetate-decarboxylase) activity.
[0526] The enzyme identified as Sequence Oxid-404 7344_g scaffold00131.pathl .gene349 scaffold00131.G586 is encoded by the nucleotides of SEQ ID No: 807 which encodes the amino acid sequence of SEQ ID No: 808. This enzyme is believed to have pyruvate dehydrogenase (acetyl-transferring GO:0015976 activity.
[0527] The enzyme identified as Sequence Oxid-405 7359_g scaffold00131.pathl .gene365 is encoded by the nucleotides of SEQ ID No: 809 which encodes the amino acid sequence of SEQ ID No: 810. This enzyme is believed to have oxidoreductase activity, acting on the CH-0 activity.
[0528] The enzyme identified as Sequence Oxid-406 7681_g scaffold00131.Gl 152 is encoded by the nucleotides of SEQ ID No : 811 which encodes the amino acid sequence of SEQ ID No: 812. This enzyme is believed to have succinate dehydrogenase activity.
[0529] The enzyme identified as Sequence Oxid-407 7688_g scaffold00131.pathl .gene645 scaffold00131.G1161 is encoded by the nucleotides of SEQ ID No: 813 which encodes the amino acid sequence of SEQ ID No: 814. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
[0530] The enzyme identified as Sequence Oxid-408 7715_g scaflbld00131.pathl .gene672 scaffold00131.G1199 is encoded by the nucleotides of SEQ ID No: 815 which encodes the amino acid sequence of SEQ ID No: 816. This enzyme is believed to have glutamate dehydrogenase (NADP+) activity.
[0531] The enzyme identified as Sequence Oxid-409 7732_g scaffold00131.pathl .gene687 is encoded by the nucleotides of SEQ ID No: 817 which encodes the amino acid sequence of SEQ ID No: 818. This enzyme is believed to have acyl-CoA dehydrogenase activity.
[0532] The enzyme identified as Sequence Oxid-410 7808_g scaffold00131.pathl .gene747 scaffold00131.G1330 is encoded by the nucleotides of SEQ ID No: 819 which encodes the amino acid sequence of SEQ ID No: 820. This enzyme is believed to have phosphoglycerate dehydrogenase activity.
[0533] The enzyme identified as Sequence Oxid-411 7981_g scaffold00131.G1610
scaffold00131.pathl .gene895 is encoded by the nucleotides of SEQ ID No: 821 which encodes the amino acid sequence of SEQ ID No: 822. This enzyme is believed to have saccharopine dehydrogenase (NADP+, L-glutamase) activity.
[0534] The enzyme identified as Sequence Oxid-412 8135_g
scaffold00131.pathl .genel039 scaffold00131.G1851 is encoded by the nucleotides of SEQ ID No: 823 which encodes the amino acid sequence of SEQ ID No: 824. This enzyme is believed to have S-(hydroxymethyl)glutathione dehydrogenase activity.
[0535] The enzyme identified as Sequence Oxid-413 8172_g
scaffold00131.pathl .genel073 is encoded by the nucleotides of SEQ ID No: 825 which encodes the amino acid sequence of SEQ ID No: 826. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
[0536] The enzyme identified as Sequence Oxid-414 8429_g scaffold00137.pathl .gene47 is encoded by the nucleotides of SEQ ID No: 827 which encodes the amino acid sequence of SEQ ID No: 828. This enzyme is believed to have carbohydrate binding, cellobiose dehydrogenase (acceptor) activity.
[0537] The enzyme identified as Sequence Oxid-415 8601_g scaffold00142.pathl .gene76 scaffold00142.G177 is encoded by the nucleotides of SEQ ID No: 829 which encodes the amino acid sequence of SEQ ID No: 830. This enzyme is believed to have iso citrate dehydrogenase (NADP+) activity.
[0538] The enzyme identified as Sequence Oxid-416 8616_g scafTold00142.G199
scaffold00142.pathl .gene91 is encoded by the nucleotides of SEQ ID No: 831 which encodes the amino acid sequence of SEQ ID No: 832. This enzyme is believed to have methylenetetrahydro folate dehydrogenase activity.
[0539] The enzyme identified as Sequence Oxid-417 8628_g scaffold00142.G216,
scaffold00142.G217 scaffold00142.pathl .genel01, scaffold00142.pathl .genel02 is encoded by the nucleotides of SEQ ID No: 833 which encodes the amino acid sequence of SEQ ID No: 834. This enzyme is believed to have NADH
dehydrogenase (ubiquinone) activity.
[0540] The enzyme identified as Sequence Oxid-418 8636_g scaffold00142.G228
scaffold00142.pathl .genel09 is encoded by the nucleotides of SEQ ID No: 835 which encodes the amino acid sequence of SEQ ID No: 836. This enzyme is believed to have aldehyde dehydrogenase [NAD(P)+] activity.
[0541] The enzyme identified as Sequence Oxid-419 8670_g scaffold00142.G282
scaffold00142.pathl .genel36 is encoded by the nucleotides of SEQ ID No: 837 which encodes the amino acid sequence of SEQ ID No: 838. This enzyme is believed to have cellobiose dehydrogenase (acceptor) activity.
[0542] The enzyme identified as Sequence Oxid-420 8710_g scaffold00142.G347
scaffold00142.patnl .genel72 is encoded by the nucleotides of SEQ ID No: 839 which encodes the amino acid sequence of SEQ ID No: 840. This enzyme is believed to have phospho gluconate dehydrogenase (decarboxylase) activity.
[0543] The enzyme identified as Sequence Oxid-421 9069_g scaffold00169.G299
scaffold00169.pathl .genel43 is encoded by the nucleotides of SEQ ID No: 841 which encodes the amino acid sequence of SEQ ID No: 842. This enzyme is believed to have alcohol dehydrogenase (NADP+) activity, hydroxymethylfurfural reductase (NADH) activity.
[0544] The enzyme identified as Sequence Oxid-422 9070_g scaffold00169.G310 is
encoded by the nucleotides of SEQ ID No: 843 which encodes the amino acid sequence of SEQ ID No: 844. This enzyme is believed to have alcohol
dehydrogenase (NADP+) activity, hydroxymethylfurfural reductase (NADH) activity.
[0545] The enzyme identified as Sequence Oxid-423 9103_g scaffold00169.G346 scaffold00169.pathl .genel70 is encoded by the nucleotides of SEQ ID No: 845 which encodes the amino acid sequence of SEQ ID No: 846. This enzyme is believed to have acyl-CoA dehydrogenase activity.
[0546] The enzyme identified as Sequence Oxid-424 9361_g scaffold00214.G90
scaffold00214.pathl .gene51 is encoded by the nucleotides of SEQ ID No: 847 which encodes the amino acid sequence of SEQ ID No: 848. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
[0547] The enzyme identified as Sequence Oxid-425 9476_g scaffold00227.G141
scaffold00227.pathl .gene78 is encoded by the nucleotides of SEQ ID No: 849 which encodes the amino acid sequence of SEQ ID No: 850. This enzyme is believed to have phosphoglycerate dehydrogenase activity.
[0548] The enzyme identified as Sequence Oxid-426 9481_g scaffold00227.G160
scaffold00227.pathl .gene80 is encoded by the nucleotides of SEQ ID No: 851 which encodes the amino acid sequence of SEQ ID No: 852. This enzyme is believed to have phosphoglycerate dehydrogenase activity.
[0549] The enzyme identified as Sequence Oxid-427 9610_g scaffold00227.G366
scaffold00227.pathl .gene204 is encoded by the nucleotides of SEQ ID No: 853 which encodes the amino acid sequence of SEQ ID No: 854. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
[0550] The enzyme identified as Sequence Oxid-428 9713_g scaffold00227.G535
scaffold00227.pathl .gene303 is encoded by the nucleotides of SEQ ID No: 855 which encodes the amino acid sequence of SEQ ID No: 856. This enzyme is believed to have homo serine dehydrogenase activity.
[0551] The enzyme identified as Sequence Oxid-429 9773_g scaffold00227.G636
scaffold00227.pathl .gene360 is encoded by the nucleotides of SEQ ID No: 857 which encodes the amino acid sequence of SEQ ID No: 858. This enzyme is believed to have NADH dehydrogenase (ubiquinone) activity.
[0552] The enzyme identified as Sequence Oxid-430 8277_g scaffold00131.G2107 scaffold00131.pathl .genel l68 is encoded by the nucleotides of SEQ ID No: 859 which encodes the amino acid sequence of SEQ ID No: 860. This enzyme is believed to have glutamate-5-semialdehyde dehydrogenase activity.
[0553] The enzyme identified as Sequence Oxid-431 8720_g scaffold00142.G365
scaffold00142.pathl .genel80 is encoded by the nucleotides of SEQ ID No: 861 which encodes the amino acid sequence of SEQ ID No: 862. This enzyme is believed to have monooxygenase activity.
[0554] The enzyme identified as Sequence Oxid-432 8723_g scaffold00142.pathl .genel81 is encoded by the nucleotides of SEQ ID No: 863 which encodes the amino acid sequence of SEQ ID No: 864. This enzyme is believed to have flavin-containing monooxygenase activity.
[0555] The enzyme identified as Sequence Oxid-433 8842_g scaffold00142.G579
scaffold00142.pathl .gene280 is encoded by the nucleotides of SEQ ID No: 865 which encodes the amino acid sequence of SEQ ID No: 866. This enzyme is believed to have monooxygenase activity.
[0556] The enzyme identified as Sequence Oxid-434 8843_g scaffold00142.G579
scaffold00142.pathl .gene280, scaffold00142.pathl .gene281 is encoded by the nucleotides of SEQ ID No: 867 which encodes the amino acid sequence of SEQ ID No: 868. This enzyme is believed to have monooxygenase activity.
[0557] The enzyme identified as Sequence Oxid-435 8853_g scaffold00142.G589
scaffold00142.pathl .gene289 is encoded by the nucleotides of SEQ ID No: 869 which encodes the amino acid sequence of SEQ ID No: 870. This enzyme is believed to have monooxygenase activity.
[0558] The enzyme identified as Sequence Oxid-436 8910_g scaffold00169.G30
scaffold00169.pathl .genel6 is encoded by the nucleotides of SEQ ID No: 871 which encodes the amino acid sequence of SEQ ID No: 872. This enzyme is believed to have monooxygenase activity.
[0559] The enzyme identified as Sequence Oxid-437 8914_g scaffold00169.G35
scaffold00169.pathl .gene20 is encoded by the nucleotides of SEQ ID No: 873 which encodes the amino acid sequence of SEQ ID No: 874. This enzyme is believed to have monooxygenase activity.
[0560] The enzyme identified as Sequence Oxid-438 9060_g scaffold00169.G288
scaffold00169.pathl .genel37 is encoded by the nucleotides of SEQ ID No: 875 which encodes the amino acid sequence of SEQ ID No: 876. This enzyme is believed to have monooxygenase activity.
[0561] The enzyme identified as Sequence Oxid-439 9085_g scaffold00169.G316
scaffold00169.pathl .genel58 is encoded by the nucleotides of SEQ ID No: 877 which encodes the amino acid sequence of SEQ ID No: 878. This enzyme is believed to have flavin-containing monooxygenase activity.
[0562] The enzyme identified as Sequence Oxid-440 9086_g scaffold00169.G317,
scaffold00169.G318 is encoded by the nucleotides of SEQ ID No: 879 which encodes the amino acid sequence of SEQ ID No: 880. This enzyme is believed to have flavin-containing monooxygenase activity.
[0563] The enzyme identified as Sequence Oxid-441 9087_g is encoded by the nucleotides of SEQ ID No: 881 which encodes the amino acid sequence of SEQ ID No: 882.
This enzyme is believed to have flavin-containing monooxygenase activity.
[0564] The enzyme identified as Sequence Oxid-442 909 l_g scaffold00169.G321
scaffold00169.pathl .genel61 is encoded by the nucleotides of SEQ ID No: 883 which encodes the amino acid sequence of SEQ ID No: 884. This enzyme is believed to have monooxygenase activity.
[0565] The enzyme identified as Sequence Oxid-443 9093_g scaffold00169.G325
scaffold00169.pathl .genel62 is encoded by the nucleotides of SEQ ID No: 885 which encodes the amino acid sequence of SEQ ID No: 886. This enzyme is believed to have flavin-containing monooxygenase activity.
[0566] The enzyme identified as Sequence Oxid-444 9137_g scaffold00169.G402
scaffold00169.pathl .genel95 is encoded by the nucleotides of SEQ ID No: 887 which encodes the amino acid sequence of SEQ ID No: 888. This enzyme is believed to have monooxygenase activity.
[0567] The enzyme identified as Sequence Oxid-445 9156_g scaffold00169.G442
scaffold00169.pathl .gene209 is encoded by the nucleotides of SEQ ID No: 889 which encodes the amino acid sequence of SEQ ID No: 890. This enzyme is believed to have monooxygenase activity.
[0568] The enzyme identified as Sequence Oxid-446 9184_g scaffold00169.G493 is
encoded by the nucleotides of SEQ ID No: 891 which encodes the amino acid sequence of SEQ ID No: 892. This enzyme is believed to have monooxygenase activity.
[0569] The enzyme identified as Sequence Oxid-447 9307_g scaffold00214.G9,
scaffold00214.G10, scaffold00214.Gl 1 scaffolg00214.pathl .gene7,
scaffblg00214.pathl .gene8 is encoded by the nucleotides of SEQ ID No: 893 which encodes the amino acid sequence of SEQ ID No: 894. This enzyme is believed to have monooxygenase activity. [0570] The enzyme identified as Sequence Oxid-448 9315_g scaffold00214.G22 scaffold00214.pathl .genel6 is encoded by the nucleotides of SEQ ID No: 895 which encodes the amino acid sequence of SEQ ID No: 896. This enzyme is believed to have monooxygenase activity.
[0571] The enzyme identified as Sequence Oxid-449 945 l_g scaffold00227.G102
scaffold00227.pathl .gene52 is encoded by the nucleotides of SEQ ID No: 897 which encodes the amino acid sequence of SEQ ID No: 898. This enzyme is believed to have monooxygenase activity.
[0572] The enzyme identified as Sequence Oxid-450 9509_g scaffold00227.G204
scaffold00227.pathl .genel06 is encoded by the nucleotides of SEQ ID No: 899 which encodes the amino acid sequence of 900. This enzyme is believed to have monooxygenase activity.
[0573] The enzyme identified as Sequence Oxid-451 9634_g scaffold00227.G400
scaffold00227.pathl .gene224 is encoded by the nucleotides of SEQ ID No: 901 which encodes the amino acid sequence of SEQ ID No: 902. This enzyme is believed to have ent-kaurene oxidase activity.
[0574] The enzyme identified as Sequence Oxid-452 9800_g scaffold00227.G683
scaffold00227.pathl .gene379 is encoded by the nucleotides of SEQ ID No: 903 which encodes the amino acid sequence of SEQ ID No: 904. This enzyme is believed to have monooxygenase activity.
[0575] The enzyme identified as Sequence Oxid-453 220_g scaffold00016.G359
scaffold00016.pathl .genel75 is encoded by the nucleotides of SEQ ID No: 905 which encodes the amino acid sequence of SEQ ID No: 906. This enzyme is believed to have phenol 2-monooxygenase activity.
[0576] The enzyme identified as Sequence Oxid-454 671_g (CL09554) is encoded by the nucleotides of SEQ ID No: 907 which encodes the amino acid sequence of SEQ ID No: 908. This enzyme is believed to have monooxygenase activity.
[0577] The enzyme identified as Sequence Oxid-455 882_g scaffold00019.G30
scaffold00019.pathl .gene7 is encoded by the nucleotides of SEQ ID No: 909 which encodes the amino acid sequence of SEQ ID No: 910. This enzyme is believed to have monooxygenase activity.
[0578] The enzyme identified as Sequence Oxid-456 887_g is encoded by the nucleotides of SEQ ID No: 911 which encodes the amino acid sequence of SEQ ID No: 912. This enzyme is believed to have monooxygenase activity.
[0579] The enzyme identified as Sequence Oxid-457 888_g scaffold00019.G40
scaffbld00019.pathl .genel5 is encoded by the nucleotides of SEQ ID No: 913 which encodes the amino acid sequence of SEQ ID No: 914. This enzyme is believed to have monooxygenase activity.
[0580] The enzyme identified as Sequence Oxid-458 946_g, scaffold00031.G17,
scaffold00031.G18, scaffold00031.pathl .genel4, scaffold00031.pathl .genel5 is encoded by the nucleotides of SEQ ID No: 915 which encodes the amino acid sequence of SEQ ID No: 916. This enzyme is believed to have monooxygenase activity.
[0581] The enzyme identified as Sequence Oxid-459 979_g scaffold00031.G86
scaffold00031.pathl .gene42, scaffold00031.pathl .gene43 is encoded by the nucleotides of SEQ ID No: 917 which encodes the amino acid sequence of SEQ ID No: 918. This enzyme is believed to have phenol 2-monooxygenase activity.
[0582] The enzyme identified as Sequence Oxid-460 1007_g scaffold00031.G144
scaffold00031.pathl .gene69 is encoded by the nucleotides of SEQ ID No: 919 which encodes the amino acid sequence of SEQ ID No: 920. This enzyme is believed to have monooxygenase activity.
[0583] The enzyme identified as Sequence Oxid-461 1063_g scaffold00031.G225
scaffold00031.pathl .genel 15 is encoded by the nucleotides of SEQ ID No: 921 which encodes the amino acid sequence of SEQ ID No: 922. This enzyme is believed to have flavin-containing monooxygenase activity.
[0584] The enzyme identified as Sequence Oxid-462 1216_g scaffold00031.G454
scaffold00031. pathl . gene252 is encoded by the nucleotides of SEQ ID No: 923 which encodes the amino acid sequence of SEQ ID No: 924. This enzyme is believed to have monooxygenase activity.
[0585] The enzyme identified as Sequence Oxid-463 1227_g scaffold00031.G472
scaffold00031. pathl . gene263 is encoded by the nucleotides of SEQ ID No: 925 which encodes the amino acid sequence of SEQ ID No: 926. This enzyme is believed to have monooxygenase activity.
[0586] The enzyme identified as Sequence Oxid-464 1526_g scaffold00031.G951
scaffold00031. pathl . gene521 is encoded by the nucleotides of SEQ ID No: 927 which encodes the amino acid sequence of SEQ ID No: 928. This enzyme is believed to have monooxygenase activity.
[0587] The enzyme identified as Sequence Oxid-465 1643_g scaffold00031.Gl 133 is encoded by the nucleotides of SEQ ID No: 929 which encodes the amino acid sequence of SEQ ID No: 930. This enzyme is believed to have monooxygenase activity.
[0588] The enzyme identified as Sequence Oxid-466 1815_g scaffold00031.G1375
scaffold00031.pathl .gene780 is encoded by the nucleotides of SEQ ID No: 931 which encodes the amino acid sequence of SEQ ID No: 932. This enzyme is believed to have monooxygenase activity.
[0589] The enzyme identified as Sequence Oxid-467 1816_g scaffold00031.G1376
scaffold00031.pathl .gene781 is encoded by the nucleotides of SEQ ID No: 933 which encodes the amino acid sequence of SEQ ID No: 934. This enzyme is believed to have monooxygenase activity.
[0590] The enzyme identified as Sequence Oxid-468 1820_g scaffold00031.pathl .gene783 CL02839 is encoded by the nucleotides of SEQ ID No: 935 which encodes the amino acid sequence of SEQ ID No: 936. This enzyme is believed to have monooxygenase activity.
[0591] The enzyme identified as Sequence Oxid-469 1872_g scaffold00031.G1485
scaffold00031.pathl .gene823 is encoded by the nucleotides of SEQ ID No: 937 which encodes the amino acid sequence of SEQ ID No: 938. This enzyme is believed to have flavin-containing monooxygenase activity.
[0592] The enzyme identified as Sequence Oxid-470 2267_g scaffold00050.G279
scaffold00050.pathl .genel 16 is encoded by the nucleotides of SEQ ID No: 939 which encodes the amino acid sequence of SEQ ID No: 940. This enzyme is believed to have flavin-containing monooxygenase activity.
[0593] The enzyme identified as Sequence Oxid-471 2280_g scaffold00050.G298
scaffold00050.pathl .genel29 is encoded by the nucleotides of SEQ ID No: 941 which encodes the amino acid sequence of SEQ ID No: 942. This enzyme is believed to have monooxygenase activity.
[0594] The enzyme identified as Sequence Oxid-472 228 l_g scaffold00050.G298
scaffold00050.pathl .genel30 is encoded by the nucleotides of SEQ ID No: 943 which encodes the amino acid sequence of SEQ ID No: 944. This enzyme is believed to have monooxygenase activity.
I l l [0595] The enzyme identified as Sequence Oxid-473 2289_g scaffold00050.G309 scaffold00050.pathl .genel39 is encoded by the nucleotides of SEQ ID No: 945 which encodes the amino acid sequence of SEQ ID No: 946. This enzyme is believed to have monooxygenase activity.
[0596] The enzyme identified as Sequence Oxid-474 2293_g scaffold00050.G316
scaffold00050.pathl .genel45 is encoded by the nucleotides of SEQ ID No: 947 which encodes the amino acid sequence of SEQ ID No: 948. This enzyme is believed to have linoleate diol synthase activity, monooxygenase activity, peroxidase activity.
[0597] The enzyme identified as Sequence Oxid-475 234 l_g scaffold00050.G397
scaffold00050.pathl .genel87 is encoded by the nucleotides of SEQ ID No: 949 which encodes the amino acid sequence of SEQ ID No: 950. This enzyme is believed to have monooxygenase activity.
[0598] The enzyme identified as Sequence Oxid-476 2342_g scaffold00050.G397 is
encoded by the nucleotides of SEQ ID No: 951 which encodes the amino acid sequence of SEQ ID No: 952. This enzyme is believed to have monooxygenase activity.
[0599] The enzyme identified as Sequence Oxid-477 2417_g scaffold00050.G524
scaffold00050.pathl .gene246 is encoded by the nucleotides of SEQ ID No: 953 which encodes the amino acid sequence of SEQ ID No: 954. This enzyme is believed to have flavin-containing monooxygenase activity.
[0600] The enzyme identified as Sequence Oxid-478 2418_g is encoded by the nucleotides of SEQ ID No: 955 which encodes the amino acid sequence of SEQ ID No: 956. This enzyme is believed to have cyclohexanone monooxygenase activity.
[0601] The enzyme identified as Sequence Oxid-479 2516_g scaffold00050.G695
scaffold00050.pathl .gene325 is encoded by the nucleotides of SEQ ID No: 957 which encodes the amino acid sequence of SEQ ID No: 958. This enzyme is believed to have kynurenine 3 -monooxygenase activity.
[0602] The enzyme identified as Sequence Oxid-480 2632_g scaffold00050.G899,
scaffold00050.G900 scaffold00050.pathl .gene425 is encoded by the nucleotides of SEQ ID No: 959 which encodes the amino acid sequence of SEQ ID No: 960. This enzyme is believed to have flavin-containing monooxygenase activity.
[0603] The enzyme identified as Sequence Oxid-481 2725_g scaffold00050.G1038 scaffold00050.pathl .gene511 is encoded by the nucleotides of SEQ ID No: 961 which encodes the amino acid sequence of SEQ ID No: 962. This enzyme is believed to have monooxygenase activity.
[0604] The enzyme identified as Sequence Oxid-482 2727_g scaffold00050.G1041
scaffold00050.pathl .gene514 is encoded by the nucleotides of SEQ ID No: 963 which encodes the amino acid sequence of SEQ ID No: 964. This enzyme is believed to have monooxygenase activity.
[0605] The enzyme identified as Sequence Oxid-483 2729_g scaffold00050.G1042
scaffold00050.pathl .gene515 is encoded by the nucleotides of SEQ ID No: 965 which encodes the amino acid sequence of SEQ ID No: 966. This enzyme is believed to have monooxygenase activity.
[0606] The enzyme identified as Sequence Oxid-484 2937_g scaffold00050.G1359
scaffold00050.pathl .gene702 is encoded by the nucleotides of SEQ ID No: 967 which encodes the amino acid sequence of SEQ ID No: 968. This enzyme is believed to have monooxygenase activity.
[0607] The enzyme identified as Sequence Oxid-485 2987_g scaffold00050.G1435
scaffold00050.pathl .gene747 is encoded by the nucleotides of SEQ ID No: 969 which encodes the amino acid sequence of SEQ ID No: 970. This enzyme is believed to have monooxygenase activity.
[0608] The enzyme identified as Sequence Oxid-486 3022_g scaffold00050.G1491, scaffold00050.G1492 scaffold00050.pathl .gene784 is encoded by the nucleotides of SEQ ID No: 971 which encodes the amino acid sequence of SEQ ID No: 972.
This enzyme is believed to have monooxygenase activity.
[0609] The enzyme identified as Sequence Oxid-487 3068_g scaffold00050.G1590
scaffold00050.pathl .gene821 is encoded by the nucleotides of SEQ ID No: 973 which encodes the amino acid sequence of SEQ ID No: 974. This enzyme is believed to have monooxygenase activity.
[0610] The enzyme identified as Sequence Oxid-488 3091_g scaffold00050.G1619
scaffold00050.pathl .gene838 is encoded by the nucleotides of SEQ ID No: 975 which encodes the amino acid sequence of SEQ ID No: 976. This enzyme is believed to have monooxygenase activity.
[0611] The enzyme identified as Sequence Oxid-489 3115_g scaffold00050.G1657
scaffold00050.pathl .gene861 is encoded by the nucleotides of SEQ ID No: 977 which encodes the amino acid sequence of SEQ ID No: 978. This enzyme is believed to have aromatase activity, NADPH-hemoprotein reductase activity.
[0612] The enzyme identified as Sequence Oxid-490 3123_g scaffold00050.G1667 is encoded by the nucleotides of SEQ ID No: 979 which encodes the amino acid sequence of SEQ ID No: 980. This enzyme is believed to have monooxygenase activity.
[0613] The enzyme identified as Sequence Oxid-491 3124_g scaffold00050.G1668
scaffold00050.pathl .gene864 is encoded by the nucleotides of SEQ ID No: 981 which encodes the amino acid sequence of SEQ ID No: 982. This enzyme is believed to have monooxygenase activity.
[0614] The enzyme identified as Sequence Oxid-492 3152_g scaffold00053.G27
scaffold00053.pathl .genel3 is encoded by the nucleotides of SEQ ID No: 983 which encodes the amino acid sequence of SEQ ID No: 984. This enzyme is believed to have monooxygenase activity.
[0615] The enzyme identified as Sequence Oxid-493 3168_g scaffold00053.G67
scaffold00053.pathl .gene26 is encoded by the nucleotides of SEQ ID No: 985 which encodes the amino acid sequence of SEQ ID No: 986. This enzyme is believed to have monooxygenase activity.
[0616] The enzyme identified as Sequence Oxid-494 3233_g scaffold00068.Gl
scaffold00068.pathl .gene2 is encoded by the nucleotides of SEQ ID No: 987 which encodes the amino acid sequence of SEQ ID No: 988. This enzyme is believed to have monooxygenase activity.
[0617] The enzyme identified as Sequence Oxid-495 3574_g scaffold00071.G571
scaffold00071.pathl .gene285 is encoded by the nucleotides of SEQ ID No: 989 which encodes the amino acid sequence of SEQ ID No: 990. This enzyme is believed to have sterol 14-demethylase activity.
[0618] The enzyme identified as Sequence Oxid-496 3618_g scaffold00071.G633
scaffold00071.pathl .gene321 is encoded by the nucleotides of SEQ ID No: 991 which encodes the amino acid sequence of SEQ ID No: 992. This enzyme is believed to have oxidoreductase activity, acting on paired d activity.
[0619] The enzyme identified as Sequence Oxid-497 3733_g scaffold00071.G796
scaffold00071.pathl .gene427 is encoded by the nucleotides of SEQ ID No: 993 which encodes the amino acid sequence of SEQ ID No: 994. This enzyme is believed to have phenol 2-monooxygenase activity.
[0620] The enzyme identified as Sequence Oxid-498 3734_g scaffold00071.G797
scaffold00071.pathl .gene427 is encoded by the nucleotides of SEQ ID No: 995 which encodes the amino acid sequence of SEQ ID No: 996. This enzyme is believed to have monooxygenase activity.
[0621] The enzyme identified as Sequence Oxid-499 3775_g scaffold00071.G852
scaffold00071.pathl .gene459 is encoded by the nucleotides of SEQ ID No: 997 which encodes the amino acid sequence of SEQ ID No: 998. This enzyme is believed to have monophenol monooxygenase activity.
[0622] The enzyme identified as Sequence Oxid-500 3805_g scaffold00071.pathl .gene492 is encoded by the nucleotides of SEQ ID No: 999 which encodes the amino acid sequence of SEQ ID No: 1000. This enzyme is believed to have dopamine beta- monooxygenase activity.
[0623] The enzyme identified as Sequence Oxid-501 3903_g scaffold00071.pathl .gene580 is encoded by the nucleotides of SEQ ID No: 1001 which encodes the amino acid sequence of SEQ ID No: 1002. This enzyme is believed to have monooxygenase activity.
[0624] The enzyme identified as Sequence Oxid-502 3965_g scaffold00071.pathl .gene621 is encoded by the nucleotides of SEQ ID No: 1003 which encodes the amino acid sequence of SEQ ID No: 1004. This enzyme is believed to have monooxygenase activity.
[0625] The enzyme identified as Sequence Oxid-503 4080_g scaffold00071.pathl .gene716 is encoded by the nucleotides of SEQ ID No: 1005 which encodes the amino acid sequence of SEQ ID No: 1006. This enzyme is believed to have oxidoreductase activity.
[0626] The enzyme identified as Sequence Oxid-504 4268_g scaffold00071.pathl .gene875 is encoded by the nucleotides of SEQ ID No: 1007 which encodes the amino acid sequence of SEQ ID No: 1008. This enzyme is believed to have monooxygenase activity.
[0627] The enzyme identified as Sequence Oxid-505 428 l_g scaffold00071.pathl .gene885 is encoded by the nucleotides of SEQ ID No: 1009 which encodes the amino acid sequence of SEQ ID No: 1010. This enzyme is believed to have monooxygenase activity. [0628] The enzyme identified as Sequence Oxid-506 4422_g
scaffold00071.pathl .gene 1013 is encoded by the nucleotides of SEQ ID No : 1011 which encodes the amino acid sequence of SEQ ID No: 1012. This enzyme is believed to have monooxygenase activity.
[0629] The enzyme identified as Sequence Oxid-507 443 l_g
scaffold00071. athl . genel020 is encoded by the nucleotides of SEQ ID No: 1013 which encodes the amino acid sequence of SEQ ID No: 1014. This enzyme is believed to have monooxygenase activity.
[0630] The enzyme identified as Sequence Oxid-508 4623_g
scaffold00071. pathl . genel 188 is encoded by the nucleotides of SEQ ID No: 1015 which encodes the amino acid sequence of SEQ ID No: 1016. This enzyme is believed to have monooxygenase activity.
[0631] The enzyme identified as Sequence Oxid-509 4698_g
scaffold00071. pathl . genel246 is encoded by the nucleotides of SEQ ID No: 1017 which encodes the amino acid sequence of SEQ ID No: 1018. This enzyme is believed to have monooxygenase activity.
[0632] The enzyme identified as Sequence Oxid-510 5346_g scaffold00071.G3395
scaffold00071.pathl .genel812 is encoded by the nucleotides of SEQ ID No: 1019 which encodes the amino acid sequence of SEQ ID No: 1020. This enzyme is believed to have monooxygenase activity.
[0633] The enzyme identified as Sequence Oxid-511 5502_g scaffold00075.G170 is
encoded by the nucleotides of SEQ ID No: 1021 which encodes the amino acid sequence of SEQ ID No: 1022. This enzyme is believed to have monooxygenase activity.
[0634] The enzyme identified as Sequence Oxid-512 581 l_g scaffold00075. pathl . gene356 is encoded by the nucleotides of SEQ ID No: 1023 which encodes the amino acid sequence of SEQ ID No: 1024. This enzyme is believed to have monooxygenase activity.
[0635] The enzyme identified as Sequence Oxid-513 5910_g is encoded by the nucleotides of SEQ ID No: 1025 which encodes the amino acid sequence of SEQ ID No: 1026. This enzyme is believed to have monooxygenase activity.
[0636] The enzyme identified as Sequence Oxid-514 591 l_g is encoded by the nucleotides of SEQ ID No: 1027 which encodes the amino acid sequence of SEQ ID No: 1028. This enzyme is believed to have monooxygenase activity.
[0637] The enzyme identified as Sequence Oxid-515 5928_g scaflbld00075.pathl .gene459 is encoded by the nucleotides of SEQ ID No: 1029 which encodes the amino acid sequence of SEQ ID No: 1030. This enzyme is believed to have monooxygenase activity.
[0638] The enzyme identified as Sequence Oxid-516 5977_g scaffold00075.pathl .gene504 is encoded by the nucleotides of SEQ ID No: 1031 which encodes the amino acid sequence of SEQ ID No: 1032. This enzyme is believed to have monooxygenase activity.
[0639] The enzyme identified as Sequence Oxid-517 6245_g scaffold00092.pathl .gene2 is encoded by the nucleotides of SEQ ID No: 1033 which encodes the amino acid sequence of SEQ ID No: 1034. This enzyme is believed to have monooxygenase activity.
[0640] The enzyme identified as Sequence Oxid-518 6253_g scaffold00092.pathl .gene9 is encoded by the nucleotides of SEQ ID No: 1035 which encodes the amino acid sequence of SEQ ID No: 1036. This enzyme is believed to have Oxidoreductase activity.
[0641] The enzyme identified as Sequence Oxid-519 6265_g scaffold00092.pathl .gene20 is encoded by the nucleotides of SEQ ID No: 1037 which encodes the amino acid sequence of SEQ ID No: 1038. This enzyme is believed to have monooxygenase activity.
[0642] The enzyme identified as Sequence Oxid-520 6288_g is encoded by the nucleotides of SEQ ID No: 1039 which encodes the amino acid sequence of SEQ ID No: 1040. This enzyme is believed to have monooxygenase activity.
[0643] The enzyme identified as Sequence Oxid-521 6289_g scaffold00092.pathl .gene41 is encoded by the nucleotides of SEQ ID No: 1041 which encodes the amino acid sequence of SEQ ID No: 1042. This enzyme is believed to have monooxygenase activity.
[0644] The enzyme identified as Sequence Oxid-522 629 l_g scaffold00092.pathl .gene42 is encoded by the nucleotides of SEQ ID No: 1043 which encodes the amino acid sequence of SEQ ID No: 1044. This enzyme is believed to have monooxygenase activity.
[0645] The enzyme identified as Sequence Oxid-523 6302_g scaffold00092.G89 scaffold00092.pathl .gene52 is encoded by the nucleotides of SEQ ID No: 1045 which encodes the amino acid sequence of SEQ ID No: 1046. This enzyme is believed to have monooxygenase activity.
[0646] The enzyme identified as Sequence Oxid-524 6303_g scaffold00092.pathl .gene52 is encoded by the nucleotides of SEQ ID No: 1047 which encodes the amino acid sequence of SEQ ID No: 1048. This enzyme is believed to have monooxygenase activity.
[0647] The enzyme identified as Sequence Oxid-525 6340_g scaffold00092.G153
scaffold00092.pathl .gene72 is encoded by the nucleotides of SEQ ID No: 1049 which encodes the amino acid sequence of SEQ ID No: 1050. This enzyme is believed to have monooxygenase activity.
[0648] The enzyme identified as Sequence Oxid-526 634 l_g is encoded by the nucleotides of SEQ ID No: 1051 which encodes the amino acid sequence of SEQ ID No: 1052. This enzyme is believed to have monooxygenase activity.
[0649] The enzyme identified as Sequence Oxid-527 6343_g scaffold00092.pathl .gene76 is encoded by the nucleotides of SEQ ID No: 1053 which encodes the amino acid sequence of SEQ ID No: 1054. This enzyme is believed to have monooxygenase activity.
[0650] The enzyme identified as Sequence Oxid-528 6368_g scaffold00092.pathl .genel03 is encoded by the nucleotides of SEQ ID No: 1055 which encodes the amino acid sequence of SEQ ID No: 1056. This enzyme is believed to have oxidoreductase activity.
[0651] The enzyme identified as Sequence Oxid-529 6423_g scaffold00092.pathl .genel47 is encoded by the nucleotides of SEQ ID No: 1057 which encodes the amino acid sequence of SEQ ID No: 1058. This enzyme is believed to have monooxygenase activity.
[0652] The enzyme identified as Sequence Oxid-530 6449_g scaffold00092.G332
scaffold00092.pathl .genel67 is encoded by the nucleotides of SEQ ID No: 1059 which encodes the amino acid sequence of SEQ ID No: 1060. This enzyme is believed to have monooxygenase activity.
[0653] The enzyme identified as Sequence Oxid-531 6808_g is encoded by the nucleotides of SEQ ID No: 1061 which encodes the amino acid sequence of SEQ ID No: 1062. This enzyme is believed to have monooxygenase activity. [0654] The enzyme identified as Sequence Oxid-532 6820_g scaflbldOOl 15.pathl .gene2 is encoded by the nucleotides of SEQ ID No: 1063 which encodes the amino acid sequence of SEQ ID No: 1064. This enzyme is believed to have monooxygenase activity.
[0655] The enzyme identified as Sequence Oxid-533 6828_g scaffold00120.pathl .genel is encoded by the nucleotides of SEQ ID No: 1065 which encodes the amino acid sequence of SEQ ID No: 1066. This enzyme is believed to have monooxygenase activity.
[0656] The enzyme identified as Sequence Oxid-534 6864_g scaffold00122.pathl .gene29 is encoded by the nucleotides of SEQ ID No: 1067 which encodes the amino acid sequence of SEQ ID No: 1068. This enzyme is believed to have monooxygenase activity.
[0657] The enzyme identified as Sequence Oxid-535 687 l_g is encoded by the nucleotides of SEQ ID No: 1069 which encodes the amino acid sequence of SEQ ID No: 1070. This enzyme is believed to have monooxygenase activity.
[0658] The enzyme identified as Sequence Oxid-536 695 l_g scaffold00122.G198
scaffold00122.pathl .genel08 is encoded by the nucleotides of SEQ ID No: 1071 which encodes the amino acid sequence of SEQ ID No: 1072. This enzyme is believed to have monooxygenase activity.
[0659] The enzyme identified as Sequence Oxid-537 6952_g scaffold00122.pathl .genel09 is encoded by the nucleotides of SEQ ID No: 1073 which encodes the amino acid sequence of SEQ ID No: 1074. This enzyme is believed to have monooxygenase activity.
[0660] The enzyme identified as Sequence Oxid-538 6954_g scaffold00122.G202
scaffold00122.pathl .genel 11 is encoded by the nucleotides of SEQ ID No: 1075 which encodes the amino acid sequence of SEQ ID No: 1076. This enzyme is believed to have monooxygenase activity.
[0661] The enzyme identified as Sequence Oxid-539 7015_g scaffold00131.pathl .gene39 is encoded by the nucleotides of SEQ ID No: 1077 which encodes the amino acid sequence of SEQ ID No: 1078. This enzyme is believed to have monooxygenase activity.
[0662] The enzyme identified as Sequence Oxid-540 7202_g scaffold00131.G363 is
encoded by the nucleotides of SEQ ID No: 1079 which encodes the amino acid sequence of SEQ ID No: 1080. This enzyme is believed to have monooxygenase activity.
[0663] The enzyme identified as Sequence Oxid-541 7247_g scaffold00131.pathl .gene258 is encoded by the nucleotides of SEQ ID No: 1081 which encodes the amino acid sequence of SEQ ID No: 1082. This enzyme is believed to have monooxygenase activity.
[0664] The enzyme identified as Sequence Oxid-542 7448_g scaffold00131.G752
scaffold00131.pathl .gene445 is encoded by the nucleotides of SEQ ID No: 1083 which encodes the amino acid sequence of SEQ ID No: 1084. This enzyme is believed to have monooxygenase activity.
[0665] The enzyme identified as Sequence Oxid-543 7522_g scaffold00131.pathl .gene518 is encoded by the nucleotides of SEQ ID No: 1085 which encodes the amino acid sequence of SEQ ID No: 1086. This enzyme is believed to have monooxygenase activity.
[0666] The enzyme identified as Sequence Oxid-544 7568_g scaffold00131.pathl .gene546 is encoded by the nucleotides of SEQ ID No: 1087 which encodes the amino acid sequence of SEQ ID No: 1088. This enzyme is believed to have monooxygenase activity.
[0667] The enzyme identified as Sequence Oxid-545 769 l_g scaffold00131.pathl .gene649 is encoded by the nucleotides of SEQ ID No: 1089 which encodes the amino acid sequence of SEQ ID No: 1090. This enzyme is believed to have monooxygenase activity.
[0668] The enzyme identified as Sequence Oxid-546 8109_g scaffold00131.G1806
scaffold00131.pathl .genel016 is encoded by the nucleotides of SEQ ID No: 1091 which encodes the amino acid sequence of SEQ ID No: 1092. This enzyme is believed to have monooxygenase activity.
[0669] The enzyme identified as Sequence Oxid-547 7203_g scaffold00131.G364
scaffold00131.pathl .gene218 is encoded by the nucleotides of SEQ ID No: 1093 which encodes the amino acid sequence of SEQ ID No: 1094. This enzyme is believed to have monooxygenase activity.
[0670] The enzyme identified as Sequence Oxid-548 7350_g scaffold00131.pathl .gene355 is encoded by the nucleotides of SEQ ID No: 1095 which encodes the amino acid sequence of SEQ ID No: 1096. This enzyme is believed to have trimethyllysine dioxygenase activity.
[0671] The enzyme identified as Sequence Oxid-549 735 l_g scaflbld00131.pathl .gene356 is encoded by the nucleotides of SEQ ID No: 1097 which encodes the amino acid sequence of SEQ ID No: 1098. This enzyme is believed to have dioxygenase activity.
[0672] The enzyme identified as Sequence Oxid-550 7482_g scaffold00131.G810
scaffold00131.pathl .gene479 is encoded by the nucleotides of SEQ ID No: 1099 which encodes the amino acid sequence of SEQ ID NO: 1100. This enzyme is believed to have oxidoreductase activity.
[0673] The enzyme identified as Sequence Oxid-551 8028_g is encoded by the nucleotides of SEQ ID No: 1101 which encodes the amino acid sequence of SEQ ID No: 1102. This enzyme is believed to have dioxygenase activity.
[0674] The enzyme identified as Sequence Oxid-552 8248_g
scaffold00131.pathl .genel l38 is encoded by the nucleotides of SEQ ID No: 1103 which encodes the amino acid sequence of SEQ ID No: 1104. This enzyme is believed to have oxidoreductase activity.
[0675] The enzyme identified as Sequence Oxid-553 8686_g scaffold00142.pathl .genel49 is encoded by the nucleotides of SEQ ID No: 1105 which encodes the amino acid sequence of SEQ ID No: 1106. This enzyme is believed to have oxidoreductase activity.
[0676] The enzyme identified as Sequence Oxid-554 8737_g scaffold00142.G386
scaffold00142.pathl .genel94 is encoded by the nucleotides of SEQ ID No: 1107 which encodes the amino acid sequence of SEQ ID No: 1108. This enzyme is believed to have dioxygenase activity.
[0677] The enzyme identified as Sequence Oxid-555 8896_g scaffold00169.pathl .gene4 is encoded by the nucleotides of SEQ ID No: 1109 which encodes the amino acid sequence of SEQ ID No: 1110. This enzyme is believed to have oxidoreductase activity.
[0678] The enzyme identified as Sequence Oxid-556 9432_g scaffold00227.G60
scaffold00227.pathl .gene32 is encoded by the nucleotides of SEQ ID No: 1111 which encodes the amino acid sequence of SEQ ID No: 1112. This enzyme is believed to have dioxygenase activity.
[0679] The enzyme identified as Sequence Oxid-557 9504_g scaffold00227.G198 scaffold00227.pathl .genel02 is encoded by the nucleotides of SEQ ID No: 1113 which encodes the amino acid sequence of SEQ ID No: 1114. This enzyme is believed to have dioxygenase activity.
[0680] The enzyme identified as Sequence Oxid-558 566_g scaffold00016.pathl .gene487 is encoded by the nucleotides of SEQ ID No: 1115 which encodes the amino acid sequence of SEQ ID No: 1116. This enzyme is believed to have dioxygenase activity.
[0681] The enzyme identified as Sequence Oxid-559 1015_g scaffold00031.G158
scaffold00031.pathl .gene76 is encoded by the nucleotides of SEQ ID No: 1117 which encodes the amino acid sequence of SEQ ID No: 1118. This enzyme is believed to have dioxygenase activity.
[0682] The enzyme identified as Sequence Oxid-560 1064_g scaffold00031.G227
scaffold00031. pathl . genel 17 is encoded by the nucleotides of SEQ ID No: 1119 which encodes the amino acid sequence of SEQ ID No: 1120. This enzyme is believed to have dioxygenase activity.
[0683] The enzyme identified as Sequence Oxid-561 1426_g scaffold00031. pathl . gene433 is encoded by the nucleotides of SEQ ID No: 1121 which encodes the amino acid sequence of SEQ ID No: 1122. This enzyme is believed to have oxidoreductase activity.
[0684] The enzyme identified as Sequence Oxid-562 1948_g scaffold00031.G1607
scaffold00031. pathl . gene891 is encoded by the nucleotides of SEQ ID No: 1123 which encodes the amino acid sequence of SEQ ID No: 1124. This enzyme is believed to have dioxygenase activity.
[0685] The enzyme identified as Sequence Oxid-563 2265_g scaffold00050.pathl . genel 14 is encoded by the nucleotides of SEQ ID No: 1125 which encodes the amino acid sequence of SEQ ID No: 1126. This enzyme is believed to have dioxygenase activity.
[0686] The enzyme identified as Sequence Oxid-564 3380_g scaffold00071.G250,
scaffold00071.G251 scaffold00071.pathl .genel 14 is encoded by the nucleotides of SEQ ID No: 1127 which encodes the amino acid sequence of SEQ ID No: 1128. This enzyme is believed to have dioxygenase activity.
[0687] The enzyme identified as Sequence Oxid-565 3432_g scaffold00071. pathl . genel66 is encoded by the nucleotides of SEQ ID No: 1129 which encodes the amino acid sequence of SEQ ID No: 1130. This enzyme is believed to have dioxygenase activity.
[0688] The enzyme identified as Sequence Oxid-566 4675_g
scaffold00071.pathl .genel225 is encoded by the nucleotides of SEQ ID No: 1131 which encodes the amino acid sequence of SEQ ID No: 1132. This enzyme is believed to have oxidoreductase activity.
[0689] The enzyme identified as Sequence Oxid-567 5234_g
scaffold00071. athl . genel717 is encoded by the nucleotides of SEQ ID No: 1133 which encodes the amino acid sequence of SEQ ID No: 1134. This enzyme is believed to have dioxygenase activity.
[0690] The enzyme identified as Sequence Oxid-568 5645_g is encoded by the nucleotides of SEQ ID No: 1135 which encodes the amino acid sequence of SEQ ID No: 1136.
This enzyme is believed to have dioxygenase activity.
[0691] The enzyme identified as Sequence Oxid-569 6086_g scaffold00075. athl . gene608 is encoded by the nucleotides of SEQ ID No: 1137 which encodes the amino acid sequence of SEQ ID No: 1138. This enzyme is believed to have sulfonate dioxygenase activity.
[0692] The enzyme identified as Sequence Oxid-570 27_g scaffold00016.G14
scaffold00016.pathl .gene5 is encoded by the nucleotides of SEQ ID No: 1139 which encodes the amino acid sequence of SEQ ID No: 1140. This enzyme is believed to have oxidoreductase activity.
[0693] The enzyme identified as Sequence Oxid-571 28_g is encoded by the nucleotides of
SEQ ID No: 1141 which encodes the amino acid sequence of SEQ ID No: 1142.
This enzyme is believed to have oxidoreductase activity.
[0694] The enzyme identified as Sequence Oxid-572 52_g is encoded by the nucleotides of
SEQ ID No: 1143 which encodes the amino acid sequence of SEQ ID No: 1144.
This enzyme is believed to have oxidoreductase activity.
[0695] The enzyme identified as Sequence Oxid-573 87_g is encoded by the nucleotides of
SEQ ID No: 1145 which encodes the amino acid sequence of SEQ ID No: 1146.
This enzyme is believed to have oxidoreductase activity.
[0696] The enzyme identified as Sequence Oxid-574 105_g is encoded by the nucleotides of SEQ ID No: 1147 which encodes the amino acid sequence of SEQ ID No: 1148.
This enzyme is believed to have oxidoreductase activity. [0697] The enzyme identified as Sequence Oxid-575 174_g is encoded by the nucleotides of SEQ ID No: 1149 which encodes the amino acid sequence of SEQ ID No: 1150.
This enzyme is believed to have oxidoreductase activity.
[0698] The enzyme identified as Sequence Oxid-576 182_g is encoded by the nucleotides of SEQ ID No: 1151 which encodes the amino acid sequence of SEQ ID No: 1152.
This enzyme is believed to have oxidoreductase activity.
[0699] The enzyme identified as Sequence Oxid-577 290_g is encoded by the nucleotides of SEQ ID No: 1153 which encodes the amino acid sequence of SEQ ID No: 1154.
This enzyme is believed to have glutamate synthase (NADPH) activity.
[0700] The enzyme identified as Sequence Oxid-578 308_g is encoded by the nucleotides of SEQ ID No: 1155 which encodes the amino acid sequence of SEQ ID No: 1156.
This enzyme is believed to have oxidoreductase activity.
[0701] The enzyme identified as Sequence Oxid-579 309_g is encoded by the nucleotides of SEQ ID No: 1157 which encodes the amino acid sequence of SEQ ID No: 1158.
This enzyme is believed to have oxidoreductase activity.
[0702] The enzyme identified as Sequence Oxid-580 367_g is encoded by the nucleotides of SEQ ID No: 1159 which encodes the amino acid sequence of SEQ ID No: 1160.
This enzyme is believed to have oxidoreductase activity.
[0703] The enzyme identified as Sequence Oxid-581 394_g is encoded by the nucleotides of SEQ ID No: 1161 which encodes the amino acid sequence of SEQ ID No: 1162.
This enzyme is believed to have Oxidase activity.
[0704] The enzyme identified as Sequence Oxid-582 429_g is encoded by the nucleotides of SEQ ID No: 1163 which encodes the amino acid sequence of SEQ ID No: 1164.
This enzyme is believed to have oxidoreductase activity.
[0705] The enzyme identified as Sequence Oxid-583 455_g is encoded by the nucleotides of SEQ ID No: 1165 which encodes the amino acid sequence of SEQ ID No: 1166.
This enzyme is believed to have oxidoreductase activity.
[0706] The enzyme identified as Sequence Oxid-584 473_g is encoded by the nucleotides of SEQ ID No: 1167 which encodes the amino acid sequence of SEQ ID No: 1168.
This enzyme is believed to have oxidoreductase activity.
[0707] The enzyme identified as Sequence Oxid-585 541_g is encoded by the nucleotides of SEQ ID No: 1169 which encodes the amino acid sequence of SEQ ID No: 1170.
This enzyme is believed to have oxidoreductase activity. [0708] The enzyme identified as Sequence Oxid-586 645_g is encoded by the nucleotides of SEQ ID No: 1171 which encodes the amino acid sequence of SEQ ID No: 1172.
This enzyme is believed to have oxidase activity.
[0709] The enzyme identified as Sequence Oxid-587 697_g is encoded by the nucleotides of SEQ ID No: 1173 which encodes the amino acid sequence of SEQ ID No: 1174.
This enzyme is believed to have oxidoreductase activity.
[0710] The enzyme identified as Sequence Oxid-588 714_g is encoded by the nucleotides of SEQ ID No: 1175 which encodes the amino acid sequence of SEQ ID No: 1176.
This enzyme is believed to have carbonyl reductase (NADPH) activity.
[0711] The enzyme identified as Sequence Oxid-589 719_g is encoded by the nucleotides of SEQ ID No: 1177 which encodes the amino acid sequence of SEQ ID No: 1178.
This enzyme is believed to have oxidoreductase activity.
[0712] The enzyme identified as Sequence Oxid-590 730_g is encoded by the nucleotides of SEQ ID No: 1179 which encodes the amino acid sequence of SEQ ID No: 1180.
This enzyme is believed to have glutathione-disulfide reductase activity.
[0713] The enzyme identified as Sequence Oxid-591 737_g is encoded by the nucleotides of SEQ ID No: 1181 which encodes the amino acid sequence of SEQ ID No: 1182.
This enzyme is believed to have oxidoreductase activity.
[0714] The enzyme identified as Sequence Oxid-592 829_g is encoded by the nucleotides of SEQ ID No: 1183 which encodes the amino acid sequence of SEQ ID No: 1184.
This enzyme is believed to have hydroxylase activity.
[0715] The enzyme identified as Sequence Oxid-593 835_g is encoded by the nucleotides of SEQ ID No: 1185 which encodes the amino acid sequence of SEQ ID No: 1186.
This enzyme is believed to have ribonucleotide reductase activity.
[0716] The enzyme identified as Sequence Oxid-594 940_g is encoded by the nucleotides of SEQ ID No: 1187 which encodes the amino acid sequence of SEQ ID No: 1188.
This enzyme is believed to have catalase activity.
[0717] The enzyme identified as Sequence Oxid-595 961_g is encoded by the nucleotides of SEQ ID No: 1189 which encodes the amino acid sequence of SEQ ID No: 1190.
This enzyme is believed to have oxidoreductase activity.
[0718] The enzyme identified as Sequence Oxid-596 987_g is encoded by the nucleotides of SEQ ID No: 1191 which encodes the amino acid sequence of SEQ ID No: 1192.
This enzyme is believed to have oxidoreductase activity. [0719] The enzyme identified as Sequence Oxid-597 999_g is encoded by the nucleotides of SEQ ID No: 1193 which encodes the amino acid sequence of SEQ ID No: 1194.
This enzyme is believed to have oxidoreductase activity.
[0720] The enzyme identified as Sequence Oxid-598 1025_g is encoded by the nucleotides of SEQ ID No: 1195 which encodes the amino acid sequence of SEQ ID No: 1196.
This enzyme is believed to have oxidoreductase activity.
[0721] The enzyme identified as Sequence Oxid-599 1040_g is encoded by the nucleotides of SEQ ID No: 1197 which encodes the amino acid sequence of SEQ ID No: 1198.
This enzyme is believed to have oxidoreductase activity.
[0722] The enzyme identified as Sequence Oxid-600 1087_g is encoded by the nucleotides of SEQ ID No: 1199 which encodes the amino acid sequence of SEQ ID No: 1200.
This enzyme is believed to have oxidoreductase activity.
[0723] The enzyme identified as Sequence Oxid-601 1115_g is encoded by the nucleotides of SEQ ID No: 1201 which encodes the amino acid sequence of SEQ ID No: 1202.
This enzyme is believed to have urate oxidase activity.
[0724] The enzyme identified as Sequence Oxid-602 1147_g is encoded by the nucleotides of SEQ ID No: 1203 which encodes the amino acid sequence of SEQ ID No: 1204.
This enzyme is believed to have ribonucleoside-diphosphate reductase activity.
[0725] The enzyme identified as Sequence Oxid-603 1220_g is encoded by the nucleotides of SEQ ID No: 1205 which encodes the amino acid sequence of SEQ ID No: 1206.
This enzyme is believed to have oxidoreductase activity.
[0726] The enzyme identified as Sequence Oxid-604 1222_g is encoded by the nucleotides of SEQ ID No: 1207 which encodes the amino acid sequence of SEQ ID No: 1208.
This enzyme is believed to have oxidoreductase activity.
[0727] The enzyme identified as Sequence Oxid-605 1223_g is encoded by the nucleotides of SEQ ID No: 1209 which encodes the amino acid sequence of SEQ ID No: 1210.
This enzyme is believed to have pyrroline-5-carboxylate reductase activity.
[0728] The enzyme identified as Sequence Oxid-606 1225_g is encoded by the nucleotides of SEQ ID No: 1211 which encodes the amino acid sequence of SEQ ID No: 1212.
This enzyme is believed to have oxidoreductase activity.
[0729] The enzyme identified as Sequence Oxid-607 1226_g is encoded by the nucleotides of SEQ ID No: 1213 which encodes the amino acid sequence of SEQ ID No: 1214.
This enzyme is believed to have oxidoreductase activity. [0730] The enzyme identified as Sequence Oxid-608 1232_g is encoded by the nucleotides of SEQ ID No: 1215 which encodes the amino acid sequence of SEQ ID No: 1216.
This enzyme is believed to have oxidoreductase activity.
[0731] The enzyme identified as Sequence Oxid-609 1250_g is encoded by the nucleotides of SEQ ID No: 1217 which encodes the amino acid sequence of SEQ ID No: 1218.
This enzyme is believed to have oxidoreductase activity.
[0732] The enzyme identified as Sequence Oxid-610 1272_g is encoded by the nucleotides of SEQ ID No: 1219 which encodes the amino acid sequence of SEQ ID No: 1220.
This enzyme is believed to have oxidoreductase activity.
[0733] The enzyme identified as Sequence Oxid-611 1273_g is encoded by the nucleotides of SEQ ID No: 1221 which encodes the amino acid sequence of SEQ ID No: 1222.
This enzyme is believed to have oxidoreductase activity.
[0734] The enzyme identified as Sequence Oxid-612 1298_g is encoded by the nucleotides of SEQ ID No: 1223 which encodes the amino acid sequence of SEQ ID No: 1224.
This enzyme is believed to have pyrroline-5-carboxylate reductase activity.
[0735] The enzyme identified as Sequence Oxid-613 1306_g is encoded by the nucleotides of SEQ ID No: 1225 which encodes the amino acid sequence of SEQ ID No: 1226.
This enzyme is believed to have oxidoreductase activity.
[0736] The enzyme identified as Sequence Oxid-614 1337_g is encoded by the nucleotides of SEQ ID No: 1227 which encodes the amino acid sequence of SEQ ID No: 1228.
This enzyme is believed to have dihydro folate reductase activity.
[0737] The enzyme identified as Sequence Oxid-615 1345_g is encoded by the nucleotides of SEQ ID No: 1229 which encodes the amino acid sequence of SEQ ID No: 1230.
This enzyme is believed to have oxidoreductase activity.
[0738] The enzyme identified as Sequence Oxid-616 1362_g is encoded by the nucleotides of SEQ ID No: 1231 which encodes the amino acid sequence of SEQ ID No: 1232.
This enzyme is believed to have oxidoreductase activity.
[0739] The enzyme identified as Sequence Oxid-617 1427_g is encoded by the nucleotides of SEQ ID No: 1233 which encodes the amino acid sequence of SEQ ID No: 1234.
This enzyme is believed to have oxidoreductase activity.
[0740] The enzyme identified as Sequence Oxid-618 145 l_g is encoded by the nucleotides of SEQ ID No: 1235 which encodes the amino acid sequence of SEQ ID No: 1236.
This enzyme is believed to have oxidoreductase activity. [0741] The enzyme identified as Sequence Oxid-619 1452_g is encoded by the nucleotides of SEQ ID No: 1237 which encodes the amino acid sequence of SEQ ID No: 1238.
This enzyme is believed to have oxidoreductase activity.
[0742] The enzyme identified as Sequence Oxid-620 1461_g is encoded by the nucleotides of SEQ ID No: 1239 which encodes the amino acid sequence of SEQ ID No: 1240.
This enzyme is believed to have oxidoreductase activity.
[0743] The enzyme identified as Sequence Oxid-621 1561_g is encoded by the nucleotides of SEQ ID No: 1241 which encodes the amino acid sequence of SEQ ID No: 1242.
This enzyme is believed to have oxidoreductase activity.
[0744] The enzyme identified as Sequence Oxid-622 1572_g is encoded by the nucleotides of SEQ ID No: 1243 which encodes the amino acid sequence of SEQ ID No: 1244.
This enzyme is believed to have oxidoreductase activity.
[0745] The enzyme identified as Sequence Oxid-623 1576_g is encoded by the nucleotides of SEQ ID No: 1245 which encodes the amino acid sequence of SEQ ID No: 1246.
This enzyme is believed to have oxidoreductase activity.
[0746] The enzyme identified as Sequence Oxid-624 1612_g is encoded by the nucleotides of SEQ ID No: 1247 which encodes the amino acid sequence of SEQ ID No: 1248.
This enzyme is believed to have oxidoreductase activity.
[0747] The enzyme identified as Sequence Oxid-625 1682_g is encoded by the nucleotides of SEQ ID No: 1249 which encodes the amino acid sequence of SEQ ID No: 1250.
This enzyme is believed to have oxidoreductase activity.
[0748] The enzyme identified as Sequence Oxid-626 1707_g is encoded by the nucleotides of SEQ ID No: 1251 which encodes the amino acid sequence of SEQ ID No: 1252.
This enzyme is believed to have ubiquinol-cytochrome-c reductase activity.
[0749] The enzyme identified as Sequence Oxid-627 1786_g is encoded by the nucleotides of SEQ ID No: 1253 which encodes the amino acid sequence of SEQ ID No: 1254.
This enzyme is believed to have amino-acid oxidase activity.
[0750] The enzyme identified as Sequence Oxid-628 1801_g is encoded by the nucleotides of SEQ ID No: 1255 which encodes the amino acid sequence of SEQ ID No: 1256.
This enzyme is believed to have oxidoreductase activity.
[0751] The enzyme identified as Sequence Oxid-629 1807_g is encoded by the nucleotides of SEQ ID No: 1257 which encodes the amino acid sequence of SEQ ID No: 1258.
This enzyme is believed to have oxidoreductase activity. [0752] The enzyme identified as Sequence Oxid-630 1810_g is encoded by the nucleotides of SEQ ID No: 1259 which encodes the amino acid sequence of SEQ ID No: 1260.
This enzyme is believed to have oxidoreductase activity.
[0753] The enzyme identified as Sequence Oxid-631 1818_g is encoded by the nucleotides of SEQ ID No: 1261 which encodes the amino acid sequence of SEQ ID No: 1262.
This enzyme is believed to have oxidoreductase activity.
[0754] The enzyme identified as Sequence Oxid-632 1835_g is encoded by the nucleotides of SEQ ID No: 1263 which encodes the amino acid sequence of SEQ ID No: 1264.
This enzyme is believed to have oxidoreductase activity.
[0755] The enzyme identified as Sequence Oxid-633 1886_g is encoded by the nucleotides of SEQ ID No: 1265 which encodes the amino acid sequence of SEQ ID No: 1266.
This enzyme is believed to have Oxidoreductase activity.
[0756] The enzyme identified as Sequence Oxid-634 1900_g is encoded by the nucleotides of SEQ ID No: 1267 which encodes the amino acid sequence of SEQ ID No: 1268.
This enzyme is believed to have oxidoreductase activity.
[0757] The enzyme identified as Sequence Oxid-635 1901_g is encoded by the nucleotides of SEQ ID No: 1269 which encodes the amino acid sequence of SEQ ID No: 1270.
This enzyme is believed to have Oxidoreductase activity.
[0758] The enzyme identified as Sequence Oxid-636 1990_g is encoded by the nucleotides of SEQ ID No: 1271 which encodes the amino acid sequence of SEQ ID No: 1272.
This enzyme is believed to have oxidoreductase activity.
[0759] The enzyme identified as Sequence Oxid-637 2020_g is encoded by the nucleotides of SEQ ID No: 1273 which encodes the amino acid sequence of SEQ ID No: 1274.
This enzyme is believed to have oxidoreductase activity.
[0760] The enzyme identified as Sequence Oxid-638 2053_g is encoded by the nucleotides of SEQ ID No: 1275 which encodes the amino acid sequence of SEQ ID No: 1276.
This enzyme is believed to have Oxidoreductase activity.
[0761] The enzyme identified as Sequence Oxid-639 2088_g is encoded by the nucleotides of SEQ ID No: 1277 which encodes the amino acid sequence of SEQ ID No: 1278.
This enzyme is believed to have cytochrome-c reductase activity.
[0762] The enzyme identified as Sequence Oxid-640 2177_g is encoded by the nucleotides of SEQ ID No: 1279 which encodes the amino acid sequence of SEQ ID No: 1280.
This enzyme is believed to have oxidoreductase activity. [0763] The enzyme identified as Sequence Oxid-641 2181_g is encoded by the nucleotides of SEQ ID No: 1281 which encodes the amino acid sequence of SEQ ID No: 1282.
This enzyme is believed to have oxidoreductase activity.
[0764] The enzyme identified as Sequence Oxid-642 220 l_g is encoded by the nucleotides of SEQ ID No: 1283 which encodes the amino acid sequence of SEQ ID No: 1284.
This enzyme is believed to have oxidoreductase activity.
[0765] The enzyme identified as Sequence Oxid-643 2213_g is encoded by the nucleotides of SEQ ID No: 1285 which encodes the amino acid sequence of SEQ ID No: 1286.
This enzyme is believed to have oxidoreductase activity.
[0766] The enzyme identified as Sequence Oxid-644 2254_g is encoded by the nucleotides of SEQ ID No: 1287 which encodes the amino acid sequence of SEQ ID No: 1288.
This enzyme is believed to have oxidoreductase activity.
[0767] The enzyme identified as Sequence Oxid-645 2262_g is encoded by the nucleotides of SEQ ID No: 1289 which encodes the amino acid sequence of SEQ ID No: 1290.
This enzyme is believed to have superoxide dismutase activity.
[0768] The enzyme identified as Sequence Oxid-646 2266_g is encoded by the nucleotides of SEQ ID No: 1291 which encodes the amino acid sequence of SEQ ID No: 1292.
This enzyme is believed to have oxidoreductase activity.
[0769] The enzyme identified as Sequence Oxid-647 2284_g is encoded by the nucleotides of SEQ ID No: 1293 which encodes the amino acid sequence of SEQ ID No: 1294.
This enzyme is believed to have oxidoreductase activity.
[0770] The enzyme identified as Sequence Oxid-648 2300_g is encoded by the nucleotides of SEQ ID No: 1295 which encodes the amino acid sequence of SEQ ID No: 1296.
This enzyme is believed to have oxidoreductase activity.
[0771] The enzyme identified as Sequence Oxid-649 2353_g is encoded by the nucleotides of SEQ ID No: 1297 which encodes the amino acid sequence of SEQ ID No: 1298.
This enzyme is believed to have oxidoreductase activity.
[0772] The enzyme identified as Sequence Oxid-650 2397_g is encoded by the nucleotides of SEQ ID No: 1299 which encodes the amino acid sequence of SEQ ID No: 1300.
This enzyme is believed to have oxidoreductase activity.
[0773] The enzyme identified as Sequence Oxid-651 2400_g is encoded by the nucleotides of SEQ ID No: 1301 which encodes the amino acid sequence of SEQ ID No: 1302.
This enzyme is believed to have oxidoreductase activity. [0774] The enzyme identified as Sequence Oxid-652 242 l_g is encoded by the nucleotides of SEQ ID No: 1303 which encodes the amino acid sequence of SEQ ID No: 1304.
This enzyme is believed to have oxidoreductase activity.
[0775] The enzyme identified as Sequence Oxid-653 2456_g is encoded by the nucleotides of SEQ ID No: 1305 which encodes the amino acid sequence of SEQ ID No: 1306.
This enzyme is believed to have nitrate reductase (NADPH) activity.
[0776] The enzyme identified as Sequence Oxid-654 2512_g is encoded by the nucleotides of SEQ ID No: 1307 which encodes the amino acid sequence of SEQ ID No: 1308.
This enzyme is believed to have oxidoreductase activity.
[0777] The enzyme identified as Sequence Oxid-655 2550_g is encoded by the nucleotides of SEQ ID No: 1309 which encodes the amino acid sequence of SEQ ID No: 1310.
This enzyme is believed to have oxidoreductase activity.
[0778] The enzyme identified as Sequence Oxid-656 2634_g is encoded by the nucleotides of SEQ ID No: 1311 which encodes the amino acid sequence of SEQ ID No: 1312.
This enzyme is believed to have oxidoreductase activity.
[0779] The enzyme identified as Sequence Oxid-657 2668_g is encoded by the nucleotides of SEQ ID No: 1313 which encodes the amino acid sequence of SEQ ID No: 1314.
This enzyme is believed to have oxidoreductase activity.
[0780] The enzyme identified as Sequence Oxid-658 2680_g is encoded by the nucleotides of SEQ ID No: 1315 which encodes the amino acid sequence of SEQ ID No: 1316.
This enzyme is believed to have oxidoreductase activity.
[0781] The enzyme identified as Sequence Oxid-659 2687_g is encoded by the nucleotides of SEQ ID No: 1317 which encodes the amino acid sequence of SEQ ID No: 1318.
This enzyme is believed to have oxidoreductase activity.
[0782] The enzyme identified as Sequence Oxid-660 2695_g is encoded by the nucleotides of SEQ ID No: 1319 which encodes the amino acid sequence of SEQ ID No: 1320.
This enzyme is believed to have amine oxidase activity.
[0783] The enzyme identified as Sequence Oxid-661 2696_g is encoded by the nucleotides of SEQ ID No: 1321 which encodes the amino acid sequence of SEQ ID No: 1322.
This enzyme is believed to have oxidoreductase activity.
[0784] The enzyme identified as Sequence Oxid-662 270 l_g is encoded by the nucleotides of SEQ ID No: 1323 which encodes the amino acid sequence of SEQ ID No: 1324.
This enzyme is believed to have laccase activity. [0785] The enzyme identified as Sequence Oxid-663 2708_g is encoded by the nucleotides of SEQ ID No: 1325 which encodes the amino acid sequence of SEQ ID No: 1326.
This enzyme is believed to have oxidoreductase activity.
[0786] The enzyme identified as Sequence Oxid-664 2712_g is encoded by the nucleotides of SEQ ID No: 1327 which encodes the amino acid sequence of SEQ ID No: 1328.
This enzyme is believed to have oxidoreductase activity, acting on CH-OH gr activity.
[0787] The enzyme identified as Sequence Oxid-665 2754_g is encoded by the nucleotides of SEQ ID No: 1329 which encodes the amino acid sequence of SEQ ID No: 1330.
This enzyme is believed to have oxidoreductase activity.
[0788] The enzyme identified as Sequence Oxid-666 2769_g is encoded by the nucleotides of SEQ ID No: 1331 which encodes the amino acid sequence of SEQ ID No: 1332.
This enzyme is believed to have thiol oxidase activity.
[0789] The enzyme identified as Sequence Oxid-667 2779_g is encoded by the nucleotides of SEQ ID No: 1333 which encodes the amino acid sequence of SEQ ID No: 1334.
This enzyme is believed to have oxidoreductase activity.
[0790] The enzyme identified as Sequence Oxid-668 2780_g is encoded by the nucleotides of SEQ ID No: 1335 which encodes the amino acid sequence of SEQ ID No: 1336.
This enzyme is believed to have oxidoreductase activity.
[0791] The enzyme identified as Sequence Oxid-669 2787_g is encoded by the nucleotides of SEQ ID No: 1337 which encodes the amino acid sequence of SEQ ID No: 1338.
This enzyme is believed to have thioredoxin peroxidase activity.
[0792] The enzyme identified as Sequence Oxid-670 2794_g is encoded by the nucleotides of SEQ ID No: 1339 which encodes the amino acid sequence of SEQ ID No: 1340.
This enzyme is believed to have oxidoreductase activity, acting on CH-OH gr activity.
[0793] The enzyme identified as Sequence Oxid-671 2803_g is encoded by the nucleotides of SEQ ID No: 1341 which encodes the amino acid sequence of SEQ ID No: 1342.
This enzyme is believed to have farnesyl-diphosphate farnesyltransferase activity, oxidoreductase activity.
[0794] The enzyme identified as Sequence Oxid-672 2804_g is encoded by the nucleotides of SEQ ID No: 1343 which encodes the amino acid sequence of SEQ ID No: 1344.
This enzyme is believed to have dTDP-4-dehydrorhamnose reductase activity. [0795] The enzyme identified as Sequence Oxid-673 2880_g is encoded by the nucleotides of SEQ ID No: 1345 which encodes the amino acid sequence of SEQ ID No: 1346.
This enzyme is believed to have oxidoreductase activity, acting on paired d activity.
[0796] The enzyme identified as Sequence Oxid-674 2966_g is encoded by the nucleotides of SEQ ID No: 1347 which encodes the amino acid sequence of SEQ ID No: 1348.
This enzyme is believed to have peroxidase activity.
[0797] The enzyme identified as Sequence Oxid-675 2968_g is encoded by the nucleotides of SEQ ID No: 1349 which encodes the amino acid sequence of SEQ ID No: 1350.
This enzyme is believed to have oxidoreductase activity.
[0798] The enzyme identified as Sequence Oxid-676 2978_g is encoded by the nucleotides of SEQ ID No: 1351 which encodes the amino acid sequence of SEQ ID No: 1352.
This enzyme is believed to have oxidoreductase activity.
[0799] The enzyme identified as Sequence Oxid-677 2979_g is encoded by the nucleotides of SEQ ID No: 1353 which encodes the amino acid sequence of SEQ ID No: 1354.
This enzyme is believed to have oxidoreductase activity.
[0800] The enzyme identified as Sequence Oxid-678 298 l_g is encoded by the nucleotides of SEQ ID No: 1355 which encodes the amino acid sequence of SEQ ID No: 1356.
This enzyme is believed to have oxidoreductase activity, acting on sulfur g activity.
[0801] The enzyme identified as Sequence Oxid-679 2996_g is encoded by the nucleotides of SEQ ID No: 1357 which encodes the amino acid sequence of SEQ ID No: 1358.
This enzyme is believed to have oxidoreductase activity.
[0802] The enzyme identified as Sequence Oxid-680 3000_g is encoded by the nucleotides of SEQ ID No: 1359 which encodes the amino acid sequence of SEQ ID No: 1360.
This enzyme is believed to have oxidoreductase activity.
[0803] The enzyme identified as Sequence Oxid-681 300 l_g is encoded by the nucleotides of SEQ ID No: 1361 which encodes the amino acid sequence of SEQ ID No: 1362.
This enzyme is believed to have oxidoreductase activity.
[0804] The enzyme identified as Sequence Oxid-682 3002_g is encoded by the nucleotides of SEQ ID No: 1363 which encodes the amino acid sequence of SEQ ID No: 1364.
This enzyme is believed to have oxidoreductase activity.
[0805] The enzyme identified as Sequence Oxid-683 3013_g is encoded by the nucleotides of SEQ ID No: 1365 which encodes the amino acid sequence of SEQ ID No: 1366.
This enzyme is believed to have oxidoreductase activity. [0806] The enzyme identified as Sequence Oxid-684 3014_g is encoded by the nucleotides of SEQ ID No: 1367 which encodes the amino acid sequence of SEQ ID No: 1368.
This enzyme is believed to have oxidoreductase activity.
[0807] The enzyme identified as Sequence Oxid-685 3017_g is encoded by the nucleotides of SEQ ID No: 1369 which encodes the amino acid sequence of SEQ ID No: 1370.
This enzyme is believed to have oxidoreductase activity.
[0808] The enzyme identified as Sequence Oxid-686 3018_g is encoded by the nucleotides of SEQ ID No: 1371 which encodes the amino acid sequence of SEQ ID No: 1372.
This enzyme is believed to have oxidoreductase activity.
[0809] The enzyme identified as Sequence Oxid-687 3047_g is encoded by the nucleotides of SEQ ID No: 1373 which encodes the amino acid sequence of SEQ ID No: 1374.
This enzyme is believed to have oxidoreductase activity, acting on the CH-0 activity.
[0810] The enzyme identified as Sequence Oxid-688 3057_g is encoded by the nucleotides of SEQ ID No: 1375 which encodes the amino acid sequence of SEQ ID No: 1376. This enzyme is believed to have acyltransferase activity, lovastatin nonaketide synthase activity, methyltransferase activity, oxidoreductase activity.
[0811] The enzyme identified as Sequence Oxid-689 3058_g is encoded by the nucleotides of SEQ ID No: 1377 which encodes the amino acid sequence of SEQ ID No: 1378. This enzyme is believed to have acyl carrier activity, oxidoreductase activity.
[0812] The enzyme identified as Sequence Oxid-690 3107_g is encoded by the nucleotides of SEQ ID No: 1379 which encodes the amino acid sequence of SEQ ID No: 1380. This enzyme is believed to have acyl carrier activity, acyltransferase activity, lovastatin nonaketide synthase activity, methyltransferase activity, oxidoreductase activity.
[0813] The enzyme identified as Sequence Oxid-691 3149_g is encoded by the nucleotides of SEQ ID No: 1381 which encodes the amino acid sequence of SEQ ID No: 1382.
This enzyme is believed to have oxidoreductase activity.
[0814] The enzyme identified as Sequence Oxid-692 3155_g is encoded by the nucleotides of SEQ ID No: 1383 which encodes the amino acid sequence of SEQ ID No: 1384.
This enzyme is believed to have 2-alkenal reductase activity, ATPase activity, coupled to transmembrane m activity.
[0815] The enzyme identified as Sequence Oxid-693 3209_g is encoded by the nucleotides of SEQ ID No: 1385 which encodes the amino acid sequence of SEQ ID No: 1386. This enzyme is believed to have laccase activity.
[0816] The enzyme identified as Sequence Oxid-694 3248_g is encoded by the nucleotides of SEQ ID No: 1387 which encodes the amino acid sequence of SEQ ID No: 1388. This enzyme is believed to have oxidoreductase activity, acting on the CH-0 activity.
[0817] The enzyme identified as Sequence Oxid-695 3250_g is encoded by the nucleotides of SEQ ID No: 1389 which encodes the amino acid sequence of SEQ ID No: 1390.
This enzyme is believed to have oxidoreductase activity.
[0818] The enzyme identified as Sequence Oxid-696 3328_g is encoded by the nucleotides of SEQ ID No: 1391 which encodes the amino acid sequence of SEQ ID No: 1392.
This enzyme is believed to have oxidoreductase activity.
[0819] The enzyme identified as Sequence Oxid-697 3348_g is encoded by the nucleotides of SEQ ID No: 1393 which encodes the amino acid sequence of SEQ ID No: 1394.
This enzyme is believed to have oxidoreductase activity.
[0820] The enzyme identified as Sequence Oxid-698 3366_g is encoded by the nucleotides of SEQ ID No: 1395 which encodes the amino acid sequence of SEQ ID No: 1396.
This enzyme is believed to have ubiquinol-cytochrome-c reductase activity.
[0821] The enzyme identified as Sequence Oxid-699 3398_g is encoded by the nucleotides of SEQ ID No: 1397 which encodes the amino acid sequence of SEQ ID No: 1398.
This enzyme is believed to have oxidoreductase activity.
[0822] The enzyme identified as Sequence Oxid-700 3410_g is encoded by the nucleotides of SEQ ID No: 1399 which encodes the amino acid sequence of SEQ ID No: 1400.
This enzyme is believed to have oxidoreductase activity.
[0823] The enzyme identified as Sequence Oxid-701 3412_g is encoded by the nucleotides of SEQ ID No: 1401 which encodes the amino acid sequence of SEQ ID No: 1402.
This enzyme is believed to have oxidoreductase activity.
[0824] The enzyme identified as Sequence Oxid-702 3485_g is encoded by the nucleotides of SEQ ID No: 1403 which encodes the amino acid sequence of SEQ ID No: 1404.
This enzyme is believed to have oxidoreductase activity.
[0825] The enzyme identified as Sequence Oxid-703 3487_g is encoded by the nucleotides of SEQ ID No: 1405 which encodes the amino acid sequence of SEQ ID No: 1406.
This enzyme is believed to have thioredoxin-disulfide reductase activity. [0826] The enzyme identified as Sequence Oxid-704 3502_g is encoded by the nucleotides of SEQ ID No: 1407 which encodes the amino acid sequence of SEQ ID No: 1408.
This enzyme is believed to have oxidoreductase activity.
[0827] The enzyme identified as Sequence Oxid-705 3518_g is encoded by the nucleotides of SEQ ID No: 1409 which encodes the amino acid sequence of SEQ ID No: 1410.
This enzyme is believed to have oxidoreductase activity, acting on sulfur g activity.
[0828] The enzyme identified as Sequence Oxid-706 355 l_g is encoded by the nucleotides of SEQ ID No: 1411 which encodes the amino acid sequence of SEQ ID No: 1412.
This enzyme is believed to have oxidoreductase activity.
[0829] The enzyme identified as Sequence Oxid-707 3564_g is encoded by the nucleotides of SEQ ID No: 1413 which encodes the amino acid sequence of SEQ ID No: 1414.
This enzyme is believed to have tRNA dihydrouridine synthase activity.
[0830] The enzyme identified as Sequence Oxid-708 361 l_g is encoded by the nucleotides of SEQ ID No: 1415 which encodes the amino acid sequence of SEQ ID No: 1416.
This enzyme is believed to have histone demethylase activity (H3-K9 specific), oxidoreductase activity.
[0831] The enzyme identified as Sequence Oxid-709 3667_g: is encoded by the nucleotides of SEQ ID No: 1417 which encodes the amino acid sequence of SEQ ID No: 1418.
This enzyme is believed to have peroxidase activity.
[0832] The enzyme identified as Sequence Oxid-710 3697_g: is encoded by the nucleotides of SEQ ID No: 1419 which encodes the amino acid sequence of SEQ ID No: 1420.
This enzyme is believed to have oxidoreductase activity.
[0833] The enzyme identified as Sequence Oxid-711 3757_g: is encoded by the nucleotides of SEQ ID No: 1421 which encodes the amino acid sequence of SEQ ID No: 1422.
This enzyme is believed to have oxidoreductase activity.
[0834] The enzyme identified as Sequence Oxid-712 3758_g: is encoded by the nucleotides of SEQ ID No: 1423 which encodes the amino acid sequence of SEQ ID No: 1424.
This enzyme is believed to have oxidoreductase activity.
[0835] The enzyme identified as Sequence Oxid-713 3857_g: is encoded by the nucleotides of SEQ ID No: 1425 which encodes the amino acid sequence of SEQ ID No: 1426.
This enzyme is believed to have oxidoreductase activity.
[0836] The enzyme identified as Sequence Oxid-714 3861_g: is encoded by the nucleotides of SEQ ID No: 1427 which encodes the amino acid sequence of SEQ ID No: 1428. This enzyme is believed to have oxidoreductase activity.
[0837] The enzyme identified as Sequence Oxid-715 3871_g: is encoded by the nucleotides of SEQ ID No: 1429 which encodes the amino acid sequence of SEQ ID No: 1430.
This enzyme is believed to have oxidoreductase activity.
[0838] The enzyme identified as Sequence Oxid-716 3877_g: is encoded by the nucleotides of SEQ ID No: 1431 which encodes the amino acid sequence of SEQ ID No: 1432.
This enzyme is believed to have hydro xymethylglutaryl-CoA reductase activity.
[0839] The enzyme identified as Sequence Oxid-717 3918_g: is encoded by the nucleotides of SEQ ID No: 1433 which encodes the amino acid sequence of SEQ ID No: 1434.
This enzyme is believed to have Protein disulfide oxidoreductase activity.
[0840] The enzyme identified as Sequence Oxid-718 3933_g: is encoded by the nucleotides of SEQ ID No: 1435 which encodes the amino acid sequence of SEQ ID No: 1436.
This enzyme is believed to have oxidoreductase activity.
[0841] The enzyme identified as Sequence Oxid-719 3946_g: is encoded by the nucleotides of SEQ ID No: 1437 which encodes the amino acid sequence of SEQ ID No: 1438.
This enzyme is believed to have oxidoreductase activity.
[0842] The enzyme identified as Sequence Oxid-720 3949_g: is encoded by the nucleotides of SEQ ID No: 1439 which encodes the amino acid sequence of SEQ ID No: 1440.
This enzyme is believed to have oxidoreductase activity.
[0843] The enzyme identified as Sequence Oxid-721 4014_g: is encoded by the nucleotides of SEQ ID No: 1441 which encodes the amino acid sequence of SEQ ID No: 1442.
This enzyme is believed to have oxidoreductase activity.
[0844] The enzyme identified as Sequence Oxid-722 4062_g: is encoded by the nucleotides of SEQ ID No: 1443 which encodes the amino acid sequence of SEQ ID No: 1444.
This enzyme is believed to have Protein disulfide oxidoreductase activity.
[0845] The enzyme identified as Sequence Oxid-723 4238_g: is encoded by the nucleotides of SEQ ID No: 1445 which encodes the amino acid sequence of SEQ ID No: 1446.
This enzyme is believed to have superoxide dismutase activity.
[0846] The enzyme identified as Sequence Oxid-724 4335_g: is encoded by the nucleotides of SEQ ID No: 1447 which encodes the amino acid sequence of SEQ ID No: 1448.
This enzyme is believed to have cytochrome reductase activity.
[0847] The enzyme identified as Sequence Oxid-725 4426_g: is encoded by the nucleotides of SEQ ID No: 1449 which encodes the amino acid sequence of SEQ ID No: 1450. This enzyme is believed to have oxidoreductase activity.
[0848] The enzyme identified as Sequence Oxid-726 444 l_g: is encoded by the nucleotides of SEQ ID No: 1451 which encodes the amino acid sequence of SEQ ID No: 1452.
This enzyme is believed to have oxidoreductase activity.
[0849] The enzyme identified as Sequence Oxid-727 4472_g: is encoded by the nucleotides of SEQ ID No: 1453 which encodes the amino acid sequence of SEQ ID No: 1454.
This enzyme is believed to have oxidoreductase activity.
[0850] The enzyme identified as Sequence Oxid-728 4613_g: is encoded by the nucleotides of SEQ ID No: 1455 which encodes the amino acid sequence of SEQ ID No: 1456.
This enzyme is believed to have oxidoreductase activity.
[0851] The enzyme identified as Sequence Oxid-729 4614_g: is encoded by the nucleotides of SEQ ID No: 1457 which encodes the amino acid sequence of SEQ ID No: 1458.
This enzyme is believed to have Protein disulfide oxidoreductase activity.
[0852] The enzyme identified as Sequence Oxid-730 4748_g: is encoded by the nucleotides of SEQ ID No: 1459 which encodes the amino acid sequence of SEQ ID No: 1460.
This enzyme is believed to have oxidoreductase activity.
[0853] The enzyme identified as Sequence Oxid-731 4752_g: is encoded by the nucleotides of SEQ ID No: 1461 which encodes the amino acid sequence of SEQ ID No: 1462.
This enzyme is believed to have oxidoreductase activity.
[0854] The enzyme identified as Sequence Oxid-732 4810_g: is encoded by the nucleotides of SEQ ID No: 1463 which encodes the amino acid sequence of SEQ ID No: 1464.
This enzyme is believed to have oxidoreductase activity.
[0855] The enzyme identified as Sequence Oxid-733 481 l_g: is encoded by the nucleotides of SEQ ID No: 1465 which encodes the amino acid sequence of SEQ ID No: 1466.
This enzyme is believed to have oxidoreductase activity.
[0856] The enzyme identified as Sequence Oxid-734 4829_g: is encoded by the nucleotides of SEQ ID No: 1467 which encodes the amino acid sequence of SEQ ID No: 1468.
This enzyme is believed to have oxidoreductase activity.
[0857] The enzyme identified as Sequence Oxid-735 485 l_g: is encoded by the nucleotides of SEQ ID No: 1469 which encodes the amino acid sequence of SEQ ID No: 1470.
This enzyme is believed to have oxidoreductase activity.
[0858] The enzyme identified as Sequence Oxid-736 4859_g: is encoded by the nucleotides of SEQ ID No: 1471 which encodes the amino acid sequence of SEQ ID No: 1472. This enzyme is believed to have laccase activity.
[0859] The enzyme identified as Sequence Oxid-737 4905_g: is encoded by the nucleotides of SEQ ID No: 1473 which encodes the amino acid sequence of SEQ ID No: 1474.
This enzyme is believed to have oxidoreductase activity.
[0860] The enzyme identified as Sequence Oxid-738 491 l_g: is encoded by the nucleotides of SEQ ID No: 1475 which encodes the amino acid sequence of SEQ ID No: 1476.
This enzyme is believed to have reductase activity.
[0861] The enzyme identified as Sequence Oxid-739 4962_g: is encoded by the nucleotides of SEQ ID No: 1477 which encodes the amino acid sequence of SEQ ID No: 1478.
This enzyme is believed to have oxidoreductase activity.
[0862] The enzyme identified as Sequence Oxid-740 4968_g: is encoded by the nucleotides of SEQ ID No: 1479 which encodes the amino acid sequence of SEQ ID No: 1480.
This enzyme is believed to have peroxidase activity.
[0863] The enzyme identified as Sequence Oxid-741 4979_g: is encoded by the nucleotides of SEQ ID No: 1481 which encodes the amino acid sequence of SEQ ID No: 1482.
This enzyme is believed to have arabinono-l,4-lactone oxidase activity.
[0864] The enzyme identified as Sequence Oxid-742 5016_g: is encoded by the nucleotides of SEQ ID No: 1483 which encodes the amino acid sequence of SEQ ID No: 1484.
This enzyme is believed to have oxidoreductase activity.
[0865] The enzyme identified as Sequence Oxid-743 5043_g: is encoded by the nucleotides of SEQ ID No: 1485 which encodes the amino acid sequence of SEQ ID No: 1486.
This enzyme is believed to have oxidoreductase activity.
[0866] The enzyme identified as Sequence Oxid-744 5060_g: is encoded by the nucleotides of SEQ ID No: 1487 which encodes the amino acid sequence of SEQ ID No: 1488.
This enzyme is believed to have superoxide dismutase activity.
[0867] The enzyme identified as Sequence Oxid-745 5095_g: is encoded by the nucleotides of SEQ ID No: 1489 which encodes the amino acid sequence of SEQ ID No: 1490.
This enzyme is believed to have oxidoreductase activity.
[0868] The enzyme identified as Sequence Oxid-746 5096_g: is encoded by the nucleotides of SEQ ID No: 1491 which encodes the amino acid sequence of SEQ ID No: 1492.
This enzyme is believed to have oxidoreductase activity.
[0869] The enzyme identified as Sequence Oxid-747 5112_g: is encoded by the nucleotides of SEQ ID No: 1493 which encodes the amino acid sequence of SEQ ID No: 1494. This enzyme is believed to have oxidoreductase activity.
[0870] The enzyme identified as Sequence Oxid-748 5129_g: is encoded by the nucleotides of SEQ ID No: 1495 which encodes the amino acid sequence of SEQ ID No: 1496.
This enzyme is believed to have oxidoreductase activity.
[0871] The enzyme identified as Sequence Oxid-749 5146_g: is encoded by the nucleotides of SEQ ID No: 1497 which encodes the amino acid sequence of SEQ ID No: 1498.
This enzyme is believed to have oxidoreductase activity.
[0872] The enzyme identified as Sequence Oxid-750 5153_g: is encoded by the nucleotides of SEQ ID No: 1499 which encodes the amino acid sequence of SEQ ID No: 1500.
This enzyme is believed to have oxidoreductase activity.
[0873] The enzyme identified as Sequence Oxid-751 5194_g: is encoded by the nucleotides of SEQ ID No: 1501 which encodes the amino acid sequence of SEQ ID No: 1502.
This enzyme is believed to have oxidoreductase activity.
[0874] The enzyme identified as Sequence Oxid-752 5196_g: is encoded by the nucleotides of SEQ ID No: 1503 which encodes the amino acid sequence of SEQ ID No: 1504.
This enzyme is believed to have ferric-chelate reductase activity.
[0875] The enzyme identified as Sequence Oxid-753 5197_g: is encoded by the nucleotides of SEQ ID No: 1505 which encodes the amino acid sequence of SEQ ID No: 1506.
This enzyme is believed to have oxidoreductase activity.
[0876] The enzyme identified as Sequence Oxid-754 5198_g: is encoded by the nucleotides of SEQ ID No: 1507 which encodes the amino acid sequence of SEQ ID No: 1508.
This enzyme is believed to have oxidoreductase activity.
[0877] The enzyme identified as Sequence Oxid-755 5207_g: is encoded by the nucleotides of SEQ ID No: 1509 which encodes the amino acid sequence of SEQ ID No: 1510.
This enzyme is believed to have ferric-chelate reductase activity.
[0878] The enzyme identified as Sequence Oxid-756 5210_g: is encoded by the nucleotides of SEQ ID No: 1511 which encodes the amino acid sequence of SEQ ID No: 1512.
This enzyme is believed to have phosphoadenylyl-sulfate reductase activity.
[0879] The enzyme identified as Sequence Oxid-757 5306_g: is encoded by the nucleotides of SEQ ID No: 1513 which encodes the amino acid sequence of SEQ ID No: 1514.
This enzyme is believed to have xylulose reductase activity.
[0880] The enzyme identified as Sequence Oxid-758 5307_g: is encoded by the nucleotides of SEQ ID No: 1515 which encodes the amino acid sequence of SEQ ID No: 1516. This enzyme is believed to have oxidoreductase activity.
[0881] The enzyme identified as Sequence Oxid-759 5367_g: is encoded by the nucleotides of SEQ ID No: 1517 which encodes the amino acid sequence of SEQ ID No: 1518.
This enzyme is believed to have alcohol oxidase activity.
[0882] The enzyme identified as Sequence Oxid-760 5368_g: is encoded by the nucleotides of SEQ ID No: 1519 which encodes the amino acid sequence of SEQ ID No: 1520.
This enzyme is believed to have alcohol oxidase activity.
[0883] The enzyme identified as Sequence Oxid-761 5373_g: is encoded by the nucleotides of SEQ ID No: 1521 which encodes the amino acid sequence of SEQ ID No: 1522.
This enzyme is believed to have oxidoreductase activity.
[0884] The enzyme identified as Sequence Oxid-762 5374_g: is encoded by the nucleotides of SEQ ID No: 1523 which encodes the amino acid sequence of SEQ ID No: 1524.
This enzyme is believed to have oxidoreductase activity.
[0885] The enzyme identified as Sequence Oxid-763 5382_g: is encoded by the nucleotides of SEQ ID No: 1525 which encodes the amino acid sequence of SEQ ID No: 1526.
This enzyme is believed to have oxidoreductase activity.
[0886] The enzyme identified as Sequence Oxid-764 5389_g: is encoded by the nucleotides of SEQ ID No: 1527 which encodes the amino acid sequence of SEQ ID No: 1528.
This enzyme is believed to have amine oxidase activity.
[0887] The enzyme identified as Sequence Oxid-765 541 l_g: is encoded by the nucleotides of SEQ ID No: 1529 which encodes the amino acid sequence of SEQ ID No: 1530.
This enzyme is believed to have oxidoreductase activity.
[0888] The enzyme identified as Sequence Oxid-766 5447_g: is encoded by the nucleotides of SEQ ID No: 1531 which encodes the amino acid sequence of SEQ ID No: 1532.
This enzyme is believed to have aldehyde reductase activity.
[0889] The enzyme identified as Sequence Oxid-767 5537_g: is encoded by the nucleotides of SEQ ID No: 1533 which encodes the amino acid sequence of SEQ ID No: 1534.
This enzyme is believed to have oxidoreductase activity.
[0890] The enzyme identified as Sequence Oxid-768 5604_g: is encoded by the nucleotides of SEQ ID No: 1535 which encodes the amino acid sequence of SEQ ID No: 1536.
This enzyme is believed to have oxidoreductase activity.
[0891] The enzyme identified as Sequence Oxid-769 5658_g: is encoded by the nucleotides of SEQ ID No: 1537 which encodes the amino acid sequence of SEQ ID No: 1538. This enzyme is believed to have oxidoreductase activity.
[0892] The enzyme identified as Sequence Oxid-770 5677_g: is encoded by the nucleotides of SEQ ID No: 1539 which encodes the amino acid sequence of SEQ ID No: 1540.
This enzyme is believed to have oxidoreductase activity.
[0893] The enzyme identified as Sequence Oxid-771 5689_g: is encoded by the nucleotides of SEQ ID No: 1541 which encodes the amino acid sequence of SEQ ID No: 1542.
This enzyme is believed to have oxidoreductase activity.
[0894] The enzyme identified as Sequence Oxid-772 5706_g: is encoded by the nucleotides of SEQ ID No: 1543 which encodes the amino acid sequence of SEQ ID No: 1544.
This enzyme is believed to have reductase activity.
[0895] The enzyme identified as Sequence Oxid-773 5744_g: is encoded by the nucleotides of SEQ ID No: 1545 which encodes the amino acid sequence of SEQ ID No: 1546.
This enzyme is believed to have oxidoreductase activity.
[0896] The enzyme identified as Sequence Oxid-774 5756_g: is encoded by the nucleotides of SEQ ID No: 1547 which encodes the amino acid sequence of SEQ ID No: 1548.
This enzyme is believed to have oxidoreductase activity.
[0897] The enzyme identified as Sequence Oxid-775 5764_g: is encoded by the nucleotides of SEQ ID No: 1549 which encodes the amino acid sequence of SEQ ID No: 1550.
This enzyme is believed to have methylenetetrahydro folate reductase activity.
[0898] The enzyme identified as Sequence Oxid-776 5804_g: is encoded by the nucleotides of SEQ ID No: 1551 which encodes the amino acid sequence of SEQ ID No: 1552.
This enzyme is believed to have reductase activity.
[0899] The enzyme identified as Sequence Oxid-777 5836_g: is encoded by the nucleotides of SEQ ID No: 1553 which encodes the amino acid sequence of SEQ ID No: 1554.
This enzyme is believed to have oxidoreductase activity.
[0900] The enzyme identified as Sequence Oxid-778 5886_g: is encoded by the nucleotides of SEQ ID No: 1555 which encodes the amino acid sequence of SEQ ID No: 1556.
This enzyme is believed to have oxidoreductase activity.
[0901] The enzyme identified as Sequence Oxid-779 5892_g: is encoded by the nucleotides of SEQ ID No: 1557 which encodes the amino acid sequence of SEQ ID No: 1558.
This enzyme is believed to have methylsterol oxidase activity.
[0902] The enzyme identified as Sequence Oxid-780 5949_g: is encoded by the nucleotides of SEQ ID No: 1559 which encodes the amino acid sequence of SEQ ID No: 1560. This enzyme is believed to have stearoyl-CoA 9-desaturase activity.
[0903] The enzyme identified as Sequence Oxid-781 5990_g: is encoded by the nucleotides of SEQ ID No: 1561 which encodes the amino acid sequence of SEQ ID No: 1562.
This enzyme is believed to have nitrate reductase activity.
[0904] The enzyme identified as Sequence Oxid-782 599 l_g: is encoded by the nucleotides of SEQ ID No: 1563 which encodes the amino acid sequence of SEQ ID No: 1564.
This enzyme is believed to have oxidoreductase activity.
[0905] The enzyme identified as Sequence Oxid-783 6069_g: is encoded by the nucleotides of SEQ ID No: 1565 which encodes the amino acid sequence of SEQ ID No: 1566.
This enzyme is believed to have 2,4-dienoyl-CoA reductase (NADPH) activity.
[0906] The enzyme identified as Sequence Oxid-784 6074_g: is encoded by the nucleotides of SEQ ID No: 1567 which encodes the amino acid sequence of SEQ ID No: 1568.
This enzyme is believed to have oxidoreductase activity.
[0907] The enzyme identified as Sequence Oxid-785 6085_g: is encoded by the nucleotides of SEQ ID No: 1569 which encodes the amino acid sequence of SEQ ID No: 1570.
This enzyme is believed to have oxidoreductase activity.
[0908] The enzyme identified as Sequence Oxid-786 6093_g: is encoded by the nucleotides of SEQ ID No: 1571 which encodes the amino acid sequence of SEQ ID No: 1572.
This enzyme is believed to have cytochrome-b5 reductase activity.
[0909] The enzyme identified as Sequence Oxid-787 6137_g: is encoded by the nucleotides of SEQ ID No: 1573 which encodes the amino acid sequence of SEQ ID No: 1574.
This enzyme is believed to have oxidoreductase activity.
[0910] The enzyme identified as Sequence Oxid-788 6169_g: is encoded by the nucleotides of SEQ ID No: 1575 which encodes the amino acid sequence of SEQ ID No: 1576.
This enzyme is believed to have oxidoreductase activity.
[0911] The enzyme identified as Sequence Oxid-789 6171_g: is encoded by the nucleotides of SEQ ID No: 1577 which encodes the amino acid sequence of SEQ ID No: 1578.
This enzyme is believed to have oxidoreductase activity.
[0912] The enzyme identified as Sequence Oxid-790 6181_g: is encoded by the nucleotides of SEQ ID No: 1579 which encodes the amino acid sequence of SEQ ID No: 1580.
This enzyme is believed to have oxidoreductase activity.
[0913] The enzyme identified as Sequence Oxid-791 6192_g: is encoded by the nucleotides of SEQ ID No: 1581 which encodes the amino acid sequence of SEQ ID No: 1582. This enzyme is believed to have oxidoreductase activity.
[0914] The enzyme identified as Sequence Oxid-792 6247_g: is encoded by the nucleotides of SEQ ID No: 1583 which encodes the amino acid sequence of SEQ ID No: 1584.
This enzyme is believed to have oxidoreductase activity.
[0915] The enzyme identified as Sequence Oxid-793 6254_g: is encoded by the nucleotides of SEQ ID No: 1585 which encodes the amino acid sequence of SEQ ID No: 1586.
This enzyme is believed to have oxidoreductase activity.
[0916] The enzyme identified as Sequence Oxid-794 6279_g: is encoded by the nucleotides of SEQ ID No: 1587 which encodes the amino acid sequence of SEQ ID No: 1588.
This enzyme is believed to have oxidoreductase activity.
[0917] The enzyme identified as Sequence Oxid-795 6283_g: is encoded by the nucleotides of SEQ ID No: 1589 which encodes the amino acid sequence of SEQ ID No: 1590.
This enzyme is believed to have oxidoreductase activity.
[0918] The enzyme identified as Sequence Oxid-796 6284_g: is encoded by the nucleotides of SEQ ID No: 1591 which encodes the amino acid sequence of SEQ ID No: 1592.
This enzyme is believed to have oxidoreductase activity.
[0919] The enzyme identified as Sequence Oxid-797 6298_g: is encoded by the nucleotides of SEQ ID No: 1593 which encodes the amino acid sequence of SEQ ID No: 1594.
This enzyme is believed to have oxidoreductase activity.
[0920] The enzyme identified as Sequence Oxid-798 6304_g: is encoded by the nucleotides of SEQ ID No: 1595 which encodes the amino acid sequence of SEQ ID No: 1596.
This enzyme is believed to have carbonyl reductase (NADPH) activity.
[0921] The enzyme identified as Sequence Oxid-799 6335_g: is encoded by the nucleotides of SEQ ID No: 1597 which encodes the amino acid sequence of SEQ ID No: 1598.
This enzyme is believed to have oxidoreductase activity.
[0922] The enzyme identified as Sequence Oxid-800 6342_g: is encoded by the nucleotides of SEQ ID No: 1599 which encodes the amino acid sequence of SEQ ID No: 1600.
This enzyme is believed to have oxidoreductase activity.
[0923] The enzyme identified as Sequence Oxid-801 6344_g: is encoded by the nucleotides of SEQ ID No: 1601 which encodes the amino acid sequence of SEQ ID No: 1602.
This enzyme is believed to have oxidoreductase activity.
[0924] The enzyme identified as Sequence Oxid-802 6345_g: is encoded by the nucleotides of SEQ ID No: 1603 which encodes the amino acid sequence of SEQ ID No: 1604. This enzyme is believed to have oxidoreductase activity.
[0925] The enzyme identified as Sequence Oxid-803 6346_g: is encoded by the nucleotides of SEQ ID No: 1605 which encodes the amino acid sequence of SEQ ID No: 1606.
This enzyme is believed to have oxidoreductase activity.
[0926] The enzyme identified as Sequence Oxid-804 6364_g: is encoded by the nucleotides of SEQ ID No: 1607 which encodes the amino acid sequence of SEQ ID No: 1608.
This enzyme is believed to have oxidoreductase activity.
[0927] The enzyme identified as Sequence Oxid-805 6365_g: is encoded by the nucleotides of SEQ ID No: 1609 which encodes the amino acid sequence of SEQ ID No: 1610.
This enzyme is believed to have oxidoreductase activity.
[0928] The enzyme identified as Sequence Oxid-806 6367_g: is encoded by the nucleotides of SEQ ID No: 1611 which encodes the amino acid sequence of SEQ ID No: 1612.
This enzyme is believed to have oxidoreductase activity.
[0929] The enzyme identified as Sequence Oxid-807 6398_g: is encoded by the nucleotides of SEQ ID No: 1613 which encodes the amino acid sequence of SEQ ID No: 1614.
This enzyme is believed to have aldehyde reductase activity.
[0930] The enzyme identified as Sequence Oxid-808 6473_g: is encoded by the nucleotides of SEQ ID No: 1615 which encodes the amino acid sequence of SEQ ID No: 1616.
This enzyme is believed to have oxidoreductase activity.
[0931] The enzyme identified as Sequence Oxid-809 6498_g: is encoded by the nucleotides of SEQ ID No: 1617 which encodes the amino acid sequence of SEQ ID No: 1618.
This enzyme is believed to have deltal4-sterol reductase activity.
[0932] The enzyme identified as Sequence Oxid-810 6503_g: is encoded by the nucleotides of SEQ ID No: 1619 which encodes the amino acid sequence of SEQ ID No: 1620.
This enzyme is believed to have oxidoreductase activity.
[0933] The enzyme identified as Sequence Oxid-811 6572_g: is encoded by the nucleotides of SEQ ID No: 1621 which encodes the amino acid sequence of SEQ ID No: 1622.
This enzyme is believed to have reductase activity.
[0934] The enzyme identified as Sequence Oxid-812 6600_g: is encoded by the nucleotides of SEQ ID No: 1623 which encodes the amino acid sequence of SEQ ID No: 1624.
This enzyme is believed to have 3-dehydrosphinganine reductase activity.
[0935] The enzyme identified as Sequence Oxid-813 6638_g: is encoded by the nucleotides of SEQ ID No: 1625 which encodes the amino acid sequence of SEQ ID No: 1626. This enzyme is believed to have oxidoreductase activity.
[0936] The enzyme identified as Sequence Oxid-814 6801_g: is encoded by the nucleotides of SEQ ID No: 1627 which encodes the amino acid sequence of SEQ ID No: 1628.
This enzyme is believed to have oxidoreductase activity.
[0937] The enzyme identified as Sequence Oxid-815 6859_g: is encoded by the nucleotides of SEQ ID No: 1629 which encodes the amino acid sequence of SEQ ID No: 1630.
This enzyme is believed to have oxidoreductase activity.
[0938] The enzyme identified as Sequence Oxid-816 6862_g: is encoded by the nucleotides of SEQ ID No: 1631 which encodes the amino acid sequence of SEQ ID No: 1632.
This enzyme is believed to have oxidoreductase activity.
[0939] The enzyme identified as Sequence Oxid-817 6863_g: is encoded by the nucleotides of SEQ ID No: 1633 which encodes the amino acid sequence of SEQ ID No: 1634.
This enzyme is believed to have oxidoreductase activity.
[0940] The enzyme identified as Sequence Oxid-818 6895_g: is encoded by the nucleotides of SEQ ID No: 1635 which encodes the amino acid sequence of SEQ ID No: 1636.
This enzyme is believed to have oxidoreductase activity.
[0941] The enzyme identified as Sequence Oxid-819 6899_g: is encoded by the nucleotides of SEQ ID No: 1637 which encodes the amino acid sequence of SEQ ID No: 1638.
This enzyme is believed to have oxidoreductase activity.
[0942] The enzyme identified as Sequence Oxid-820 6913_g: is encoded by the nucleotides of SEQ ID No: 1639 which encodes the amino acid sequence of SEQ ID No: 1640.
This enzyme is believed to have oxidoreductase activity.
[0943] The enzyme identified as Sequence Oxid-821 6943_g: is encoded by the nucleotides of SEQ ID No: 1641 which encodes the amino acid sequence of SEQ ID No: 1642.
This enzyme is believed to have oxidoreductase activity.
[0944] The enzyme identified as Sequence Oxid-822 6967_g: is encoded by the nucleotides of SEQ ID No: 1643 which encodes the amino acid sequence of SEQ ID No: 1644.
This enzyme is believed to have Protein disulfide oxidoreductase activity.
[0945] The enzyme identified as Sequence Oxid-823 697 l_g: is encoded by the nucleotides of SEQ ID No: 1645 which encodes the amino acid sequence of SEQ ID No: 1646.
This enzyme is believed to have oxidoreductase activity activity.
[0946] The enzyme identified as Sequence Oxid-824 6973_g is encoded by the nucleotides of SEQ ID No: 1647 which encodes the amino acid sequence of SEQ ID No: 1648. This enzyme is believed to have polyketide synthase activity.
[0947] The enzyme identified as Sequence Oxid-825 7030_g is encoded by the nucleotides of SEQ ID No: 1649 which encodes the amino acid sequence of SEQ ID No: 1650.
This enzyme is believed to have aldo/keto reductase activity.
[0948] The enzyme identified as Sequence Oxid-826 7045_g is encoded by the nucleotides of SEQ ID No: 1651 which encodes the amino acid sequence of SEQ ID No: 1652.
This enzyme is believed to have dioxygenase activity.
[0949] The enzyme identified as Sequence Oxid-827 7098_g is encoded by the nucleotides of SEQ ID No: 1653 which encodes the amino acid sequence of SEQ ID No: 1654.
This enzyme is believed to have oxidoreductase activity.
[0950] The enzyme identified as Sequence Oxid-828 7100_g is encoded by the nucleotides of SEQ ID No: 1655 which encodes the amino acid sequence of SEQ ID No: 1656.
This enzyme is believed to have oxidoreductase activity.
[0951] The enzyme identified as Sequence Oxid-829 7103_g is encoded by the nucleotides of SEQ ID No: 1657 which encodes the amino acid sequence of SEQ ID No: 1658.
This enzyme is believed to have oxidoreductase activity.
[0952] The enzyme identified as Sequence Oxid-830 7110_g is encoded by the nucleotides of SEQ ID No: 1659 which encodes the amino acid sequence of SEQ ID No: 1660.
This enzyme is believed to have oxidoreductase activity.
[0953] The enzyme identified as Sequence Oxid-831 7156_g is encoded by the nucleotides of SEQ ID No: 1661 which encodes the amino acid sequence of SEQ ID No: 1662.
This enzyme is believed to have oxidoreductase activity.
[0954] The enzyme identified as Sequence Oxid-832 7279_g is encoded by the nucleotides of SEQ ID No: 1663 which encodes the amino acid sequence of SEQ ID No: 1664.
This enzyme is believed to have dehydrogenase/reductase activity.
[0955] The enzyme identified as Sequence Oxid-833 7352_g is encoded by the nucleotides of SEQ ID No: 1665 which encodes the amino acid sequence of SEQ ID No: 1666.
This enzyme is believed to have reductase activity.
[0956] The enzyme identified as Sequence Oxid-834 7405_g is encoded by the nucleotides of SEQ ID No: 1667 which encodes the amino acid sequence of SEQ ID No: 1668.
This enzyme is believed to have oxidoreductase activity.
[0957] The enzyme identified as Sequence Oxid-835 7406_g is encoded by the nucleotides of SEQ ID No: 1669 which encodes the amino acid sequence of SEQ ID No: 1670. This enzyme is believed to have oxidoreductase activity.
[0958] The enzyme identified as Sequence Oxid-836 7409_g is encoded by the nucleotides of SEQ ID No: 1671 which encodes the amino acid sequence of SEQ ID No: 1672.
This enzyme is believed to have oxidoreductase activity.
[0959] The enzyme identified as Sequence Oxid-837 7423_g is encoded by the nucleotides of SEQ ID No: 1673 which encodes the amino acid sequence of SEQ ID No: 1674.
This enzyme is believed to have oxidase activity.
[0960] The enzyme identified as Sequence Oxid-838 7462_g is encoded by the nucleotides of SEQ ID No: 1675 which encodes the amino acid sequence of SEQ ID No: 1676.
This enzyme is believed to have oxidoreductase activity.
[0961] The enzyme identified as Sequence Oxid-839 7470_g is encoded by the nucleotides of SEQ ID No: 1677 which encodes the amino acid sequence of SEQ ID No: 1678.
This enzyme is believed to have Oxidase activity.
[0962] The enzyme identified as Sequence Oxid-840 7474_g is encoded by the nucleotides of SEQ ID No: 1679 which encodes the amino acid sequence of SEQ ID No: 1680.
This enzyme is believed to have oxidoreductase activity.
[0963] The enzyme identified as Sequence Oxid-841 7479_g is encoded by the nucleotides of SEQ ID No: 1681 which encodes the amino acid sequence of SEQ ID No: 1682.
This enzyme is believed to have oxidoreductase activity.
[0964] The enzyme identified as Sequence Oxid-842 7485_g is encoded by the nucleotides of SEQ ID No: 1683 which encodes the amino acid sequence of SEQ ID No: 1684.
This enzyme is believed to have oxidoreductase activity.
[0965] The enzyme identified as Sequence Oxid-843 7496_g is encoded by the nucleotides of SEQ ID No: 1685 which encodes the amino acid sequence of SEQ ID No: 1686.
This enzyme is believed to have oxidoreductase activity.
[0966] The enzyme identified as Sequence Oxid-844 7513_g is encoded by the nucleotides of SEQ ID No: 1687 which encodes the amino acid sequence of SEQ ID No: 1688.
This enzyme is believed to have oxidoreductase activity.
[0967] The enzyme identified as Sequence Oxid-845 7533_g is encoded by the nucleotides of SEQ ID No: 1689 which encodes the amino acid sequence of SEQ ID No: 1690.
This enzyme is believed to have oxygenase activity.
[0968] The enzyme identified as Sequence Oxid-846 7536_g is encoded by the nucleotides of SEQ ID No: 1691 which encodes the amino acid sequence of SEQ ID No: 1692. This enzyme is believed to have oxidoreductase activity.
[0969] The enzyme identified as Sequence Oxid-847 7556_g is encoded by the nucleotides of SEQ ID No: 1693 which encodes the amino acid sequence of SEQ ID No: 1694.
This enzyme is believed to have dehydrogenase activity.
[0970] The enzyme identified as Sequence Oxid-848 7592_g is encoded by the nucleotides of SEQ ID No: 1695 which encodes the amino acid sequence of SEQ ID No: 1696.
This enzyme is believed to have dehydrogenase activity.
[0971] The enzyme identified as Sequence Oxid-849 7596_g is encoded by the nucleotides of SEQ ID No: 1697 which encodes the amino acid sequence of SEQ ID No: 1698.
This enzyme is believed to have dehydrogenase activity.
[0972] The enzyme identified as Sequence Oxid-850 7628_g is encoded by the nucleotides of SEQ ID No: 1699 which encodes the amino acid sequence of SEQ ID No: 1700.
This enzyme is believed to have oxidoreductase activity.
[0973] The enzyme identified as Sequence Oxid-851 7635_g is encoded by the nucleotides of SEQ ID No: 1701 which encodes the amino acid sequence of SEQ ID No: 1702.
This enzyme is believed to have oxidoreductase activity.
[0974] The enzyme identified as Sequence Oxid-852 7684_g is encoded by the nucleotides of SEQ ID No: 1703 which encodes the amino acid sequence of SEQ ID No: 1704.
This enzyme is believed to have dehydrogenases/reductase activity.
[0975] The enzyme identified as Sequence Oxid-853 7714_g is encoded by the nucleotides of SEQ ID No: 1705 which encodes the amino acid sequence of SEQ ID No: 1706.
This enzyme is believed to have oxidoreductase activity.
[0976] The enzyme identified as Sequence Oxid-854 7716_g is encoded by the nucleotides of SEQ ID No: 1707 which encodes the amino acid sequence of SEQ ID No: 1708.
This enzyme is believed to have oxidoreductase activity.
[0977] The enzyme identified as Sequence Oxid-855 772 l_g is encoded by the nucleotides of SEQ ID No: 1709 which encodes the amino acid sequence of SEQ ID No: 1710.
This enzyme is believed to have oxidase activity.
[0978] The enzyme identified as Sequence Oxid-856 7736_g is encoded by the nucleotides of SEQ ID No: 1711 which encodes the amino acid sequence of SEQ ID No: 1712.
This enzyme is believed to have oxidoreductase activity.
[0979] The enzyme identified as Sequence Oxid-857 7795_g is encoded by the nucleotides of SEQ ID No: 1713 which encodes the amino acid sequence of SEQ ID No: 1714. This enzyme is believed to have dehydrogenase/reductase activity.
[0980] The enzyme identified as Sequence Oxid-858 7829_g is encoded by the nucleotides of SEQ ID No: 1715 which encodes the amino acid sequence of SEQ ID No: 1716.
This enzyme is believed to have oxidoreductase activity.
[0981] The enzyme identified as Sequence Oxid-859 7854_g is encoded by the nucleotides of SEQ ID No: 1717 which encodes the amino acid sequence of SEQ ID No: 1718.
This enzyme is believed to have oxidoreductase activity.
[0982] The enzyme identified as Sequence Oxid-860 7859_g is encoded by the nucleotides of SEQ ID No: 1719 which encodes the amino acid sequence of SEQ ID No: 1720.
This enzyme is believed to have oxidoreductase activity.
[0983] The enzyme identified as Sequence Oxid-861 7860_g is encoded by the nucleotides of SEQ ID No: 1721 which encodes the amino acid sequence of SEQ ID No: 1722.
This enzyme is believed to have Glutathione peroxidase activity.
[0984] The enzyme identified as Sequence Oxid-862 7888_g is encoded by the nucleotides of SEQ ID No: 1723 which encodes the amino acid sequence of SEQ ID No: 1724.
This enzyme is believed to have oxidoreductase activity.
[0985] The enzyme identified as Sequence Oxid-863 7897_g is encoded by the nucleotides of SEQ ID No: 1725 which encodes the amino acid sequence of SEQ ID No: 1726.
This enzyme is believed to have oxidoreductase activity.
[0986] The enzyme identified as Sequence Oxid-864 7935_g is encoded by the nucleotides of SEQ ID No: 1727 which encodes the amino acid sequence of SEQ ID No: 1728.
This enzyme is believed to have oxidoreductase activity.
[0987] The enzyme identified as Sequence Oxid-865 7936_g is encoded by the nucleotides of SEQ ID No: 1729 which encodes the amino acid sequence of SEQ ID No: 1730.
This enzyme is believed to have oxidoreductase activity.
[0988] The enzyme identified as Sequence Oxid-866 8000_g is encoded by the nucleotides of SEQ ID No: 1731 which encodes the amino acid sequence of SEQ ID No: 1732.
This enzyme is believed to have oxidoreductase activity.
[0989] The enzyme identified as Sequence Oxid-867 8089_g is encoded by the nucleotides of SEQ ID No: 1733 which encodes the amino acid sequence of SEQ ID No: 1734.
This enzyme is believed to have sterol reductase activity.
[0990] The enzyme identified as Sequence Oxid-868 8156_g is encoded by the nucleotides of SEQ ID No: 1735 which encodes the amino acid sequence of SEQ ID No: 1736. This enzyme is believed to have oxidoreductase activity.
[0991] The enzyme identified as Sequence Oxid-869 8260_g is encoded by the nucleotides of SEQ ID No: 1737 which encodes the amino acid sequence of SEQ ID No: 1738.
This enzyme is believed to have dehydrogenase/reductase activity.
[0992] The enzyme identified as Sequence Oxid-870 8270_g is encoded by the nucleotides of SEQ ID No: 1739 which encodes the amino acid sequence of SEQ ID No: 1740.
This enzyme is believed to have oxidoreductase activity.
[0993] The enzyme identified as Sequence Oxid-871 8293_g is encoded by the nucleotides of SEQ ID No: 1741 which encodes the amino acid sequence of SEQ ID No: 1742.
This enzyme is believed to have oxidoreductase activity.
[0994] The enzyme identified as Sequence Oxid-872 8299_g is encoded by the nucleotides of SEQ ID No: 1743 which encodes the amino acid sequence of SEQ ID No: 1744.
This enzyme is believed to have oxidoreductase activity.
[0995] The enzyme identified as Sequence Oxid-873 8300_g is encoded by the nucleotides of SEQ ID No: 1745 which encodes the amino acid sequence of SEQ ID No: 1746.
This enzyme is believed to have oxidoreductase activity.
[0996] The enzyme identified as Sequence Oxid-874 8310_g is encoded by the nucleotides of SEQ ID No: 1747 which encodes the amino acid sequence of SEQ ID No: 1748.
This enzyme is believed to have oxidoreductase activity.
[0997] The enzyme identified as Sequence Oxid-875 8332_g is encoded by the nucleotides of SEQ ID No: 1749 which encodes the amino acid sequence of SEQ ID No: 1750.
This enzyme is believed to have reductase activity.
[0998] The enzyme identified as Sequence Oxid-876 8378_g is encoded by the nucleotides of SEQ ID No: 1751 which encodes the amino acid sequence of SEQ ID No: 1752.
This enzyme is believed to have polyketide synthase activity.
[0999] The enzyme identified as Sequence Oxid-877 8459_g is encoded by the nucleotides of SEQ ID No: 1753 which encodes the amino acid sequence of SEQ ID No: 1754.
This enzyme is believed to have polyketide synthase activity.
[01000] The enzyme identified as Sequence Oxid-878 8485_g is encoded by the nucleotides of SEQ ID No: 1755 which encodes the amino acid sequence of SEQ
ID No: 1756. This enzyme is believed to have oxidoreductase activity.
[01001] The enzyme identified as Sequence Oxid-879 8525_g is encoded by the nucleotides of SEQ ID No: 1757 which encodes the amino acid sequence of SEQ ID No: 1758. This enzyme is believed to have oxidoreductase activity.
[01002] The enzyme identified as Sequence Oxid-880 8548_g is encoded by the nucleotides of SEQ ID No: 1759 which encodes the amino acid sequence of SEQ ID No: 1760. This enzyme is believed to have dehydrogenase activity.
[01003] The enzyme identified as Sequence Oxid-881 8558_g is encoded by the nucleotides of SEQ ID No: 1761 which encodes the amino acid sequence of SEQ ID No: 1762. This enzyme is believed to have oxidoreductase activity.
[01004] The enzyme identified as Sequence Oxid-882 8559_g is encoded by the nucleotides of SEQ ID No: 1763 which encodes the amino acid sequence of SEQ ID No: 1764. This enzyme is believed to have aldo-keto reductase activity.
[01005] The enzyme identified as Sequence Oxid-883 8565_g is encoded by the nucleotides of SEQ ID No: 1765 which encodes the amino acid sequence of SEQ ID No: 1766. This enzyme is believed to have oxidoreductase activity.
[01006] The enzyme identified as Sequence Oxid-884 8566_g is encoded by the nucleotides of SEQ ID No: 1767 which encodes the amino acid sequence of SEQ ID No: 1768. This enzyme is believed to have oxidoreductase activity.
[01007] The enzyme identified as Sequence Oxid-885 8609_g is encoded by the nucleotides of SEQ ID No: 1769 which encodes the amino acid sequence of SEQ ID No: 1770. This enzyme is believed to have reductase activity.
[01008] The enzyme identified as Sequence Oxid-886 8625_g is encoded by the nucleotides of SEQ ID No: 1771 which encodes the amino acid sequence of SEQ ID No: 1772. This enzyme is believed to have oxidoreductase activity.
[01009] The enzyme identified as Sequence Oxid-887 8668_g is encoded by the nucleotides of SEQ ID No: 1773 which encodes the amino acid sequence of SEQ ID No: 1774. This enzyme is believed to have oxidoreductase activity.
[01010] The enzyme identified as Sequence Oxid-888 8695_g is encoded by the nucleotides of SEQ ID No: 1775 which encodes the amino acid sequence of SEQ ID No: 1776. This enzyme is believed to have oxidoreductase activity.
[01011] The enzyme identified as Sequence Oxid-889 8696_g is encoded by the nucleotides of SEQ ID No: 1777 which encodes the amino acid sequence of SEQ ID No: 1778. This enzyme is believed to have oxidoreductase activity.
[01012] The enzyme identified as Sequence Oxid-890 8747_g is encoded by the nucleotides of SEQ ID No: 1779 which encodes the amino acid sequence of SEQ ID No: 1780. This enzyme is believed to have dehydrogenase/reductase activity.
[01013] The enzyme identified as Sequence Oxid-891 8754_g is encoded by the nucleotides of SEQ ID No: 1781 which encodes the amino acid sequence of SEQ ID No: 1782. This enzyme is believed to have Oxidoreductase activity.
[01014] The enzyme identified as Sequence Oxid-892 8755_g is encoded by the nucleotides of SEQ ID No: 1783 which encodes the amino acid sequence of SEQ ID No: 1784. This enzyme is believed to have oxidoreductase activity.
[01015] The enzyme identified as Sequence Oxid-893 8832_g is encoded by the nucleotides of SEQ ID No: 1785 which encodes the amino acid sequence of SEQ ID No: 1786. This enzyme is believed to have dehydrogenase activity.
[01016] The enzyme identified as Sequence Oxid-894 8844_g is encoded by the nucleotides of SEQ ID No: 1787 which encodes the amino acid sequence of SEQ ID No: 1788. This enzyme is believed to have oxidoreductase activity.
[01017] The enzyme identified as Sequence Oxid-895 8852_g is encoded by the nucleotides of SEQ ID No: 1789 which encodes the amino acid sequence of SEQ ID No: 1790. This enzyme is believed to have oxidoreductase activity.
[01018] The enzyme identified as Sequence Oxid-896 8882_g is encoded by the nucleotides of SEQ ID No: 1791 which encodes the amino acid sequence of SEQ ID No: 1792. This enzyme is believed to have oxidoreductase activity.
[01019] The enzyme identified as Sequence Oxid-897 8899_g is encoded by the nucleotides of SEQ ID No: 1793 which encodes the amino acid sequence of SEQ ID No: 1794. This enzyme is believed to have oxidoreductase activity.
[01020] The enzyme identified as Sequence Oxid-898 8929_g is encoded by the nucleotides of SEQ ID No: 1795 which encodes the amino acid sequence of SEQ ID No: 1796. This enzyme is believed to have oxidoreductase activity.
[01021] The enzyme identified as Sequence Oxid-899 8930_g is encoded by the nucleotides of SEQ ID No: 1797 which encodes the amino acid sequence of SEQ ID No: 1798. This enzyme is believed to have oxidoreductase activity.
[01022] The enzyme identified as Sequence Oxid-900 8932_g is encoded by the nucleotides of SEQ ID No: 1799 which encodes the amino acid sequence of SEQ ID No: 1800. This enzyme is believed to have polyketide synthase activity.
[01023] The enzyme identified as Sequence Oxid-901 8939_g is encoded by the nucleotides of SEQ ID No: 1801 which encodes the amino acid sequence of SEQ ID No: 1802. This enzyme is believed to have oxidoreductase activity.
[01024] The enzyme identified as Sequence Oxid-902 8974_g is encoded by the nucleotides of SEQ ID No: 1803 which encodes the amino acid sequence of SEQ ID No: 1804. This enzyme is believed to have oxidoreductase activity.
[01025] The enzyme identified as Sequence Oxid-903 8996_g is encoded by the nucleotides of SEQ ID No: 1805 which encodes the amino acid sequence of SEQ ID No: 1806. This enzyme is believed to have oxidoreductase activity.
[01026] The enzyme identified as Sequence Oxid-904 9018_g is encoded by the nucleotides of SEQ ID No: 1807 which encodes the amino acid sequence of SEQ ID No: 1808. This enzyme is believed to have oxidoreductase activity.
[01027] The enzyme identified as Sequence Oxid-905 9037_g is encoded by the nucleotides of SEQ ID No: 1809 which encodes the amino acid sequence of SEQ ID No: 1810. This enzyme is believed to have oxidoreductase activity.
[01028] The enzyme identified as Sequence Oxid-906 9088_g is encoded by the nucleotides of SEQ ID No: 1811 which encodes the amino acid sequence of SEQ ID No: 1812. This enzyme is believed to have oxidoreductase activity.
[01029] The enzyme identified as Sequence Oxid-907 9105_g is encoded by the nucleotides of SEQ ID No: 1813 which encodes the amino acid sequence of SEQ ID No: 1814. This enzyme is believed to have reductase activity.
[01030] The enzyme identified as Sequence Oxid-908 9129_g is encoded by the nucleotides of SEQ ID No: 1815 which encodes the amino acid sequence of SEQ ID No: 1816. This enzyme is believed to have oxidoreductase activity.
[01031] The enzyme identified as Sequence Oxid-909 9133_g is encoded by the nucleotides of SEQ ID No: 1817 which encodes the amino acid sequence of SEQ ID No: 1818. This enzyme is believed to have oxidoreductase activity.
[01032] The enzyme identified as Sequence Oxid-910 9134_g is encoded by the nucleotides of SEQ ID No: 1819 which encodes the amino acid sequence of SEQ ID No: 1820. This enzyme is believed to have oxidoreductase activity.
[01033] The enzyme identified as Sequence Oxid-911 9141_g is encoded by the nucleotides of SEQ ID No: 1821 which encodes the amino acid sequence of SEQ ID No: 1822. This enzyme is believed to have oxidoreductase activity.
[01034] The enzyme identified as Sequence Oxid-912 9145_g is encoded by the nucleotides of SEQ ID No: 1823 which encodes the amino acid sequence of SEQ ID No: 1824. This enzyme is believed to have oxidoreductase activity.
[01035] The enzyme identified as Sequence Oxid-913 9162_g is encoded by the nucleotides of SEQ ID No: 1825 which encodes the amino acid sequence of SEQ ID No: 1826. This enzyme is believed to have laccase activity.
[01036] The enzyme identified as Sequence Oxid-914 9189_g is encoded by the nucleotides of SEQ ID No: 1827 which encodes the amino acid sequence of SEQ ID No: 1828. This enzyme is believed to have oxidoreductase activity.
[01037] The enzyme identified as Sequence Oxid-915 9204_g is encoded by the nucleotides of SEQ ID No: 1829 which encodes the amino acid sequence of SEQ ID No: 1830. This enzyme is believed to have oxidoreductase activity.
[01038] The enzyme identified as Sequence Oxid-916 9207_g is encoded by the nucleotides of SEQ ID No: 1831 which encodes the amino acid sequence of SEQ ID No: 1832. This enzyme is believed to have oxidoreductase activity.
[01039] The enzyme identified as Sequence Oxid-917 9240_g is encoded by the nucleotides of SEQ ID No: 1833 which encodes the amino acid sequence of SEQ ID No: 1834. This enzyme is believed to have oxidoreductase activity.
[01040] The enzyme identified as Sequence Oxid-918 9288_g is encoded by the nucleotides of SEQ ID No: 1835 which encodes the amino acid sequence of SEQ ID No: 1836. This enzyme is believed to have oxidoreductase activity.
[01041] The enzyme identified as Sequence Oxid-919 9322_g is encoded by the nucleotides of SEQ ID No: 1837 which encodes the amino acid sequence of SEQ ID No: 1838. This enzyme is believed to have oxidoreductase activity.
[01042] The enzyme identified as Sequence Oxid-920 9339_g is encoded by the nucleotides of SEQ ID No: 1839 which encodes the amino acid sequence of SEQ ID No: 1840. This enzyme is believed to have oxidoreductase activity.
[01043] The enzyme identified as Sequence Oxid-921 9344_g is encoded by the nucleotides of SEQ ID No: 1841 which encodes the amino acid sequence of SEQ ID No: 1842. This enzyme is believed to have oxidoreductase activity.
[01044] The enzyme identified as Sequence Oxid-922 9353_g is encoded by the nucleotides of SEQ ID No: 1843 which encodes the amino acid sequence of SEQ ID No: 1844. This enzyme is believed to have oxidoreductase activity.
[01045] The enzyme identified as Sequence Oxid-923 9369_g is encoded by the nucleotides of SEQ ID No: 1845 which encodes the amino acid sequence of SEQ ID No: 1846. This enzyme is believed to have oxidoreductase activity.
[01046] The enzyme identified as Sequence Oxid-924 944 l_g is encoded by the nucleotides of SEQ ID No: 1847 which encodes the amino acid sequence of SEQ ID No: 1848. This enzyme is believed to have oxidoreductase activity.
[01047] The enzyme identified as Sequence Oxid-925 9450_g is encoded by the nucleotides of SEQ ID No: 1849 which encodes the amino acid sequence of SEQ ID No: 1850. This enzyme is believed to have oxidoreductase activity.
[01048] The enzyme identified as Sequence Oxid-926 9469_g is encoded by the nucleotides of SEQ ID No: 1851 which encodes the amino acid sequence of SEQ ID No: 1852. This enzyme is believed to have oxidoreductase activity.
[01049] The enzyme identified as Sequence Oxid-927 9518_g is encoded by the nucleotides of SEQ ID No: 1853 which encodes the amino acid sequence of SEQ ID No: 1854. This enzyme is believed to have oxidoreductase activity.
[01050] The enzyme identified as Sequence Oxid-928 9529_g is encoded by the nucleotides of SEQ ID No: 1855 which encodes the amino acid sequence of SEQ ID No: 1856. This enzyme is believed to have oxidoreductase activity.
[01051] The enzyme identified as Sequence Oxid-929 954 l_g is encoded by the nucleotides of SEQ ID No: 1857 which encodes the amino acid sequence of SEQ ID No: 1858. This enzyme is believed to have oxidoreductase activity.
[01052] The enzyme identified as Sequence Oxid-930 9543_g is encoded by the nucleotides of SEQ ID No: 1859 which encodes the amino acid sequence of SEQ ID No: 1860. This enzyme is believed to have oxidoreductase activity.
[01053] The enzyme identified as Sequence Oxid-931 9576_g is encoded by the nucleotides of SEQ ID No: 1861 which encodes the amino acid sequence of SEQ ID No: 1862. This enzyme is believed to have oxidoreductase activity.
[01054] The enzyme identified as Sequence Oxid-932 9643_g is encoded by the nucleotides of SEQ ID No: 1863 which encodes the amino acid sequence of SEQ ID No: 1864. This enzyme is believed to have oxidoreductase activity.
[01055] The enzyme identified as Sequence Oxid-933 9655_g is encoded by the nucleotides of SEQ ID No: 1865 which encodes the amino acid sequence of SEQ ID No: 1866. This enzyme is believed to have oxidoreductase activity.
[01056] The enzyme identified as Sequence Oxid-934 9702_g is encoded by the nucleotides of SEQ ID No: 1867 which encodes the amino acid sequence of SEQ ID No: 1868. This enzyme is believed to have oxidoreductase activity.
[01057] The enzyme identified as Sequence Oxid-935 9707_g is encoded by the nucleotides of SEQ ID No: 1869 which encodes the amino acid sequence of SEQ ID No: 1870. This enzyme is believed to have oxidoreductase activity.
[01058] The enzyme identified as Sequence Oxid-936 9708_g is encoded by the nucleotides of SEQ ID No: 1871 which encodes the amino acid sequence of SEQ ID No: 1872. This enzyme is believed to have oxidoreductase activity.
[01059] The enzyme identified as Sequence Oxid-937 9737_g is encoded by the nucleotides of SEQ ID No: 1873 which encodes the amino acid sequence of SEQ ID No: 1874. This enzyme is believed to have reductase/dehydrogenase activity.
[01060] The enzyme identified as Sequence Oxid-938 9739_g is encoded by the nucleotides of SEQ ID No: 1875 which encodes the amino acid sequence of SEQ ID No: 1876. This enzyme is believed to have oxidoreductase activity.
[01061] The enzyme identified as Sequence Oxid-939 9779_g is encoded by the nucleotides of SEQ ID No: 1877 which encodes the amino acid sequence of SEQ ID No: 1878. This enzyme is believed to have oxidoreductase activity.
[01062] The enzyme identified as Sequence Oxid-940 9780_g is encoded by the nucleotides of SEQ ID No: 1879 which encodes the amino acid sequence of SEQ ID No: 1880. This enzyme is believed to have oxidoreductase activity.
[01063] The enzyme identified as Sequence Oxid-941 9790_g is encoded by the nucleotides of SEQ ID No: 1881 which encodes the amino acid sequence of SEQ ID No: 1882. This enzyme is believed to have oxidoreductase activity.
[01064] The enzyme identified as Sequence Oxid-942 8509_g is encoded by the nucleotides of SEQ ID No: 1883 which encodes the amino acid sequence of SEQ ID No: 1884. This enzyme is believed to have oxidoreductase activity.
[01065] The enzyme identified as Sequence Oxid-943 8567_g is encoded by the nucleotides of SEQ ID No: 1885 which encodes the amino acid sequence of SEQ ID No: 1886. This enzyme is believed to have oxidoreductase activity.
[01066] The enzyme identified as Sequence Oxid-944 2139_g is encoded by the nucleotides of SEQ ID No: 1887 which encodes the amino acid sequence of SEQ ID No: 1888. This enzyme is believed to have oxidoreductase activity.
[01067] The enzyme identified as Sequence Oxid-945 6123_g is encoded by the nucleotides of SEQ ID No: 1889 which encodes the amino acid sequence of SEQ ID No: 1890. This enzyme is believed to have oxidoreductase activity.
[01068] The enzyme identified as Sequence Oxid-946 (CIO 1470) is encoded by the nucleotides of SEQ ID No: 1891 which encodes the amino acid sequence of SEQ ID No: 1892. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01069] The enzyme identified as Sequence Oxid-947 (CL02838) is encoded by the nucleotides of SEQ ID No: 1893 which encodes the amino acid sequence of SEQ ID No: 1894. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01070] The enzyme identified as Sequence Oxid-948 (C103248) is encoded by the nucleotides of SEQ ID No: 1895 which encodes the amino acid sequence of SEQ ID No: 1896. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01071] The enzyme identified as Sequence Oxid-949 (C103723) is encoded by the nucleotides of SEQ ID No: 1897 which encodes the amino acid sequence of SEQ ID No: 1898. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01072] The enzyme identified as Sequence Oxid-950 (C103778) is encoded by the nucleotides of SEQ ID No: 1899 which encodes the amino acid sequence of SEQ ID No: 1900. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01073] The enzyme identified as Sequence Oxid-951 (C104725) is encoded by the nucleotides of SEQ ID No: 1901 which encodes the amino acid sequence of SEQ ID No: 1902. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01074] The enzyme identified as Sequence Oxid-952 (C104750) is encoded by the nucleotides of SEQ ID No: 1903 which encodes the amino acid sequence of SEQ ID No: 1904. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01075] The enzyme identified as Sequence Oxid-953 (C104859) is encoded by the nucleotides of SEQ ID No: 1905 which encodes the amino acid sequence of SEQ ID No: 1906. This enzyme is believed to have Family GH61 oxidoreductase activity. [01076] The enzyme identified as Sequence Oxid-954 (C104874) is encoded by the nucleotides of SEQ ID No: 1907 which encodes the amino acid sequence of SEQ ID No: 1908. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01077] The enzyme identified as Sequence Oxid-955 (C105022) is encoded by the nucleotides of SEQ ID No: 1909 which encodes the amino acid sequence of SEQ ID No: 1910. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01078] The enzyme identified as Sequence Oxid-956 (C105366) is encoded by the nucleotides of SEQ ID No: 1911 which encodes the amino acid sequence of SEQ ID No: 1912. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01079] The enzyme identified as Sequence Oxid-957 (C106186) is encoded by the nucleotides of SEQ ID No: 1913 which encodes the amino acid sequence of SEQ ID No: 1914. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01080] The enzyme identified as Sequence Oxid-958 (C106230) is encoded by the nucleotides of SEQ ID No: 1915 which encodes the amino acid sequence of SEQ ID No: 1916. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01081] The enzyme identified as Sequence Oxid-959 (C108101) is encoded by the nucleotides of SEQ ID No: 1917 which encodes the amino acid sequence of SEQ ID No: 1918. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01082] The enzyme identified as Sequence Oxid-960 (C108507) is encoded by the nucleotides of SEQ ID No: 1919 which encodes the amino acid sequence of SEQ ID No: 1920. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01083] The enzyme identified as Sequence Oxid-961 (C109767) is encoded by the nucleotides of SEQ ID No: 1921 which encodes the amino acid sequence of SEQ ID No: 1922. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01084] The enzyme identified as Sequence Oxid-962 (C109768) is encoded by the nucleotides of SEQ ID No: 1923 which encodes the amino acid sequence of SEQ ID No: 1924. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01085] The enzyme identified as Sequence Oxid-963 (C110366) is encoded by the nucleotides of SEQ ID No: 1925 which encodes the amino acid sequence of SEQ ID No: 1926. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01086] The enzyme identified as Sequence Oxid-964 (C110391) is encoded by the nucleotides of SEQ ID No: 1927 which encodes the amino acid sequence of SEQ ID No: 1928. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01087] The enzyme identified as Sequence Oxid-965 (C110518) is encoded by the nucleotides of SEQ ID No: 1929 which encodes the amino acid sequence of SEQ ID No: 1930. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01088] The enzyme identified as Sequence Oxid-966 (C110824) is encoded by the nucleotides of SEQ ID No: 1931 which encodes the amino acid sequence of SEQ ID No: 1932. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01089] The enzyme identified as Sequence Oxid-967 (Cll 1443) is encoded by the nucleotides of SEQ ID No: 1933 which encodes the amino acid sequence of SEQ ID No: 1934. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01090] The enzyme identified as Sequence Oxid-968 (C105111) is encoded by the nucleotides of SEQ ID No: 1935 which encodes the amino acid sequence of SEQ ID No: 1936. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01091] The enzyme identified as Sequence Oxid-969 (C103830) is encoded by the nucleotides of SEQ ID No: 1937 which encodes the amino acid sequence of SEQ ID No: 1938. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01092] The enzyme identified as Sequence Oxid-970 (C109131) is encoded by the nucleotides of SEQ ID No: 1939 which encodes the amino acid sequence of SEQ ID No: 1940. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01093] The enzyme identified as Sequence Oxid-971 (C100632) is encoded by the nucleotides of SEQ ID No: 1941 which encodes the amino acid sequence of SEQ ID No: 1942. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01094] The enzyme identified as Sequence Oxid-972 (C104931) is encoded by the nucleotides of SEQ ID No: 1943 which encodes the amino acid sequence of SEQ ID No: 1944. This enzyme is believed to have Family GH61 oxidoreductase activity.
[01095] As used herein, reference to an isolated protein or polypeptide in the present invention, including any of the enzymes disclosed herein, includes full-length proteins and their glycosylated or otherwise modified forms forms, fusion proteins, or any fragment or homologue or variant of such a protein. More specifically, an isolated protein, such as an enzyme according to the present invention, is a protein (including a polypeptide or peptide) that has been removed from its natural milieu (i.e., that has been subject to human manipulation) and can include purified proteins, partially purified proteins, recombinantly produced proteins, synthetically produced proteins, proteins complexed with lipids, soluble proteins, and isolated proteins associated with other proteins, for example. As such, "isolated" does not reflect the extent to which the protein has been purified. Preferably, an isolated protein of the present invention is produced recombinantly. In addition, and by way of example, a "M. thermophila protein" or "M. thermophila enzyme" refers to a protein (generally including a homologue or variant of a naturally occurring protein) from Myceliophthora thermophila or to a protein that has been otherwise produced from the knowledge of the structure (e.g., sequence) and perhaps the function of a naturally occurring protein from Myceliophthora thermophila. In other words, a M. thermophila protein includes any protein that has substantially similar structure and function of a naturally occurring M. thermophila protein or that is a biologically active (i.e., has biological activity) homologue or variant of a naturally occurring protein from M. thermophila as described in detail herein. As such, a M. thermophila protein can include purified, partially purified, recombinant, mutated/modified and synthetic proteins. [01096] According to the present invention, the terms "modification," "mutation," and "variant" can be used interchangeably, particularly with regard to the modifications/mutations to the amino acid sequence of a M. thermophila protein (or nucleic acid sequences) described herein. An isolated protein according to the present invention can be isolated from its natural source, produced recombinantly or produced synthetically.
[01097] According to the present invention, the terms "modification" and "mutation" can be used interchangeably, particularly with regard to the modifications/mutations to the primary amino acid sequences of a protein or peptide (or nucleic acid sequences) described herein. The term "modification" can also be used to describe post-translational modifications to a protein or peptide including, but not limited to, methylation, farnesylation, carboxymethylation, geranyl geranylation, glycosylation, phosphorylation, acetylation, myristoylation, prenylation, palmitation, and/or amidation. Modification can also included the cleavage of a signal peptide, or methionine, or other portions of the peptide that require cleavage to generate the mature peptide.
[01098] As used herein, the terms "homologue" or "variants" are used to refer to a protein or peptide which differs from a naturally occurring protein or peptide (i.e., the "prototype" or "wild-type" protein) by minor modifications to the naturally occurring protein or peptide, but which maintains the basic protein and side chain structure of the naturally occurring form. Such changes include, but are not limited to: changes in one or a few amino acid side chains; changes one or a few amino acids, including deletions (e.g., a truncated version of the protein or peptide), insertions and/or substitutions; changes in stereochemistry of one or a few atoms; and/or minor derivatizations, including but not limited to for example: methylation, glycosylation and phosphorylation. A homologue or variant can have either enhanced, decreased, or substantially similar properties as compared to the naturally occurring protein or peptide. A homologue or variant can include an agonist of a protein or an antagonist of a protein.
[01099] Homologues or variants can be the result of natural allelic variation or natural mutation. A naturally occurring allelic variant of a nucleic acid encoding a protein is a gene that occurs at essentially the same locus (or loci) in the genome as the gene which encodes such protein, but which, due to natural variations caused by, for example, mutation or recombination, has a similar but not identical sequence. Homologous can also be the result of a gene duplication and rearrangement, resulting in a different location. Allelic variants typically encode proteins having similar activity to that of the protein encoded by the gene to which they are being compared. One class of allelic variants can encode the same protein but have different nucleic acid sequences due to the degeneracy of the genetic code. Allelic variants can also comprise alterations in the 5' or 3' untranslated regions of the gene (e.g., in regulatory control regions). Allelic variants are well known to those skilled in the art. Homo logues or variants can be produced using techniques known in the art for the production of proteins including, but not limited to, direct modifications to the isolated, naturally occurring protein, direct protein synthesis, or modifications to the nucleic acid sequence encoding the protein using, for example, classic or recombinant DNA techniques to effect random or targeted mutagenesis.
[01100] Modifications of a protein, such as in a homologue or variant, may result in proteins having the same biological activity as the naturally occurring protein, or in proteins having decreased or increased biological activity as compared to the naturally occurring protein. Modifications which result in a decrease in protein expression or a decrease in the activity of the protein, can be referred to as inactivation (complete or partial), down-regulation, or decreased action of a protein. Similarly, modifications which result in an increase in protein expression or an increase in the activity of the protein, can be referred to as amplification, overproduction, activation, enhancement, up-regulation or increased action of a protein.
[01101] According to the present invention, an isolated protein, including a biologically active homologue, variant, or fragment thereof, has at least one characteristic of biological activity of a wild-type, or naturally occurring, protein. As discussed above, in general, the biological activity or biological action of a protein refers to any function(s) exhibited or performed by the protein that is ascribed to the naturally occurring form of the protein as measured or observed in vivo (i.e., in the natural physiological environment of the protein) or in vitro (i.e., under laboratory conditions). The biological activity of a protein of the present invention can include an enzyme activity (catalytic activity and/or substrate binding activity), such as oxidases, oxygenases, monoxygenases, Baeyer-Villiger monooxygenases, dioxygenases, peroxidases, dehydrogenases, reductases that catalyze an oxidation-reduction reaction or any other activity disclosed herein. Specific biological activities of the proteins disclosed herein are described in detail above and in the Examples. Methods of detecting and measuring the biological activity of a protein of the invention include, but are not limited to, the assays described in the Examples section below. Such assays include, but are not limited to, measurement of enzyme activity (e.g., catalytic activity), measurement of substrate binding, and the like. It is noted that an isolated protein of the present invention (including homologues or variants) is not required to have a biological activity such as catalytic activity. A protein can be a truncated, mutated or inactive protein, or lack at least one activity of the wild-type enzyme, for example. Inactive proteins may be useful in some screening assays, for example, or for other purposes such as antibody production. Methods to measure protein expression levels of a protein according to the invention include, but are not limited to: western blotting, immuno cytochemistry, flow cytometry or other immuno logic-based assays; assays based on a property of the protein including but not limited to, ligand binding or interaction with other protein partners.
Many of the enzymes and proteins of the present invention may be desirable targets for modification and use in the processes described herein. These proteins have been described in terms of function and amino acid sequence (and nucleic acid sequence encoding the same) of representative wild-type proteins. In one embodiment of the invention, homologues or variants of a given protein (which can include related proteins from other organisms or modified forms of the given protein) are encompassed for use in the invention. Homologues or variants of a protein encompassed by the present invention can comprise, consist essentially of, or consist of, in one embodiment, an amino acid sequence that is at least about 35% identical, and more preferably at least about 40% identical, and more preferably at least about 45% identical, and more preferably at least about 50% identical, and more preferably at least about 55% identical, and more preferably at least about 60% identical, and more preferably at least about 65% identical, and more preferably at least about 70% identical, and more preferably at least about 75% identical, and more preferably at least about 80% identical, and more preferably at least about 85% identical, and more preferably at least about 90% identical, and more preferably at least about 95% identical, and more preferably at least about 96% identical, and more preferably at least about 97% identical, and more preferably at least about 98% identical, and more preferably at least about 99% identical, or any percent identity between 35% and 99%, in whole integers (i.e., 36%), 37%), etc.), to an amino acid sequence disclosed herein that represents the amino acid sequence of an enzyme or protein according to the invention (including a biologically active domain of a full-length protein). Preferably, the amino acid sequence of the homologue or variant has a biological activity of the wild-type or reference protein or of a biologically active domain thereof (e.g., a catalytic domain). When denoting mutation positions, the amino acid position of the wild- type is typically used. The wild-type can also be referred to as the "parent." Additionally, any generation before the variant at issue can be a parent.
In one embodiment, a protein of the present invention comprises, consists essentially of, or consists of an amino acid sequence that, alone or in combination with other characteristics of such proteins disclosed herein, is less than 100% identical to an amino acid sequence selected from SEQ ID NO: 2, SEQ ID No: 4, SEQ ID No: 6, SEQ ID No: 8, SEQ ID No: 10, SEQ ID No: 12, SEQ ID No: 14, SEQ ID No: 16, SEQ ID No: 18, SEQ ID No: 20, SEQ ID No: 22, SEQ ID No: 24, SEQ ID No: 26, SEQ ID No: 28, SEQ ID No: 30, SEQ ID No: 32, SEQ ID No: 34, SEQ ID No: 36, SEQ ID No: 38, SEQ ID No: 40, SEQ ID No: 42, SEQ ID No: 44, SEQ ID No: 46, SEQ ID No: 48, SEQ ID No: 50, SEQ ID No: 52, SEQ ID No: 54, SEQ ID No: 56, SEQ ID No: 58, SEQ ID No: 60, SEQ ID No: 62, SEQ ID No: 64, SEQ ID No: 66, SEQ ID No: 68, SEQ ID No: 70, SEQ ID No: 72, SEQ ID No: 74, SEQ ID No: 76, SEQ ID No: 78, SEQ ID No: 80, SEQ ID No: 82, SEQ ID No: 84, SEQ ID No: 86, SEQ ID No: 88, SEQ ID No: 90, SEQ ID No: 92, SEQ ID No: 94, SEQ ID No: 96, SEQ ID No: 98, SEQ ID No: 100, SEQ ID No: 102, SEQ ID No: 104, SEQ ID No: 106, SEQ ID No: 108, SEQ ID No: 1 10, SEQ ID No: 1 12, SEQ ID No: 1 14, SEQ ID No: 1 16, SEQ ID No: 1 18, SEQ ID No: 120, SEQ ID No: 122, SEQ ID No: 124, SEQ ID No: 126, SEQ ID No: 128, SEQ ID No: 130, SEQ ID No: 132, SEQ ID No: 134, SEQ ID No: 136, SEQ ID No: 138, SEQ ID No: 140, SEQ ID No: 142, SEQ ID No: 144, SEQ ID No: 146, SEQ ID No: 148, SEQ ID No: 150, SEQ ID No: 152, SEQ ID No: 154, SEQ ID No: 156, SEQ ID No: 158, SEQ ID No: 160, SEQ ID No: 162, SEQ ID No: 164, SEQ ID No: 166, SEQ ID No: 168, SEQ ID No: 170, SEQ ID No: 172, SEQ ID No: 174, SEQ ID No: 176, SEQ ID No: 178, SEQ ID No: 180, SEQ ID No: 182, SEQ ID No: 184, SEQ ID No: 186, SEQ ID No: 188, SEQ ID No: 190, SEQ ID No: 192, SEQ ID No: 194, SEQ ID No: 196, SEQ ID No: 198, SEQ ID No: 200, SEQ ID No: 202, SEQ ID No: 204, SEQ ID No: 206, SEQ ID No: 208, SEQ ID No: 210, SEQ ID No: 212, SEQ ID No: 214, SEQ ID No: 216, SEQ ID No: 218, SEQ ID No: 220, SEQ ID No: 222, SEQ ID No: 224, SEQ ID No: 226, SEQ ID No: 228, SEQ ID No: 230, SEQ ID No: 232, SEQ ID No: 234, SEQ ID No: 236, SEQ ID No: 238, SEQ ID No: 240, SEQ ID No: 242, SEQ ID No: 244, SEQ ID No: 246, SEQ ID No: 248, SEQ ID No: 250, SEQ ID No: 252, SEQ ID No: 254, SEQ ID No: 256, SEQ ID No: 258, SEQ ID No: 260, SEQ ID No: 262, SEQ ID No: 264, SEQ ID No: 266, SEQ ID No: 268, SEQ ID No: 270, SEQ ID No: 272, SEQ ID No: 274, SEQ ID No: 276, SEQ ID No: 278, SEQ ID No: 280, SEQ ID No: 282, SEQ ID No: 284, SEQ ID No: 286, SEQ ID No: 288, SEQ ID No: 290, SEQ ID No: 292, SEQ ID No: 294, SEQ ID No: 296, SEQ ID No: 298, SEQ ID No: 300, SEQ ID No: 302, SEQ ID No: 304, SEQ ID No: 306, SEQ ID No: 308, SEQ ID No: 310, SEQ ID No: 312, SEQ ID No: 314, SEQ ID No: 316, SEQ ID No: 318, SEQ ID No: 320, SEQ ID No: 322, SEQ ID No: 324, SEQ ID No: 326, SEQ ID No: 328, SEQ ID No: 330, SEQ ID No: 332, SEQ ID No: 334, SEQ ID No: 336, SEQ ID No: 338, SEQ ID No: 340, SEQ ID No: 342, SEQ ID No: 344, SEQ ID No: 346, SEQ ID No: 348, SEQ ID No: 350, SEQ ID No: 352, SEQ ID No: 354, SEQ ID No: 356, SEQ ID No: 358, SEQ ID No: 360, SEQ ID No: 362, SEQ ID No: 364, SEQ ID No: 366, SEQ ID No: 368, SEQ ID No: 370, SEQ ID No: 372, SEQ ID No: 374, SEQ ID No: 376, SEQ ID No: 378, SEQ ID No: 380, SEQ ID No: 382, SEQ ID No: 384, SEQ ID No: 386, SEQ ID No: 388, SEQ ID No: 390, SEQ ID No: 392, SEQ ID No: 394, SEQ ID No: 396, SEQ ID No: 398, SEQ ID No: 400, SEQ ID No: 402, SEQ ID No: 404, SEQ ID No: 406, SEQ ID No: 408, SEQ ID No: 410, SEQ ID No: 412, SEQ ID No: 414, SEQ ID No: 416, SEQ ID No: 418, SEQ ID No: 420, SEQ ID No: 422, SEQ ID No: 424, SEQ ID No: 426, SEQ ID No: 428, SEQ ID No: 430, SEQ ID No: 432, SEQ ID No: 434, SEQ ID No: 436, SEQ ID No: 438, SEQ ID No: 440, SEQ ID No: 442, SEQ ID No: 444, SEQ ID No: 446, SEQ ID No: 448, SEQ ID No: 450, SEQ ID No: 452, SEQ ID No: 454, SEQ ID No: 456, SEQ ID No: 458, SEQ ID No: 460, SEQ ID No: 462, SEQ ID No: 464, SEQ ID No: 466, SEQ ID No: 468, SEQ ID No: 470, SEQ ID No: 472, SEQ ID No: 474, SEQ ID No: 476, SEQ ID No: 478, SEQ ID No: 480, SEQ ID No: 482, SEQ ID No: 484, SEQ ID No: 486, SEQ ID No: 488, SEQ ID No: 490, SEQ ID No: 492, SEQ ID No: 494, SEQ ID No: 496, SEQ ID No: 498, SEQ ID No: 500, SEQ ID No: 502, SEQ ID No: 504, SEQ ID No: 506, SEQ ID No: 508, SEQ ID No: 510, SEQ ID No: 512, SEQ ID No: 514, SEQ ID No: 516, SEQ ID No: 518, SEQ ID No: 520, SEQ ID No: 522, SEQ ID No: 524, SEQ ID No: 526, SEQ ID No: 528, SEQ ID No: 530, SEQ ID No: 532, SEQ ID No: 534, SEQ ID No: 536, SEQ ID No: 538, SEQ ID No: 540, SEQ ID No: 542, SEQ ID No: 544, SEQ ID No: 546, SEQ ID No: 548, SEQ ID No: 550, SEQ ID No: 552, SEQ ID No: 554, SEQ ID No: 556, SEQ ID No: 558, SEQ ID No: 560, SEQ ID No: 562, SEQ ID No: 564, SEQ ID No: 566, SEQ ID No: 568, SEQ ID No: 570, SEQ ID No: 572, SEQ ID No: 574, SEQ ID No: 576, SEQ ID No: 578, SEQ ID No: 580, SEQ ID No: 582, SEQ ID No: 584, SEQ ID No: 586, SEQ ID No: 588, SEQ ID No: 590, SEQ ID No: 592, SEQ ID No: 594, SEQ ID No: 596, SEQ ID No: 598, SEQ ID No: 600, SEQ ID No: 602, SEQ ID No: 604, SEQ ID No: 606, SEQ ID No: 608, SEQ ID No: 610, SEQ ID No: 612, SEQ ID No: 614, SEQ ID No: 616, SEQ ID No: 618, SEQ ID No: 620, SEQ ID No: 622, SEQ ID No: 624, SEQ ID No: 626, SEQ ID No: 628, SEQ ID No: 630, SEQ ID No: 632, SEQ ID No: 634, SEQ ID No: 636, SEQ ID No: 638, SEQ ID No: 640, SEQ ID No: 642, SEQ ID No: 644, SEQ ID No: 646, SEQ ID No: 648, SEQ ID No: 650, SEQ ID No: 652, SEQ ID No: 654, SEQ ID No: 656, SEQ ID No: 658, SEQ ID No: 660, SEQ ID No: 662, SEQ ID No: 664, SEQ ID No: 666, SEQ ID No: 668, SEQ ID No: 670, SEQ ID No: 672, SEQ ID No: 674, SEQ ID No: 676, SEQ ID No: 678, SEQ ID No: 680, SEQ ID No: 682, SEQ ID No: 684, SEQ ID No: 686, SEQ ID No: 688, SEQ ID No: 690, SEQ ID No: 692, SEQ ID No: 694, SEQ ID No: 696, SEQ ID No: 698, SEQ ID No: 700, SEQ ID No: 702, SEQ ID No: 704, SEQ ID No: 706, SEQ ID No: 708, SEQ ID No: 710, SEQ ID No: 712, SEQ ID No: 714, SEQ ID No: 716, SEQ ID No: 718, SEQ ID No: 720, SEQ ID No: 722, SEQ ID No: 724, SEQ ID No: 726, SEQ ID No: 728, SEQ ID No: 730, SEQ ID No: 732, SEQ ID No: 734, SEQ ID No: 736, SEQ ID No: 738, SEQ ID No: 740, SEQ ID No: 742, SEQ ID No: 744, SEQ ID No: 746, SEQ ID No: 748, SEQ ID No: 750, SEQ ID No: 752, SEQ ID No: 754, SEQ ID No: 756, SEQ ID No: 758, SEQ ID No: 760, SEQ ID No: 762, SEQ ID No: 764, SEQ ID No: 766, SEQ ID No: 768, SEQ ID No: 770, SEQ ID No: 772, SEQ ID No: 774, SEQ ID No: 776, SEQ ID No: 778, SEQ ID No: 780, SEQ ID No: 782, SEQ ID No: 784, SEQ ID No: 786, SEQ ID No: 788, SEQ ID No: 790, SEQ ID No: 792, SEQ ID No: 794, SEQ ID No: 796, SEQ ID No: SEQ ID No: 798, SEQ ID No: 800, SEQ ID No: 802, SEQ ID No: 804, SEQ ID No: 806, SEQ ID No: 808, SEQ ID No: 810, SEQ ID No: 812, SEQ ID No: 814, SEQ ID No: 816, SEQ ID No: 818, SEQ ID No: 820, SEQ ID No: 822, SEQ ID No: 824, SEQ ID No: 826, SEQ ID No: 828, SEQ ID No: 830, SEQ ID No: 832, SEQ ID No: 834, SEQ ID No: 836, SEQ ID No: 838, SEQ ID No: 840, SEQ ID No: 842, SEQ ID No: 844, SEQ ID No: 846, SEQ ID No: 848, SEQ ID No: 850, SEQ ID No: 852, SEQ ID No: 854, SEQ ID No: 856, SEQ ID No: 858, SEQ ID No: 860, SEQ ID No: 862, SEQ ID No: 864, SEQ ID No: 866, SEQ ID No: 868, SEQ ID No: 870, SEQ ID No: 872, SEQ ID No: 874, SEQ ID No: 876, SEQ ID No: 878, SEQ ID No: 880, SEQ ID No: 882, SEQ ID No: 884, SEQ ID No: 886, SEQ ID No: 888, SEQ ID No: 890, SEQ ID No: 892, SEQ ID No: 894, SEQ ID No: 896, SEQ ID No: 898, SEQ ID No: 900, SEQ ID No: 902, SEQ ID No: 904, SEQ ID No: 906, SEQ ID No: 908, SEQ ID No: 910, SEQ ID No: 912, SEQ ID No: 914, SEQ ID No: 916, SEQ ID No: 918, SEQ ID No: 920, SEQ ID No: 922, SEQ ID No: 924, SEQ ID No: 926, SEQ ID No: 928, SEQ ID No: 930, SEQ ID No: 932, SEQ ID No: 934, SEQ ID No: 936, SEQ ID No: 938, SEQ ID No: 940, SEQ ID No: 942, SEQ ID No: 944, SEQ ID No: 946, SEQ ID No: 948, SEQ ID No: 950, SEQ ID No: 952, SEQ ID No: 954, SEQ ID No: 956, SEQ ID No: 958, SEQ ID No: 960, SEQ ID No: 962, SEQ ID No: 964, SEQ ID No: 966, SEQ ID No: 968, SEQ ID No: 970, SEQ ID No: 972, SEQ ID No: 974, SEQ ID No: 976, SEQ ID No: 978, SEQ ID No: 980, SEQ ID No: 982, SEQ ID No: 984, SEQ ID No: 986, SEQ ID No: 988, SEQ ID No: 990, SEQ ID No: 992, SEQ ID No: 994, SEQ ID No: 996, SEQ ID No: 998, SEQ ID No: 1000, SEQ ID No: 1002, SEQ ID No: 1004, SEQ ID No: 1006, SEQ ID No: 1008, SEQ ID No: 1010, SEQ ID No: 1012, SEQ ID No: 1014, SEQ ID No: 1016, SEQ ID No: 1018, SEQ ID No: 1020, SEQ ID No: 1022, SEQ ID No: 1024, SEQ ID No: 1026, SEQ ID No: 1028, SEQ ID No: 1030, SEQ ID No: 1032, SEQ ID No: 1034, SEQ ID No: 1036, SEQ ID No: 1038, SEQ ID No: 1040, SEQ ID No: 1042, SEQ ID No: 1044, SEQ ID No: 1046, SEQ ID No: 1048, SEQ ID No: 1050, SEQ ID No: 1052, SEQ ID No: 1054, SEQ ID No: 1056, SEQ ID No: 1058, SEQ ID No: 1060, SEQ ID No: 1062, SEQ ID No: 1064, SEQ ID No: 1066, SEQ ID No: 1068, SEQ ID No: 1070, SEQ ID No: 1072, SEQ ID No: 1074, SEQ ID No: 1076, SEQ ID No: 1078, SEQ ID No: 1080, SEQ ID No: 1082, SEQ ID No: 1084, SEQ ID No: 1086, SEQ ID No: 1088, SEQ ID No: 1090, SEQ ID No: 1092, SEQ ID No: 1094, SEQ ID No: 1096, SEQ ID No: 1098, SEQ ID NO: 1100, SEQ ID No: 1102, SEQ ID No: 1104, SEQ ID No: 1106, SEQ ID No: 1108, SEQ ID No: 1110, SEQ ID No: 1112, SEQ ID No: 1114, SEQ ID No: 1116, SEQ ID No: 1118, SEQ ID No: 1120, SEQ ID No: 1122, SEQ ID No: 1124, SEQ ID No: 1126, SEQ ID No: 1128, SEQ ID No: 1130, SEQ ID No: 1132, SEQ ID No: 1134, SEQ ID No: 1136, SEQ ID No: 1138, SEQ ID No: 1140, SEQ ID No: 1142, SEQ ID No: 1144, SEQ ID No: 1146, SEQ ID No: 1148, SEQ ID No: 1150, SEQ ID No: 1152, SEQ ID No: 1154, SEQ ID No: 1156, SEQ ID No: 1158, SEQ ID No: 1160, SEQ ID No: 1162, SEQ ID No: 1164, SEQ ID No: 1166, SEQ ID No: 1168, SEQ ID No: 1170, SEQ ID No: 1172, SEQ ID No: 1174, SEQ ID No: 1176, SEQ ID No: 1178, SEQ ID No: 1180, SEQ ID No: 1182, SEQ ID No: 1184, SEQ ID No: 1186, SEQ ID No: 1188, SEQ ID No: 1190, SEQ ID No: 1192, SEQ ID No: 1194, SEQ ID No: 1196, SEQ ID No: 1198, SEQ ID No: 1200, SEQ ID No: 1202, SEQ ID No: 1204, SEQ ID No: 1206, SEQ ID No: 1208, SEQ ID No: 1210, SEQ ID No: 1212, SEQ ID No: 1214, SEQ ID No: 1216, SEQ ID No: 1218, SEQ ID No: 1220, SEQ ID No: 1222, SEQ ID No: 1224, SEQ ID No: 1226, SEQ ID No: 1228, SEQ ID No: 1230, SEQ ID No: 1232, SEQ ID No: 1234, SEQ ID No: 1236, SEQ ID No: 1238, SEQ ID No: 1240, SEQ ID No: 1242, SEQ ID No: 1244, SEQ ID No: 1246, SEQ ID No: 1248, SEQ ID No: 1250, SEQ ID No: 1252, SEQ ID No: 1254, SEQ ID No: 1256, SEQ ID No: 1258, SEQ ID No: 1260, SEQ ID No: 1262, SEQ ID No: 1264, SEQ ID No: 1266, SEQ ID No: 1268, SEQ ID No: 1270, SEQ ID No: 1272, SEQ ID No: 1274, SEQ ID No: 1276, SEQ ID No: 1278, SEQ ID No: 1280, SEQ ID No: 1282, SEQ ID No: 1284, SEQ ID No: 1286, SEQ ID No: 1288, SEQ ID No: 1290, SEQ ID No: 1292, SEQ ID No: 1294, SEQ ID No: 1296, SEQ ID No: 1298, SEQ ID No: 1300, SEQ ID No: 1302, SEQ ID No: 1304, SEQ ID No: 1306, SEQ ID No: 1308, SEQ ID No: 1310, SEQ ID No: 1312, SEQ ID No: 1314, SEQ ID No: 1316, SEQ ID No: 1318, SEQ ID No: 1320, SEQ ID No: 1322, SEQ ID No: 1324, SEQ ID No: 1326, SEQ ID No: 1328, SEQ ID No: 1330, SEQ ID No: 1332, SEQ ID No: 1334, SEQ ID No: 1336, SEQ ID No: 1338, SEQ ID No: 1340, SEQ ID No: 1342, SEQ ID No: 1344, SEQ ID No: 1346, SEQ ID No: 1348, SEQ ID No: 1350, SEQ ID No: 1352, SEQ ID No: 1354, SEQ ID No: 1356, SEQ ID No: 1358, SEQ ID No: 1360, SEQ ID No: 1362, SEQ ID No: 1364, SEQ ID No: 1366, SEQ ID No: 1368, SEQ ID No: 1370, SEQ ID No: 1372, SEQ ID No: 1374, SEQ ID No: 1376, SEQ ID No: 1378, SEQ ID No: 1380, SEQ ID No: 1382, SEQ ID No: 1384, SEQ ID No: 1386, SEQ ID No: 1388, SEQ ID No: 1390, SEQ ID No: 1392, SEQ ID No: 1394, SEQ ID No: 1396, SEQ ID No: 1398, SEQ ID No: 1400, SEQ ID No: 1402, SEQ ID No: 1404, SEQ ID No: 1406, SEQ ID No: 1408, SEQ ID No: 1410, SEQ ID No: 1412, SEQ ID No: 1414, SEQ ID No: 1416, SEQ ID No: 1418, SEQ ID No: 1420, SEQ ID No: 1422, SEQ ID No: 1424, SEQ ID No: 1426, SEQ ID No: 1428, SEQ ID No: 1430, SEQ ID No: 1432, SEQ ID No: 1434, SEQ ID No: 1436, SEQ ID No: 1438, SEQ ID No: 1440, SEQ ID No: 1442, SEQ ID No: 1444, SEQ ID No: 1446, SEQ ID No: 1448, SEQ ID No: 1450, SEQ ID No: 1452, SEQ ID No: 1454, SEQ ID No: 1456, SEQ ID No: 1458, SEQ ID No: 1460, SEQ ID No: 1462, SEQ ID No: 1464, SEQ ID No: 1466, SEQ ID No: 1468, SEQ ID No: 1470, SEQ ID No: 1472, SEQ ID No: 1474, SEQ ID No: 1476, SEQ ID No: 1478, SEQ ID No: 1480, SEQ ID No: 1482, SEQ ID No: 1484, SEQ ID No: 1486, SEQ ID No: 1488, SEQ ID No: 1490, SEQ ID No: 1492, SEQ ID No: 1494, SEQ ID No: 1496, SEQ ID No: 1498, SEQ ID No: 1500, SEQ ID No: 1502, SEQ ID No: 1504, SEQ ID No: 1506, SEQ ID No: 1508, SEQ ID No: 1510, SEQ ID No: 1512, SEQ ID No: 1514, SEQ ID No: 1516, SEQ ID No: 1518, SEQ ID No: 1520, SEQ ID No: 1522, SEQ ID No: 1524, SEQ ID No: 1526, SEQ ID No: 1528, SEQ ID No: 1530, SEQ ID No: 1532, SEQ ID No: 1534, SEQ ID No: 1536, SEQ ID No: 1538, SEQ ID No: 1540, SEQ ID No: 1542, SEQ ID No: 1544, SEQ ID No: 1546, SEQ ID No: 1548, SEQ ID No: 1550, SEQ ID No: 1552, SEQ ID No: 1554, SEQ ID No: 1556, SEQ ID No: 1558, SEQ ID No: 1560, SEQ ID No: 1562, SEQ ID No: 1564, SEQ ID No: 1566, SEQ ID No: 1568, SEQ ID No: 1570, SEQ ID No: 1572, SEQ ID No: 1574, SEQ ID No: 1576, SEQ ID No: 1578, SEQ ID No: 1580, SEQ ID No: 1582, SEQ ID No: 1584, SEQ ID No: 1586, SEQ ID No: 1588, SEQ ID No: 1590, SEQ ID No: 1592, SEQ ID No: 1594, SEQ ID No: 1596, SEQ ID No: 1598, SEQ ID No: 1600, SEQ ID No: 1602, SEQ ID No: 1604, SEQ ID No: 1606, SEQ ID No: 1608, SEQ ID No: 1610, SEQ ID No: 1612, SEQ ID No: 1614, SEQ ID No: 1616, SEQ ID No: 1618, SEQ ID No: 1620, SEQ ID No: 1622, SEQ ID No: 1624, SEQ ID No: 1626, SEQ ID No: 1628, SEQ ID No: 1630, SEQ ID No: 1632, SEQ ID No: 1634, SEQ ID No: 1636, SEQ ID No: 1638, SEQ ID No: 1640, SEQ ID No: 1642, SEQ ID No: 1644, SEQ ID No: 1646, SEQ ID No: 1648, SEQ ID No: 1650, SEQ ID No: 1652, SEQ ID No: 1654, SEQ ID No: 1656, SEQ ID No: 1658, SEQ ID No: 1660, SEQ ID No: 1662, SEQ ID No: 1664, SEQ ID No: 1666, SEQ ID No: 1668, SEQ ID No: 1670, SEQ ID No: 1672, SEQ ID No: 1674, SEQ ID No: 1676, SEQ ID No: 1678, SEQ ID No: 1680, SEQ ID No: 1682, SEQ ID No: 1684, SEQ ID No: 1686, SEQ ID No: 1688, SEQ ID No: 1690, SEQ ID No: 1692, SEQ ID No: 1694, SEQ ID No: 1696, SEQ ID No: 1698, SEQ ID No: 1700, SEQ ID No: 1702, SEQ ID No: 1704, SEQ ID No: 1706, SEQ ID No: 1708, SEQ ID No: 1710, SEQ ID No: 1712, SEQ ID No: 1714, SEQ ID No: 1716, SEQ ID No: 1718, SEQ ID No: 1720, SEQ ID No: 1722, SEQ ID No: 1724, SEQ ID No: 1726, SEQ ID No: 1728, SEQ ID No: 1730, SEQ ID No: 1732, SEQ ID No: 1734, SEQ ID No: 1736, SEQ ID No: 1738, SEQ ID No: 1740, SEQ ID No: 1742, SEQ ID No: 1744, SEQ ID No: 1746, SEQ ID No: 1748, SEQ ID No: 1750, SEQ ID No: 1752, SEQ ID No: 1754, SEQ ID No: 1756, SEQ ID No: 1758, SEQ ID No: 1760, SEQ ID No: 1762, SEQ ID No: 1764, SEQ ID No: 1766, SEQ ID No: 1768, SEQ ID No: 1770, SEQ ID No: 1772, SEQ ID No: 1774, SEQ ID No: 1776, SEQ ID No: 1778, SEQ ID No: 1780, SEQ ID No: 1782, SEQ ID No: 1784, SEQ ID No: 1786, SEQ ID No: 1788, SEQ ID No: 1790, SEQ ID No: 1792, SEQ ID No: 1794, SEQ ID No: 1796, SEQ ID No: 1798, SEQ ID No: 1800, SEQ ID No: 1802, SEQ ID No: 1804, SEQ ID No: 1806, SEQ ID No: 1808, SEQ ID No: 1810, SEQ ID No: 1812, SEQ ID No: 1814, SEQ ID No: 1816, SEQ ID No: 1818, SEQ ID No: 1820, SEQ ID No: 1822, SEQ ID No: 1824, SEQ ID No: 1826, SEQ ID No: 1828, SEQ ID No: 1830, SEQ ID No: 1832, SEQ ID No: 1834, SEQ ID No: 1836, SEQ ID No: 1838, SEQ ID No: 1840, SEQ ID No: 1842, SEQ ID No: 1844, SEQ ID No: 1846, SEQ ID No: 1848, SEQ ID No: 1850, SEQ ID No: 1852, SEQ ID No: 1854, SEQ ID No: 1856, SEQ ID No: 1858, SEQ ID No: 1860, SEQ ID No: 1862, SEQ ID No: 1864, SEQ ID No: 1866, SEQ ID No: 1868, SEQ ID No: 1870, SEQ ID No: 1872, SEQ ID No: 1874, SEQ ID No: 1876, SEQ ID No: 1878, SEQ ID No: 1880, SEQ ID No: 1882, SEQ ID No: 1884, SEQ ID No: 1886, SEQ ID No: 1888, SEQ ID No: 1890, SEQ ID No: 1892, SEQ ID No: 1894, SEQ ID No: 1896, SEQ ID No: 1898, SEQ ID No: 1900, SEQ ID No: 1902, SEQ ID No: 1904, SEQ ID No: 1906, SEQ ID No: 1908, SEQ ID No: 1910, SEQ ID No: 1912, SEQ ID No: 1914, SEQ ID No: 1916, SEQ ID No: 1918, SEQ ID No: 1920, SEQ ID No: 1922, SEQ ID No: 1924, SEQ ID No: 1926, SEQ ID No: 1928, SEQ ID No: 1930, SEQ ID No: 1932, SEQ ID No: 1934, SEQ ID No: 1936, SEQ ID No: 1938, SEQ ID No: 1940, SEQ ID No: 1942, SEQ ID No: 1944, SEQ ID No: 1946, SEQ ID No: 1948, SEQ ID No: 1950, SEQ ID No: 1952, SEQ ID No: 1954, SEQ ID No: 1956, SEQ ID No: 1958, SEQ ID No: 1960, SEQ ID No: 1962, SEQ ID No: 1964, SEQ ID No: 1966, SEQ ID No: 1968, SEQ ID No: 1970, SEQ ID No: 1972, SEQ ID No: 1974 (i.e., a homologue or variant). For example, a protein of the present invention can be less than 100% identical, in combination with being at least about 35% identical, to a given disclosed sequence. In another aspect of the invention, a homologue or variant according to the present invention has an amino acid sequence that is less than about 99% identical to any of such amino acid sequences, and in another embodiment, is less than about 98%> identical to any of such amino acid sequences, and in another embodiment, is less than about 97% identical to any of such amino acid sequences, and in another embodiment, is less than about 96% identical to any of such amino acid sequences, and in another embodiment, is less than about 95% identical to any of such amino acid sequences, and in another embodiment, is less than about 94% identical to any of such amino acid sequences, and in another embodiment, is less than about 93% identical to any of such amino acid sequences, and in another embodiment, is less than about 92% identical to any of such amino acid sequences, and in another embodiment, is less than about 91% identical to any of such amino acid sequences, and in another embodiment, is less than about 90%> identical to any of such amino acid sequences, and so on, in increments of whole integers.
As used herein, unless otherwise specified, reference to a percent (%) identity refers to an evaluation of homology which is performed using: (1) a BLAST 2.0 Basic BLAST homology search using blastp for amino acid searches and blastn for nucleic acid searches with standard default parameters, wherein the query sequence is filtered for low complexity regions by default (described in Altschul, S.F., Madden, T.L., Schaaffer, A.A., Zhang, J., Zhang, Z., Miller, W. & Lipman, D.J. (1997) "Gapped BLAST and PSI-BLAST: a new generation of protein database search programs." Nucleic Acids Res. 25:3389-3402); (2) a BLAST 2 alignment (using the parameters described below); (3) PSI-BLAST with the standard default parameters (Position-Specific Iterated BLAST; and/or (4) CAZy homology determined using standard default parameters from the Carbohydrate Active EnZymes database (Coutinho, P.M. & Henrissat, B. (1999) Carbohydrate-active enzymes: an integrated database approach. In "Recent Advances in Carbohydrate Bioengineering", H.J. Gilbert, G. Davies, B. Henrissat and B. Svensson eds., The Royal Society of Chemistry, Cambridge, pp. 3-12) and/or applying a similar strategy using databases such as the Foly database (website: foly.esil.univ-mrs.fr) and the PeroxiBase (website: peroxibase.isb-sib.ch)
[01105] It is noted that due to some differences in the standard parameters between
BLAST 2.0 Basic BLAST and BLAST 2, two specific sequences might be recognized as having significant homology using the BLAST 2 program, whereas a search performed in BLAST 2.0 Basic BLAST using one of the sequences as the query sequence may not identify the second sequence in the top matches. In addition, PSI-BLAST provides an automated, easy-to-use version of a "profile" search, which is a sensitive way to look for sequence homologues or variants. The program first performs a gapped BLAST database search. The PSI-BLAST program uses the information from any significant alignments returned to construct a position-specific score matrix, which replaces the query sequence for the next round of database searching. Therefore, it is to be understood that percent identity can be determined by using any one of these programs.
[01106] Two specific sequences can be aligned to one another using BLAST 2 sequence as described in Tatusova and Madden, (1999), "Blast 2 sequences - a new tool for comparing protein and nucleotide sequences", FEMS Microbiol Lett. 174:247-250. BLAST 2 sequence alignment is performed in blastp or blastn using the BLAST 2.0 algorithm to perform a Gapped BLAST search (BLAST 2.0) between the two sequences allowing for the introduction of gaps (deletions and insertions) in the resulting alignment. For purposes of clarity herein, a BLAST 2 sequence alignment is performed using the standard default parameters as follows.
For blastn, using 0 BLOSUM62 matrix:
Reward for match = 1 Penalty for mismatch = -2
Open gap (5) and extension gap (2) penalties
gap x dropoff (50) expect (10) word size (11) filter (on)
For blastp, using 0 BLOSUM62 matrix:
Open gap (11) and extension gap (1) penalties
gap x dropoff (50) expect (10) word size (3) filter (on).
A protein of the present invention can also include proteins having an amino acid sequence comprising at least 10 contiguous amino acid residues of any of the sequences described herein (i.e., 10 contiguous amino acid residues having 100% identity with 10 contiguous amino acids of the amino acid sequences of SEQ ID NO: 2, SEQ ID No: 4, SEQ ID No: 6, SEQ ID No: 8, SEQ ID No: 10, SEQ ID No: 12, SEQ ID No: 14, SEQ ID No: 16, SEQ ID No: 18, SEQ ID No: 20, SEQ ID No: 22, SEQ ID No: 24, SEQ ID No: 26, SEQ ID No: 28, SEQ ID No: 30, SEQ ID No: 32, SEQ ID No: 34, SEQ ID No: 36, SEQ ID No: 38, SEQ ID No: 40, SEQ ID No: 42, SEQ ID No: 44, SEQ ID No: 46, SEQ ID No: 48, SEQ ID No: 50, SEQ ID No: 52, SEQ ID No: 54, SEQ ID No: 56, SEQ ID No: 58, SEQ ID No: 60, SEQ ID No: 62, SEQ ID No: 64, SEQ ID No: 66, SEQ ID No: 68, SEQ ID No: 70, SEQ ID No: 72, SEQ ID No: 74, SEQ ID No: 76, SEQ ID No: 78, SEQ ID No: 80, SEQ ID No: 82, SEQ ID No: 84, SEQ ID No: 86, SEQ ID No: 88, SEQ ID No: 90, SEQ ID No: 92, SEQ ID No: 94, SEQ ID No: 96, SEQ ID No: 98, SEQ ID No: 100, SEQ ID No: 102, SEQ ID No: 104, SEQ ID No: 106, SEQ ID No: 108, SEQ ID No: 110, SEQ ID No: 112, SEQ ID No: 114, SEQ ID No: 116, SEQ ID No: 118, SEQ ID No: 120, SEQ ID No: 122, SEQ ID No: 124, SEQ ID No: 126, SEQ ID No: 128, SEQ ID No: 130, SEQ ID No: 132, SEQ ID No: 134, SEQ ID No: 136, SEQ ID No: 138, SEQ ID No: 140, SEQ ID No: 142, SEQ ID No: 144, SEQ ID No: 146, SEQ ID No: 148, SEQ ID No: 150, SEQ ID No: 152, SEQ ID No: 154, SEQ ID No: 156, SEQ ID No: 158, SEQ ID No: 160, SEQ ID No: 162, SEQ ID No: 164, SEQ ID No: 166, SEQ ID No: 168, SEQ ID No: 170, SEQ ID No: 172, SEQ ID No: 174, SEQ ID No: 176, SEQ ID No: 178, SEQ ID No: 180, SEQ ID No: 182, SEQ ID No: 184, SEQ ID No: 186, SEQ ID No: 188, SEQ ID No: 190, SEQ ID No: 192, SEQ ID No: 194, SEQ ID No: 196, SEQ ID No: 198, SEQ ID No: 200, SEQ ID No: 202, SEQ ID No: 204, SEQ ID No: 206, SEQ ID No: 208, SEQ ID No: 210, SEQ ID No: 212, SEQ ID No: 214, SEQ ID No: 216, SEQ ID No: 218, SEQ ID No: 220, SEQ ID No: 222, SEQ ID No: 224, SEQ ID No: 226, SEQ ID No: 228, SEQ ID No: 230, SEQ ID No: 232, SEQ ID No: 234, SEQ ID No: 236, SEQ ID No: 238, SEQ ID No: 240, SEQ ID No: 242, SEQ ID No: 244, SEQ ID No: 246, SEQ ID No: 248, SEQ ID No: 250, SEQ ID No: 252, SEQ ID No: 254, SEQ ID No: 256, SEQ ID No: 258, SEQ ID No: 260, SEQ ID No: 262, SEQ ID No: 264, SEQ ID No: 266, SEQ ID No: 268, SEQ ID No: 270, SEQ ID No: 272, SEQ ID No: 274, SEQ ID No: 276, SEQ ID No: 278, SEQ ID No: 280, SEQ ID No: 282, SEQ ID No: 284, SEQ ID No: 286, SEQ ID No: 288, SEQ ID No: 290, SEQ ID No: 292, SEQ ID No: 294, SEQ ID No: 296, SEQ ID No: 298, SEQ ID No: 300, SEQ ID No: 302, SEQ ID No: 304, SEQ ID No: 306, SEQ ID No: 308, SEQ ID No: 310, SEQ ID No: 312, SEQ ID No: 314, SEQ ID No: 316, SEQ ID No: 318, SEQ ID No: 320, SEQ ID No: 322, SEQ ID No: 324, SEQ ID No: 326, SEQ ID No: 328, SEQ ID No: 330, SEQ ID No: 332, SEQ ID No: 334, SEQ ID No: 336, SEQ ID No: 338, SEQ ID No: 340, SEQ ID No: 342, SEQ ID No: 344, SEQ ID No: 346, SEQ ID No: 348, SEQ ID No: 350, SEQ ID No: 352, SEQ ID No: 354, SEQ ID No: 356, SEQ ID No: 358, SEQ ID No: 360, SEQ ID No: 362, SEQ ID No: 364, SEQ ID No: 366, SEQ ID No: 368, SEQ ID No: 370, SEQ ID No: 372, SEQ ID No: 374, SEQ ID No: 376, SEQ ID No: 378, SEQ ID No: 380, SEQ ID No: 382, SEQ ID No: 384, SEQ ID No: 386, SEQ ID No: 388, SEQ ID No: 390, SEQ ID No: 392, SEQ ID No: 394, SEQ ID No: 396, SEQ ID No: 398, SEQ ID No: 400, SEQ ID No: 402, SEQ ID No: 404, SEQ ID No: 406, SEQ ID No: 408, SEQ ID No: 410, SEQ ID No: 412, SEQ ID No: 414, SEQ ID No: 416, SEQ ID No: 418, SEQ ID No: 420, SEQ ID No: 422, SEQ ID No: 424, SEQ ID No: 426, SEQ ID No: 428, SEQ ID No: 430, SEQ ID No: 432, SEQ ID No: 434, SEQ ID No: 436, SEQ ID No: 438, SEQ ID No: 440, SEQ ID No: 442, SEQ ID No: 444, SEQ ID No: 446, SEQ ID No: 448, SEQ ID No: 450, SEQ ID No: 452, SEQ ID No: 454, SEQ ID No: 456, SEQ ID No: 458, SEQ ID No: 460, SEQ ID No: 462, SEQ ID No: 464, SEQ ID No: 466, SEQ ID No: 468, SEQ ID No: 470, SEQ ID No: 472, SEQ ID No: 474, SEQ ID No: 476, SEQ ID No: 478, SEQ ID No: 480, SEQ ID No: 482, SEQ ID No: 484, SEQ ID No: 486, SEQ ID No: 488, SEQ ID No: 490, SEQ ID No: 492, SEQ ID No: 494, SEQ ID No: 496, SEQ ID No: 498, SEQ ID No: 500, SEQ ID No: 502, SEQ ID No: 504, SEQ ID No: 506, SEQ ID No: 508, SEQ ID No: 510, SEQ ID No: 512, SEQ ID No: 514, SEQ ID No: 516, SEQ ID No: 518, SEQ ID No: 520, SEQ ID No: 522, SEQ ID No: 524, SEQ ID No: 526, SEQ ID No: 528, SEQ ID No: 530, SEQ ID No: 532, SEQ ID No: 534, SEQ ID No: 536, SEQ ID No: 538, SEQ ID No: 540, SEQ ID No: 542, SEQ ID No: 544, SEQ ID No: 546, SEQ ID No: 548, SEQ ID No: 550, SEQ ID No: 552, SEQ ID No: 554, SEQ ID No: 556, SEQ ID No: 558, SEQ ID No: 560, SEQ ID No: 562, SEQ ID No: 564, SEQ ID No: 566, SEQ ID No: 568, SEQ ID No: 570, SEQ ID No: 572, SEQ ID No: 574, SEQ ID No: 576, SEQ ID No: 578, SEQ ID No: 580, SEQ ID No: 582, SEQ ID No: 584, SEQ ID No: 586, SEQ ID No: 588, SEQ ID No: 590, SEQ ID No: 592, SEQ ID No: 594, SEQ ID No: 596, SEQ ID No: 598, SEQ ID No: 600, SEQ ID No: 602, SEQ ID No: 604, SEQ ID No: 606, SEQ ID No: 608, SEQ ID No: 610, SEQ ID No: 612, SEQ ID No: 614, SEQ ID No: 616, SEQ ID No: 618, SEQ ID No: 620, SEQ ID No: 622, SEQ ID No: 624, SEQ ID No: 626, SEQ ID No: 628, SEQ ID No: 630, SEQ ID No: 632, SEQ ID No: 634, SEQ ID No: 636, SEQ ID No: 638, SEQ ID No: 640, SEQ ID No: 642, SEQ ID No: 644, SEQ ID No: 646, SEQ ID No: 648, SEQ ID No: 650, SEQ ID No: 652, SEQ ID No: 654, SEQ ID No: 656, SEQ ID No: 658, SEQ ID No: 660, SEQ ID No: 662, SEQ ID No: 664, SEQ ID No: 666, SEQ ID No: 668, SEQ ID No: 670, SEQ ID No: 672, SEQ ID No: 674, SEQ ID No: 676, SEQ ID No: 678, SEQ ID No: 680, SEQ ID No: 682, SEQ ID No: 684, SEQ ID No: 686, SEQ ID No: 688, SEQ ID No: 690, SEQ ID No: 692, SEQ ID No: 694, SEQ ID No: 696, SEQ ID No: 698, SEQ ID No: 700, SEQ ID No: 702, SEQ ID No: 704, SEQ ID No: 706, SEQ ID No: 708, SEQ ID No: 710, SEQ ID No: 712, SEQ ID No: 714, SEQ ID No: 716, SEQ ID No: 718, SEQ ID No: 720, SEQ ID No: 722, SEQ ID No: 724, SEQ ID No: 726, SEQ ID No: 728, SEQ ID No: 730, SEQ ID No: 732, SEQ ID No: 734, SEQ ID No: 736, SEQ ID No: 738, SEQ ID No: 740, SEQ ID No: 742, SEQ ID No: 744, SEQ ID No: 746, SEQ ID No: 748, SEQ ID No: 750, SEQ ID No: 752, SEQ ID No: 754, SEQ ID No: 756, SEQ ID No: 758, SEQ ID No: 760, SEQ ID No: 762, SEQ ID No: 764, SEQ ID No: 766, SEQ ID No: 768, SEQ ID No: 770, SEQ ID No: 772, SEQ ID No: 774, SEQ ID No: 776, SEQ ID No: 778, SEQ ID No: 780, SEQ ID No: 782, SEQ ID No: 784, SEQ ID No: 786, SEQ ID No: 788, SEQ ID No: 790, SEQ ID No: 792, SEQ ID No: 794 , SEQ ID No: 796, SEQ ID No: SEQ ID No: 798, SEQ ID No: 800, SEQ ID No: 802, SEQ ID No: 804, SEQ ID No: 806, SEQ ID No: 808, SEQ ID No: 810, SEQ ID No: 812, SEQ ID No: 814, SEQ ID No: 816, SEQ ID No: 818, SEQ ID No: 820, SEQ ID No: 822, SEQ ID No: 824, SEQ ID No: 826, SEQ ID No: 828, SEQ ID No: 830, SEQ ID No: 832, SEQ ID No: 834, SEQ ID No: 836, SEQ ID No: 838, SEQ ID No: 840, SEQ ID No: 842, SEQ ID No: 844, SEQ ID No: 846, SEQ ID No: 848, SEQ ID No: 850, SEQ ID No: 852, SEQ ID No: 854, SEQ ID No: 856, SEQ ID No: 858, SEQ ID No: 860, SEQ ID No: 862, SEQ ID No: 864, SEQ ID No: 866, SEQ ID No: 868, SEQ ID No: 870, SEQ ID No: 872, SEQ ID No: 874, SEQ ID No: 876, SEQ ID No: 878, SEQ ID No: 880, SEQ ID No: 882, SEQ ID No: 884, SEQ ID No: 886, SEQ ID No: 888, SEQ ID No: 890, SEQ ID No: 892, SEQ ID No: 894, SEQ ID No: 896, SEQ ID No: 898, SEQ ID No: 900, SEQ ID No: 902, SEQ ID No: 904, SEQ ID No: 906, SEQ ID No: 908, SEQ ID No: 910, SEQ ID No: 912, SEQ ID No: 914, SEQ ID No: 916, SEQ ID No: 918, SEQ ID No: 920, SEQ ID No: 922, SEQ ID No: 924, SEQ ID No: 926, SEQ ID No: 928, SEQ ID No: 930, SEQ ID No: 932, SEQ ID No: 934, SEQ ID No: 936, SEQ ID No: 938, SEQ ID No: 940, SEQ ID No: 942, SEQ ID No: 944, SEQ ID No: 946, SEQ ID No: 948, SEQ ID No: 950, SEQ ID No: 952, SEQ ID No: 954, SEQ ID No: 956, SEQ ID No: 958, SEQ ID No: 960, SEQ ID No: 962, SEQ ID No: 964, SEQ ID No: 966, SEQ ID No: 968, SEQ ID No: 970, SEQ ID No: 972, SEQ ID No: 974, SEQ ID No: 976, SEQ ID No: 978, SEQ ID No: 980, SEQ ID No: 982, SEQ ID No: 984, SEQ ID No: 986, SEQ ID No: 988, SEQ ID No: 990, SEQ ID No: 992, SEQ ID No: 994, SEQ ID No: 996, SEQ ID No: 998, SEQ ID No: 1000, SEQ ID No: 1002, SEQ ID No: 1004, SEQ ID No: 1006, SEQ ID No: 1008, SEQ ID No: 1010, SEQ ID No: 1012, SEQ ID No: 1014, SEQ ID No: 1016, SEQ ID No: 1018, SEQ ID No: 1020, SEQ ID No: 1022, SEQ ID No: 1024, SEQ ID No: 1026, SEQ ID No: 1028, SEQ ID No: 1030, SEQ ID No: 1032, SEQ ID No: 1034, SEQ ID No: 1036, SEQ ID No: 1038, SEQ ID No: 1040, SEQ ID No: 1042, SEQ ID No: 1044, SEQ ID No: 1046, SEQ ID No: 1048, SEQ ID No: 1050, SEQ ID No: 1052, SEQ ID No: 1054, SEQ ID No: 1056, SEQ ID No: 1058, SEQ ID No: 1060, SEQ ID No: 1062, SEQ ID No: 1064, SEQ ID No: 1066, SEQ ID No: 1068, SEQ ID No: 1070, SEQ ID No: 1072, SEQ ID No: 1074, SEQ ID No: 1076, SEQ ID No: 1078, SEQ ID No: 1080, SEQ ID No: 1082, SEQ ID No: 1084, SEQ ID No: 1086, SEQ ID No: 1088, SEQ ID No: 1090, SEQ ID No: 1092, SEQ ID No: 1094, SEQ ID No: 1096, SEQ ID No: 1098, SEQ ID NO: 1100, SEQ ID No: 1102, SEQ ID No: 1104, SEQ ID No: 1106, SEQ ID No: 1108, SEQ ID No: 1110, SEQ ID No: 1112, SEQ ID No: 1114, SEQ ID No: 1116, SEQ ID No: 1118, SEQ ID No: 1120, SEQ ID No: 1122, SEQ ID No: 1124, SEQ ID No: 1126, SEQ ID No: 1128, SEQ ID No: 1130, SEQ ID No: 1132, SEQ ID No: 1134, SEQ ID No: 1136, SEQ ID No: 1138, SEQ ID No: 1140, SEQ ID No: 1142, SEQ ID No: 1144, SEQ ID No: 1146, SEQ ID No: 1148, SEQ ID No: 1150, SEQ ID No: 1152, SEQ ID No: 1154, SEQ ID No: 1156, SEQ ID No: 1158, SEQ ID No: 1160, SEQ ID No: 1162, SEQ ID No: 1164, SEQ ID No: 1166, SEQ ID No: 1168, SEQ ID No: 1170, SEQ ID No: 1172, SEQ ID No: 1174, SEQ ID No: 1176, SEQ ID No: 1178, SEQ ID No: 1180, SEQ ID No: 1182, SEQ ID No: 1184, SEQ ID No: 1186, SEQ ID No: 1188, SEQ ID No: 1190, SEQ ID No: 1192, SEQ ID No: 1194, SEQ ID No: 1196, SEQ ID No: 1198, SEQ ID No: 1200, SEQ ID No: 1202, SEQ ID No: 1204, SEQ ID No: 1206, SEQ ID No: 1208, SEQ ID No: 1210, SEQ ID No: 1212, SEQ ID No: 1214, SEQ ID No: 1216, SEQ ID No: 1218, SEQ ID No: 1220, SEQ ID No: 1222, SEQ ID No: 1224, SEQ ID No: 1226, SEQ ID No: 1228, SEQ ID No: 1230, SEQ ID No: 1232, SEQ ID No: 1234, SEQ ID No: 1236, SEQ ID No: 1238, SEQ ID No: 1240, SEQ ID No: 1242, SEQ ID No: 1244, SEQ ID No: 1246, SEQ ID No: 1248, SEQ ID No: 1250, SEQ ID No: 1252, SEQ ID No: 1254, SEQ ID No: 1256, SEQ ID No: 1258, SEQ ID No: 1260, SEQ ID No: 1262, SEQ ID No: 1264, SEQ ID No: 1266, SEQ ID No: 1268, SEQ ID No: 1270, SEQ ID No: 1272, SEQ ID No: 1274, SEQ ID No: 1276, SEQ ID No: 1278, SEQ ID No: 1280, SEQ ID No: 1282, SEQ ID No: 1284, SEQ ID No: 1286, SEQ ID No: 1288, SEQ ID No: 1290, SEQ ID No: 1292, SEQ ID No: 1294, SEQ ID No: 1296, SEQ ID No: 1298, SEQ ID No: 1300, SEQ ID No: 1302, SEQ ID No: 1304, SEQ ID No: 1306, SEQ ID No: 1308, SEQ ID No: 1310, SEQ ID No: 1312, SEQ ID No: 1314, SEQ ID No: 1316, SEQ ID No: 1318, SEQ ID No: 1320, SEQ ID No: 1322, SEQ ID No: 1324, SEQ ID No: 1326, SEQ ID No: 1328, SEQ ID No: 1330, SEQ ID No: 1332, SEQ ID No: 1334, SEQ ID No: 1336, SEQ ID No: 1338, SEQ ID No: 1340, SEQ ID No: 1342, SEQ ID No: 1344, SEQ ID No: 1346, SEQ ID No: 1348, SEQ ID No: 1350, SEQ ID No: 1352, SEQ ID No: 1354, SEQ ID No: 1356, SEQ ID No: 1358, SEQ ID No: 1360, SEQ ID No: 1362, SEQ ID No: 1364, SEQ ID No: 1366, SEQ ID No: 1368, SEQ ID No: 1370, SEQ ID No: 1372, SEQ ID No: 1374, SEQ ID No: 1376, SEQ ID No: 1378, SEQ ID No: 1380, SEQ ID No: 1382, SEQ ID No: 1384, SEQ ID No: 1386, SEQ ID No: 1388, SEQ ID No: 1390, SEQ ID No: 1392, SEQ ID No: 1394, SEQ ID No: 1396, SEQ ID No: 1398, SEQ ID No: 1400, SEQ ID No: 1402, SEQ ID No: 1404, SEQ ID No: 1406, SEQ ID No: 1408, SEQ ID No: 1410, SEQ ID No: 1412, SEQ ID No: 1414, SEQ ID No: 1416, SEQ ID No: 1418, SEQ ID No: 1420, SEQ ID No: 1422, SEQ ID No: 1424, SEQ ID No: 1426, SEQ ID No: 1428, SEQ ID No: 1430, SEQ ID No: 1432, SEQ ID No: 1434, SEQ ID No: 1436, SEQ ID No: 1438, SEQ ID No: 1440, SEQ ID No: 1442, SEQ ID No: 1444, SEQ ID No: 1446, SEQ ID No: 1448, SEQ ID No: 1450, SEQ ID No: 1452, SEQ ID No: 1454, SEQ ID No: 1456, SEQ ID No: 1458, SEQ ID No: 1460, SEQ ID No: 1462, SEQ ID No: 1464, SEQ ID No: 1466, SEQ ID No: 1468, SEQ ID No: 1470, SEQ ID No: 1472, SEQ ID No: 1474, SEQ ID No: 1476, SEQ ID No: 1478, SEQ ID No: 1480, SEQ ID No: 1482, SEQ ID No: 1484, SEQ ID No: 1486, SEQ ID No: 1488, SEQ ID No: 1490, SEQ ID No: 1492, SEQ ID No: 1494, SEQ ID No: 1496, SEQ ID No: 1498, SEQ ID No: 1500, SEQ ID No: 1502, SEQ ID No: 1504, SEQ ID No: 1506, SEQ ID No: 1508, SEQ ID No: 1510, SEQ ID No: 1512, SEQ ID No: 1514, SEQ ID No: 1516, SEQ ID No: 1518, SEQ ID No: 1520, SEQ ID No: 1522, SEQ ID No: 1524, SEQ ID No: 1526, SEQ ID No: 1528, SEQ ID No: 1530, SEQ ID No: 1532, SEQ ID No: 1534, SEQ ID No: 1536, SEQ ID No: 1538, SEQ ID No: 1540, SEQ ID No: 1542, SEQ ID No: 1544, SEQ ID No: 1546, SEQ ID No: 1548, SEQ ID No: 1550, SEQ ID No: 1552, SEQ ID No: 1554, SEQ ID No: 1556, SEQ ID No: 1558, SEQ ID No: 1560, SEQ ID No: 1562, SEQ ID No: 1564, SEQ ID No: 1566, SEQ ID No: 1568, SEQ ID No: 1570, SEQ ID No: 1572, SEQ ID No: 1574, SEQ ID No: 1576, SEQ ID No: 1578, SEQ ID No: 1580, SEQ ID No: 1582, SEQ ID No: 1584, SEQ ID No: 1586, SEQ ID No: 1588, SEQ ID No: 1590, SEQ ID No: 1592, SEQ ID No: 1594, SEQ ID No: 1596, SEQ ID No: 1598, SEQ ID No: 1600, SEQ ID No: 1602, SEQ ID No: 1604, SEQ ID No: 1606, SEQ ID No: 1608, SEQ ID No: 1610, SEQ ID No: 1612, SEQ ID No: 1614, SEQ ID No: 1616, SEQ ID No: 1618, SEQ ID No: 1620, SEQ ID No: 1622, SEQ ID No: 1624, SEQ ID No: 1626, SEQ ID No: 1628, SEQ ID No: 1630, SEQ ID No: 1632, SEQ ID No: 1634, SEQ ID No: 1636, SEQ ID No: 1638, SEQ ID No: 1640, SEQ ID No: 1642, SEQ ID No: 1644, SEQ ID No: 1646, SEQ ID No: 1648, SEQ ID No: 1650, SEQ ID No: 1652, SEQ ID No: 1654, SEQ ID No: 1656, SEQ ID No: 1658, SEQ ID No: 1660, SEQ ID No: 1662, SEQ ID No: 1664, SEQ ID No: 1666, SEQ ID No: 1668, SEQ ID No: 1670, SEQ ID No: 1672, SEQ ID No: 1674, SEQ ID No: 1676, SEQ ID No: 1678, SEQ ID No: 1680, SEQ ID No: 1682, SEQ ID No: 1684, SEQ ID No: 1686, SEQ ID No: 1688, SEQ ID No: 1690, SEQ ID No: 1692, SEQ ID No: 1694, SEQ ID No: 1696, SEQ ID No: 1698, SEQ ID No: 1700, SEQ ID No: 1702, SEQ ID No: 1704, SEQ ID No: 1706, SEQ ID No: 1708, SEQ ID No: 1710, SEQ ID No: 1712, SEQ ID No: 1714, SEQ ID No: 1716, SEQ ID No: 1718, SEQ ID No: 1720, SEQ ID No: 1722, SEQ ID No: 1724, SEQ ID No: 1726, SEQ ID No: 1728, SEQ ID No: 1730, SEQ ID No: 1732, SEQ ID No: 1734, SEQ ID No: 1736, SEQ ID No: 1738, SEQ ID No: 1740, SEQ ID No: 1742, SEQ ID No: 1744, SEQ ID No: 1746, SEQ ID No: 1748, SEQ ID No: 1750, SEQ ID No: 1752, SEQ ID No: 1754, SEQ ID No: 1756, SEQ ID No: 1758, SEQ ID No: 1760, SEQ ID No: 1762, SEQ ID No: 1764, SEQ ID No: 1766, SEQ ID No: 1768, SEQ ID No: 1770, SEQ ID No: 1772, SEQ ID No: 1774, SEQ ID No: 1776, SEQ ID No: 1778, SEQ ID No: 1780, SEQ ID No: 1782, SEQ ID No: 1784, SEQ ID No: 1786, SEQ ID No: 1788, SEQ ID No: 1790, SEQ ID No: 1792, SEQ ID No: 1794, SEQ ID No: 1796, SEQ ID No: 1798, SEQ ID No: 1800, SEQ ID No: 1802, SEQ ID No: 1804, SEQ ID No: 1806, SEQ ID No: 1808, SEQ ID No: 1810, SEQ ID No: 1812, SEQ ID No: 1814, SEQ ID No: 1816, SEQ ID No: 1818, SEQ ID No: 1820, SEQ ID No: 1822, SEQ ID No: 1824, SEQ ID No: 1826, SEQ ID No: 1828, SEQ ID No: 1830, SEQ ID No: 1832, SEQ ID No: 1834, SEQ ID No: 1836, SEQ ID No: 1838, SEQ ID No: 1840, SEQ ID No: 1842, SEQ ID No: 1844, SEQ ID No: 1846, SEQ ID No: 1848, SEQ ID No: 1850, SEQ ID No: 1852, SEQ ID No: 1854, SEQ ID No: 1856, SEQ ID No: 1858, SEQ ID No: 1860, SEQ ID No: 1862, SEQ ID No: 1864, SEQ ID No: 1866, SEQ ID No: 1868, SEQ ID No: 1870, SEQ ID No: 1872, SEQ ID No: 1874, SEQ ID No: 1876, SEQ ID No: 1878, SEQ ID No: 1880, SEQ ID No: 1882, SEQ ID No: 1884, SEQ ID No: 1886, SEQ ID No: 1888, SEQ ID No: 1890, SEQ ID No: 1892, SEQ ID No: 1894, SEQ ID No: 1896, SEQ ID No: 1898, SEQ ID No: 1900, SEQ ID No: 1902, SEQ ID No: 1904, SEQ ID No: 1906, SEQ ID No: 1908, SEQ ID No: 1910, SEQ ID No: 1912, SEQ ID No: 1914, SEQ ID No: 1916, SEQ ID No: 1918, SEQ ID No: 1920, SEQ ID No: 1922, SEQ ID No: 1924, SEQ ID No: 1926, SEQ ID No: 1928, SEQ ID No: 1930, SEQ ID No: 1932, SEQ ID No: 1934, SEQ ID No: 1936, SEQ ID No: 1938, SEQ ID No: 1940, SEQ ID No: 1942, SEQ ID No: 1944, SEQ ID No: 1946, SEQ ID No: 1948, SEQ ID No: 1950, SEQ ID No: 1952, SEQ ID No: 1954, SEQ ID No: 1956, SEQ ID No: 1958, SEQ ID No: 1960, SEQ ID No: 1962, SEQ ID No: 1964, SEQ ID No: 1966, SEQ ID No: 1968, SEQ ID No: 1970, SEQ ID No: 1972, SEQ ID No: 1974). In other embodiments, a homologue or variant of a protein amino acid sequence includes amino acid sequences comprising at least 20, or at least 30, or at least 40, or at least 50, or at least 75, or at least 100, or at least 125, or at least 150, or at least 175, or at least 150, or at least 200, or at least 250, or at least 300, or at least 350 contiguous amino acid residues of any of the amino acid sequence represented disclosed herein. Even small fragments of proteins without biological activity are useful in the present invention, for example, in the preparation of antibodies against the full-length protein or in a screening assay (e.g., a binding assay). Fragments can also be used to construct fusion proteins, for example, where the fusion protein comprises functional domains from two or more different proteins (e.g., a CBM from one protein linked to a CD from another protein). In one embodiment, a homologue or variant has a measurable or detectable biological activity associated with the wild-type protein (e.g., enzymatic activity).
[01108] According to the present invention, the term "contiguous" or "consecutive", with regard to nucleic acid or amino acid sequences described herein, means to be connected in an unbroken sequence. For example, for a first sequence to comprise 30 contiguous (or consecutive) amino acids of a second sequence, means that the first sequence includes an unbroken sequence of 30 amino acid residues that is 100% identical to an unbroken sequence of 30 amino acid residues in the second sequence. Similarly, for a first sequence to have "100% identity" with a second sequence means that the first sequence exactly matches the second sequence with no gaps between nucleotides or amino acids.
[01109] In another embodiment, a protein of the present invention, including a homologue or variant, includes a protein having an amino acid sequence that is sufficiently similar to a natural amino acid sequence that a nucleic acid sequence encoding the homologue or variant is capable of hybridizing under moderate, high or very high stringency conditions (described below) to (i.e., with) a nucleic acid molecule encoding the natural protein (i.e., to the complement of the nucleic acid strand encoding the natural amino acid sequence). Preferably, a homologue or variant of a protein of the present invention is encoded by a nucleic acid molecule comprising a nucleic acid sequence that hybridizes under low, moderate, or high stringency conditions to the complement of a nucleic acid sequence that encodes a protein comprising, consisting essentially of, or consisting of, an amino acid sequence represented by any of SEQ ID NO: 2, SEQ ID No: 4, SEQ ID No: 6, SEQ ID No: 8, SEQ ID No: 10, SEQ ID No: 12, SEQ ID No: 14, SEQ ID No: 16, SEQ ID No: 18, SEQ ID No: 20, SEQ ID No: 22, SEQ ID No: 24, SEQ ID No: 26, SEQ ID No: 28, SEQ ID No: 30, SEQ ID No: 32, SEQ ID No: 34, SEQ ID No: 36, SEQ ID No: 38, SEQ ID No: 40, SEQ ID No: 42, SEQ ID No: 44, SEQ ID No: 46, SEQ ID No: 48, SEQ ID No: 50, SEQ ID No: 52, SEQ ID No: 54, SEQ ID No: 56, SEQ ID No: 58, SEQ ID No: 60, SEQ ID No: 62, SEQ ID No: 64, SEQ ID No: 66, SEQ ID No: 68, SEQ ID No: 70, SEQ ID No: 72, SEQ ID No: 74, SEQ ID No: 76, SEQ ID No: 78, SEQ ID No: 80, SEQ ID No: 82, SEQ ID No: 84, SEQ ID No: 86, SEQ ID No: 88, SEQ ID No: 90, SEQ ID No: 92, SEQ ID No: 94, SEQ ID No: 96, SEQ ID No: 98, SEQ ID No: 100, SEQ ID No: 102, SEQ ID No: 104, SEQ ID No: 106, SEQ ID No: 108, SEQ ID No: 110, SEQ ID No: 112, SEQ ID No: 114, SEQ ID No: 116, SEQ ID No: 118, SEQ ID No: 120, SEQ ID No: 122, SEQ ID No: 124, SEQ ID No: 126, SEQ ID No: 128, SEQ ID No: 130, SEQ ID No: 132, SEQ ID No: 134, SEQ ID No: 136, SEQ ID No: 138, SEQ ID No: 140, SEQ ID No: 142, SEQ ID No: 144, SEQ ID No: 146, SEQ ID No: 148, SEQ ID No: 150, SEQ ID No: 152, SEQ ID No: 154, SEQ ID No: 156, SEQ ID No: 158, SEQ ID No: 160, SEQ ID No: 162, SEQ ID No: 164, SEQ ID No: 166, SEQ ID No: 168, SEQ ID No: 170, SEQ ID No: 172, SEQ ID No: 174, SEQ ID No: 176, SEQ ID No: 178, SEQ ID No: 180, SEQ ID No: 182, SEQ ID No: 184, SEQ ID No: 186, SEQ ID No: 188, SEQ ID No: 190, SEQ ID No: 192, SEQ ID No: 194, SEQ ID No: 196, SEQ ID No: 198, SEQ ID No: 200, SEQ ID No: 202, SEQ ID No: 204, SEQ ID No: 206, SEQ ID No: 208, SEQ ID No: 210, SEQ ID No: 212, SEQ ID No: 214, SEQ ID No: 216, SEQ ID No: 218, SEQ ID No: 220, SEQ ID No: 222, SEQ ID No: 224, SEQ ID No: 226, SEQ ID No: 228, SEQ ID No: 230, SEQ ID No: 232, SEQ ID No: 234, SEQ ID No: 236, SEQ ID No: 238, SEQ ID No: 240, SEQ ID No: 242, SEQ ID No: 244, SEQ ID No: 246, SEQ ID No: 248, SEQ ID No: 250, SEQ ID No: 252, SEQ ID No: 254, SEQ ID No: 256, SEQ ID No: 258, SEQ ID No: 260, SEQ ID No: 262, SEQ ID No: 264, SEQ ID No: 266, SEQ ID No: 268, SEQ ID No: 270, SEQ ID No: 272, SEQ ID No: 274, SEQ ID No: 276, SEQ ID No: 278, SEQ ID No: 280, SEQ ID No: 282, SEQ ID No: 284, SEQ ID No: 286, SEQ ID No: 288, SEQ ID No: 290, SEQ ID No: 292, SEQ ID No: 294, SEQ ID No: 296, SEQ ID No: 298, SEQ ID No: 300, SEQ ID No: 302, SEQ ID No: 304, SEQ ID No: 306, SEQ ID No: 308, SEQ ID No: 310, SEQ ID No: 312, SEQ ID No: 314, SEQ ID No: 316, SEQ ID No: 318, SEQ ID No: 320, SEQ ID No: 322, SEQ ID No: 324, SEQ ID No: 326, SEQ ID No: 328, SEQ ID No: 330, SEQ ID No: 332, SEQ ID No: 334, SEQ ID No: 336, SEQ ID No: 338, SEQ ID No: 340, SEQ ID No: 342, SEQ ID No: 344, SEQ ID No: 346, SEQ ID No: 348, SEQ ID No: 350, SEQ ID No: 352, SEQ ID No: 354, SEQ ID No: 356, SEQ ID No: 358, SEQ ID No: 360, SEQ ID No: 362, SEQ ID No: 364, SEQ ID No: 366, SEQ ID No: 368, SEQ ID No: 370, SEQ ID No: 372, SEQ ID No: 374, SEQ ID No: 376, SEQ ID No: 378, SEQ ID No: 380, SEQ ID No: 382, SEQ ID No: 384, SEQ ID No: 386, SEQ ID No: 388, SEQ ID No: 390, SEQ ID No: 392, SEQ ID No: 394, SEQ ID No: 396, SEQ ID No: 398, SEQ ID No: 400, SEQ ID No: 402, SEQ ID No: 404, SEQ ID No: 406, SEQ ID No: 408, SEQ ID No: 410, SEQ ID No: 412, SEQ ID No: 414, SEQ ID No: 416, SEQ ID No: 418, SEQ ID No: 420, SEQ ID No: 422, SEQ ID No: 424, SEQ ID No: 426, SEQ ID No: 428, SEQ ID No: 430, SEQ ID No: 432, SEQ ID No: 434, SEQ ID No: 436, SEQ ID No: 438, SEQ ID No: 440, SEQ ID No: 442, SEQ ID No: 444, SEQ ID No: 446, SEQ ID No: 448, SEQ ID No: 450, SEQ ID No: 452, SEQ ID No: 454, SEQ ID No: 456, SEQ ID No: 458, SEQ ID No: 460, SEQ ID No: 462, SEQ ID No: 464, SEQ ID No: 466, SEQ ID No: 468, SEQ ID No: 470, SEQ ID No: 472, SEQ ID No: 474, SEQ ID No: 476, SEQ ID No: 478, SEQ ID No: 480, SEQ ID No: 482, SEQ ID No: 484, SEQ ID No: 486, SEQ ID No: 488, SEQ ID No: 490, SEQ ID No: 492, SEQ ID No: 494, SEQ ID No: 496, SEQ ID No: 498, SEQ ID No: 500, SEQ ID No: 502, SEQ ID No: 504, SEQ ID No: 506, SEQ ID No: 508, SEQ ID No: 510, SEQ ID No: 512, SEQ ID No: 514, SEQ ID No: 516, SEQ ID No: 518, SEQ ID No: 520, SEQ ID No: 522, SEQ ID No: 524, SEQ ID No: 526, SEQ ID No: 528, SEQ ID No: 530, SEQ ID No: 532, SEQ ID No: 534, SEQ ID No: 536, SEQ ID No: 538, SEQ ID No: 540, SEQ ID No: 542, SEQ ID No: 544, SEQ ID No: 546, SEQ ID No: 548, SEQ ID No: 550, SEQ ID No: 552, SEQ ID No: 554, SEQ ID No: 556, SEQ ID No: 558, SEQ ID No: 560, SEQ ID No: 562, SEQ ID No: 564, SEQ ID No: 566, SEQ ID No: 568, SEQ ID No: 570, SEQ ID No: 572, SEQ ID No: 574, SEQ ID No: 576, SEQ ID No: 578, SEQ ID No: 580, SEQ ID No: 582, SEQ ID No: 584, SEQ ID No: 586, SEQ ID No: 588, SEQ ID No: 590, SEQ ID No: 592, SEQ ID No: 594, SEQ ID No: 596, SEQ ID No: 598, SEQ ID No: 600, SEQ ID No: 602, SEQ ID No: 604, SEQ ID No: 606, SEQ ID No: 608, SEQ ID No: 610, SEQ ID No: 612, SEQ ID No: 614, SEQ ID No: 616, SEQ ID No: 618, SEQ ID No: 620, SEQ ID No: 622, SEQ ID No: 624, SEQ ID No: 626, SEQ ID No: 628, SEQ ID No: 630, SEQ ID No: 632, SEQ ID No: 634, SEQ ID No: 636, SEQ ID No: 638, SEQ ID No: 640, SEQ ID No: 642, SEQ ID No: 644, SEQ ID No: 646, SEQ ID No: 648, SEQ ID No: 650, SEQ ID No: 652, SEQ ID No: 654, SEQ ID No: 656, SEQ ID No: 658, SEQ ID No: 660, SEQ ID No: 662, SEQ ID No: 664, SEQ ID No: 666, SEQ ID No: 668, SEQ ID No: 670, SEQ ID No: 672, SEQ ID No: 674, SEQ ID No: 676, SEQ ID No: 678, SEQ ID No: 680, SEQ ID No: 682, SEQ ID No: 684, SEQ ID No: 686, SEQ ID No: 688, SEQ ID No: 690, SEQ ID No: 692, SEQ ID No: 694, SEQ ID No: 696, SEQ ID No: 698, SEQ ID No: 700, SEQ ID No: 702, SEQ ID No: 704, SEQ ID No: 706, SEQ ID No: 708, SEQ ID No: 710, SEQ ID No: 712, SEQ ID No: 714, SEQ ID No: 716, SEQ ID No: 718, SEQ ID No: 720, SEQ ID No: 722, SEQ ID No: 724, SEQ ID No: 726, SEQ ID No: 728, SEQ ID No: 730, SEQ ID No: 732, SEQ ID No: 734, SEQ ID No: 736, SEQ ID No: 738, SEQ ID No: 740, SEQ ID No: 742, SEQ ID No: 744, SEQ ID No: 746, SEQ ID No: 748, SEQ ID No: 750, SEQ ID No: 752, SEQ ID No: 754, SEQ ID No: 756, SEQ ID No: 758, SEQ ID No: 760, SEQ ID No: 762, SEQ ID No: 764, SEQ ID No: 766, SEQ ID No: 768, SEQ ID No: 770, SEQ ID No: 772, SEQ ID No: 774, SEQ ID No: 776, SEQ ID No: 778, SEQ ID No: 780, SEQ ID No: 782, SEQ ID No: 784, SEQ ID No: 786, SEQ ID No: 788, SEQ ID No: 790, SEQ ID No: 792, SEQ ID No: 794, SEQ ID No: 796, SEQ ID No: SEQ ID No: 798, SEQ ID No: 800, SEQ ID No: 802, SEQ ID No: 804, SEQ ID No: 806, SEQ ID No: 808, SEQ ID No: 810, SEQ ID No: 812, SEQ ID No: 814, SEQ ID No: 816, SEQ ID No: 818, SEQ ID No: 820, SEQ ID No: 822, SEQ ID No: 824, SEQ ID No: 826, SEQ ID No: 828, SEQ ID No: 830, SEQ ID No: 832, SEQ ID No: 834, SEQ ID No: 836, SEQ ID No: 838, SEQ ID No: 840, SEQ ID No: 842, SEQ ID No: 844, SEQ ID No: 846, SEQ ID No: 848, SEQ ID No: 850, SEQ ID No: 852, SEQ ID No: 854, SEQ ID No: 856, SEQ ID No: 858, SEQ ID No: 860, SEQ ID No: 862, SEQ ID No: 864, SEQ ID No: 866, SEQ ID No: 868, SEQ ID No: 870, SEQ ID No: 872, SEQ ID No: 874, SEQ ID No: 876, SEQ ID No: 878, SEQ ID No: 880, SEQ ID No: 882, SEQ ID No: 884, SEQ ID No: 886, SEQ ID No: 888, SEQ ID No: 890, SEQ ID No: 892, SEQ ID No: 894, SEQ ID No: 896, SEQ ID No: 898, SEQ ID No: 900, SEQ ID No: 902, SEQ ID No: 904, SEQ ID No: 906, SEQ ID No: 908, SEQ ID No: 910, SEQ ID No: 912, SEQ ID No: 914, SEQ ID No: 916, SEQ ID No: 918, SEQ ID No: 920, SEQ ID No: 922, SEQ ID No: 924, SEQ ID No: 926, SEQ ID No: 928, SEQ ID No: 930, SEQ ID No: 932, SEQ ID No: 934, SEQ ID No: 936, SEQ ID No: 938, SEQ ID No: 940, SEQ ID No: 942, SEQ ID No: 944, SEQ ID No: 946, SEQ ID No: 948, SEQ ID No: 950, SEQ ID No: 952, SEQ ID No: 954, SEQ ID No: 956, SEQ ID No: 958, SEQ ID No: 960, SEQ ID No: 962, SEQ ID No: 964, SEQ ID No: 966, SEQ ID No: 968, SEQ ID No: 970, SEQ ID No: 972, SEQ ID No: 974, SEQ ID No: 976, SEQ ID No: 978, SEQ ID No: 980, SEQ ID No: 982, SEQ ID No: 984, SEQ ID No: 986, SEQ ID No: 988, SEQ ID No: 990, SEQ ID No: 992, SEQ ID No: 994, SEQ ID No: 996, SEQ ID No: 998, SEQ ID No: 1000, SEQ ID No: 1002, SEQ ID No: 1004, SEQ ID No: 1006, SEQ ID No: 1008, SEQ ID No: 1010, SEQ ID No: 1012, SEQ ID No: 1014, SEQ ID No: 1016, SEQ ID No: 1018, SEQ ID No: 1020, SEQ ID No: 1022, SEQ ID No: 1024, SEQ ID No: 1026, SEQ ID No: 1028, SEQ ID No: 1030, SEQ ID No: 1032, SEQ ID No: 1034, SEQ ID No: 1036, SEQ ID No: 1038, SEQ ID No: 1040, SEQ ID No: 1042, SEQ ID No: 1044, SEQ ID No: 1046, SEQ ID No: 1048, SEQ ID No: 1050, SEQ ID No: 1052, SEQ ID No: 1054, SEQ ID No: 1056, SEQ ID No: 1058, SEQ ID No: 1060, SEQ ID No: 1062, SEQ ID No: 1064, SEQ ID No: 1066, SEQ ID No: 1068, SEQ ID No: 1070, SEQ ID No: 1072, SEQ ID No: 1074, SEQ ID No: 1076, SEQ ID No: 1078, SEQ ID No: 1080, SEQ ID No: 1082, SEQ ID No: 1084, SEQ ID No: 1086, SEQ ID No: 1088, SEQ ID No: 1090, SEQ ID No: 1092, SEQ ID No: 1094, SEQ ID No: 1096, SEQ ID No: 1098, SEQ ID NO: 1100, SEQ ID No: 1102, SEQ ID No: 1104, SEQ ID No: 1106, SEQ ID No: 1108, SEQ ID No: 1110, SEQ ID No: 1112, SEQ ID No: 1114, SEQ ID No: 1116, SEQ ID No: 1118, SEQ ID No: 1120, SEQ ID No: 1122, SEQ ID No: 1124, SEQ ID No: 1126, SEQ ID No: 1128, SEQ ID No: 1130, SEQ ID No: 1132, SEQ ID No: 1134, SEQ ID No: 1136, SEQ ID No: 1138, SEQ ID No: 1140, SEQ ID No: 1142, SEQ ID No: 1144, SEQ ID No: 1146, SEQ ID No: 1148, SEQ ID No: 1150, SEQ ID No: 1152, SEQ ID No: 1154, SEQ ID No: 1156, SEQ ID No: 1158, SEQ ID No: 1160, SEQ ID No: 1162, SEQ ID No: 1164, SEQ ID No: 1166, SEQ ID No: 1168, SEQ ID No: 1170, SEQ ID No: 1172, SEQ ID No: 1174, SEQ ID No: 1176, SEQ ID No: 1178, SEQ ID No: 1180, SEQ ID No: 1182, SEQ ID No: 1184, SEQ ID No: 1186, SEQ ID No: 1188, SEQ ID No: 1190, SEQ ID No: 1192, SEQ ID No: 1194, SEQ ID No: 1196, SEQ ID No: 1198, SEQ ID No: 1200, SEQ ID No: 1202, SEQ ID No: 1204, SEQ ID No: 1206, SEQ ID No: 1208, SEQ ID No: 1210, SEQ ID No: 1212, SEQ ID No: 1214, SEQ ID No: 1216, SEQ ID No: 1218, SEQ ID No: 1220, SEQ ID No: 1222, SEQ ID No: 1224, SEQ ID No: 1226, SEQ ID No: 1228, SEQ ID No: 1230, SEQ ID No: 1232, SEQ ID No: 1234, SEQ ID No: 1236, SEQ ID No: 1238, SEQ ID No: 1240, SEQ ID No: 1242, SEQ ID No: 1244, SEQ ID No: 1246, SEQ ID No: 1248, SEQ ID No: 1250, SEQ ID No: 1252, SEQ ID No: 1254, SEQ ID No: 1256, SEQ ID No: 1258, SEQ ID No: 1260, SEQ ID No: 1262, SEQ ID No: 1264, SEQ ID No: 1266, SEQ ID No: 1268, SEQ ID No: 1270, SEQ ID No: 1272, SEQ ID No: 1274, SEQ ID No: 1276, SEQ ID No: 1278, SEQ ID No: 1280, SEQ ID No: 1282, SEQ ID No: 1284, SEQ ID No: 1286, SEQ ID No: 1288, SEQ ID No: 1290, SEQ ID No: 1292, SEQ ID No: 1294, SEQ ID No: 1296, SEQ ID No: 1298, SEQ ID No: 1300, SEQ ID No: 1302, SEQ ID No: 1304, SEQ ID No: 1306, SEQ ID No: 1308, SEQ ID No: 1310, SEQ ID No: 1312, SEQ ID No: 1314, SEQ ID No: 1316, SEQ ID No: 1318, SEQ ID No: 1320, SEQ ID No: 1322, SEQ ID No: 1324, SEQ ID No: 1326, SEQ ID No: 1328, SEQ ID No: 1330, SEQ ID No: 1332, SEQ ID No: 1334, SEQ ID No: 1336, SEQ ID No: 1338, SEQ ID No: 1340, SEQ ID No: 1342, SEQ ID No: 1344, SEQ ID No: 1346, SEQ ID No: 1348, SEQ ID No: 1350, SEQ ID No: 1352, SEQ ID No: 1354, SEQ ID No: 1356, SEQ ID No: 1358, SEQ ID No: 1360, SEQ ID No: 1362, SEQ ID No: 1364, SEQ ID No: 1366, SEQ ID No: 1368, SEQ ID No: 1370, SEQ ID No: 1372, SEQ ID No: 1374, SEQ ID No: 1376, SEQ ID No: 1378, SEQ ID No: 1380, SEQ ID No: 1382, SEQ ID No: 1384, SEQ ID No: 1386, SEQ ID No: 1388, SEQ ID No: 1390, SEQ ID No: 1392, SEQ ID No: 1394, SEQ ID No: 1396, SEQ ID No: 1398, SEQ ID No: 1400, SEQ ID No: 1402, SEQ ID No: 1404, SEQ ID No: 1406, SEQ ID No: 1408, SEQ ID No: 1410, SEQ ID No: 1412, SEQ ID No: 1414, SEQ ID No: 1416, SEQ ID No: 1418, SEQ ID No: 1420, SEQ ID No: 1422, SEQ ID No: 1424, SEQ ID No: 1426, SEQ ID No: 1428, SEQ ID No: 1430, SEQ ID No: 1432, SEQ ID No: 1434, SEQ ID No: 1436, SEQ ID No: 1438, SEQ ID No: 1440, SEQ ID No: 1442, SEQ ID No: 1444, SEQ ID No: 1446, SEQ ID No: 1448, SEQ ID No: 1450, SEQ ID No: 1452, SEQ ID No: 1454, SEQ ID No: 1456, SEQ ID No: 1458, SEQ ID No: 1460, SEQ ID No: 1462, SEQ ID No: 1464, SEQ ID No: 1466, SEQ ID No: 1468, SEQ ID No: 1470, SEQ ID No: 1472, SEQ ID No: 1474, SEQ ID No: 1476, SEQ ID No: 1478, SEQ ID No: 1480, SEQ ID No: 1482, SEQ ID No: 1484, SEQ ID No: 1486, SEQ ID No: 1488, SEQ ID No: 1490, SEQ ID No: 1492, SEQ ID No: 1494, SEQ ID No: 1496, SEQ ID No: 1498, SEQ ID No: 1500, SEQ ID No: 1502, SEQ ID No: 1504, SEQ ID No: 1506, SEQ ID No: 1508, SEQ ID No: 1510, SEQ ID No: 1512, SEQ ID No: 1514, SEQ ID No: 1516, SEQ ID No: 1518, SEQ ID No: 1520, SEQ ID No: 1522, SEQ ID No: 1524, SEQ ID No: 1526, SEQ ID No: 1528, SEQ ID No: 1530, SEQ ID No: 1532, SEQ ID No: 1534, SEQ ID No: 1536, SEQ ID No: 1538, SEQ ID No: 1540, SEQ ID No: 1542, SEQ ID No: 1544, SEQ ID No: 1546, SEQ ID No: 1548, SEQ ID No: 1550, SEQ ID No: 1552, SEQ ID No: 1554, SEQ ID No: 1556, SEQ ID No: 1558, SEQ ID No: 1560, SEQ ID No: 1562, SEQ ID No: 1564, SEQ ID No: 1566, SEQ ID No: 1568, SEQ ID No: 1570, SEQ ID No: 1572, SEQ ID No: 1574, SEQ ID No: 1576, SEQ ID No: 1578, SEQ ID No: 1580, SEQ ID No: 1582, SEQ ID No: 1584, SEQ ID No: 1586, SEQ ID No: 1588, SEQ ID No: 1590, SEQ ID No: 1592, SEQ ID No: 1594, SEQ ID No: 1596, SEQ ID No: 1598, SEQ ID No: 1600, SEQ ID No: 1602, SEQ ID No: 1604, SEQ ID No: 1606, SEQ ID No: 1608, SEQ ID No: 1610, SEQ ID No: 1612, SEQ ID No: 1614, SEQ ID No: 1616, SEQ ID No: 1618, SEQ ID No: 1620, SEQ ID No: 1622, SEQ ID No: 1624, SEQ ID No: 1626, SEQ ID No: 1628, SEQ ID No: 1630, SEQ ID No: 1632, SEQ ID No: 1634, SEQ ID No: 1636, SEQ ID No: 1638, SEQ ID No: 1640, SEQ ID No: 1642, SEQ ID No: 1644, SEQ ID No: 1646, SEQ ID No: 1648, SEQ ID No: 1650, SEQ ID No: 1652, SEQ ID No: 1654, SEQ ID No: 1656, SEQ ID No: 1658, SEQ ID No: 1660, SEQ ID No: 1662, SEQ ID No: 1664, SEQ ID No: 1666, SEQ ID No: 1668, SEQ ID No: 1670, SEQ ID No: 1672, SEQ ID No: 1674, SEQ ID No: 1676, SEQ ID No: 1678, SEQ ID No: 1680, SEQ ID No: 1682, SEQ ID No: 1684, SEQ ID No: 1686, SEQ ID No: 1688, SEQ ID No: 1690, SEQ ID No: 1692, SEQ ID No: 1694, SEQ ID No: 1696, SEQ ID No: 1698, SEQ ID No: 1700, SEQ ID No: 1702, SEQ ID No: 1704, SEQ ID No: 1706, SEQ ID No: 1708, SEQ ID No: 1710, SEQ ID No: 1712, SEQ ID No: 1714, SEQ ID No: 1716, SEQ ID No: 1718, SEQ ID No: 1720, SEQ ID No: 1722, SEQ ID No: 1724, SEQ ID No: 1726, SEQ ID No: 1728, SEQ ID No: 1730, SEQ ID No: 1732, SEQ ID No: 1734, SEQ ID No: 1736, SEQ ID No: 1738, SEQ ID No: 1740, SEQ ID No: 1742, SEQ ID No: 1744, SEQ ID No: 1746, SEQ ID No: 1748, SEQ ID No: 1750, SEQ ID No: 1752, SEQ ID No: 1754, SEQ ID No: 1756, SEQ ID No: 1758, SEQ ID No: 1760, SEQ ID No: 1762, SEQ ID No: 1764, SEQ ID No: 1766, SEQ ID No: 1768, SEQ ID No: 1770, SEQ ID No: 1772, SEQ ID No: 1774, SEQ ID No: 1776, SEQ ID No: 1778, SEQ ID No: 1780, SEQ ID No: 1782, SEQ ID No: 1784, SEQ ID No: 1786, SEQ ID No: 1788, SEQ ID No: 1790, SEQ ID No: 1792, SEQ ID No: 1794, SEQ ID No: 1796, SEQ ID No: 1798, SEQ ID No: 1800, SEQ ID No: 1802, SEQ ID No: 1804, SEQ ID No: 1806, SEQ ID No: 1808, SEQ ID No: 1810, SEQ ID No: 1812, SEQ ID No: 1814, SEQ ID No: 1816, SEQ ID No: 1818, SEQ ID No: 1820, SEQ ID No: 1822, SEQ ID No: 1824, SEQ ID No: 1826, SEQ ID No: 1828, SEQ ID No: 1830, SEQ ID No: 1832, SEQ ID No: 1834, SEQ ID No: 1836, SEQ ID No: 1838, SEQ ID No: 1840, SEQ ID No: 1842, SEQ ID No: 1844, SEQ ID No: 1846, SEQ ID No: 1848, SEQ ID No: 1850, SEQ ID No: 1852, SEQ ID No: 1854, SEQ ID No: 1856, SEQ ID No: 1858, SEQ ID No: 1860, SEQ ID No: 1862, SEQ ID No: 1864, SEQ ID No: 1866, SEQ ID No: 1868, SEQ ID No: 1870, SEQ ID No: 1872, SEQ ID No: 1874, SEQ ID No: 1876, SEQ ID No: 1878, SEQ ID No: 1880, SEQ ID No: 1882, SEQ ID No: 1884, SEQ ID No: 1886, SEQ ID No: 1888, SEQ ID No: 1890, SEQ ID No: 1892, SEQ ID No: 1894, SEQ ID No: 1896, SEQ ID No: 1898, SEQ ID No: 1900, SEQ ID No: 1902, SEQ ID No: 1904, SEQ ID No: 1906, SEQ ID No: 1908, SEQ ID No: 1910, SEQ ID No: 1912, SEQ ID No: 1914, SEQ ID No: 1916, SEQ ID No: 1918, SEQ ID No: 1920, SEQ ID No: 1922, SEQ ID No: 1924, SEQ ID No: 1926, SEQ ID No: 1928, SEQ ID No: 1930, SEQ ID No: 1932, SEQ ID No: 1934, SEQ ID No: 1936, SEQ ID No: 1938, SEQ ID No: 1940, SEQ ID No: 1942, SEQ ID No: 1944, SEQ ID No: 1946, SEQ ID No: 1948, SEQ ID No: 1950, SEQ ID No: 1952, SEQ ID No: 1954, SEQ ID No: 1956, SEQ ID No: 1958, SEQ ID No: 1960, SEQ ID No: 1962, SEQ ID No: 1964, SEQ ID No: 1966, SEQ ID No: 1968, SEQ ID No: 1970, SEQ ID No: 1972, SEQ ID No: 1974. Such hybridization conditions are described in detail below. ] A nucleic acid sequence complement of nucleic acid sequence encoding a protein of the present invention refers to the nucleic acid sequence of the nucleic acid strand that is complementary to the strand which encodes the protein. It will be appreciated that a double stranded DNA which encodes a given amino acid sequence comprises a single strand DNA and its complementary strand having a sequence that is a complement to the single strand DNA. As such, nucleic acid molecules of the present invention can be either double-stranded or single-stranded, and include those nucleic acid molecules that form stable hybrids under stringent hybridization conditions with a nucleic acid sequence that encodes an amino acid sequence such as the amino acid sequences of SEQ ID NO: 2, SEQ ID No: 4, SEQ ID No: 6, SEQ ID No: 8, SEQ ID No: 10, SEQ ID No: 12, SEQ ID No: 14, SEQ ID No: 16, SEQ ID No: 18, SEQ ID No: 20, SEQ ID No: 22, SEQ ID No: 24, SEQ ID No: 26, SEQ ID No: 28, SEQ ID No: 30, SEQ ID No: 32, SEQ ID No: 34, SEQ ID No: 36, SEQ ID No: 38, SEQ ID No: 40, SEQ ID No: 42, SEQ ID No: 44, SEQ ID No: 46, SEQ ID No: 48, SEQ ID No: 50, SEQ ID No: 52, SEQ ID No: 54, SEQ ID No: 56, SEQ ID No: 58, SEQ ID No: 60, SEQ ID No: 62, SEQ ID No: 64, SEQ ID No: 66, SEQ ID No: 68, SEQ ID No: 70, SEQ ID No: 72, SEQ ID No: 74, SEQ ID No: 76, SEQ ID No: 78, SEQ ID No: 80, SEQ ID No: 82, SEQ ID No: 84, SEQ ID No: 86, SEQ ID No: 88, SEQ ID No: 90, SEQ ID No: 92, SEQ ID No: 94, SEQ ID No: 96, SEQ ID No: 98, SEQ ID No: 100, SEQ ID No: 102, SEQ ID No: 104, SEQ ID No: 106, SEQ ID No: 108, SEQ ID No: 110, SEQ ID No: 112, SEQ ID No: 114, SEQ ID No: 116, SEQ ID No: 118, SEQ ID No: 120, SEQ ID No: 122, SEQ ID No: 124, SEQ ID No: 126, SEQ ID No: 128, SEQ ID No: 130, SEQ ID No: 132, SEQ ID No: 134, SEQ ID No: 136, SEQ ID No: 138, SEQ ID No: 140, SEQ ID No: 142, SEQ ID No: 144, SEQ ID No: 146, SEQ ID No: 148, SEQ ID No: 150, SEQ ID No: 152, SEQ ID No: 154, SEQ ID No: 156, SEQ ID No: 158, SEQ ID No: 160, SEQ ID No: 162, SEQ ID No: 164, SEQ ID No: 166, SEQ ID No: 168, SEQ ID No: 170, SEQ ID No: 172, SEQ ID No: 174, SEQ ID No: 176, SEQ ID No: 178, SEQ ID No: 180, SEQ ID No: 182, SEQ ID No: 184, SEQ ID No: 186, SEQ ID No: 188, SEQ ID No: 190, SEQ ID No: 192, SEQ ID No: 194, SEQ ID No: 196, SEQ ID No: 198, SEQ ID No: 200, SEQ ID No: 202, SEQ ID No: 204, SEQ ID No: 206, SEQ ID No: 208, SEQ ID No: 210, SEQ ID No: 212, SEQ ID No: 214, SEQ ID No: 216, SEQ ID No: 218, SEQ ID No: 220, SEQ ID No: 222, SEQ ID No: 224, SEQ ID No: 226, SEQ ID No: 228, SEQ ID No: 230, SEQ ID No: 232, SEQ ID No: 234, SEQ ID No: 236, SEQ ID No: 238, SEQ ID No: 240, SEQ ID No: 242, SEQ ID No: 244, SEQ ID No: 246, SEQ ID No: 248, SEQ ID No: 250, SEQ ID No: 252, SEQ ID No: 254, SEQ ID No: 256, SEQ ID No: 258, SEQ ID No: 260, SEQ ID No: 262, SEQ ID No: 264, SEQ ID No: 266, SEQ ID No: 268, SEQ ID No: 270, SEQ ID No: 272, SEQ ID No: 274, SEQ ID No: 276, SEQ ID No: 278, SEQ ID No: 280, SEQ ID No: 282, SEQ ID No: 284, SEQ ID No: 286, SEQ ID No: 288, SEQ ID No: 290, SEQ ID No: 292, SEQ ID No: 294, SEQ ID No: 296, SEQ ID No: 298, SEQ ID No: 300, SEQ ID No: 302, SEQ ID No: 304, SEQ ID No: 306, SEQ ID No: 308, SEQ ID No: 310, SEQ ID No: 312, SEQ ID No: 314, SEQ ID No: 316, SEQ ID No: 318, SEQ ID No: 320, SEQ ID No: 322, SEQ ID No: 324, SEQ ID No: 326, SEQ ID No: 328, SEQ ID No: 330, SEQ ID No: 332, SEQ ID No: 334, SEQ ID No: 336, SEQ ID No: 338, SEQ ID No: 340, SEQ ID No: 342, SEQ ID No: 344, SEQ ID No: 346, SEQ ID No: 348, SEQ ID No: 350, SEQ ID No: 352, SEQ ID No: 354, SEQ ID No: 356, SEQ ID No: 358, SEQ ID No: 360, SEQ ID No: 362, SEQ ID No: 364, SEQ ID No: 366, SEQ ID No: 368, SEQ ID No: 370, SEQ ID No: 372, SEQ ID No: 374, SEQ ID No: 376, SEQ ID No: 378, SEQ ID No: 380, SEQ ID No: 382, SEQ ID No: 384, SEQ ID No: 386, SEQ ID No: 388, SEQ ID No: 390, SEQ ID No: 392, SEQ ID No: 394, SEQ ID No: 396, SEQ ID No: 398, SEQ ID No: 400, SEQ ID No: 402, SEQ ID No: 404, SEQ ID No: 406, SEQ ID No: 408, SEQ ID No: 410, SEQ ID No: 412, SEQ ID No: 414, SEQ ID No: 416, SEQ ID No: 418, SEQ ID No: 420, SEQ ID No: 422, SEQ ID No: 424, SEQ ID No: 426, SEQ ID No: 428, SEQ ID No: 430, SEQ ID No: 432, SEQ ID No: 434, SEQ ID No: 436, SEQ ID No: 438, SEQ ID No: 440, SEQ ID No: 442, SEQ ID No: 444, SEQ ID No: 446, SEQ ID No: 448, SEQ ID No: 450, SEQ ID No: 452, SEQ ID No: 454, SEQ ID No: 456, SEQ ID No: 458, SEQ ID No: 460, SEQ ID No: 462, SEQ ID No: 464, SEQ ID No: 466, SEQ ID No: 468, SEQ ID No: 470, SEQ ID No: 472, SEQ ID No: 474, SEQ ID No: 476, SEQ ID No: 478, SEQ ID No: 480, SEQ ID No: 482, SEQ ID No: 484, SEQ ID No: 486, SEQ ID No: 488, SEQ ID No: 490, SEQ ID No: 492, SEQ ID No: 494, SEQ ID No: 496, SEQ ID No: 498, SEQ ID No: 500, SEQ ID No: 502, SEQ ID No: 504, SEQ ID No: 506, SEQ ID No: 508, SEQ ID No: 510, SEQ ID No: 512, SEQ ID No: 514, SEQ ID No: 516, SEQ ID No: 518, SEQ ID No: 520, SEQ ID No: 522, SEQ ID No: 524, SEQ ID No: 526, SEQ ID No: 528, SEQ ID No: 530, SEQ ID No: 532, SEQ ID No: 534, SEQ ID No: 536, SEQ ID No: 538, SEQ ID No: 540, SEQ ID No: 542, SEQ ID No: 544, SEQ ID No: 546, SEQ ID No: 548, SEQ ID No: 550, SEQ ID No: 552, SEQ ID No: 554, SEQ ID No: 556, SEQ ID No: 558, SEQ ID No: 560, SEQ ID No: 562, SEQ ID No: 564, SEQ ID No: 566, SEQ ID No: 568, SEQ ID No: 570, SEQ ID No: 572, SEQ ID No: 574, SEQ ID No: 576, SEQ ID No: 578, SEQ ID No: 580, SEQ ID No: 582, SEQ ID No: 584, SEQ ID No: 586, SEQ ID No: 588, SEQ ID No: 590, SEQ ID No: 592, SEQ ID No: 594, SEQ ID No: 596, SEQ ID No: 598, SEQ ID No: 600, SEQ ID No: 602, SEQ ID No: 604, SEQ ID No: 606, SEQ ID No: 608, SEQ ID No: 610, SEQ ID No: 612, SEQ ID No: 614, SEQ ID No: 616, SEQ ID No: 618, SEQ ID No: 620, SEQ ID No: 622, SEQ ID No: 624, SEQ ID No: 626, SEQ ID No: 628, SEQ ID No: 630, SEQ ID No: 632, SEQ ID No: 634, SEQ ID No: 636, SEQ ID No: 638, SEQ ID No: 640, SEQ ID No: 642, SEQ ID No: 644, SEQ ID No: 646, SEQ ID No: 648, SEQ ID No: 650, SEQ ID No: 652, SEQ ID No: 654, SEQ ID No: 656, SEQ ID No: 658, SEQ ID No: 660, SEQ ID No: 662, SEQ ID No: 664, SEQ ID No: 666, SEQ ID No: 668, SEQ ID No: 670, SEQ ID No: 672, SEQ ID No: 674, SEQ ID No: 676, SEQ ID No: 678, SEQ ID No: 680, SEQ ID No: 682, SEQ ID No: 684, SEQ ID No: 686, SEQ ID No: 688, SEQ ID No: 690, SEQ ID No: 692, SEQ ID No: 694, SEQ ID No: 696, SEQ ID No: 698, SEQ ID No: 700, SEQ ID No: 702, SEQ ID No: 704, SEQ ID No: 706, SEQ ID No: 708, SEQ ID No: 710, SEQ ID No: 712, SEQ ID No: 714, SEQ ID No: 716, SEQ ID No: 718, SEQ ID No: 720, SEQ ID No: 722, SEQ ID No: 724, SEQ ID No: 726, SEQ ID No: 728, SEQ ID No: 730, SEQ ID No: 732, SEQ ID No: 734, SEQ ID No: 736, SEQ ID No: 738, SEQ ID No: 740, SEQ ID No: 742, SEQ ID No: 744, SEQ ID No: 746, SEQ ID No: 748, SEQ ID No: 750, SEQ ID No: 752, SEQ ID No: 754, SEQ ID No: 756, SEQ ID No: 758, SEQ ID No: 760, SEQ ID No: 762, SEQ ID No: 764, SEQ ID No: 766, SEQ ID No: 768, SEQ ID No: 770, SEQ ID No: 772, SEQ ID No: 774, SEQ ID No: 776, SEQ ID No: 778, SEQ ID No: 780, SEQ ID No: 782, SEQ ID No: 784, SEQ ID No: 786, SEQ ID No: 788, SEQ ID No: 790, SEQ ID No: 792, SEQ ID No: 794, SEQ ID No: 796, SEQ ID No: SEQ ID No: 798, SEQ ID No: 800, SEQ ID No: 802, SEQ ID No: 804, SEQ ID No: 806, SEQ ID No: 808, SEQ ID No: 810, SEQ ID No: 812, SEQ ID No: 814, SEQ ID No: 816, SEQ ID No: 818, SEQ ID No: 820, SEQ ID No: 822, SEQ ID No: 824, SEQ ID No: 826, SEQ ID No: 828, SEQ ID No: 830, SEQ ID No: 832, SEQ ID No: 834, SEQ ID No: 836, SEQ ID No: 838, SEQ ID No: 840, SEQ ID No: 842, SEQ ID No: 844, SEQ ID No: 846, SEQ ID No: 848, SEQ ID No: 850, SEQ ID No: 852, SEQ ID No: 854, SEQ ID No: 856, SEQ ID No: 858, SEQ ID No: 860, SEQ ID No: 862, SEQ ID No: 864, SEQ ID No: 866, SEQ ID No: 868, SEQ ID No: 870, SEQ ID No: 872, SEQ ID No: 874, SEQ ID No: 876, SEQ ID No: 878, SEQ ID No: 880, SEQ ID No: 882, SEQ ID No: 884, SEQ ID No: 886, SEQ ID No: 888, SEQ ID No: 890, SEQ ID No: 892, SEQ ID No: 894, SEQ ID No: 896, SEQ ID No: 898, SEQ ID No: 900, SEQ ID No: 902, SEQ ID No: 904, SEQ ID No: 906, SEQ ID No: 908, SEQ ID No: 910, SEQ ID No: 912, SEQ ID No: 914, SEQ ID No: 916, SEQ ID No: 918, SEQ ID No: 920, SEQ ID No: 922, SEQ ID No: 924, SEQ ID No: 926, SEQ ID No: 928, SEQ ID No: 930, SEQ ID No: 932, SEQ ID No: 934, SEQ ID No: 936, SEQ ID No: 938, SEQ ID No: 940, SEQ ID No: 942, SEQ ID No: 944, SEQ ID No: 946, SEQ ID No: 948, SEQ ID No: 950, SEQ ID No: 952, SEQ ID No: 954, SEQ ID No: 956, SEQ ID No: 958, SEQ ID No: 960, SEQ ID No: 962, SEQ ID No: 964, SEQ ID No: 966, SEQ ID No: 968, SEQ ID No: 970, SEQ ID No: 972, SEQ ID No: 974, SEQ ID No: 976, SEQ ID No: 978, SEQ ID No: 980, SEQ ID No: 982, SEQ ID No: 984, SEQ ID No: 986, SEQ ID No: 988, SEQ ID No: 990, SEQ ID No: 992, SEQ ID No: 994, SEQ ID No: 996, SEQ ID No: 998, SEQ ID No: 1000, SEQ ID No: 1002, SEQ ID No: 1004, SEQ ID No: 1006, SEQ ID No: 1008, SEQ ID No: 1010, SEQ ID No: 1012, SEQ ID No: 1014, SEQ ID No: 1016, SEQ ID No: 1018, SEQ ID No: 1020, SEQ ID No: 1022, SEQ ID No: 1024, SEQ ID No: 1026, SEQ ID No: 1028, SEQ ID No: 1030, SEQ ID No: 1032, SEQ ID No: 1034, SEQ ID No: 1036, SEQ ID No: 1038, SEQ ID No: 1040, SEQ ID No: 1042, SEQ ID No: 1044, SEQ ID No: 1046, SEQ ID No: 1048, SEQ ID No: 1050, SEQ ID No: 1052, SEQ ID No: 1054, SEQ ID No: 1056, SEQ ID No: 1058, SEQ ID No: 1060, SEQ ID No: 1062, SEQ ID No: 1064, SEQ ID No: 1066, SEQ ID No: 1068, SEQ ID No: 1070, SEQ ID No: 1072, SEQ ID No: 1074, SEQ ID No: 1076, SEQ ID No: 1078, SEQ ID No: 1080, SEQ ID No: 1082, SEQ ID No: 1084, SEQ ID No: 1086, SEQ ID No: 1088, SEQ ID No: 1090, SEQ ID No: 1092, SEQ ID No: 1094, SEQ ID No: 1096, SEQ ID No: 1098, SEQ ID NO: 1100, SEQ ID No: 1102, SEQ ID No: 1104, SEQ ID No: 1106, SEQ ID No: 1108, SEQ ID No: 1110, SEQ ID No: 1112, SEQ ID No: 1114, SEQ ID No: 1116, SEQ ID No: 1118, SEQ ID No: 1120, SEQ ID No: 1122, SEQ ID No: 1124, SEQ ID No: 1126, SEQ ID No: 1128, SEQ ID No: 1130, SEQ ID No: 1132, SEQ ID No: 1134, SEQ ID No: 1136, SEQ ID No: 1138, SEQ ID No: 1140, SEQ ID No: 1142, SEQ ID No: 1144, SEQ ID No: 1146, SEQ ID No: 1148, SEQ ID No: 1150, SEQ ID No: 1152, SEQ ID No: 1154, SEQ ID No: 1156, SEQ ID No: 1158, SEQ ID No: 1160, SEQ ID No: 1162, SEQ ID No: 1164, SEQ ID No: 1166, SEQ ID No: 1168, SEQ ID No: 1170, SEQ ID No: 1172, SEQ ID No: 1174, SEQ ID No: 1176, SEQ ID No: 1178, SEQ ID No: 1180, SEQ ID No: 1182, SEQ ID No: 1184, SEQ ID No: 1186, SEQ ID No: 1188, SEQ ID No: 1190, SEQ ID No: 1192, SEQ ID No: 1194, SEQ ID No: 1196, SEQ ID No: 1198, SEQ ID No: 1200, SEQ ID No: 1202, SEQ ID No: 1204, SEQ ID No: 1206, SEQ ID No: 1208, SEQ ID No: 1210, SEQ ID No: 1212, SEQ ID No: 1214, SEQ ID No: 1216, SEQ ID No: 1218, SEQ ID No: 1220, SEQ ID No: 1222, SEQ ID No: 1224, SEQ ID No: 1226, SEQ ID No: 1228, SEQ ID No: 1230, SEQ ID No: 1232, SEQ ID No: 1234, SEQ ID No: 1236, SEQ ID No: 1238, SEQ ID No: 1240, SEQ ID No: 1242, SEQ ID No: 1244, SEQ ID No: 1246, SEQ ID No: 1248, SEQ ID No: 1250, SEQ ID No: 1252, SEQ ID No: 1254, SEQ ID No: 1256, SEQ ID No: 1258, SEQ ID No: 1260, SEQ ID No: 1262, SEQ ID No: 1264, SEQ ID No: 1266, SEQ ID No: 1268, SEQ ID No: 1270, SEQ ID No: 1272, SEQ ID No: 1274, SEQ ID No: 1276, SEQ ID No: 1278, SEQ ID No: 1280, SEQ ID No: 1282, SEQ ID No: 1284, SEQ ID No: 1286, SEQ ID No: 1288, SEQ ID No: 1290, SEQ ID No: 1292, SEQ ID No: 1294, SEQ ID No: 1296, SEQ ID No: 1298, SEQ ID No: 1300, SEQ ID No: 1302, SEQ ID No: 1304, SEQ ID No: 1306, SEQ ID No: 1308, SEQ ID No: 1310, SEQ ID No: 1312, SEQ ID No: 1314, SEQ ID No: 1316, SEQ ID No: 1318, SEQ ID No: 1320, SEQ ID No: 1322, SEQ ID No: 1324, SEQ ID No: 1326, SEQ ID No: 1328, SEQ ID No: 1330, SEQ ID No: 1332, SEQ ID No: 1334, SEQ ID No: 1336, SEQ ID No: 1338, SEQ ID No: 1340, SEQ ID No: 1342, SEQ ID No: 1344, SEQ ID No: 1346, SEQ ID No: 1348, SEQ ID No: 1350, SEQ ID No: 1352, SEQ ID No: 1354, SEQ ID No: 1356, SEQ ID No: 1358, SEQ ID No: 1360, SEQ ID No: 1362, SEQ ID No: 1364, SEQ ID No: 1366, SEQ ID No: 1368, SEQ ID No: 1370, SEQ ID No: 1372, SEQ ID No: 1374, SEQ ID No: 1376, SEQ ID No: 1378, SEQ ID No: 1380, SEQ ID No: 1382, SEQ ID No: 1384, SEQ ID No: 1386, SEQ ID No: 1388, SEQ ID No: 1390, SEQ ID No: 1392, SEQ ID No: 1394, SEQ ID No: 1396, SEQ ID No: 1398, SEQ ID No: 1400, SEQ ID No: 1402, SEQ ID No: 1404, SEQ ID No: 1406, SEQ ID No: 1408, SEQ ID No: 1410, SEQ ID No: 1412, SEQ ID No: 1414, SEQ ID No: 1416, SEQ ID No: 1418, SEQ ID No: 1420, SEQ ID No: 1422, SEQ ID No: 1424, SEQ ID No: 1426, SEQ ID No: 1428, SEQ ID No: 1430, SEQ ID No: 1432, SEQ ID No: 1434, SEQ ID No: 1436, SEQ ID No: 1438, SEQ ID No: 1440, SEQ ID No: 1442, SEQ ID No: 1444, SEQ ID No: 1446, SEQ ID No: 1448, SEQ ID No: 1450, SEQ ID No: 1452, SEQ ID No: 1454, SEQ ID No: 1456, SEQ ID No: 1458, SEQ ID No: 1460, SEQ ID No: 1462, SEQ ID No: 1464, SEQ ID No: 1466, SEQ ID No: 1468, SEQ ID No: 1470, SEQ ID No: 1472, SEQ ID No: 1474, SEQ ID No: 1476, SEQ ID No: 1478, SEQ ID No: 1480, SEQ ID No: 1482, SEQ ID No: 1484, SEQ ID No: 1486, SEQ ID No: 1488, SEQ ID No: 1490, SEQ ID No: 1492, SEQ ID No: 1494, SEQ ID No: 1496, SEQ ID No: 1498, SEQ ID No: 1500, SEQ ID No: 1502, SEQ ID No: 1504, SEQ ID No: 1506, SEQ ID No: 1508, SEQ ID No: 1510, SEQ ID No: 1512, SEQ ID No: 1514, SEQ ID No: 1516, SEQ ID No: 1518, SEQ ID No: 1520, SEQ ID No: 1522, SEQ ID No: 1524, SEQ ID No: 1526, SEQ ID No: 1528, SEQ ID No: 1530, SEQ ID No: 1532, SEQ ID No: 1534, SEQ ID No: 1536, SEQ ID No: 1538, SEQ ID No: 1540, SEQ ID No: 1542, SEQ ID No: 1544, SEQ ID No: 1546, SEQ ID No: 1548, SEQ ID No: 1550, SEQ ID No: 1552, SEQ ID No: 1554, SEQ ID No: 1556, SEQ ID No: 1558, SEQ ID No: 1560, SEQ ID No: 1562, SEQ ID No: 1564, SEQ ID No: 1566, SEQ ID No: 1568, SEQ ID No: 1570, SEQ ID No: 1572, SEQ ID No: 1574, SEQ ID No: 1576, SEQ ID No: 1578, SEQ ID No: 1580, SEQ ID No: 1582, SEQ ID No: 1584, SEQ ID No: 1586, SEQ ID No: 1588, SEQ ID No: 1590, SEQ ID No: 1592, SEQ ID No: 1594, SEQ ID No: 1596, SEQ ID No: 1598, SEQ ID No: 1600, SEQ ID No: 1602, SEQ ID No: 1604, SEQ ID No: 1606, SEQ ID No: 1608, SEQ ID No: 1610, SEQ ID No: 1612, SEQ ID No: 1614, SEQ ID No: 1616, SEQ ID No: 1618, SEQ ID No: 1620, SEQ ID No: 1622, SEQ ID No: 1624, SEQ ID No: 1626, SEQ ID No: 1628, SEQ ID No: 1630, SEQ ID No: 1632, SEQ ID No: 1634, SEQ ID No: 1636, SEQ ID No: 1638, SEQ ID No: 1640, SEQ ID No: 1642, SEQ ID No: 1644, SEQ ID No: 1646, SEQ ID No: 1648, SEQ ID No: 1650, SEQ ID No: 1652, SEQ ID No: 1654, SEQ ID No: 1656, SEQ ID No: 1658, SEQ ID No: 1660, SEQ ID No: 1662, SEQ ID No: 1664, SEQ ID No: 1666, SEQ ID No: 1668, SEQ ID No: 1670, SEQ ID No: 1672, SEQ ID No: 1674, SEQ ID No: 1676, SEQ ID No: 1678, SEQ ID No: 1680, SEQ ID No: 1682, SEQ ID No: 1684, SEQ ID No: 1686, SEQ ID No: 1688, SEQ ID No: 1690, SEQ ID No: 1692, SEQ ID No: 1694, SEQ ID No: 1696, SEQ ID No: 1698, SEQ ID No: 1700, SEQ ID No: 1702, SEQ ID No: 1704, SEQ ID No: 1706, SEQ ID No: 1708, SEQ ID No: 1710, SEQ ID No: 1712, SEQ ID No: 1714, SEQ ID No: 1716, SEQ ID No: 1718, SEQ ID No: 1720, SEQ ID No: 1722, SEQ ID No: 1724, SEQ ID No: 1726, SEQ ID No: 1728, SEQ ID No: 1730, SEQ ID No: 1732, SEQ ID No: 1734, SEQ ID No: 1736, SEQ ID No: 1738, SEQ ID No: 1740, SEQ ID No: 1742, SEQ ID No: 1744, SEQ ID No: 1746, SEQ ID No: 1748, SEQ ID No: 1750, SEQ ID No: 1752, SEQ ID No: 1754, SEQ ID No: 1756, SEQ ID No: 1758, SEQ ID No: 1760, SEQ ID No: 1762, SEQ ID No: 1764, SEQ ID No: 1766, SEQ ID No: 1768, SEQ ID No: 1770, SEQ ID No: 1772, SEQ ID No: 1774, SEQ ID No: 1776, SEQ ID No: 1778, SEQ ID No: 1780, SEQ ID No: 1782, SEQ ID No: 1784, SEQ ID No: 1786, SEQ ID No: 1788, SEQ ID No: 1790, SEQ ID No: 1792, SEQ ID No: 1794, SEQ ID No: 1796, SEQ ID No: 1798, SEQ ID No: 1800, SEQ ID No: 1802, SEQ ID No: 1804, SEQ ID No: 1806, SEQ ID No: 1808, SEQ ID No: 1810, SEQ ID No: 1812, SEQ ID No: 1814, SEQ ID No: 1816, SEQ ID No: 1818, SEQ ID No: 1820, SEQ ID No: 1822, SEQ ID No: 1824, SEQ ID No: 1826, SEQ ID No: 1828, SEQ ID No: 1830, SEQ ID No: 1832, SEQ ID No: 1834, SEQ ID No: 1836, SEQ ID No: 1838, SEQ ID No: 1840, SEQ ID No: 1842, SEQ ID No: 1844, SEQ ID No: 1846, SEQ ID No: 1848, SEQ ID No: 1850, SEQ ID No: 1852, SEQ ID No: 1854, SEQ ID No: 1856, SEQ ID No: 1858, SEQ ID No: 1860, SEQ ID No: 1862, SEQ ID No: 1864, SEQ ID No: 1866, SEQ ID No: 1868, SEQ ID No: 1870, SEQ ID No: 1872, SEQ ID No: 1874, SEQ ID No: 1876, SEQ ID No: 1878, SEQ ID No: 1880, SEQ ID No: 1882, SEQ ID No: 1884, SEQ ID No: 1886, SEQ ID No: 1888, SEQ ID No: 1890, SEQ ID No: 1892, SEQ ID No: 1894, SEQ ID No: 1896, SEQ ID No: 1898, SEQ ID No: 1900, SEQ ID No: 1902, SEQ ID No: 1904, SEQ ID No: 1906, SEQ ID No: 1908, SEQ ID No: 1910, SEQ ID No: 1912, SEQ ID No: 1914, SEQ ID No: 1916, SEQ ID No: 1918, SEQ ID No: 1920, SEQ ID No: 1922, SEQ ID No: 1924, SEQ ID No: 1926, SEQ ID No: 1928, SEQ ID No: 1930, SEQ ID No: 1932, SEQ ID No: 1934, SEQ ID No: 1936, SEQ ID No: 1938, SEQ ID No: 1940, SEQ ID No: 1942, SEQ ID No: 1944, SEQ ID No: 1946, SEQ ID No: 1948, SEQ ID No: 1950, SEQ ID No: 1952, SEQ ID No: 1954, SEQ ID No: 1956, SEQ ID No: 1958, SEQ ID No: 1960, SEQ ID No: 1962, SEQ ID No: 1964, SEQ ID No: 1966, SEQ ID No: 1968, SEQ ID No: 1970, SEQ ID No: 1972, SEQ ID No: 1974, and/or with the complement of the nucleic acid sequence that encodes an amino acid sequence such as the amino acid sequences of Sequences SEQ ID NO: 2, SEQ ID No: 4, SEQ ID No: 6, SEQ ID No: 8, SEQ ID No: 10, SEQ ID No: 12, SEQ ID No: 14, SEQ ID No: 16, SEQ ID No: 18, SEQ ID No: 20, SEQ ID No: 22, SEQ ID No: 24, SEQ ID No: 26, SEQ ID No: 28, SEQ ID No: 30, SEQ ID No: 32, SEQ ID No: 34, SEQ ID No: 36, SEQ ID No: 38, SEQ ID No: 40, SEQ ID No: 42, SEQ ID No: 44, SEQ ID No: 46, SEQ ID No: 48, SEQ ID No: 50, SEQ ID No: 52, SEQ ID No: 54, SEQ ID No: 56, SEQ ID No: 58, SEQ ID No: 60, SEQ ID No: 62, SEQ ID No: 64, SEQ ID No: 66, SEQ ID No: 68, SEQ ID No: 70, SEQ ID No: 72, SEQ ID No: 74, SEQ ID No: 76, SEQ ID No: 78, SEQ ID No: 80, SEQ ID No: 82, SEQ ID No: 84, SEQ ID No: 86, SEQ ID No: 88, SEQ ID No: 90, SEQ ID No: 92, SEQ ID No: 94, SEQ ID No: 96, SEQ ID No: 98, SEQ ID No: 100, SEQ ID No: 102, SEQ ID No: 104, SEQ ID No: 106, SEQ ID No: 108, SEQ ID No: 110, SEQ ID No: 112, SEQ ID No: 114, SEQ ID No: 116, SEQ ID No: 118, SEQ ID No: 120, SEQ ID No: 122, SEQ ID No: 124, SEQ ID No: 126, SEQ ID No: 128, SEQ ID No: 130, SEQ ID No: 132, SEQ ID No: 134, SEQ ID No: 136, SEQ ID No: 138, SEQ ID No: 140, SEQ ID No: 142, SEQ ID No: 144, SEQ ID No: 146, SEQ ID No: 148, SEQ ID No: 150, SEQ ID No: 152, SEQ ID No: 154, SEQ ID No: 156, SEQ ID No: 158, SEQ ID No: 160, SEQ ID No: 162, SEQ ID No: 164, SEQ ID No: 166, SEQ ID No: 168, SEQ ID No: 170, SEQ ID No: 172, SEQ ID No: 174, SEQ ID No: 176, SEQ ID No: 178, SEQ ID No: 180, SEQ ID No: 182, SEQ ID No: 184, SEQ ID No: 186, SEQ ID No: 188, SEQ ID No: 190, SEQ ID No: 192, SEQ ID No: 194, SEQ ID No: 196, SEQ ID No: 198, SEQ ID No: 200, SEQ ID No: 202, SEQ ID No: 204, SEQ ID No: 206, SEQ ID No: 208, SEQ ID No: 210, SEQ ID No: 212, SEQ ID No: 214, SEQ ID No: 216, SEQ ID No: 218, SEQ ID No: 220, SEQ ID No: 222, SEQ ID No: 224, SEQ ID No: 226, SEQ ID No: 228, SEQ ID No: 230, SEQ ID No: 232, SEQ ID No: 234, SEQ ID No: 236, SEQ ID No: 238, SEQ ID No: 240, SEQ ID No: 242, SEQ ID No: 244, SEQ ID No: 246, SEQ ID No: 248, SEQ ID No: 250, SEQ ID No: 252, SEQ ID No: 254, SEQ ID No: 256, SEQ ID No: 258, SEQ ID No: 260, SEQ ID No: 262, SEQ ID No: 264, SEQ ID No: 266, SEQ ID No: 268, SEQ ID No: 270, SEQ ID No: 272, SEQ ID No: 274, SEQ ID No: 276, SEQ ID No: 278, SEQ ID No: 280, SEQ ID No: 282, SEQ ID No: 284, SEQ ID No: 286, SEQ ID No: 288, SEQ ID No: 290, SEQ ID No: 292, SEQ ID No: 294, SEQ ID No: 296, SEQ ID No: 298, SEQ ID No: 300, SEQ ID No: 302, SEQ ID No: 304, SEQ ID No: 306, SEQ ID No: 308, SEQ ID No: 310, SEQ ID No: 312, SEQ ID No: 314, SEQ ID No: 316, SEQ ID No: 318, SEQ ID No: 320, SEQ ID No: 322, SEQ ID No: 324, SEQ ID No: 326, SEQ ID No: 328, SEQ ID No: 330, SEQ ID No: 332, SEQ ID No: 334, SEQ ID No: 336, SEQ ID No: 338, SEQ ID No: 340, SEQ ID No: 342, SEQ ID No: 344, SEQ ID No: 346, SEQ ID No: 348, SEQ ID No: 350, SEQ ID No: 352, SEQ ID No: 354, SEQ ID No: 356, SEQ ID No: 358, SEQ ID No: 360, SEQ ID No: 362, SEQ ID No: 364, SEQ ID No: 366, SEQ ID No: 368, SEQ ID No: 370, SEQ ID No: 372, SEQ ID No: 374, SEQ ID No: 376, SEQ ID No: 378, SEQ ID No: 380, SEQ ID No: 382, SEQ ID No: 384, SEQ ID No: 386, SEQ ID No: 388, SEQ ID No: 390, SEQ ID No: 392, SEQ ID No: 394, SEQ ID No: 396, SEQ ID No: 398, SEQ ID No: 400, SEQ ID No: 402, SEQ ID No: 404, SEQ ID No: 406, SEQ ID No: 408, SEQ ID No: 410, SEQ ID No: 412, SEQ ID No: 414, SEQ ID No: 416, SEQ ID No: 418, SEQ ID No: 420, SEQ ID No: 422, SEQ ID No: 424, SEQ ID No: 426, SEQ ID No: 428, SEQ ID No: 430, SEQ ID No: 432, SEQ ID No: 434, SEQ ID No: 436, SEQ ID No: 438, SEQ ID No: 440, SEQ ID No: 442, SEQ ID No: 444, SEQ ID No: 446, SEQ ID No: 448, SEQ ID No: 450, SEQ ID No: 452, SEQ ID No: 454, SEQ ID No: 456, SEQ ID No: 458, SEQ ID No: 460, SEQ ID No: 462, SEQ ID No: 464, SEQ ID No: 466, SEQ ID No: 468, SEQ ID No: 470, SEQ ID No: 472, SEQ ID No: 474, SEQ ID No: 476, SEQ ID No: 478, SEQ ID No: 480, SEQ ID No: 482, SEQ ID No: 484, SEQ ID No: 486, SEQ ID No: 488, SEQ ID No: 490, SEQ ID No: 492, SEQ ID No: 494, SEQ ID No: 496, SEQ ID No: 498, SEQ ID No: 500, SEQ ID No: 502, SEQ ID No: 504, SEQ ID No: 506, SEQ ID No: 508, SEQ ID No: 510, SEQ ID No: 512, SEQ ID No: 514, SEQ ID No: 516, SEQ ID No: 518, SEQ ID No: 520, SEQ ID No: 522, SEQ ID No: 524, SEQ ID No: 526, SEQ ID No: 528, SEQ ID No: 530, SEQ ID No: 532, SEQ ID No: 534, SEQ ID No: 536, SEQ ID No: 538, SEQ ID No: 540, SEQ ID No: 542, SEQ ID No: 544, SEQ ID No: 546, SEQ ID No: 548, SEQ ID No: 550, SEQ ID No: 552, SEQ ID No: 554, SEQ ID No: 556, SEQ ID No: 558, SEQ ID No: 560, SEQ ID No: 562, SEQ ID No: 564, SEQ ID No: 566, SEQ ID No: 568, SEQ ID No: 570, SEQ ID No: 572, SEQ ID No: 574, SEQ ID No: 576, SEQ ID No: 578, SEQ ID No: 580, SEQ ID No: 582, SEQ ID No: 584, SEQ ID No: 586, SEQ ID No: 588, SEQ ID No: 590, SEQ ID No: 592, SEQ ID No: 594, SEQ ID No: 596, SEQ ID No: 598, SEQ ID No: 600, SEQ ID No: 602, SEQ ID No: 604, SEQ ID No: 606, SEQ ID No: 608, SEQ ID No: 610, SEQ ID No: 612, SEQ ID No: 614, SEQ ID No: 616, SEQ ID No: 618, SEQ ID No: 620, SEQ ID No: 622, SEQ ID No: 624, SEQ ID No: 626, SEQ ID No: 628, SEQ ID No: 630, SEQ ID No: 632, SEQ ID No: 634, SEQ ID No: 636, SEQ ID No: 638, SEQ ID No: 640, SEQ ID No: 642, SEQ ID No: 644, SEQ ID No: 646, SEQ ID No: 648, SEQ ID No: 650, SEQ ID No: 652, SEQ ID No: 654, SEQ ID No: 656, SEQ ID No: 658, SEQ ID No: 660, SEQ ID No: 662, SEQ ID No: 664, SEQ ID No: 666, SEQ ID No: 668, SEQ ID No: 670, SEQ ID No: 672, SEQ ID No: 674, SEQ ID No: 676, SEQ ID No: 678, SEQ ID No: 680, SEQ ID No: 682, SEQ ID No: 684, SEQ ID No: 686, SEQ ID No: 688, SEQ ID No: 690, SEQ ID No: 692, SEQ ID No: 694, SEQ ID No: 696, SEQ ID No: 698, SEQ ID No: 700, SEQ ID No: 702, SEQ ID No: 704, SEQ ID No: 706, SEQ ID No: 708, SEQ ID No: 710, SEQ ID No: 712, SEQ ID No: 714, SEQ ID No: 716, SEQ ID No: 718, SEQ ID No: 720, SEQ ID No: 722, SEQ ID No: 724, SEQ ID No: 726, SEQ ID No: 728, SEQ ID No: 730, SEQ ID No: 732, SEQ ID No: 734, SEQ ID No: 736, SEQ ID No: 738, SEQ ID No: 740, SEQ ID No: 742, SEQ ID No: 744, SEQ ID No: 746, SEQ ID No: 748, SEQ ID No: 750, SEQ ID No: 752, SEQ ID No: 754, SEQ ID No: 756, SEQ ID No: 758, SEQ ID No: 760, SEQ ID No: 762, SEQ ID No: 764, SEQ ID No: 766, SEQ ID No: 768, SEQ ID No: 770, SEQ ID No: 772, SEQ ID No: 774, SEQ ID No: 776, SEQ ID No: 778, SEQ ID No: 780, SEQ ID No: 782, SEQ ID No: 784, SEQ ID No: 786, SEQ ID No: 788, SEQ ID No: 790, SEQ ID No: 792, SEQ ID No: 794, SEQ ID No: 796, SEQ ID No: SEQ ID No: 798, SEQ ID No: 800, SEQ ID No: 802, SEQ ID No: 804, SEQ ID No: 806, SEQ ID No: 808, SEQ ID No: 810, SEQ ID No: 812, SEQ ID No: 814, SEQ ID No: 816, SEQ ID No: 818, SEQ ID No: 820, SEQ ID No: 822, SEQ ID No: 824, SEQ ID No: 826, SEQ ID No: 828, SEQ ID No: 830, SEQ ID No: 832, SEQ ID No: 834, SEQ ID No: 836, SEQ ID No: 838, SEQ ID No: 840, SEQ ID No: 842, SEQ ID No: 844, SEQ ID No: 846, SEQ ID No: 848, SEQ ID No: 850, SEQ ID No: 852, SEQ ID No: 854, SEQ ID No: 856, SEQ ID No: 858, SEQ ID No: 860, SEQ ID No: 862, SEQ ID No: 864, SEQ ID No: 866, SEQ ID No: 868, SEQ ID No: 870, SEQ ID No: 872, SEQ ID No: 874, SEQ ID No: 876, SEQ ID No: 878, SEQ ID No: 880, SEQ ID No: 882, SEQ ID No: 884, SEQ ID No: 886, SEQ ID No: 888, SEQ ID No: 890, SEQ ID No: 892, SEQ ID No: 894, SEQ ID No: 896, SEQ ID No: 898, SEQ ID No: 900, SEQ ID No: 902, SEQ ID No: 904, SEQ ID No: 906, SEQ ID No: 908, SEQ ID No: 910, SEQ ID No: 912, SEQ ID No: 914, SEQ ID No: 916, SEQ ID No: 918, SEQ ID No: 920, SEQ ID No: 922, SEQ ID No: 924, SEQ ID No: 926, SEQ ID No: 928, SEQ ID No: 930, SEQ ID No: 932, SEQ ID No: 934, SEQ ID No: 936, SEQ ID No: 938, SEQ ID No: 940, SEQ ID No: 942, SEQ ID No: 944, SEQ ID No: 946, SEQ ID No: 948, SEQ ID No: 950, SEQ ID No: 952, SEQ ID No: 954, SEQ ID No: 956, SEQ ID No: 958, SEQ ID No: 960, SEQ ID No: 962, SEQ ID No: 964, SEQ ID No: 966, SEQ ID No: 968, SEQ ID No: 970, SEQ ID No: 972, SEQ ID No: 974, SEQ ID No: 976, SEQ ID No: 978, SEQ ID No: 980, SEQ ID No: 982, SEQ ID No: 984, SEQ ID No: 986, SEQ ID No: 988, SEQ ID No: 990, SEQ ID No: 992, SEQ ID No: 994, SEQ ID No: 996, SEQ ID No: 998, SEQ ID No: 1000, SEQ ID No: 1002, SEQ ID No: 1004, SEQ ID No: 1006, SEQ ID No: 1008, SEQ ID No: 1010, SEQ ID No: 1012, SEQ ID No: 1014, SEQ ID No: 1016, SEQ ID No: 1018, SEQ ID No: 1020, SEQ ID No: 1022, SEQ ID No: 1024, SEQ ID No: 1026, SEQ ID No: 1028, SEQ ID No: 1030, SEQ ID No: 1032, SEQ ID No: 1034, SEQ ID No: 1036, SEQ ID No: 1038, SEQ ID No: 1040, SEQ ID No: 1042, SEQ ID No: 1044, SEQ ID No: 1046, SEQ ID No: 1048, SEQ ID No: 1050, SEQ ID No: 1052, SEQ ID No: 1054, SEQ ID No: 1056, SEQ ID No: 1058, SEQ ID No: 1060, SEQ ID No: 1062, SEQ ID No: 1064, SEQ ID No: 1066, SEQ ID No: 1068, SEQ ID No: 1070, SEQ ID No: 1072, SEQ ID No: 1074, SEQ ID No: 1076, SEQ ID No: 1078, SEQ ID No: 1080, SEQ ID No: 1082, SEQ ID No: 1084, SEQ ID No: 1086, SEQ ID No: 1088, SEQ ID No: 1090, SEQ ID No: 1092, SEQ ID No: 1094, SEQ ID No: 1096, SEQ ID No: 1098, SEQ ID NO: 1100, SEQ ID No: 1102, SEQ ID No: 1104, SEQ ID No: 1106, SEQ ID No: 1108, SEQ ID No: 1110, SEQ ID No: 1112, SEQ ID No: 1114, SEQ ID No: 1116, SEQ ID No: 1118, SEQ ID No: 1120, SEQ ID No: 1122, SEQ ID No: 1124, SEQ ID No: 1126, SEQ ID No: 1128, SEQ ID No: 1130, SEQ ID No: 1132, SEQ ID No: 1134, SEQ ID No: 1136, SEQ ID No: 1138, SEQ ID No: 1140, SEQ ID No: 1142, SEQ ID No: 1144, SEQ ID No: 1146, SEQ ID No: 1148, SEQ ID No: 1150, SEQ ID No: 1152, SEQ ID No: 1154, SEQ ID No: 1156, SEQ ID No: 1158, SEQ ID No: 1160, SEQ ID No: 1162, SEQ ID No: 1164, SEQ ID No: 1166, SEQ ID No: 1168, SEQ ID No: 1170, SEQ ID No: 1172, SEQ ID No: 1174, SEQ ID No: 1176, SEQ ID No: 1178, SEQ ID No: 1180, SEQ ID No: 1182, SEQ ID No: 1184, SEQ ID No: 1186, SEQ ID No: 1188, SEQ ID No: 1190, SEQ ID No: 1192, SEQ ID No: 1194, SEQ ID No: 1196, SEQ ID No: 1198, SEQ ID No: 1200, SEQ ID No: 1202, SEQ ID No: 1204, SEQ ID No: 1206, SEQ ID No: 1208, SEQ ID No: 1210, SEQ ID No: 1212, SEQ ID No: 1214, SEQ ID No: 1216, SEQ ID No: 1218, SEQ ID No: 1220, SEQ ID No: 1222, SEQ ID No: 1224, SEQ ID No: 1226, SEQ ID No: 1228, SEQ ID No: 1230, SEQ ID No: 1232, SEQ ID No: 1234, SEQ ID No: 1236, SEQ ID No: 1238, SEQ ID No: 1240, SEQ ID No: 1242, SEQ ID No: 1244, SEQ ID No: 1246, SEQ ID No: 1248, SEQ ID No: 1250, SEQ ID No: 1252, SEQ ID No: 1254, SEQ ID No: 1256, SEQ ID No: 1258, SEQ ID No: 1260, SEQ ID No: 1262, SEQ ID No: 1264, SEQ ID No: 1266, SEQ ID No: 1268, SEQ ID No: 1270, SEQ ID No: 1272, SEQ ID No: 1274, SEQ ID No: 1276, SEQ ID No: 1278, SEQ ID No: 1280, SEQ ID No: 1282, SEQ ID No: 1284, SEQ ID No: 1286, SEQ ID No: 1288, SEQ ID No: 1290, SEQ ID No: 1292, SEQ ID No: 1294, SEQ ID No: 1296, SEQ ID No: 1298, SEQ ID No: 1300, SEQ ID No: 1302, SEQ ID No: 1304, SEQ ID No: 1306, SEQ ID No: 1308, SEQ ID No: 1310, SEQ ID No: 1312, SEQ ID No: 1314, SEQ ID No: 1316, SEQ ID No: 1318, SEQ ID No: 1320, SEQ ID No: 1322, SEQ ID No: 1324, SEQ ID No: 1326, SEQ ID No: 1328, SEQ ID No: 1330, SEQ ID No: 1332, SEQ ID No: 1334, SEQ ID No: 1336, SEQ ID No: 1338, SEQ ID No: 1340, SEQ ID No: 1342, SEQ ID No: 1344, SEQ ID No: 1346, SEQ ID No: 1348, SEQ ID No: 1350, SEQ ID No: 1352, SEQ ID No: 1354, SEQ ID No: 1356, SEQ ID No: 1358, SEQ ID No: 1360, SEQ ID No: 1362, SEQ ID No: 1364, SEQ ID No: 1366, SEQ ID No: 1368, SEQ ID No: 1370, SEQ ID No: 1372, SEQ ID No: 1374, SEQ ID No: 1376, SEQ ID No: 1378, SEQ ID No: 1380, SEQ ID No: 1382, SEQ ID No: 1384, SEQ ID No: 1386, SEQ ID No: 1388, SEQ ID No: 1390, SEQ ID No: 1392, SEQ ID No: 1394, SEQ ID No: 1396, SEQ ID No: 1398, SEQ ID No: 1400, SEQ ID No: 1402, SEQ ID No: 1404, SEQ ID No: 1406, SEQ ID No: 1408, SEQ ID No: 1410, SEQ ID No: 1412, SEQ ID No: 1414, SEQ ID No: 1416, SEQ ID No: 1418, SEQ ID No: 1420, SEQ ID No: 1422, SEQ ID No: 1424, SEQ ID No: 1426, SEQ ID No: 1428, SEQ ID No: 1430, SEQ ID No: 1432, SEQ ID No: 1434, SEQ ID No: 1436, SEQ ID No: 1438, SEQ ID No: 1440, SEQ ID No: 1442, SEQ ID No: 1444, SEQ ID No: 1446, SEQ ID No: 1448, SEQ ID No: 1450, SEQ ID No: 1452, SEQ ID No: 1454, SEQ ID No: 1456, SEQ ID No: 1458, SEQ ID No: 1460, SEQ ID No: 1462, SEQ ID No: 1464, SEQ ID No: 1466, SEQ ID No: 1468, SEQ ID No: 1470, SEQ ID No: 1472, SEQ ID No: 1474, SEQ ID No: 1476, SEQ ID No: 1478, SEQ ID No: 1480, SEQ ID No: 1482, SEQ ID No: 1484, SEQ ID No: 1486, SEQ ID No: 1488, SEQ ID No: 1490, SEQ ID No: 1492, SEQ ID No: 1494, SEQ ID No: 1496, SEQ ID No: 1498, SEQ ID No: 1500, SEQ ID No: 1502, SEQ ID No: 1504, SEQ ID No: 1506, SEQ ID No: 1508, SEQ ID No: 1510, SEQ ID No: 1512, SEQ ID No: 1514, SEQ ID No: 1516, SEQ ID No: 1518, SEQ ID No: 1520, SEQ ID No: 1522, SEQ ID No: 1524, SEQ ID No: 1526, SEQ ID No: 1528, SEQ ID No: 1530, SEQ ID No: 1532, SEQ ID No: 1534, SEQ ID No: 1536, SEQ ID No: 1538, SEQ ID No: 1540, SEQ ID No: 1542, SEQ ID No: 1544, SEQ ID No: 1546, SEQ ID No: 1548, SEQ ID No: 1550, SEQ ID No: 1552, SEQ ID No: 1554, SEQ ID No: 1556, SEQ ID No: 1558, SEQ ID No: 1560, SEQ ID No: 1562, SEQ ID No: 1564, SEQ ID No: 1566, SEQ ID No: 1568, SEQ ID No: 1570, SEQ ID No: 1572, SEQ ID No: 1574, SEQ ID No: 1576, SEQ ID No: 1578, SEQ ID No: 1580, SEQ ID No: 1582, SEQ ID No: 1584, SEQ ID No: 1586, SEQ ID No: 1588, SEQ ID No: 1590, SEQ ID No: 1592, SEQ ID No: 1594, SEQ ID No: 1596, SEQ ID No: 1598, SEQ ID No: 1600, SEQ ID No: 1602, SEQ ID No: 1604, SEQ ID No: 1606, SEQ ID No: 1608, SEQ ID No: 1610, SEQ ID No: 1612, SEQ ID No: 1614, SEQ ID No: 1616, SEQ ID No: 1618, SEQ ID No: 1620, SEQ ID No: 1622, SEQ ID No: 1624, SEQ ID No: 1626, SEQ ID No: 1628, SEQ ID No: 1630, SEQ ID No: 1632, SEQ ID No: 1634, SEQ ID No: 1636, SEQ ID No: 1638, SEQ ID No: 1640, SEQ ID No: 1642, SEQ ID No: 1644, SEQ ID No: 1646, SEQ ID No: 1648, SEQ ID No: 1650, SEQ ID No: 1652, SEQ ID No: 1654, SEQ ID No: 1656, SEQ ID No: 1658, SEQ ID No: 1660, SEQ ID No: 1662, SEQ ID No: 1664, SEQ ID No: 1666, SEQ ID No: 1668, SEQ ID No: 1670, SEQ ID No: 1672, SEQ ID No: 1674, SEQ ID No: 1676, SEQ ID No: 1678, SEQ ID No: 1680, SEQ ID No: 1682, SEQ ID No: 1684, SEQ ID No: 1686, SEQ ID No: 1688, SEQ ID No: 1690, SEQ ID No: 1692, SEQ ID No: 1694, SEQ ID No: 1696, SEQ ID No: 1698, SEQ ID No: 1700, SEQ ID No: 1702, SEQ ID No: 1704, SEQ ID No: 1706, SEQ ID No: 1708, SEQ ID No: 1710, SEQ ID No: 1712, SEQ ID No: 1714, SEQ ID No: 1716, SEQ ID No: 1718, SEQ ID No: 1720, SEQ ID No: 1722, SEQ ID No: 1724, SEQ ID No: 1726, SEQ ID No: 1728, SEQ ID No: 1730, SEQ ID No: 1732, SEQ ID No: 1734, SEQ ID No: 1736, SEQ ID No: 1738, SEQ ID No: 1740, SEQ ID No: 1742, SEQ ID No: 1744, SEQ ID No: 1746, SEQ ID No: 1748, SEQ ID No: 1750, SEQ ID No: 1752, SEQ ID No: 1754, SEQ ID No: 1756, SEQ ID No: 1758, SEQ ID No: 1760, SEQ ID No: 1762, SEQ ID No: 1764, SEQ ID No: 1766, SEQ ID No: 1768, SEQ ID No: 1770, SEQ ID No: 1772, SEQ ID No: 1774, SEQ ID No: 1776, SEQ ID No: 1778, SEQ ID No: 1780, SEQ ID No: 1782, SEQ ID No: 1784, SEQ ID No: 1786, SEQ ID No: 1788, SEQ ID No: 1790, SEQ ID No: 1792, SEQ ID No: 1794, SEQ ID No: 1796, SEQ ID No: 1798, SEQ ID No: 1800, SEQ ID No: 1802, SEQ ID No: 1804, SEQ ID No: 1806, SEQ ID No: 1808, SEQ ID No: 1810, SEQ ID No: 1812, SEQ ID No: 1814, SEQ ID No: 1816, SEQ ID No: 1818, SEQ ID No: 1820, SEQ ID No: 1822, SEQ ID No: 1824, SEQ ID No: 1826, SEQ ID No: 1828, SEQ ID No: 1830, SEQ ID No: 1832, SEQ ID No: 1834, SEQ ID No: 1836, SEQ ID No: 1838, SEQ ID No: 1840, SEQ ID No: 1842, SEQ ID No: 1844, SEQ ID No: 1846, SEQ ID No: 1848, SEQ ID No: 1850, SEQ ID No: 1852, SEQ ID No: 1854, SEQ ID No: 1856, SEQ ID No: 1858, SEQ ID No: 1860, SEQ ID No: 1862, SEQ ID No: 1864, SEQ ID No: 1866, SEQ ID No: 1868, SEQ ID No: 1870, SEQ ID No: 1872, SEQ ID No: 1874, SEQ ID No: 1876, SEQ ID No: 1878, SEQ ID No: 1880, SEQ ID No: 1882, SEQ ID No: 1884, SEQ ID No: 1886, SEQ ID No: 1888, SEQ ID No: 1890, SEQ ID No: 1892, SEQ ID No: 1894, SEQ ID No: 1896, SEQ ID No: 1898, SEQ ID No: 1900, SEQ ID No: 1902, SEQ ID No: 1904, SEQ ID No: 1906, SEQ ID No: 1908, SEQ ID No: 1910, SEQ ID No: 1912, SEQ ID No: 1914, SEQ ID No: 1916, SEQ ID No: 1918, SEQ ID No: 1920, SEQ ID No: 1922, SEQ ID No: 1924, SEQ ID No: 1926, SEQ ID No: 1928, SEQ ID No: 1930, SEQ ID No: 1932, SEQ ID No: 1934, SEQ ID No: 1936, SEQ ID No: 1938, SEQ ID No: 1940, SEQ ID No: 1942, SEQ ID No: 1944, SEQ ID No: 1946, SEQ ID No: 1948, SEQ ID No: 1950, SEQ ID No: 1952, SEQ ID No: 1954, SEQ ID No: 1956, SEQ ID No: 1958, SEQ ID No: 1960, SEQ ID No: 1962, SEQ ID No: 1964, SEQ ID No: 1966, SEQ ID No: 1968, SEQ ID No: 1970, SEQ ID No: 1972, SEQ ID No: 1974. Methods to deduce a complementary sequence are known to those skilled in the art. It should be noted that since nucleic acid sequencing technologies are not entirely error-free, the sequences presented herein, at best, represent apparent sequences of the proteins of the present invention.
[01111] As used herein, reference to hybridization conditions refers to standard hybridization conditions under which nucleic acid molecules are used to identify similar nucleic acid molecules. Such standard conditions are disclosed, for example, in Sambrook et al, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Labs Press, 1989. Sambrook et al, ibid., (see specifically, pages 9.31-9.62). In addition, formulae to calculate the appropriate hybridization and wash conditions to achieve hybridization permitting varying degrees of mismatch of nucleotides are disclosed, for example, in Meinkoth et al, 1984, Anal. Biochem. 138, 267-284; Meinkoth et al, ibid.
[01112] More particularly, moderate stringency hybridization and washing conditions, as referred to herein, refer to conditions which permit isolation of nucleic acid molecules having at least about 70% nucleic acid sequence identity with the nucleic acid molecule being used to probe in the hybridization reaction (i.e., conditions permitting about 30% or less mismatch of nucleotides). High stringency hybridization and washing conditions, as referred to herein, refer to conditions which permit isolation of nucleic acid molecules having at least about 80% nucleic acid sequence identity with the nucleic acid molecule being used to probe in the hybridization reaction (i.e., conditions permitting about 20% or less mismatch of nucleotides). Very high stringency hybridization and washing conditions, as referred to herein, refer to conditions which permit isolation of nucleic acid molecules having at least about 90%> nucleic acid sequence identity with the nucleic acid molecule being used to probe in the hybridization reaction (i.e., conditions permitting about 10%> or less mismatch of nucleotides). As discussed above, one of skill in the art can use the formulae in Meinkoth et al, ibid, to calculate the appropriate hybridization and wash conditions to achieve these particular levels of nucleotide mismatch. Such conditions will vary, depending on whether DNA:R A or DNA:DNA hybrids are being formed. Calculated melting temperatures for DNA:DNA hybrids are 10°C less than for DNA:R A hybrids. In particular embodiments, stringent hybridization conditions for DNA:DNA hybrids include hybridization at an ionic strength of 6X SSC (0.9 M Na ) at a temperature of between about 20°C and about 35°C (lower stringency), more preferably, between about 28°C and about 40°C (more stringent), and even more preferably, between about 35°C and about 45°C (even more stringent), with appropriate wash conditions. In particular embodiments, stringent hybridization conditions for DNA:R A hybrids include hybridization at an ionic strength of 6X SSC (0.9 M Na+) at a temperature of between about 30°C and about 45°C, more preferably, between about 38°C and about 50°C, and even more preferably, between about 45°C and about 55°C, with similarly stringent wash conditions. These values are based on calculations of a melting temperature for molecules larger than about 100 nucleotides, 0% formamide and a G + C content of about 40%. Alternatively, Tm can be calculated empirically as set forth in Sambrook et al, supra, pages 9.31 to 9.62. In general, the wash conditions should be as stringent as possible, and should be appropriate for the chosen hybridization conditions. For example, hybridization conditions can include a combination of salt and temperature conditions that are approximately 20-25°C below the calculated Tm of a particular hybrid, and wash conditions typically include a combination of salt and temperature conditions that are approximately 12-20°C below the calculated Tm of the particular hybrid. One example of hybridization conditions suitable for use with DNA:DNA hybrids includes a 2-24 hour hybridization in 6X SSC (50% formamide) at about 42°C, followed by washing steps that include one or more washes at room temperature in about 2X SSC, followed by additional washes at higher temperatures and lower ionic strength (e.g., at least one wash as about 37°C in about 0.1X-0.5X SSC, followed by at least one wash at about 68°C in about 0.1X-0.5X SSC).
] The minimum size of a protein and/or homologue or variant of the present invention is a size sufficient to have biological activity or, when the protein is not required to have such activity, sufficient to be useful for another purpose associated with a protein of the present invention, such as for the production of antibodies that bind to a naturally occurring protein. In one embodiment, the protein of the present invention is at least 20 amino acids in length, or at least about 25 amino acids in length, or at least about 30 amino acids in length, or at least about 40 amino acids in length, or at least about 50 amino acids in length, or at least about 60 amino acids in length, or at least about 70 amino acids in length, or at least about 80 amino acids in length, or at least about 90 amino acids in length, or at least about 100 amino acids in length, or at least about 125 amino acids in length, or at least about 150 amino acids in length, or at least about 175 amino acids in length, or at least about 200 amino acids in length, or at least about 250 amino acids in length, and so on up to a full length of each protein, and including any size in between in increments of one whole integer (one amino acid). There is no limit, other than a practical limit, on the maximum size of such a protein in that the protein can include a portion of a protein or a full-length protein, plus additional sequence (e.g., a fusion protein sequence), if desired.
[01114] The present invention also includes a fusion protein that includes a domain of a protein of the present invention (including a homologue or variant) attached to one or more fusion segments, which are typically heterologous in sequence to the protein sequence (i.e., different than protein sequence). Suitable fusion segments for use with the present invention include, but are not limited to, segments that can: enhance a protein's stability; provide other desirable biological activity; and/or assist with the purification of the protein (e.g., by affinity chromatography). A suitable fusion segment can be a domain of any size that has the desired function (e.g., imparts increased stability, solubility, action or biological activity; and/or simplifies purification of a protein). Fusion segments can be joined to amino and/or carboxyl teirnini of the domain of a protein of the present invention and can be susceptible to cleavage in order to enable straight-forward recovery of the protein. Fusion proteins are preferably produced by culturing a recombinant cell transfected with a fusion nucleic acid molecule that encodes a protein including the fusion segment attached to either the carboxyl and/or amino temiinal end of a domain of a protein of the present invention. Accordingly, proteins of the present invention also include expression products of gene fusions (for example, used to overexpress soluble, active forms of the recombinant protein), of mutagenized genes (such as genes having codon modifications to enhance gene transcription and translation), and of truncated genes (such as genes having membrane binding modules removed to generate soluble forms of a membrane protein, or genes having signal sequences removed which are poorly tolerated in a particular recombinant host).
[01115] In one embodiment of the present invention, any of the amino acid sequences described herein can be produced with from at least one, and up to about 20, additional heterologous amino acids flanking each of the C- and/or N-terminal ends of the specified amino acid sequence. The resulting protein or polypeptide can be referred to as "consisting essentially of the specified amino acid sequence. According to the present invention, the heterologous amino acids are a sequence of amino acids that are not naturally found (i.e., not found in nature, in vivo) flanking the specified amino acid sequence, or that are not related to the function of the specified amino acid sequence, or that would not be encoded by the nucleotides that flank the naturally occurring nucleic acid sequence encoding the specified amino acid sequence as it occurs in the gene, if such nucleotides in the naturally occurring sequence were translated using standard codon usage for the organism from which the given amino acid sequence is derived.
[01116] The present invention also provides enzyme combinations that break down or modify lignin material, reducing or preventing unwanted adsorption of other components of multi-enzyme compositions applied Such enzyme combinations or mixtures can include a multi-enzyme composition that contains at least one protein of the present invention in combination with one or more additional proteins of the present invention or one or more enzymes or other proteins from other microorganisms, plants, or similar organisms. Synergistic enzyme combinations and related methods are contemplated. The invention includes methods to identify the optimum ratios and compositions of enzymes with which to degrade each lignin and lignocellulosic material. These methods entail tests to identify the optimum enzyme composition and ratios for efficient conversion of any biomass substrate to its constituent sugars. The Examples below include assays that may be used to identify optimum ratios and compositions of enzymes with which to degrade lignocellulosic materials.
[01117] Any combination of the proteins disclosed herein is suitable for use in the multi-enzyme compositions of the present invention. It is to be understood that any of the enzymes described specifically herein can be combined with any one or more of the enzymes described herein or with any other available and suitable enzymes, to produce a multi-enzyme composition. The invention is not restricted or limited to the specific exemplary combinations listed below.
[01118] One or more components of a multi-enzyme composition (other than proteins of the present invention) can be obtained from or derived from a microbial, plant, or other source or combination thereof, and will contain enzymes capable of performing oxidation-reduction reactions. Examples of enzymes included in the multi-enzyme compositions of the invention include oxidases, oxygenases, monoxygenases, Baeyer-Villiger monooxygenases, dioxygenases, peroxidases, dehydrogenases, reductases that catalyze an oxidation-reduction reaction
[01119] The multi-enzyme compositions of the invention can also include cellulases, hemicellulases (such as xylanases, including endoxylanases, exoxylanases, and β- xylosidases; mannanases, including endomannanases, exomannanases, and β- mannosidases), ligninases, amylases, glucuronidases, proteases, esterases (including ferulic acid esterase), lipases, glucosidases (such as β-glucosidase), and xyloglucanases.
[01120] While the multi-enzyme composition may contain many types of enzymes, mixtures comprising enzymes that increase or enhance sugar release from biomass are contemplated, which may include hemicellulases. In one embodiment, the hemicellulase is selected from a xylanase, an arabinofuranosidase, an acetyl xylan esterase, a glucuronidase, an endo-galactanase, a mannanase, an endo-arabinase, an exo-arabinase, an exo-galactanase, a ferulic acid esterase, a galactomannanase, a xyloglucanase, or mixtures of any of these. In particular, the enzymes can include glucoamylase, β-xylosidase and/or β-glucosidase. Also preferred are mixtures comprising enzymes that are capable of degrading cell walls and releasing cellular contents.
[01121] The enzymes of the multi-enzyme composition can be provided by a variety of sources. In one embodiment, the enzymes can be produced by growing organisms such as bacteria, algae, fungi, and plants which produce the enzymes naturally or by virtue of being genetically modified to express the enzyme or enzymes. In another embodiment, at least one enzyme of the multi-enzyme composition is a commercially available enzyme.
[01122] In some embodiments, the multi-enzyme compositions comprise an accessory enzyme. An accessory enzyme can have the same or similar function or a different function as an enzyme or enzymes in the core set of enzymes. These enzymes have been described elsewhere herein, and can generally include cellulases, xylanases, ligninases, amylases, lipidases, or glucuronidases, for example. For example, some accessory enzymes can include enzymes that when contacted with biomass in a reaction, allow for an increase in the activity of enzymes (e.g. , hemicellulases) in the multi-enzyme composition. An accessory enzyme or enzyme mix may be composed of enzymes from (1) commercial suppliers; (2) cloned genes expressing enzymes; (3) complex broth (such as that resulting from growth of a microbial strain in media, wherein the strains secrete proteins and enzymes into the media); (4) cell lysates of strains grown as in (3); and, (5) plant material expressing enzymes capable of degrading ligno cellulose. In some embodiments, the accessory enzyme is a glucoamylase, a pectinase, or a ligninase.
[01 123] As used herein, a ligninase is an enzyme that can hydrolyze or break down the structure of lignin polymers, including lignin peroxidases, manganese peroxidases, laccases, and other enzymes described in the art known to depolymerize or otherwise break lignin polymers. Also included are enzymes capable of hydrolyzing bonds formed between hemicellulosic sugars (notably arabinose) and lignin.
[01 124] The multi-enzyme compositions, in some embodiments, comprise a biomass comprising microorganisms or a crude fermentation product of microorganisms. A crude fermentation product refers to the fermentation broth which has been separated from the microorganism biomass (by filtration, for example). In general, the microorganisms are grown in fermentors, optionally centrifuged or filtered to remove biomass, and optionally concentrated, formulated, and dried to produce an enzyme(s) or a multi-enzyme composition that is a crude fermentation product. In other embodiments, enzyme(s) or multi-enzyme compositions produced by the microorganism (including a genetically modified microorganism as described below) are subjected to one or more purification steps, such as ammonium sulfate precipitation, chromatography, and/or ultrafiltration, which result in a partially purified or purified enzyme(s). If the microorganism has been genetically modified to express the enzyme(s), the enzyme(s) will include recombinant enzymes. If the genetically modified microorganism also naturally expresses the enzyme(s) or other enzymes useful for ligno cellulo sic saccharification or any other useful application mentioned herein, the enzyme(s) may include both naturally occurring and recombinant enzymes.
[01 125] Another embodiment of the present invention relates to a composition comprising at least about 500 ng, and preferably at least about 1 μg, and more preferably at least about 5 μg, and more preferably at least about 10 μg, and more preferably at least about 25 μg, and more preferably at least about 50 μg, and more preferably at least about 75 μg, and more preferably at least about 100 μg, and more preferably at least about 250 μg, and more preferably at least about 500 μg, and more preferably at least about 750 μg, and more preferably at least about 1 mg, and more preferably at least about 5 mg, of an isolated protein comprising any of the proteins or homologues, variants, or fragments thereof discussed herein. Such a composition of the present invention may include any carrier with which the protein is associated by virtue of the protein preparation method, a protein purification method, or a preparation of the protein for use in any method according to the present invention. For example, such a carrier can include any suitable buffer, extract, or medium that is suitable for combining with the protein of the present invention so that the protein can be used in any method described herein according to the present invention.
[01126] In one embodiment of the invention, one or more enzymes of the invention is bound to a solid support, i.e., an immobilized enzyme. As used herein, an immobilized enzyme includes immobilized isolated enzymes, immobilized microbial cells which contain one or more enzymes of the invention, other stabilized intact cells that produce one or more enzymes of the invention, and stabilized cell/membrane homogenates. Stabilized intact cells and stabilized cell/membrane homogenates include cells and homogenates from naturally occurring microorganisms expressing the enzymes of the invention and preferably, from genetically modified microorganisms as disclosed elsewhere herein. Thus, although methods for immobilizing enzymes are discussed below, it will be appreciated that such methods are equally applicable to immobilizing microbial cells and in such an embodiment, the cells can be lysed, if desired.
[01127] A variety of methods for immobilizing an enzyme are disclosed in Industrial
Enzymology 2nd Ed., Godfrey, T. and West, S. Eds., Stockton Press, New York, N.Y., 1996, pp. 267-272; Immobilized Enzymes, Chibata, I. Ed., Halsted Press, New York, N.Y., 1978; Enzymes and Immobilized Cells in Biotechnology, Laskin, A. Ed., BenjamiiVCummings Publishing Co., Inc., Menlo Park, California, 1985; and Applied Biochemistry and Bioengineering, Vol. 4, Chibata, I. and Wingard, Jr., L. Eds, Academic Press, New York, N.Y., 1983. [01 128] Further embodiments of the present invention include nucleic acid molecules that encode a protein of the present invention, as well as homologues, variants, or fragments of such nucleic acid molecules. A nucleic acid molecule of the present invention includes a nucleic acid molecule comprising, consisting essentially of, or consisting of, a nucleic acid sequence encoding any of the isolated proteins disclosed herein, including a fragment or a homologue or variant of such proteins, described above. Nucleic acid molecules can include a nucleic acid sequence that encodes a fragment of a protein that does not have biological activity, and can also include portions of a gene or polynucleotide encoding the protein that are not part of the coding region for the protein (e.g., introns or regulatory regions of a gene encoding the protein). Nucleic acid molecules can include a nucleic acid sequence that is useful as a probe or primer (oligonucleotide sequences).
[01 129] In one embodiment, a nucleic acid molecule of the present invention includes a nucleic acid molecule comprising, consisting essentially of, or consisting of, a nucleic acid sequence represented in SEQ ID No: 1 , SEQ ID No: 3, SEQ ID No: 5, SEQ ID No: 7, SEQ ID No: 9, SEQ ID No: 1 1 , SEQ ID No: 13, SEQ ID No: 15, SEQ ID No: 17, SEQ ID No: 19, SEQ ID No: 21 , SEQ ID No: 23, SEQ ID No: 25, SEQ ID No: 27, SEQ ID No: 29, SEQ ID No: 31 , SEQ ID No: 33, SEQ ID No: 35, SEQ ID No: 37, SEQ ID No: 39, SEQ ID No: 41 , SEQ ID No: 43, SEQ ID No: 45, SEQ ID No: 47, SEQ ID No: 49, SEQ ID No: 51 , SEQ ID No: 53, SEQ ID No: 55, SEQ ID No: 56, SEQ ID No: 57, SEQ ID No: 59, SEQ ID No: 61 , SEQ ID No: 63, SEQ ID No: 65, SEQ ID No: 67, SEQ ID No: 69, SEQ ID No: 71 , SEQ ID No: 73, SEQ ID No: 75, SEQ ID No: 77, SEQ ID No: 79, SEQ ID No: 81 , SEQ ID No: 83, SEQ ID No: 85, SEQ ID No: 87, SEQ ID No: 89, SEQ ID No: 91 , SEQ ID No: 93, SEQ ID No: 95, SEQ ID No: 97, SEQ ID No: 99, SEQ ID No: 101 , SEQ ID No: 103, SEQ ID No: 105, SEQ ID No: 107, SEQ ID No: 109, SEQ ID No: 1 1 1 , SEQ ID No: 1 13, SEQ ID No: 1 15, SEQ ID No: 1 17, SEQ ID No: 1 19, SEQ ID No: 121 , SEQ ID No: 123, SEQ ID No: 125, SEQ ID No: 127, SEQ ID No: 129, SEQ ID No: 131 , SEQ ID No: 133, SEQ ID No: 135, SEQ ID No: 137, SEQ ID No: 139, SEQ ID No: 141 , SEQ ID No: 143, SEQ ID No: 145, SEQ ID No: 147, SEQ ID No: 149, SEQ ID No: 151 , SEQ ID No: 153, SEQ ID No: 155, SEQ ID No: 157, SEQ ID No: 159, SEQ ID No: 161 , SEQ ID No: 163, SEQ ID No: 165, SEQ ID No: 167, SEQ ID No: 169, SEQ ID No: 171, SEQ ID No: 173, SEQ ID No: 175, SEQ ID No: 177, SEQ ID No: 179, SEQ ID No: 181 , SEQ ID No: 183, SEQ ID No: 185, SEQ ID No: 187, SEQ ID No: 189, SEQ ID No: 191, SEQ ID No: 193, SEQ ID No: 195, SEQ ID No: 197, SEQ ID No: 199 , SEQ ID No: 201, SEQ ID No: 203, SEQ ID No: 205, SEQ ID No: 207, SEQ ID No: 209, SEQ ID No: 211, SEQ ID No: 213, SEQ ID No: 215, SEQ ID No: 217 , SEQ ID No: 219, SEQ ID No: 221, SEQ ID No: 223, SEQ ID No: 225, SEQ ID No: 227, SEQ ID No: 229, SEQ ID No: 231, SEQ ID No: 233, SEQ ID No: 235. SEQ ID No: 237, SEQ ID No: 239, SEQ ID No: 241, SEQ ID No: 243, SEQ ID No: 245, SEQ ID No: 247, SEQ ID No: 249, SEQ ID No: 251, SEQ ID No: 253 , SEQ ID No: 255, SEQ ID No: 257, SEQ ID No: 259, SEQ ID No: 261, SEQ ID No: 263, SEQ ID No: 265, SEQ ID No: 267, SEQ ID No: 269, SEQ ID No: 271 , SEQ ID No: 273, SEQ ID No: 275, SEQ ID No: 277, SEQ ID No: 279, SEQ ID No: 281, SEQ ID No: 283, SEQ ID No: 285, SEQ ID No: 287, SEQ ID No: 289 , SEQ ID No: 291, SEQ ID No: 293, SEQ ID No: 295, SEQ ID No: 297, SEQ ID No: 299, SEQ ID No: 301, SEQ ID No: 303, SEQ ID No: 305, SEQ ID No: 307 , SEQ ID No: 309, SEQ ID No: 311, SEQ ID No: 313, SEQ ID No: 315, SEQ ID No: 317, SEQ ID No: 319, SEQ ID No: 321, SEQ ID No: 323, SEQ ID No: 325 , SEQ ID No: 327, SEQ ID No: 329, SEQ ID No: 331, SEQ ID No: 333, SEQ ID No: 335, SEQ ID No: 337, SEQ ID No: 339, SEQ ID No: 341, SEQ ID No: 343 , SEQ ID No: 345, SEQ ID No: 347, SEQ ID No: 349, SEQ ID No: 351, SEQ ID No: 353, SEQ ID No: 355, SEQ ID No: 357, SEQ ID No: 359, SEQ ID No: 361 , SEQ ID No: 363, SEQ ID No: 365, SEQ ID No: 367, SEQ ID No: 369, SEQ ID No: 371, SEQ ID No: 373, SEQ ID No: 375, SEQ ID No: 377, SEQ ID No: 379 , SEQ ID No: 381, SEQ ID No: 383, SEQ ID No: 385, SEQ ID No: 387, SEQ ID No: 389, SEQ ID No: 391, SEQ ID No: 393, SEQ ID No: 395, SEQ ID No: 397 , SEQ ID No: 399, SEQ ID No: 401, SEQ ID No: 403, SEQ ID No: 405, SEQ ID No: 407, SEQ ID No: 409, SEQ ID No: 411, SEQ ID No: 413, SEQ ID No: 415 , SEQ ID No: 417, SEQ ID No: 419, SEQ ID No: 421, SEQ ID No: 423, SEQ ID No: 425, SEQ ID No: 427, SEQ ID No: 429, SEQ ID No: 431, SEQ ID No: 433 , SEQ ID No: 435, SEQ ID No: 437, SEQ ID No: 439, SEQ ID No: 441, SEQ ID No: 443, SEQ ID No: 445, SEQ ID No: 447, SEQ ID No: 449, SEQ ID No: 451 , SEQ ID No: 453, SEQ ID No: 455, SEQ ID No: 457, SEQ ID No: 459, SEQ ID No: 461, SEQ ID No: 463, SEQ ID No: 465, SEQ ID No: 467, SEQ ID No: 469, SEQ ID No: 471, SEQ ID No: 473, SEQ ID No: 475, SEQ ID No: 477, SEQ ID No: 479, SEQ ID No: 481, SEQ ID No: 483, SEQ ID No: 485, SEQ ID No: 487, SEQ ID No: 489, SEQ ID No: 491, SEQ ID No: 493, SEQ ID No: 495, SEQ ID No: 497, SEQ ID No: 499, SEQ ID No: 501, SEQ ID No: 503, SEQ ID No: 505, SEQ ID No: 507, SEQ ID No: 509, SEQ ID No: 511, SEQ ID No: 513, SEQ ID No: 515, SEQ ID No: 517, SEQ ID No: 519, SEQ ID No: 521, SEQ ID No: 523, SEQ ID No: 525, SEQ ID No: 527, SEQ ID No: 529, SEQ ID No: 531, SEQ ID No: 533, SEQ ID No: 535, SEQ ID No: 537, SEQ ID No: 539, SEQ ID No: 541, SEQ ID No: 543, SEQ ID No: 545, SEQ ID No: 547, SEQ ID No: 549, SEQ ID No: 551, SEQ ID No: 553, SEQ ID No: 555, SEQ ID No: 557, SEQ ID No: 559, SEQ ID No: 561, SEQ ID No: 563, SEQ ID No: 565, SEQ ID No: 567, SEQ ID No: 569, SEQ ID No: 571, SEQ ID No: 573, SEQ ID No: 575, SEQ ID No: 577, SEQ ID No: 579, SEQ ID No: 581, SEQ ID No: 583, SEQ ID No: 585, SEQ ID No: 587, SEQ ID No: 589, SEQ ID No: 591, SEQ ID No: 593, SEQ ID No: 595, SEQ ID No: 597, SEQ ID No: 599, SEQ ID No: 601, SEQ ID No: 603, SEQ ID No: 605, SEQ ID No: 607, SEQ ID No: 609, SEQ ID No: 611, SEQ ID No: 613, SEQ ID No: 615, SEQ ID No: 617, SEQ ID No: 619, SEQ ID No: 621, SEQ ID No: 623, SEQ ID No: 625, SEQ ID No: 627, SEQ ID No: 629, SEQ ID No: 631, SEQ ID No: 633, SEQ ID No: 635, SEQ ID No: 637, SEQ ID No: 639, SEQ ID No: 641, SEQ ID No: 643, SEQ ID No: 645, SEQ ID No: 647, SEQ ID No: 649, SEQ ID No: 651, SEQ ID No: 653, SEQ ID No: 655, SEQ ID No: 657, SEQ ID No: 659, SEQ ID No: 661, SEQ ID No: 663, SEQ ID No: 665, SEQ ID No: 667, SEQ ID No: 669, SEQ ID No: 671, SEQ ID No: 673, SEQ ID No: 675, SEQ ID No: 677, SEQ ID No: 679, SEQ ID No: 681, SEQ ID No: 683, SEQ ID No: 685, SEQ ID No: 687, SEQ ID No: 689, SEQ ID No: 691, SEQ ID No: 693, SEQ ID No: 695, SEQ ID No: 697, SEQ ID No: 699, SEQ ID No: 701, SEQ ID No: 703, SEQ ID No: 705, SEQ ID No: 707, SEQ ID No: 709, SEQ ID No: 711, SEQ ID No: 713, SEQ ID No: 715, SEQ ID No: 717, SEQ ID No: 719, SEQ ID No: 721, SEQ ID No: 723, SEQ ID No: 725, SEQ ID No: 727, SEQ ID No: 729, SEQ ID No: 731, SEQ ID No: 733, SEQ ID No: 735, SEQ ID No: 737, SEQ ID No: 739, SEQ ID No: 741, SEQ ID No: 743, SEQ ID No: 745, SEQ ID No: 747, SEQ ID No: 749, SEQ ID No: 751, SEQ ID No: 753, SEQ ID No: 755, SEQ ID No: 757, SEQ ID No: 759, SEQ ID No: 761, SEQ ID No: 763, SEQ ID No: 765, SEQ ID No: 767, SEQ ID No: 769, SEQ ID No: 771, SEQ ID No: 773, SEQ ID No: 775, SEQ ID No: 777, SEQ ID No: 779, SEQ ID No: 781, SEQ ID No: 783, SEQ ID No: 785, SEQ ID No: 787, SEQ ID No: 789, SEQ ID No: 791, SEQ ID No: 793, SEQ ID No: 795, SEQ ID No: 797, SEQ ID No: 799, SEQ ID No: 801, SEQ ID No: 803, SEQ ID No: 805, SEQ ID No: 807, SEQ ID No: 809, SEQ ID No: 811, SEQ ID No: 813, SEQ ID No: 815, SEQ ID No: 817, SEQ ID No: 819, SEQ ID No: 821, SEQ ID No: 823, SEQ ID No: 825, SEQ ID No: 827, SEQ ID No: 829, SEQ ID No: 831, SEQ ID No: 833, SEQ ID No: 835, SEQ ID No: 837, SEQ ID No: 839, SEQ ID No: 841, SEQ ID No: 843, SEQ ID No: 845, SEQ ID No: 847, SEQ ID No: 849, SEQ ID No: 851, SEQ ID No: 853, SEQ ID No: 855, SEQ ID No: 857, SEQ ID No: 859, SEQ ID No: 861, SEQ ID No: 863, SEQ ID No: 865, SEQ ID No: 867, SEQ ID No: 869, SEQ ID No: 871, SEQ ID No: 873, SEQ ID No: 875, SEQ ID No: 877, SEQ ID No: 879, SEQ ID No: 881, SEQ ID No: 883, SEQ ID No: 885, SEQ ID No: 887, SEQ ID No: 889, SEQ ID No: 891, SEQ ID No: 893, SEQ ID No: 895, SEQ ID No: 897, SEQ ID No: 899, SEQ ID No: 901, SEQ ID No: 903, SEQ ID No: 905, SEQ ID No: 907, SEQ ID No: 909, SEQ ID No: 911, SEQ ID No: 913, SEQ ID No: 915, SEQ ID No: 917, SEQ ID No: 919, SEQ ID No: 921, SEQ ID No: 923, SEQ ID No: 925, SEQ ID No: 927, SEQ ID No: 929, SEQ ID No: 931, SEQ ID No: 933, SEQ ID No: 935, SEQ ID No: 937, SEQ ID No: 939, SEQ ID No: 941, SEQ ID No: 943, SEQ ID No: 945, SEQ ID No: 947, SEQ ID No: 949, SEQ ID No: 951, SEQ ID No: 953, SEQ ID No: 955, SEQ ID No: 957, SEQ ID No: 959, SEQ ID No: 961, SEQ ID No: 963, SEQ ID No: 965, SEQ ID No: 967, SEQ ID No: 969, SEQ ID No: 971, SEQ ID No: 973, SEQ ID No: 975, SEQ ID No: 977, SEQ ID No: 979, SEQ ID No: 981, SEQ ID No: 983, SEQ ID No: 985, SEQ ID No: 987, SEQ ID No: 989, SEQ ID No: 991, SEQ ID No: 993, SEQ ID No: 995, SEQ ID No: 997, SEQ ID No: 999, SEQ ID No: 1001, SEQ ID No: 1003, SEQ ID No: 1005, SEQ ID No: 1007, SEQ ID No: 1009, SEQ ID No: 1011, SEQ ID No: 1013, SEQ ID No: 1015, SEQ ID No: 1017, SEQ ID No: 1019, SEQ ID No: 1021, SEQ ID No: 1023, SEQ ID No: 1025, SEQ ID No: 1027, SEQ ID No: 1029, SEQ ID No: 1031, SEQ ID No: 1033, SEQ ID No: 1035, SEQ ID No: 1037, SEQ ID No: 1039, SEQ ID No: 1041, SEQ ID No: 1043, SEQ ID No: 1045, SEQ ID No: 1047, SEQ ID No: 1049, SEQ ID No: 1051, SEQ ID No: 1053, SEQ ID No: 1055, SEQ ID No: 1057, SEQ ID No: 1059, SEQ ID No: 1061, SEQ ID No: 1063, SEQ ID No: 1065, SEQ ID No: 1067, SEQ ID No: 1069, SEQ ID No: 1071, SEQ ID No: 1073, SEQ ID No: 1075, SEQ ID No: 1077, SEQ ID No: 1079, SEQ ID No: 1081, SEQ ID No: 1083, SEQ ID No: 1085, SEQ ID No: 1087, SEQ ID No: 1089, SEQ ID No: 1091, SEQ ID No: 1093, SEQ ID No: 1095, SEQ ID No: 1097, SEQ ID No: 1099, SEQ ID No: 1101, SEQ ID No: 1103, SEQ ID No: 1105, SEQ ID No: 1107, SEQ ID No: 1109, SEQ ID No: 1111, SEQ ID No: 1113, SEQ ID No: 1115, SEQ ID No: 1117, SEQ ID No: 1119, SEQ ID No: 1121, SEQ ID No: 1123, SEQ ID No: 1125, SEQ ID No: 1127, SEQ ID No: 1129, SEQ ID No: 1131, SEQ ID No: 1133, SEQ ID No: 1135, SEQ ID No: 1137, SEQ ID No: 1139, SEQ ID No: 1141, SEQ ID No: 1143, SEQ ID No: 1145, SEQ ID No: 1147, SEQ ID No: 1149, SEQ ID No: 1151, SEQ ID No: 1153, SEQ ID No: 1155, SEQ ID No: 1157, SEQ ID No: 1159, SEQ ID No: 1161, SEQ ID No: 1163, SEQ ID No: 1165, SEQ ID No: 1167, SEQ ID No: 1169, SEQ ID No: 1171, SEQ ID No: 1173, SEQ ID No: 1175, SEQ ID No: 1177, SEQ ID No: 1179, SEQ ID No: 1181, SEQ ID No: 1183, SEQ ID No: 1185, SEQ ID No: 1187, SEQ ID No: 1189, SEQ ID No: 1191, SEQ ID No: 1193, SEQ ID No: 1195, SEQ ID No: 1197, SEQ ID No: 1199, SEQ ID No: 1201, SEQ ID No: 1203, SEQ ID No: 1205, SEQ ID No: 1207, SEQ ID No: 1209, SEQ ID No: 1211, SEQ ID No: 1213, SEQ ID No: 1215, SEQ ID No: 1217, SEQ ID No: 1219, SEQ ID No: 1221, SEQ ID No: 1223, SEQ ID No: 1225, SEQ ID No: 1227, SEQ ID No: 1229, SEQ ID No: 1231, SEQ ID No: 1233, SEQ ID No: 1235, SEQ ID No: 1237, SEQ ID No: 1239, SEQ ID No: 1241, SEQ ID No: 1243, SEQ ID No: 1245, SEQ ID No: 1247, SEQ ID No: 1249, SEQ ID No: 1251, SEQ ID No: 1253, SEQ ID No: 1255, SEQ ID No: 1257, SEQ ID No: 1259, SEQ ID No: 1261, SEQ ID No: 1263, SEQ ID No: 1265, SEQ ID No: 1267, SEQ ID No: 1269, SEQ ID No: 1271, SEQ ID No: 1273, SEQ ID No: 1275, SEQ ID No: 1277, SEQ ID No: 1279, SEQ ID No: 1281, SEQ ID No: 1283, SEQ ID No: 1285, SEQ ID No: 1287, SEQ ID No: 1289, SEQ ID No: 1291, SEQ ID No: 1293, SEQ ID No: 1295, SEQ ID No: 1297, SEQ ID No: 1299, SEQ ID No: 1301, SEQ ID No: 1303, SEQ ID No: 1305, SEQ ID No: 1307, SEQ ID No: 1309, SEQ ID No: 1311, SEQ ID No: 1313, SEQ ID No: 1315, SEQ ID No: 1317, SEQ ID No: 1319, SEQ ID No: 1321, SEQ ID No: 1323, SEQ ID No: 1325, SEQ ID No: 1327, SEQ ID No: 1329, SEQ ID No: 1331, SEQ ID No: 1333, SEQ ID No: 1335, SEQ ID No: 1337, SEQ ID No: 1339, SEQ ID No: 1341, SEQ ID No: 1343, SEQ ID No: 1345, SEQ ID No: 1347, SEQ ID No: 1349, SEQ ID No: 1351, SEQ ID No: 1353, SEQ ID No: 1355, SEQ ID No: 1357, SEQ ID No: 1359, SEQ ID No: 1361, SEQ ID No: 1363, SEQ ID No: 1365, SEQ ID No: 1367, SEQ ID No: 1369, SEQ ID No: 1371, SEQ ID No: 1373, SEQ ID No: 1375, SEQ ID No: 1377, SEQ ID No: 1379, SEQ ID No: 1381, SEQ ID No: 1383, SEQ ID No: 1385, SEQ ID No: 1387, SEQ ID No: 1389, SEQ ID No: 1391, SEQ ID No: 1393, SEQ ID No: 1395, SEQ ID No: 1397, SEQ ID No: 1399, SEQ ID No: 1401, SEQ ID No: 1403, SEQ ID No: 1405, SEQ ID No: 1407, SEQ ID No: 1409, SEQ ID No: 1411, SEQ ID No: 1413, SEQ ID No: 1415, SEQ ID No: 1417, SEQ ID No: 1419, SEQ ID No: 1421, SEQ ID No: 1423, SEQ ID No: 1425, SEQ ID No: 1427, SEQ ID No: 1429, SEQ ID No: 1431, SEQ ID No: 1433, SEQ ID No: 1435, SEQ ID No: 1437, SEQ ID No: 1439, SEQ ID No: 1441, SEQ ID No: 1443, SEQ ID No: 1445, SEQ ID No: 1447, SEQ ID No: 1449, SEQ ID No: 1451, SEQ ID No: 1453, SEQ ID No: 1455, SEQ ID No: 1457, SEQ ID No: 1459, SEQ ID No: 1461, SEQ ID No: 1463, SEQ ID No: 1465, SEQ ID No: 1467, SEQ ID No: 1469, SEQ ID No: 1471, SEQ ID No: 1473, SEQ ID No: 1475, SEQ ID No: 1477, SEQ ID No: 1479, SEQ ID No: 1481, SEQ ID No: 1483, SEQ ID No: 1485, SEQ ID No: 1487, SEQ ID No: 1489, SEQ ID No: 1491, SEQ ID No: 1493, SEQ ID No: 1495, SEQ ID No: 1497, SEQ ID No: 1499, SEQ ID No: 1501, SEQ ID No: 1503, SEQ ID No: 1505, SEQ ID No: 1507, SEQ ID No: 1509, SEQ ID No: 1511, SEQ ID No: 1513, SEQ ID No: 1515, SEQ ID No: 1517, SEQ ID No: 1519, SEQ ID No: 1521, SEQ ID No: 1523, SEQ ID No: 1525, SEQ ID No: 1527, SEQ ID No: 1529, SEQ ID No: 1531, SEQ ID No: 1533, SEQ ID No: 1535, SEQ ID No: 1537, SEQ ID No: 1539, SEQ ID No: 1541, SEQ ID No: 1543, SEQ ID No: 1545, SEQ ID No: 1547, SEQ ID No: 1549, SEQ ID No: 1551, SEQ ID No: 1553, SEQ ID No: 1555, SEQ ID No: 1557, SEQ ID No: 1559, SEQ ID No: 1561, SEQ ID No: 1563, SEQ ID No: 1565, SEQ ID No: 1567, SEQ ID No: 1569, SEQ ID No: 1571, SEQ ID No: 1573, SEQ ID No: 1575, SEQ ID No: 1577, SEQ ID No: 1579, SEQ ID No: 1581, SEQ ID No: 1583, SEQ ID No: 1585, SEQ ID No: 1587, SEQ ID No: 1589, SEQ ID No: 1591, SEQ ID No: 1593, SEQ ID No: 1595, SEQ ID No: 1597, SEQ ID No: 1599, SEQ ID No: 1601, SEQ ID No: 1603, SEQ ID No: 1605, SEQ ID No: 1607, SEQ ID No: 1609, SEQ ID No: 1611, SEQ ID No: 1613, SEQ ID No: 1615, SEQ ID No: 1617, SEQ ID No: 1619, SEQ ID No: 1621, SEQ ID No: 1623, SEQ ID No: 1625, SEQ ID No: 1627, SEQ ID No: 1629, SEQ ID No: 1631, SEQ ID No: 1633, SEQ ID No: 1635, SEQ ID No: 1637, SEQ ID No: 1639, SEQ ID No: 1641, SEQ ID No: 1643, SEQ ID No: 1645, SEQ ID No: 1647, SEQ ID No: 1649, SEQ ID No: 1651, SEQ ID No: 1653, SEQ ID No: 1655, SEQ ID No: 1657, SEQ ID No: 1659, SEQ ID No: 1661, SEQ ID No: 1663, SEQ ID No: 1665, SEQ ID No: 1667, SEQ ID No: 1669, SEQ ID No: 1671, SEQ ID No: 1673, SEQ ID No: 1675, SEQ ID No: 1677, SEQ ID No: 1679, SEQ ID No: 1681, SEQ ID No: 1683, SEQ ID No: 1685, SEQ ID No: 1687, SEQ ID No: 1689, SEQ ID No: 1691, SEQ ID No: 1693, SEQ ID No: 1695, SEQ ID No: 1697, SEQ ID No: 1699, SEQ ID No: 1701, SEQ ID No: 1703, SEQ ID No: 1705, SEQ ID No: 1707, SEQ ID No: 1709, SEQ ID No: 1711, SEQ ID No: 1713, SEQ ID No: 1715, SEQ ID No: 1717, SEQ ID No: 1719, SEQ ID No: 1721, SEQ ID No: 1723, SEQ ID No: 1725, SEQ ID No: 1727, SEQ ID No: 1729, SEQ ID No: 1731, SEQ ID No: 1733, SEQ ID No: 1735, SEQ ID No: 1737, SEQ ID No: 1739, SEQ ID No: 1741, SEQ ID No: 1743, SEQ ID No: 1745, SEQ ID No: 1747, SEQ ID No: 1749, SEQ ID No: 1751, SEQ ID No: 1753, SEQ ID No: 1755, SEQ ID No: 1757, SEQ ID No: 1759, SEQ ID No: 1761, SEQ ID No: 1763, SEQ ID No: 1765, SEQ ID No: 1767, SEQ ID No: 1769, SEQ ID No: 1771, SEQ ID No: 1773, SEQ ID No: 1775, SEQ ID No: 1777, SEQ ID No: 1779, SEQ ID No: 1781, SEQ ID No: 1783, SEQ ID No: 1785, SEQ ID No: 1787, SEQ ID No: 1789, SEQ ID No: 1791, SEQ ID No: 1793, SEQ ID No: 1795, SEQ ID No: 1797, SEQ ID No: 1799, SEQ ID No: 1801, SEQ ID No: 1803, SEQ ID No: 1805, SEQ ID No: 1807, SEQ ID No: 1809, SEQ ID No: 1811, SEQ ID No: 1813, SEQ ID No: 1815, SEQ ID No: 1817, SEQ ID No: 1819, SEQ ID No: 1821, SEQ ID No: 1823, SEQ ID No: 1825, SEQ ID No: 1827, SEQ ID No: 1829, SEQ ID No: 1831, SEQ ID No: 1833, SEQ ID No: 1835, SEQ ID No: 1837, SEQ ID No: 1839, SEQ ID No: 1841, SEQ ID No: 1843, SEQ ID No: 1845, SEQ ID No: 1847, SEQ ID No: 1849, SEQ ID No: 1851, SEQ ID No: 1853, SEQ ID No: 1855, SEQ ID No: 1857, SEQ ID No: 1859, SEQ ID No: 1861, SEQ ID No: 1863, SEQ ID No: 1865, SEQ ID No: 1867, SEQ ID No: 1869, SEQ ID No: 1871, SEQ ID No: 1873, SEQ ID No: 1875, SEQ ID No: 1877, SEQ ID No: 1879, SEQ ID No: 1881, SEQ ID No: 1883, SEQ ID No: 1885, SEQ ID No: 1887, SEQ ID No: 1889, SEQ ID No: 1891, SEQ ID No: 1893, SEQ ID No: 1895, SEQ ID No: 1897, SEQ ID No: 1899, SEQ ID No: 1901, SEQ ID No: 1903, SEQ ID No: 1905, SEQ ID No: 1907, SEQ ID No: 1909, SEQ ID No: 1911, SEQ ID No: 1913, SEQ ID No: 1915, SEQ ID No: 1917, SEQ ID No: 1919, SEQ ID No: 1921, SEQ ID No: 1923, SEQ ID No: 1925, SEQ ID No: 1927, SEQ ID No: 1929, SEQ ID No: 1931, SEQ ID No: 1933, SEQ ID No: 1935, SEQ ID No: 1937, SEQ ID No: 1939, SEQ ID No: 1941, SEQ ID No: 1943, SEQ ID No: 1945, SEQ ID No: 1947, SEQ ID No: 1949, SEQ ID No: 1951, SEQ ID No: 1953, SEQ ID No: 1955, SEQ ID No: 1957, SEQ ID No: 1959, SEQ ID No: 1961, SEQ ID No: 1963, SEQ ID No: 1965, SEQ ID No: 1967, SEQ ID No: 1969, SEQ ID No: 1971, SEQ ID No: 1973 or fragments or homologues or variants thereof. Preferably, the nucleic acid sequence encodes a protein (including fragments and homologues or variants thereof) useful in the invention, or encompasses useful oligonucleotides or complementary nucleic acid sequences.
In one embodiment, a nucleic molecule of the present invention includes a nucleic acid molecule comprising, consisting essentially of, or consisting of, a nucleic acid sequence encoding an amino acid sequence represented in SEQ ID No: 1, SEQ ID No: 3, SEQ ID No: 5, SEQ ID No: 7, SEQ ID No: 9, SEQ ID No: 11, SEQ ID No: 13, SEQ ID No: 15, SEQ ID No: 17, SEQ ID No: 19, SEQ ID No: 21, SEQ ID No: 23, SEQ ID No: 25, SEQ ID No: 27, SEQ ID No: 29, SEQ ID No: 31, SEQ ID No: 33, SEQ ID No: 35, SEQ ID No: 37, SEQ ID No: 39, SEQ ID No: 41, SEQ ID No: 43, SEQ ID No: 45, SEQ ID No: 47, SEQ ID No: 49, SEQ ID No: 51, SEQ ID No: 53, SEQ ID No: 55, SEQ ID No: 56, SEQ ID No: 57, SEQ ID No: 59, SEQ ID No: 61, SEQ ID No: 63, SEQ ID No: 65, SEQ ID No: 67, SEQ ID No: 69, SEQ ID No: 71, SEQ ID No: 73, SEQ ID No: 75, SEQ ID No: 77, SEQ ID No: 79, SEQ ID No: 81, SEQ ID No: 83, SEQ ID No: 85, SEQ ID No: 87, SEQ ID No: 89, SEQ ID No: 91, SEQ ID No: 93, SEQ ID No: 95, SEQ ID No: 97, SEQ ID No: 99, SEQ ID No: 101, SEQ ID No: 103, SEQ ID No: 105, SEQ ID No: 107, SEQ ID No: 109, SEQ ID No: 111, SEQ ID No: 113, SEQ ID No: 115, SEQ ID No: 117, SEQ ID No: 119, SEQ ID No: 121, SEQ ID No: 123, SEQ ID No: 125, SEQ ID No: 127, SEQ ID No: 129, SEQ ID No: 131, SEQ ID No: 133, SEQ ID No: 135, SEQ ID No: 137, SEQ ID No: 139, SEQ ID No: 141, SEQ ID No: 143, SEQ ID No: 145, SEQ ID No: 147, SEQ ID No: 149, SEQ ID No: 151, SEQ ID No: 153, SEQ ID No: 155, SEQ ID No: 157, SEQ ID No: 159, SEQ ID No: 161, SEQ ID No: 163, SEQ ID No: 165, SEQ ID No: 167, SEQ ID No: 169, SEQ ID No: 171, SEQ ID No: 173, SEQ ID No: 175, SEQ ID No: 177, SEQ ID No: 179, SEQ ID No: 181, SEQ ID No: 183, SEQ ID No: 185, SEQ ID No: 187, SEQ ID No: 189, SEQ ID No: 191, SEQ ID No: 193, SEQ ID No: 195, SEQ ID No: 197, SEQ ID No: 199, SEQ ID No: 201, SEQ ID No: 203, SEQ ID No: 205, SEQ ID No: 207, SEQ ID No: 209, SEQ ID No: 211, SEQ ID No: 213, SEQ ID No: 215, SEQ ID No: 217, SEQ ID No: 219, SEQ ID No: 221, SEQ ID No: 223, SEQ ID No: 225, SEQ ID No: 227, SEQ ID No: 229, SEQ ID No: 231, SEQ ID No: 233, SEQ ID No: 235. SEQ ID No: 237, SEQ ID No: 239, SEQ ID No: 241, SEQ ID No: 243, SEQ ID No: 245, SEQ ID No: 247, SEQ ID No: 249, SEQ ID No: 251, SEQ ID No: 253, SEQ ID No: 255, SEQ ID No: 257, SEQ ID No: 259, SEQ ID No: 261, SEQ ID No: 263, SEQ ID No: 265, SEQ ID No: 267, SEQ ID No: 269, SEQ ID No: 271, SEQ ID No: 273, SEQ ID No: 275, SEQ ID No: 277, SEQ ID No: 279, SEQ ID No: 281, SEQ ID No: 283, SEQ ID No: 285, SEQ ID No: 287, SEQ ID No: 289, SEQ ID No: 291, SEQ ID No: 293, SEQ ID No: 295, SEQ ID No: 297, SEQ ID No: 299, SEQ ID No: 301, SEQ ID No: 303, SEQ ID No: 305, SEQ ID No: 307, SEQ ID No: 309, SEQ ID No: 311, SEQ ID No: 313, SEQ ID No: 315, SEQ ID No: 317, SEQ ID No: 319, SEQ ID No: 321, SEQ ID No: 323, SEQ ID No: 325, SEQ ID No: 327, SEQ ID No: 329, SEQ ID No: 331, SEQ ID No: 333, SEQ ID No: 335, SEQ ID No: 337, SEQ ID No: 339, SEQ ID No: 341, SEQ ID No: 343, SEQ ID No: 345, SEQ ID No: 347, SEQ ID No: 349, SEQ ID No: 351, SEQ ID No: 353, SEQ ID No: 355, SEQ ID No: 357, SEQ ID No: 359, SEQ ID No: 361, SEQ ID No: 363, SEQ ID No: 365, SEQ ID No: 367, SEQ ID No: 369, SEQ ID No: 371, SEQ ID No: 373, SEQ ID No: 375, SEQ ID No: 377, SEQ ID No: 379, SEQ ID No: 381, SEQ ID No: 383, SEQ ID No: 385, SEQ ID No: 387, SEQ ID No: 389, SEQ ID No: 391, SEQ ID No: 393, SEQ ID No: 395, SEQ ID No: 397, SEQ ID No: 399, SEQ ID No: 401, SEQ ID No: 403, SEQ ID No: 405, SEQ ID No: 407, SEQ ID No: 409, SEQ ID No: 411, SEQ ID No: 413, SEQ ID No: 415, SEQ ID No: 417, SEQ ID No: 419, SEQ ID No: 421, SEQ ID No: 423, SEQ ID No: 425, SEQ ID No: 427, SEQ ID No: 429, SEQ ID No: 431, SEQ ID No: 433, SEQ ID No: 435, SEQ ID No: 437, SEQ ID No: 439, SEQ ID No: 441, SEQ ID No: 443, SEQ ID No: 445, SEQ ID No: 447, SEQ ID No: 449, SEQ ID No: 451, SEQ ID No: 453, SEQ ID No: 455, SEQ ID No: 457, SEQ ID No: 459, SEQ ID No: 461, SEQ ID No: 463, SEQ ID No: 465, SEQ ID No: 467, SEQ ID No: 469, SEQ ID No: 471, SEQ ID No: 473, SEQ ID No: 475, SEQ ID No: 477, SEQ ID No: 479, SEQ ID No: 481, SEQ ID No: 483, SEQ ID No: 485, SEQ ID No: 487, SEQ ID No: 489, SEQ ID No: 491, SEQ ID No: 493, SEQ ID No: 495, SEQ ID No: 497, SEQ ID No: 499, SEQ ID No: 501, SEQ ID No: 503, SEQ ID No: 505, SEQ ID No: 507, SEQ ID No: 509, SEQ ID No: 511, SEQ ID No: 513, SEQ ID No: 515, SEQ ID No: 517, SEQ ID No: 519, SEQ ID No: 521, SEQ ID No: 523, SEQ ID No: 525, SEQ ID No: 527, SEQ ID No: 529, SEQ ID No: 531, SEQ ID No: 533, SEQ ID No: 535, SEQ ID No: 537, SEQ ID No: 539, SEQ ID No: 541, SEQ ID No: 543, SEQ ID No: 545, SEQ ID No: 547, SEQ ID No: 549, SEQ ID No: 551, SEQ ID No: 553, SEQ ID No: 555, SEQ ID No: 557, SEQ ID No: 559, SEQ ID No: 561, SEQ ID No: 563, SEQ ID No: 565, SEQ ID No: 567, SEQ ID No: 569, SEQ ID No: 571, SEQ ID No: 573, SEQ ID No: 575, SEQ ID No: 577, SEQ ID No: 579, SEQ ID No: 581, SEQ ID No: 583, SEQ ID No: 585, SEQ ID No: 587, SEQ ID No: 589, SEQ ID No: 591, SEQ ID No: 593, SEQ ID No: 595, SEQ ID No: 597, SEQ ID No: 599, SEQ ID No: 601, SEQ ID No: 603, SEQ ID No: 605, SEQ ID No: 607, SEQ ID No: 609, SEQ ID No: 611, SEQ ID No: 613, SEQ ID No: 615, SEQ ID No: 617, SEQ ID No: 619, SEQ ID No: 621, SEQ ID No: 623, SEQ ID No: 625, SEQ ID No: 627, SEQ ID No: 629, SEQ ID No: 631, SEQ ID No: 633, SEQ ID No: 635, SEQ ID No: 637, SEQ ID No: 639, SEQ ID No: 641, SEQ ID No: 643, SEQ ID No: 645, SEQ ID No: 647, SEQ ID No: 649, SEQ ID No: 651, SEQ ID No: 653, SEQ ID No: 655, SEQ ID No: 657, SEQ ID No: 659, SEQ ID No: 661, SEQ ID No: 663, SEQ ID No: 665, SEQ ID No: 667, SEQ ID No: 669, SEQ ID No: 671, SEQ ID No: 673, SEQ ID No: 675, SEQ ID No: 677, SEQ ID No: 679, SEQ ID No: 681, SEQ ID No: 683, SEQ ID No: 685, SEQ ID No: 687, SEQ ID No: 689, SEQ ID No: 691, SEQ ID No: 693, SEQ ID No: 695, SEQ ID No: 697, SEQ ID No: 699, SEQ ID No: 701, SEQ ID No: 703, SEQ ID No: 705, SEQ ID No: 707, SEQ ID No: 709, SEQ ID No: 711, SEQ ID No: 713, SEQ ID No: 715, SEQ ID No: 717, SEQ ID No: 719, SEQ ID No: 721, SEQ ID No: 723, SEQ ID No: 725, SEQ ID No: 727, SEQ ID No: 729, SEQ ID No: 731, SEQ ID No: 733, SEQ ID No: 735, SEQ ID No: 737, SEQ ID No: 739, SEQ ID No: 741, SEQ ID No: 743, SEQ ID No: 745, SEQ ID No: 747, SEQ ID No: 749, SEQ ID No: 751, SEQ ID No: 753, SEQ ID No: 755, SEQ ID No: 757, SEQ ID No: 759, SEQ ID No: 761, SEQ ID No: 763, SEQ ID No: 765, SEQ ID No: 767, SEQ ID No: 769, SEQ ID No: 771, SEQ ID No: 773, SEQ ID No: 775, SEQ ID No: 777, SEQ ID No: 779, SEQ ID No: 781, SEQ ID No: 783, SEQ ID No: 785, SEQ ID No: 787, SEQ ID No: 789, SEQ ID No: 791, SEQ ID No: 793, SEQ ID No: 795, SEQ ID No: 797, SEQ ID No: 799, SEQ ID No: 801, SEQ ID No: 803, SEQ ID No: 805, SEQ ID No: 807, SEQ ID No: 809, SEQ ID No: 811, SEQ ID No: 813, SEQ ID No: 815, SEQ ID No: 817, SEQ ID No: 819, SEQ ID No: 821, SEQ ID No: 823, SEQ ID No: 825, SEQ ID No: 827, SEQ ID No: 829, SEQ ID No: 831, SEQ ID No: 833, SEQ ID No: 835, SEQ ID No: 837, SEQ ID No: 839, SEQ ID No: 841, SEQ ID No: 843, SEQ ID No: 845, SEQ ID No: 847, SEQ ID No: 849, SEQ ID No: 851, SEQ ID No: 853, SEQ ID No: 855, SEQ ID No: 857, SEQ ID No: 859, SEQ ID No: 861, SEQ ID No: 863, SEQ ID No: 865, SEQ ID No: 867, SEQ ID No: 869, SEQ ID No: 871, SEQ ID No: 873, SEQ ID No: 875, SEQ ID No: 877, SEQ ID No: 879, SEQ ID No: 881, SEQ ID No: 883, SEQ ID No: 885, SEQ ID No: 887, SEQ ID No: 889, SEQ ID No: 891, SEQ ID No: 893, SEQ ID No: 895, SEQ ID No: 897, SEQ ID No: 899, SEQ ID No: 901, SEQ ID No: 903, SEQ ID No: 905, SEQ ID No: 907, SEQ ID No: 909, SEQ ID No: 911, SEQ ID No: 913, SEQ ID No: 915, SEQ ID No: 917, SEQ ID No: 919, SEQ ID No: 921, SEQ ID No: 923, SEQ ID No: 925, SEQ ID No: 927, SEQ ID No: 929, SEQ ID No: 931, SEQ ID No: 933, SEQ ID No: 935, SEQ ID No: 937, SEQ ID No: 939, SEQ ID No: 941, SEQ ID No: 943, SEQ ID No: 945, SEQ ID No: 947, SEQ ID No: 949, SEQ ID No: 951, SEQ ID No: 953, SEQ ID No: 955, SEQ ID No: 957, SEQ ID No: 959, SEQ ID No: 961, SEQ ID No: 963, SEQ ID No: 965, SEQ ID No: 967, SEQ ID No: 969, SEQ ID No: 971, SEQ ID No: 973, SEQ ID No: 975, SEQ ID No: 977, SEQ ID No: 979, SEQ ID No: 981, SEQ ID No: 983, SEQ ID No: 985, SEQ ID No: 987, SEQ ID No: 989, SEQ ID No: 991, SEQ ID No: 993, SEQ ID No: 995, SEQ ID No: 997, SEQ ID No: 999, SEQ ID No: 1001, SEQ ID No: 1003, SEQ ID No: 1005, SEQ ID No: 1007, SEQ ID No: 1009, SEQ ID No: 1011, SEQ ID No: 1013, SEQ ID No: 1015, SEQ ID No: 1017, SEQ ID No: 1019, SEQ ID No: 1021, SEQ ID No: 1023, SEQ ID No: 1025, SEQ ID No: 1027, SEQ ID No: 1029, SEQ ID No: 1031, SEQ ID No: 1033, SEQ ID No: 1035, SEQ ID No: 1037, SEQ ID No: 1039, SEQ ID No: 1041, SEQ ID No: 1043, SEQ ID No: 1045, SEQ ID No: 1047, SEQ ID No: 1049, SEQ ID No: 1051, SEQ ID No: 1053, SEQ ID No: 1055, SEQ ID No: 1057, SEQ ID No: 1059, SEQ ID No: 1061, SEQ ID No: 1063, SEQ ID No: 1065, SEQ ID No: 1067, SEQ ID No: 1069, SEQ ID No: 1071, SEQ ID No: 1073, SEQ ID No: 1075, SEQ ID No: 1077, SEQ ID No: 1079, SEQ ID No: 1081, SEQ ID No: 1083, SEQ ID No: 1085, SEQ ID No: 1087, SEQ ID No: 1089, SEQ ID No: 1091, SEQ ID No: 1093, SEQ ID No: 1095, SEQ ID No: 1097, SEQ ID No: 1099, SEQ ID No: 1101, SEQ ID No: 1103, SEQ ID No: 1105, SEQ ID No: 1107, SEQ ID No: 1109, SEQ ID No: 1111, SEQ ID No: 1113, SEQ ID No: 1115, SEQ ID No: 1117, SEQ ID No: 1119, SEQ ID No: 1121, SEQ ID No: 1123, SEQ ID No: 1125, SEQ ID No: 1127, SEQ ID No: 1129, SEQ ID No: 1131, SEQ ID No: 1133, SEQ ID No: 1135, SEQ ID No: 1137, SEQ ID No: 1139, SEQ ID No: 1141, SEQ ID No: 1143, SEQ ID No: 1145, SEQ ID No: 1147, SEQ ID No: 1149, SEQ ID No: 1151, SEQ ID No: 1153, SEQ ID No: 1155, SEQ ID No: 1157, SEQ ID No: 1159, SEQ ID No: 1161, SEQ ID No: 1163, SEQ ID No: 1165, SEQ ID No: 1167, SEQ ID No: 1169, SEQ ID No: 1171, SEQ ID No: 1173, SEQ ID No: 1175, SEQ ID No: 1177, SEQ ID No: 1179, SEQ ID No: 1181, SEQ ID No: 1183, SEQ ID No: 1185, SEQ ID No: 1187, SEQ ID No: 1189, SEQ ID No: 1191, SEQ ID No: 1193, SEQ ID No: 1195, SEQ ID No: 1197, SEQ ID No: 1199, SEQ ID No: 1201, SEQ ID No: 1203, SEQ ID No: 1205, SEQ ID No: 1207, SEQ ID No: 1209, SEQ ID No: 1211, SEQ ID No: 1213, SEQ ID No: 1215, SEQ ID No: 1217, SEQ ID No: 1219, SEQ ID No: 1221, SEQ ID No: 1223, SEQ ID No: 1225, SEQ ID No: 1227, SEQ ID No: 1229, SEQ ID No: 1231, SEQ ID No: 1233, SEQ ID No: 1235, SEQ ID No: 1237, SEQ ID No: 1239, SEQ ID No: 1241, SEQ ID No: 1243, SEQ ID No: 1245, SEQ ID No: 1247, SEQ ID No: 1249, SEQ ID No: 1251, SEQ ID No: 1253, SEQ ID No: 1255, SEQ ID No: 1257, SEQ ID No: 1259, SEQ ID No: 1261, SEQ ID No: 1263, SEQ ID No: 1265, SEQ ID No: 1267, SEQ ID No: 1269, SEQ ID No: 1271, SEQ ID No: 1273, SEQ ID No: 1275, SEQ ID No: 1277, SEQ ID No: 1279, SEQ ID No: 1281, SEQ ID No: 1283, SEQ ID No: 1285, SEQ ID No: 1287, SEQ ID No: 1289, SEQ ID No: 1291, SEQ ID No: 1293, SEQ ID No: 1295, SEQ ID No: 1297, SEQ ID No: 1299, SEQ ID No: 1301, SEQ ID No: 1303, SEQ ID No: 1305, SEQ ID No: 1307, SEQ ID No: 1309, SEQ ID No: 1311, SEQ ID No: 1313, SEQ ID No: 1315, SEQ ID No: 1317, SEQ ID No: 1319, SEQ ID No: 1321, SEQ ID No: 1323, SEQ ID No: 1325, SEQ ID No: 1327, SEQ ID No: 1329, SEQ ID No: 1331, SEQ ID No: 1333, SEQ ID No: 1335, SEQ ID No: 1337, SEQ ID No: 1339, SEQ ID No: 1341, SEQ ID No: 1343, SEQ ID No: 1345, SEQ ID No: 1347, SEQ ID No: 1349, SEQ ID No: 1351, SEQ ID No: 1353, SEQ ID No: 1355, SEQ ID No: 1357, SEQ ID No: 1359, SEQ ID No: 1361, SEQ ID No: 1363, SEQ ID No: 1365, SEQ ID No: 1367, SEQ ID No: 1369, SEQ ID No: 1371, SEQ ID No: 1373, SEQ ID No: 1375, SEQ ID No: 1377, SEQ ID No: 1379, SEQ ID No: 1381, SEQ ID No: 1383, SEQ ID No: 1385, SEQ ID No: 1387, SEQ ID No: 1389, SEQ ID No: 1391, SEQ ID No: 1393, SEQ ID No: 1395, SEQ ID No: 1397, SEQ ID No: 1399, SEQ ID No: 1401, SEQ ID No: 1403, SEQ ID No: 1405, SEQ ID No: 1407, SEQ ID No: 1409, SEQ ID No: 1411, SEQ ID No: 1413, SEQ ID No: 1415, SEQ ID No: 1417, SEQ ID No: 1419, SEQ ID No: 1421, SEQ ID No: 1423, SEQ ID No: 1425, SEQ ID No: 1427, SEQ ID No: 1429, SEQ ID No: 1431, SEQ ID No: 1433, SEQ ID No: 1435, SEQ ID No: 1437, SEQ ID No: 1439, SEQ ID No: 1441, SEQ ID No: 1443, SEQ ID No: 1445, SEQ ID No: 1447, SEQ ID No: 1449, SEQ ID No: 1451, SEQ ID No: 1453, SEQ ID No: 1455, SEQ ID No: 1457, SEQ ID No: 1459, SEQ ID No: 1461, SEQ ID No: 1463, SEQ ID No: 1465, SEQ ID No: 1467, SEQ ID No: 1469, SEQ ID No: 1471, SEQ ID No: 1473, SEQ ID No: 1475, SEQ ID No: 1477, SEQ ID No: 1479, SEQ ID No: 1481, SEQ ID No: 1483, SEQ ID No: 1485, SEQ ID No: 1487, SEQ ID No: 1489, SEQ ID No: 1491, SEQ ID No: 1493, SEQ ID No: 1495, SEQ ID No: 1497, SEQ ID No: 1499, SEQ ID No: 1501, SEQ ID No: 1503, SEQ ID No: 1505, SEQ ID No: 1507, SEQ ID No: 1509, SEQ ID No: 1511, SEQ ID No: 1513, SEQ ID No: 1515, SEQ ID No: 1517, SEQ ID No: 1519, SEQ ID No: 1521, SEQ ID No: 1523, SEQ ID No: 1525, SEQ ID No: 1527, SEQ ID No: 1529, SEQ ID No: 1531, SEQ ID No: 1533, SEQ ID No: 1535, SEQ ID No: 1537, SEQ ID No: 1539, SEQ ID No: 1541, SEQ ID No: 1543, SEQ ID No: 1545, SEQ ID No: 1547, SEQ ID No: 1549, SEQ ID No: 1551, SEQ ID No: 1553, SEQ ID No: 1555, SEQ ID No: 1557, SEQ ID No: 1559, SEQ ID No: 1561, SEQ ID No: 1563, SEQ ID No: 1565, SEQ ID No: 1567, SEQ ID No: 1569, SEQ ID No: 1571, SEQ ID No: 1573, SEQ ID No: 1575, SEQ ID No: 1577, SEQ ID No: 1579, SEQ ID No: 1581, SEQ ID No: 1583, SEQ ID No: 1585, SEQ ID No: 1587, SEQ ID No: 1589, SEQ ID No: 1591, SEQ ID No: 1593, SEQ ID No: 1595, SEQ ID No: 1597, SEQ ID No: 1599, SEQ ID No: 1601, SEQ ID No: 1603, SEQ ID No: 1605, SEQ ID No: 1607, SEQ ID No: 1609, SEQ ID No: 1611, SEQ ID No: 1613, SEQ ID No: 1615, SEQ ID No: 1617, SEQ ID No: 1619, SEQ ID No: 1621, SEQ ID No: 1623, SEQ ID No: 1625, SEQ ID No: 1627, SEQ ID No: 1629, SEQ ID No: 1631, SEQ ID No: 1633, SEQ ID No: 1635, SEQ ID No: 1637, SEQ ID No: 1639, SEQ ID No: 1641, SEQ ID No: 1643, SEQ ID No: 1645, SEQ ID No: 1647, SEQ ID No: 1649, SEQ ID No: 1651, SEQ ID No: 1653, SEQ ID No: 1655, SEQ ID No: 1657, SEQ ID No: 1659, SEQ ID No: 1661, SEQ ID No: 1663, SEQ ID No: 1665, SEQ ID No: 1667, SEQ ID No: 1669, SEQ ID No: 1671, SEQ ID No: 1673, SEQ ID No: 1675, SEQ ID No: 1677, SEQ ID No: 1679, SEQ ID No: 1681, SEQ ID No: 1683, SEQ ID No: 1685, SEQ ID No: 1687, SEQ ID No: 1689, SEQ ID No: 1691, SEQ ID No: 1693, SEQ ID No: 1695, SEQ ID No: 1697, SEQ ID No: 1699, SEQ ID No: 1701, SEQ ID No: 1703, SEQ ID No: 1705, SEQ ID No: 1707, SEQ ID No: 1709, SEQ ID No: 1711, SEQ ID No: 1713, SEQ ID No: 1715, SEQ ID No: 1717, SEQ ID No: 1719, SEQ ID No: 1721, SEQ ID No: 1723, SEQ ID No: 1725, SEQ ID No: 1727, SEQ ID No: 1729, SEQ ID No: 1731, SEQ ID No: 1733, SEQ ID No: 1735, SEQ ID No: 1737, SEQ ID No: 1739, SEQ ID No: 1741, SEQ ID No: 1743, SEQ ID No: 1745, SEQ ID No: 1747, SEQ ID No: 1749, SEQ ID No: 1751, SEQ ID No: 1753, SEQ ID No: 1755, SEQ ID No: 1757, SEQ ID No: 1759, SEQ ID No: 1761, SEQ ID No: 1763, SEQ ID No: 1765, SEQ ID No: 1767, SEQ ID No: 1769, SEQ ID No: 1771, SEQ ID No: 1773, SEQ ID No: 1775, SEQ ID No: 1777, SEQ ID No: 1779, SEQ ID No: 1781, SEQ ID No: 1783, SEQ ID No: 1785, SEQ ID No: 1787, SEQ ID No: 1789, SEQ ID No: 1791, SEQ ID No: 1793, SEQ ID No: 1795, SEQ ID No: 1797, SEQ ID No: 1799, SEQ ID No: 1801, SEQ ID No: 1803, SEQ ID No: 1805, SEQ ID No: 1807, SEQ ID No: 1809, SEQ ID No: 1811, SEQ ID No: 1813, SEQ ID No: 1815, SEQ ID No: 1817, SEQ ID No: 1819, SEQ ID No: 1821, SEQ ID No: 1823, SEQ ID No: 1825, SEQ ID No: 1827, SEQ ID No: 1829, SEQ ID No: 1831, SEQ ID No: 1833, SEQ ID No: 1835, SEQ ID No: 1837, SEQ ID No: 1839, SEQ ID No: 1841, SEQ ID No: 1843, SEQ ID No: 1845, SEQ ID No: 1847, SEQ ID No: 1849, SEQ ID No: 1851, SEQ ID No: 1853, SEQ ID No: 1855, SEQ ID No: 1857, SEQ ID No: 1859, SEQ ID No: 1861, SEQ ID No: 1863, SEQ ID No: 1865, SEQ ID No: 1867, SEQ ID No: 1869, SEQ ID No: 1871, SEQ ID No: 1873, SEQ ID No: 1875, SEQ ID No: 1877, SEQ ID No: 1879, SEQ ID No: 1881, SEQ ID No: 1883, SEQ ID No: 1885, SEQ ID No: 1887, SEQ ID No: 1889, SEQ ID No: 1891, SEQ ID No: 1893, SEQ ID No: 1895, SEQ ID No: 1897, SEQ ID No: 1899, SEQ ID No: 1901, SEQ ID No: 1903, SEQ ID No: 1905, SEQ ID No: 1907, SEQ ID No: 1909, SEQ ID No: 1911, SEQ ID No: 1913, SEQ ID No: 1915, SEQ ID No: 1917, SEQ ID No: 1919, SEQ ID No: 1921, SEQ ID No: 1923, SEQ ID No: 1925, SEQ ID No: 1927, SEQ ID No: 1929, SEQ ID No: 1931, SEQ ID No: 1933, SEQ ID No: 1935, SEQ ID No: 1937, SEQ ID No: 1939, SEQ ID No: 1941, SEQ ID No: 1943, SEQ ID No: 1945, SEQ ID No: 1947, SEQ ID No: 1949, SEQ ID No: 1951, SEQ ID No: 1953, SEQ ID No: 1955, SEQ ID No: 1957, SEQ ID No: 1959, SEQ ID No: 1961, SEQ ID No: 1963, SEQ ID No: 1965, SEQ ID No: 1967, SEQ ID No: 1969, SEQ ID No: 1971, SEQ ID No: 1973 or fragments or homologues or variants thereof. Preferably, the nucleic acid sequence encodes a protein (including fragments and homologues or variants thereof) useful in the invention, or encompasses useful oligonucleotides or complementary nucleic acid sequences.
In one embodiment, such nucleic acid molecules include isolated nucleic acid molecules that hybridize under moderate stringency conditions, and more preferably under high stringency conditions, and even more preferably under very high stringency conditions, as described above, with the complement of a nucleic acid sequence encoding a protein of the present invention (i.e., including naturally occurring allelic variants encoding a protein of the present invention). Preferably, an isolated nucleic acid molecule encoding a protein of the present invention comprises a nucleic acid sequence that hybridizes under moderate, high, or very high stringency conditions to the complement of a nucleic acid sequence that encodes a protein comprising an amino acid sequence represented in SEQ ID NO: 2, SEQ ID No: 4, SEQ ID No: 6, SEQ ID No: 8, SEQ ID No: 10, SEQ ID No: 12, SEQ ID No: 14, SEQ ID No: 16, SEQ ID No: 18, SEQ ID No: 20, SEQ ID No: 22, SEQ ID No: 24, SEQ ID No: 26, SEQ ID No: 28, SEQ ID No: 30, SEQ ID No: 32, SEQ ID No: 34, SEQ ID No: 36, SEQ ID No: 38, SEQ ID No: 40, SEQ ID No: 42, SEQ ID No: 44, SEQ ID No: 46, SEQ ID No: 48, SEQ ID No: 50, SEQ ID No: 52, SEQ ID No: 54, SEQ ID No: 56, SEQ ID No: 58, SEQ ID No: 60, SEQ ID No: 62, SEQ ID No: 64, SEQ ID No: 66, SEQ ID No: 68, SEQ ID No: 70, SEQ ID No: 72, SEQ ID No: 74, SEQ ID No: 76, SEQ ID No: 78, SEQ ID No: 80, SEQ ID No: 82, SEQ ID No: 84, SEQ ID No: 86, SEQ ID No: 88, SEQ ID No: 90, SEQ ID No: 92, SEQ : [D No: 94, SEQ ID No: 96, SEQ ID No: 98, SEQ ID No: 100, SEQ ID No: 102, SEQ ID No: 104, SEQ ID No: 106, SEQ ID No: 108, SEQ ID No: 110, SEQ ID No: 112, SEQ ID No: 114, SEQ ID No: 116, SEQ ID No: 118, SEQ ID No: 120, SEQ ID No: 122, SEQ ID No: 124, SEQ ID No: 126, SEQ ID No: 128, SEQ ID No: 130, SEQ ID No: 132, SEQ ID No: 134, SEQ ID No: 136, SEQ ID No: 138, SEQ ID No: 140, SEQ ID No: 142, SEQ ID No: 144, SEQ ID No: 146, SEQ ID No: 148, SEQ ID No: 150, SEQ ID No: 152, SEQ ID No: 154, SEQ ID No: 156, SEQ ID No: 158, SEQ ID No: 160, SEQ ID No: 162, SEQ ID No: 164, SEQ ID No: 166, SEQ ID No: 168, SEQ ID No: 170, SEQ ID No: 172, SEQ ID No: 174, SEQ ID No: 176, SEQ ID No: 178, SEQ ID No: 180, SEQ ID No: 182, SEQ ID No: 184, SEQ ID No: 186, SEQ ID No: 188, SEQ ID No: 190, SEQ ID No: 192, SEQ ID No: 194, SEQ ID No: 196, SEQ ID No: 198, SEQ ID No: 200, SEQ ID No: 202, SEQ ID No: 204, SEQ ID No: 206, SEQ ID No: 208, SEQ ID No: 210, SEQ ID No: 212, SEQ ID No: 214, SEQ ID No: 216, SEQ ID No: 218, SEQ ID No: 220, SEQ ID No: 222, SEQ ID No: 224, SEQ ID No: 226, SEQ ID No: 228, SEQ ID No: 230, SEQ ID No: 232, SEQ ID No: 234, SEQ ID No: 236, SEQ ID No: 238, SEQ ID No: 240, SEQ ID No: 242, SEQ ID No: 244, SEQ ID No: 246, SEQ ID No: 248, SEQ ID No: 250, SEQ ID No: 252, SEQ ID No: 254, SEQ ID No: 256, SEQ ID No: 258, SEQ ID No: 260, SEQ ID No: 262, SEQ ID No: 264, SEQ ID No: 266, SEQ ID No: 268, SEQ ID No: 270, SEQ ID No: 272, SEQ ID No: 274, SEQ ID No: 276, SEQ ID No: 278, SEQ ID No: 280, SEQ ID No: 282, SEQ ID No: 284, SEQ ID No: 286, SEQ ID No: 288, SEQ ID No: 290, SEQ ID No: 292, SEQ ID No: 294, SEQ ID No: 296, SEQ ID No: 298, SEQ ID No: 300, SEQ ID No: 302, SEQ ID No: 304, SEQ ID No: 306, SEQ ID No: 308, SEQ ID No: 310, SEQ ID No: 312, SEQ ID No: 314, SEQ ID No: 316, SEQ ID No: 318, SEQ ID No: 320, SEQ ID No: 322, SEQ ID No: 324, SEQ ID No: 326, SEQ ID No: 328, SEQ ID No: 330, SEQ ID No: 332, SEQ ID No: 334, SEQ ID No: 336, SEQ ID No: 338, SEQ ID No: 340, SEQ ID No: 342, SEQ ID No: 344, SEQ ID No: 346, SEQ ID No: 348, SEQ ID No: 350, SEQ ID No: 352, SEQ ID No: 354, SEQ ID No: 356, SEQ ID No: 358, SEQ ID No: 360, SEQ ID No: 362, SEQ ID No: 364, SEQ ID No: 366, SEQ ID No: 368, SEQ ID No: 370, SEQ ID No: 372, SEQ ID No: 374, SEQ ID No: 376, SEQ ID No: 378, SEQ ID No: 380, SEQ ID No: 382, SEQ ID No: 384, SEQ ID No: 386, SEQ ID No: 388, SEQ ID No: 390, SEQ ID No: 392, SEQ ID No: 394, SEQ ID No: 396, SEQ ID No: 398, SEQ ID No: 400, SEQ ID No: 402, SEQ ID No: 404, SEQ ID No: 406, SEQ ID No: 408, SEQ ID No: 410, SEQ ID No: 412, SEQ ID No: 414, SEQ ID No: 416, SEQ ID No: 418, SEQ ID No: 420, SEQ ID No: 422, SEQ ID No: 424, SEQ ID No: 426, SEQ ID No: 428, SEQ ID No: 430, SEQ ID No: 432, SEQ ID No: 434, SEQ ID No: 436, SEQ ID No: 438, SEQ ID No: 440, SEQ ID No: 442, SEQ ID No: 444, SEQ ID No: 446, SEQ ID No: 448, SEQ ID No: 450, SEQ ID No: 452, SEQ ID No: 454, SEQ ID No: 456, SEQ ID No: 458, SEQ ID No: 460, SEQ ID No: 462, SEQ ID No: 464, SEQ ID No: 466, SEQ ID No: 468, SEQ ID No: 470, SEQ ID No: 472, SEQ ID No: 474, SEQ ID No: 476, SEQ ID No: 478, SEQ ID No: 480, SEQ ID No: 482, SEQ ID No: 484, SEQ ID No: 486, SEQ ID No: 488, SEQ ID No: 490, SEQ ID No: 492, SEQ ID No: 494, SEQ ID No: 496, SEQ ID No: 498, SEQ ID No: 500, SEQ ID No: 502, SEQ ID No: 504, SEQ ID No: 506, SEQ ID No: 508, SEQ ID No: 510, SEQ ID No: 512, SEQ ID No: 514, SEQ ID No: 516, SEQ ID No: 518, SEQ ID No: 520, SEQ ID No: 522, SEQ ID No: 524, SEQ ID No: 526, SEQ ID No: 528, SEQ ID No: 530, SEQ ID No: 532, SEQ ID No: 534, SEQ ID No: 536, SEQ ID No: 538, SEQ ID No: 540, SEQ ID No: 542, SEQ ID No: 544, SEQ ID No: 546, SEQ ID No: 548, SEQ ID No: 550, SEQ ID No: 552, SEQ ID No: 554, SEQ ID No: 556, SEQ ID No: 558, SEQ ID No: 560, SEQ ID No: 562, SEQ ID No: 564, SEQ ID No: 566, SEQ ID No: 568, SEQ ID No: 570, SEQ ID No: 572, SEQ ID No: 574, SEQ ID No: 576, SEQ ID No: 578, SEQ ID No: 580, SEQ ID No: 582, SEQ ID No: 584, SEQ ID No: 586, SEQ ID No: 588, SEQ ID No: 590, SEQ ID No: 592, SEQ ID No: 594, SEQ ID No: 596, SEQ ID No: 598, SEQ ID No: 600, SEQ ID No: 602, SEQ ID No: 604, SEQ ID No: 606, SEQ ID No: 608, SEQ ID No: 610, SEQ ID No: 612, SEQ ID No: 614, SEQ ID No: 616, SEQ ID No: 618, SEQ ID No: 620, SEQ ID No: 622, SEQ ID No: 624, SEQ ID No: 626, SEQ ID No: 628, SEQ ID No: 630, SEQ ID No: 632, SEQ ID No: 634, SEQ ID No: 636, SEQ ID No: 638, SEQ ID No: 640, SEQ ID No: 642, SEQ ID No: 644, SEQ ID No: 646, SEQ ID No: 648, SEQ ID No: 650, SEQ ID No: 652, SEQ ID No: 654, SEQ ID No: 656, SEQ ID No: 658, SEQ ID No: 660, SEQ ID No: 662, SEQ ID No: 664, SEQ ID No: 666, SEQ ID No: 668, SEQ ID No: 670, SEQ ID No: 672, SEQ ID No: 674, SEQ ID No: 676, SEQ ID No: 678, SEQ ID No: 680, SEQ ID No: 682, SEQ ID No: 684, SEQ ID No: 686, SEQ ID No: 688, SEQ ID No: 690, SEQ ID No: 692, SEQ ID No: 694, SEQ ID No: 696, SEQ ID No: 698, SEQ ID No: 700, SEQ ID No: 702, SEQ ID No: 704, SEQ ID No: 706, SEQ ID No: 708, SEQ ID No: 710, SEQ ID No: 712, SEQ ID No: 714, SEQ ID No: 716, SEQ ID No: 718, SEQ ID No: 720, SEQ ID No: 722, SEQ ID No: 724, SEQ ID No: 726, SEQ ID No: 728, SEQ ID No: 730, SEQ ID No: 732, SEQ ID No: 734, SEQ ID No: 736, SEQ ID No: 738, SEQ ID No: 740, SEQ ID No: 742, SEQ ID No: 744, SEQ ID No: 746, SEQ ID No: 748, SEQ ID No: 750, SEQ ID No: 752, SEQ ID No: 754, SEQ ID No: 756, SEQ ID No: 758, SEQ ID No: 760, SEQ ID No: 762, SEQ ID No: 764, SEQ ID No: 766, SEQ ID No: 768, SEQ ID No: 770, SEQ ID No: 772, SEQ ID No: 774, SEQ ID No: 776, SEQ ID No: 778, SEQ ID No: 780, SEQ ID No: 782, SEQ ID No: 784, SEQ ID No: 786, SEQ ID No: 788, SEQ ID No: 790, SEQ ID No: 792, SEQ ID No: 794, SEQ ID No: 796, SEQ ID No: SEQ ID No: 798, SEQ ID No: 800, SEQ ID No: 802, SEQ ID No: 804, SEQ ID No: 806, SEQ ID No: 808, SEQ ID No: 810, SEQ ID No: 812, SEQ ID No: 814, SEQ ID No: 816, SEQ ID No: 818, SEQ ID No: 820, SEQ ID No: 822, SEQ ID No: 824, SEQ ID No: 826, SEQ ID No: 828, SEQ ID No: 830, SEQ ID No: 832, SEQ ID No: 834, SEQ ID No: 836, SEQ ID No: 838, SEQ ID No: 840, SEQ ID No: 842, SEQ ID No: 844, SEQ ID No: 846, SEQ ID No: 848, SEQ ID No: 850, SEQ ID No: 852, SEQ ID No: 854, SEQ ID No: 856, SEQ ID No: 858, SEQ ID No: 860, SEQ ID No: 862, SEQ ID No: 864, SEQ ID No: 866, SEQ ID No: 868, SEQ ID No: 870, SEQ ID No: 872, SEQ ID No: 874, SEQ ID No: 876, SEQ ID No: 878, SEQ ID No: 880, SEQ ID No: 882, SEQ ID No: 884, SEQ ID No: 886, SEQ ID No: 888, SEQ ID No: 890, SEQ ID No: 892, SEQ ID No: 894, SEQ ID No: 896, SEQ ID No: 898, SEQ ID No: 900, SEQ ID No: 902, SEQ ID No: 904, SEQ ID No: 906, SEQ ID No: 908, SEQ ID No: 910, SEQ ID No: 912, SEQ ID No: 914, SEQ ID No: 916, SEQ ID No: 918, SEQ ID No: 920, SEQ ID No: 922, SEQ ID No: 924, SEQ ID No: 926, SEQ ID No: 928, SEQ ID No: 930, SEQ ID No: 932, SEQ ID No: 934, SEQ ID No: 936, SEQ ID No: 938, SEQ ID No: 940, SEQ ID No: 942, SEQ ID No: 944, SEQ ID No: 946, SEQ ID No: 948, SEQ ID No: 950, SEQ ID No: 952, SEQ ID No: 954, SEQ ID No: 956, SEQ ID No: 958, SEQ ID No: 960, SEQ ID No: 962, SEQ ID No: 964, SEQ ID No: 966, SEQ ID No: 968, SEQ ID No: 970, SEQ ID No: 972, SEQ ID No: 974, SEQ ID No: 976, SEQ ID No: 978, SEQ ID No: 980, SEQ ID No: 982, SEQ ID No: 984, SEQ ID No: 986, SEQ ID No: 988, SEQ ID No: 990, SEQ ID No: 992, SEQ ID No: 994, SEQ ID No: 996, SEQ ID No: 998, SEQ ID No: 1000, SEQ ID No: 1002, SEQ ID No: 1004, SEQ ID No: 1006, SEQ ID No: 1008, SEQ ID No: 1010, SEQ ID No: 1012, SEQ ID No: 1014, SEQ ID No: 1016, SEQ ID No: 1018, SEQ ID No: 1020, SEQ ID No: 1022, SEQ ID No: 1024, SEQ ID No: 1026, SEQ ID No: 1028, SEQ ID No: 1030, SEQ ID No: 1032, SEQ ID No: 1034, SEQ ID No: 1036, SEQ ID No: 1038, SEQ ID No: 1040, SEQ ID No: 1042, SEQ ID No: 1044, SEQ ID No: 1046, SEQ ID No: 1048, SEQ ID No: 1050, SEQ ID No: 1052, SEQ ID No: 1054, SEQ ID No: 1056, SEQ ID No: 1058, SEQ ID No: 1060, SEQ ID No: 1062, SEQ ID No: 1064, SEQ ID No: 1066, SEQ ID No: 1068, SEQ ID No: 1070, SEQ ID No: 1072, SEQ ID No: 1074, SEQ ID No: 1076, SEQ ID No: 1078, SEQ ID No: 1080, SEQ ID No: 1082, SEQ ID No: 1084, SEQ ID No: 1086, SEQ ID No: 1088, SEQ ID No: 1090, SEQ ID No: 1092, SEQ ID No: 1094, SEQ ID No: 1096, SEQ ID No: 1098, SEQ ID NO: 1100, SEQ ID No: 1102, SEQ ID No: 1104, SEQ ID No: 1106, SEQ ID No: 1108, SEQ ID No: 1110, SEQ ID No: 1112, SEQ ID No: 1114, SEQ ID No: 1116, SEQ ID No: 1118, SEQ ID No: 1120, SEQ ID No: 1122, SEQ ID No: 1124, SEQ ID No: 1126, SEQ ID No: 1128, SEQ ID No: 1130, SEQ ID No: 1132, SEQ ID No: 1134, SEQ ID No: 1136, SEQ ID No: 1138, SEQ ID No: 1140, SEQ ID No: 1142, SEQ ID No: 1144, SEQ ID No: 1146, SEQ ID No: 1148, SEQ ID No: 1150, SEQ ID No: 1152, SEQ ID No: 1154, SEQ ID No: 1156, SEQ ID No: 1158, SEQ ID No: 1160, SEQ ID No: 1162, SEQ ID No: 1164, SEQ ID No: 1166, SEQ ID No: 1168, SEQ ID No: 1170, SEQ ID No: 1172, SEQ ID No: 1174, SEQ ID No: 1176, SEQ ID No: 1178, SEQ ID No: 1180, SEQ ID No: 1182, SEQ ID No: 1184, SEQ ID No: 1186, SEQ ID No: 1188, SEQ ID No: 1190, SEQ ID No: 1192, SEQ ID No: 1194, SEQ ID No: 1196, SEQ ID No: 1198, SEQ ID No: 1200, SEQ ID No: 1202, SEQ ID No: 1204, SEQ ID No: 1206, SEQ ID No: 1208, SEQ ID No: 1210, SEQ ID No: 1212, SEQ ID No: 1214, SEQ ID No: 1216, SEQ ID No: 1218, SEQ ID No: 1220, SEQ ID No: 1222, SEQ ID No: 1224, SEQ ID No: 1226, SEQ ID No: 1228, SEQ ID No: 1230, SEQ ID No: 1232, SEQ ID No: 1234, SEQ ID No: 1236, SEQ ID No: 1238, SEQ ID No: 1240, SEQ ID No: 1242, SEQ ID No: 1244, SEQ ID No: 1246, SEQ ID No: 1248, SEQ ID No: 1250, SEQ ID No: 1252, SEQ ID No: 1254, SEQ ID No: 1256, SEQ ID No: 1258, SEQ ID No: 1260, SEQ ID No: 1262, SEQ ID No: 1264, SEQ ID No: 1266, SEQ ID No: 1268, SEQ ID No: 1270, SEQ ID No: 1272, SEQ ID No: 1274, SEQ ID No: 1276, SEQ ID No: 1278, SEQ ID No: 1280, SEQ ID No: 1282, SEQ ID No: 1284, SEQ ID No: 1286, SEQ ID No: 1288, SEQ ID No: 1290, SEQ ID No: 1292, SEQ ID No: 1294, SEQ ID No: 1296, SEQ ID No: 1298, SEQ ID No: 1300, SEQ ID No: 1302, SEQ ID No: 1304, SEQ ID No: 1306, SEQ ID No: 1308, SEQ ID No: 1310, SEQ ID No: 1312, SEQ ID No: 1314, SEQ ID No: 1316, SEQ ID No: 1318, SEQ ID No: 1320, SEQ ID No: 1322, SEQ ID No: 1324, SEQ ID No: 1326, SEQ ID No: 1328, SEQ ID No: 1330, SEQ ID No: 1332, SEQ ID No: 1334, SEQ ID No: 1336, SEQ ID No: 1338, SEQ ID No: 1340, SEQ ID No: 1342, SEQ ID No: 1344, SEQ ID No: 1346, SEQ ID No: 1348, SEQ ID No: 1350, SEQ ID No: 1352, SEQ ID No: 1354, SEQ ID No: 1356, SEQ ID No: 1358, SEQ ID No: 1360, SEQ ID No: 1362, SEQ ID No: 1364, SEQ ID No: 1366, SEQ ID No: 1368, SEQ ID No: 1370, SEQ ID No: 1372, SEQ ID No: 1374, SEQ ID No: 1376, SEQ ID No: 1378, SEQ ID No: 1380, SEQ ID No: 1382, SEQ ID No: 1384, SEQ ID No: 1386, SEQ ID No: 1388, SEQ ID No: 1390, SEQ ID No: 1392, SEQ ID No: 1394, SEQ ID No: 1396, SEQ ID No: 1398, SEQ ID No: 1400, SEQ ID No: 1402, SEQ ID No: 1404, SEQ ID No: 1406, SEQ ID No: 1408, SEQ ID No: 1410, SEQ ID No: 1412, SEQ ID No: 1414, SEQ ID No: 1416, SEQ ID No: 1418, SEQ ID No: 1420, SEQ ID No: 1422, SEQ ID No: 1424, SEQ ID No: 1426, SEQ ID No: 1428, SEQ ID No: 1430, SEQ ID No: 1432, SEQ ID No: 1434, SEQ ID No: 1436, SEQ ID No: 1438, SEQ ID No: 1440, SEQ ID No: 1442, SEQ ID No: 1444, SEQ ID No: 1446, SEQ ID No: 1448, SEQ ID No: 1450, SEQ ID No: 1452, SEQ ID No: 1454, SEQ ID No: 1456, SEQ ID No: 1458, SEQ ID No: 1460, SEQ ID No: 1462, SEQ ID No: 1464, SEQ ID No: 1466, SEQ ID No: 1468, SEQ ID No: 1470, SEQ ID No: 1472, SEQ ID No: 1474, SEQ ID No: 1476, SEQ ID No: 1478, SEQ ID No: 1480, SEQ ID No: 1482, SEQ ID No: 1484, SEQ ID No: 1486, SEQ ID No: 1488, SEQ ID No: 1490, SEQ ID No: 1492, SEQ ID No: 1494, SEQ ID No: 1496, SEQ ID No: 1498, SEQ ID No: 1500, SEQ ID No: 1502, SEQ ID No: 1504, SEQ ID No: 1506, SEQ ID No: 1508, SEQ ID No: 1510, SEQ ID No: 1512, SEQ ID No: 1514, SEQ ID No: 1516, SEQ ID No: 1518, SEQ ID No: 1520, SEQ ID No: 1522, SEQ ID No: 1524, SEQ ID No: 1526, SEQ ID No: 1528, SEQ ID No: 1530, SEQ ID No: 1532, SEQ ID No: 1534, SEQ ID No: 1536, SEQ ID No: 1538, SEQ ID No: 1540, SEQ ID No: 1542, SEQ ID No: 1544, SEQ ID No: 1546, SEQ ID No: 1548, SEQ ID No: 1550, SEQ ID No: 1552, SEQ ID No: 1554, SEQ ID No: 1556, SEQ ID No: 1558, SEQ ID No: 1560, SEQ ID No: 1562, SEQ ID No: 1564, SEQ ID No: 1566, SEQ ID No: 1568, SEQ ID No: 1570, SEQ ID No: 1572, SEQ ID No: 1574, SEQ ID No: 1576, SEQ ID No: 1578, SEQ ID No: 1580, SEQ ID No: 1582, SEQ ID No: 1584, SEQ ID No: 1586, SEQ ID No: 1588, SEQ ID No: 1590, SEQ ID No: 1592, SEQ ID No: 1594, SEQ ID No: 1596, SEQ ID No: 1598, SEQ ID No: 1600, SEQ ID No: 1602, SEQ ID No: 1604, SEQ ID No: 1606, SEQ ID No: 1608, SEQ ID No: 1610, SEQ ID No: 1612, SEQ ID No: 1614, SEQ ID No: 1616, SEQ ID No: 1618, SEQ ID No: 1620, SEQ ID No: 1622, SEQ ID No: 1624, SEQ ID No: 1626, SEQ ID No: 1628, SEQ ID No: 1630, SEQ ID No: 1632, SEQ ID No: 1634, SEQ ID No: 1636, SEQ ID No: 1638, SEQ ID No: 1640, SEQ ID No: 1642, SEQ ID No: 1644, SEQ ID No: 1646, SEQ ID No: 1648, SEQ ID No: 1650, SEQ ID No: 1652, SEQ ID No: 1654, SEQ ID No: 1656, SEQ ID No: 1658, SEQ ID No: 1660, SEQ ID No: 1662, SEQ ID No: 1664, SEQ ID No: 1666, SEQ ID No: 1668, SEQ ID No: 1670, SEQ ID No: 1672, SEQ ID No: 1674, SEQ ID No: 1676, SEQ ID No: 1678, SEQ ID No: 1680, SEQ ID No: 1682, SEQ ID No: 1684, SEQ ID No: 1686, SEQ ID No: 1688, SEQ ID No: 1690, SEQ ID No: 1692, SEQ ID No: 1694, SEQ ID No: 1696, SEQ ID No: 1698, SEQ ID No: 1700, SEQ ID No: 1702, SEQ ID No: 1704, SEQ ID No: 1706, SEQ ID No: 1708, SEQ ID No: 1710, SEQ ID No: 1712, SEQ ID No: 1714, SEQ ID No: 1716, SEQ ID No: 1718, SEQ ID No: 1720, SEQ ID No: 1722, SEQ ID No: 1724, SEQ ID No: 1726, SEQ ID No: 1728, SEQ ID No: 1730, SEQ ID No: 1732, SEQ ID No: 1734, SEQ ID No: 1736, SEQ ID No: 1738, SEQ ID No: 1740, SEQ ID No: 1742, SEQ ID No: 1744, SEQ ID No: 1746, SEQ ID No: 1748, SEQ ID No: 1750, SEQ ID No: 1752, SEQ ID No: 1754, SEQ ID No: 1756, SEQ ID No: 1758, SEQ ID No: 1760, SEQ ID No: 1762, SEQ ID No: 1764, SEQ ID No: 1766, SEQ ID No: 1768, SEQ ID No: 1770, SEQ ID No: 1772, SEQ ID No: 1774, SEQ ID No: 1776, SEQ ID No: 1778, SEQ ID No: 1780, SEQ ID No: 1782, SEQ ID No: 1784, SEQ ID No: 1786, SEQ ID No: 1788, SEQ ID No: 1790, SEQ ID No: 1792, SEQ ID No: 1794, SEQ ID No: 1796, SEQ ID No: 1798, SEQ ID No: 1800, SEQ ID No: 1802, SEQ ID No: 1804, SEQ ID No: 1806, SEQ ID No: 1808, SEQ ID No: 1810, SEQ ID No: 1812, SEQ ID No: 1814, SEQ ID No: 1816, SEQ ID No: 1818, SEQ ID No: 1820, SEQ ID No: 1822, SEQ ID No: 1824, SEQ ID No: 1826, SEQ ID No: 1828, SEQ ID No: 1830, SEQ ID No: 1832, SEQ ID No: 1834, SEQ ID No: 1836, SEQ ID No: 1838, SEQ ID No: 1840, SEQ ID No: 1842, SEQ ID No: 1844, SEQ ID No: 1846, SEQ ID No: 1848, SEQ ID No: 1850, SEQ ID No: 1852, SEQ ID No: 1854, SEQ ID No: 1856, SEQ ID No: 1858, SEQ ID No: 1860, SEQ ID No: 1862, SEQ ID No: 1864, SEQ ID No: 1866, SEQ ID No: 1868, SEQ ID No: 1870, SEQ ID No: 1872, SEQ ID No: 1874, SEQ ID No: 1876, SEQ ID No: 1878, SEQ ID No: 1880, SEQ ID No: 1882, SEQ ID No: 1884, SEQ ID No: 1886, SEQ ID No: 1888, SEQ ID No: 1890, SEQ ID No: 1892, SEQ ID No: 1894, SEQ ID No: 1896, SEQ ID No: 1898, SEQ ID No: 1900, SEQ ID No: 1902, SEQ ID No: 1904, SEQ ID No: 1906, SEQ ID No: 1908, SEQ ID No: 1910, SEQ ID No: 1912, SEQ ID No: 1914, SEQ ID No: 1916, SEQ ID No: 1918, SEQ ID No: 1920, SEQ ID No: 1922, SEQ ID No: 1924, SEQ ID No: 1926, SEQ ID No: 1928, SEQ ID No: 1930, SEQ ID No: 1932, SEQ ID No: 1934, SEQ ID No: 1936, SEQ ID No: 1938, SEQ ID No: 1940, SEQ ID No: 1942, SEQ ID No: 1944, SEQ ID No: 1946, SEQ ID No: 1948, SEQ ID No: 1950, SEQ ID No: 1952, SEQ ID No: 1954, SEQ ID No: 1956, SEQ ID No: 1958, SEQ ID No: 1960, SEQ ID No: 1962, SEQ ID No: 1964, SEQ ID No: 1966, SEQ ID No: 1968, SEQ ID No: 1970, SEQ ID No: 1972, SEQ ID No: 1974.
In accordance with the present invention, an isolated nucleic acid molecule is a nucleic acid molecule (polynucleotide) that has been removed from its natural milieu (i.e., that has been subject to human manipulation) and can include DNA, RNA, or derivatives of either DNA or RNA, including cDNA. As such, "isolated" does not reflect the extent to which the nucleic acid molecule has been purified. Although the phrase "nucleic acid molecule" primarily refers to the physical nucleic acid molecule, and the phrase "nucleic acid sequence" primarily refers to the sequence of nucleotides on the nucleic acid molecule, the two phrases can be used interchangeably, especially with respect to a nucleic acid molecule, or a nucleic acid sequence, being capable of encoding a protein. An isolated nucleic acid molecule of the present invention can be isolated from its natural source or produced using recombinant DNA technology (e.g., polymerase chain reaction (PCR) amplification, cloning) or chemical synthesis. Isolated nucleic acid molecules can include, for example, genes, natural allelic variants of genes, coding regions or portions thereof, and coding and/or regulatory regions modified by nucleotide insertions, deletions, substitutions, and/or inversions in a manner such that the modifications do not substantially interfere with the nucleic acid molecule's ability to encode a protein of the present invention or to form stable hybrids under stringent conditions with natural gene isolates. An isolated nucleic acid molecule can include degeneracies. As used herein, nucleotide degeneracy refers to the phenomenon that one amino acid can be encoded by different nucleotide codons. Thus, the nucleic acid sequence of a nucleic acid molecule that encodes a protein of the present invention can vary due to degeneracies. It is noted that a nucleic acid molecule of the present invention is not required to encode a protein having protein activity. A nucleic acid molecule can encode a truncated, mutated or inactive protein, for example. In addition, nucleic acid molecules of the invention are useful as probes and primers for the identification, isolation and/or purification of other nucleic acid molecules. If the nucleic acid molecule is an oligonucleotide, such as a probe or primer, the oligonucleotide preferably ranges from about 5 to about 50 or about 500 nucleotides, more preferably from about 10 to about 40 nucleotides, and most preferably from about 15 to about 40 nucleotides in length.
[01133] According to the present invention, reference to a gene includes all nucleic acid sequences related to a natural (i.e. wild-type) gene, such as regulatory regions that control production of the protein encoded by that gene (such as, but not limited to, transcription, translation or post-translation control regions) as well as the coding region itself. In another embodiment, a gene can be a naturally occurring allelic variant that includes a similar but not identical sequence to the nucleic acid sequence encoding a given protein. Allelic variants have been previously described above. Genes can include or exclude one or more introns or any portions thereof or any other sequences or which are not included in the cDNA for that protein. The phrases "nucleic acid molecule" and "gene" can be used interchangeably when the nucleic acid molecule comprises a gene as described above.
[01134] Preferably, an isolated nucleic acid molecule of the present invention is produced using recombinant DNA technology (e.g., polymerase chain reaction (PCR) amplification, cloning, etc.) or chemical synthesis. Isolated nucleic acid molecules include any nucleic acid molecules and homologues or variants thereof that are part of a gene described herein and/or that encode a protein described herein, including, but not limited to, natural allelic variants and modified nucleic acid molecules (homologues or variants) in which nucleotides have been inserted, deleted, substituted, and/or inverted in such a manner that such modifications provide the desired effect on protein biological activity or on the activity of the nucleic acid molecule. Allelic variants and protein homologues or variants (e.g., proteins encoded by nucleic acid homologues or variants) have been discussed in detail above.
[01135] A nucleic acid molecule homologue or variant (i.e., encoding a homologue or variant of a protein of the present invention) can be produced using a number of methods known to those skilled in the art (see, for example, Sambrook et al.). For example, nucleic acid molecules can be modified using a variety of techniques including, but not limited to, by classic mutagenesis and recombinant DNA techniques (e.g., site-directed mutagenesis, chemical treatment, restriction enzyme cleavage, ligation of nucleic acid fragments and/or PCR amplification), or synthesis of oligonucleotide mixtures and ligation of mixture groups to "build" a mixture of nucleic acid molecules and combinations thereof. Another method for modifying a recombinant nucleic acid molecule encoding a protein is gene shuffling (i.e., molecular breeding) (See, for example, U.S. Patent No. 5,605,793 to Stemmer; Minshull and Stemmer; 1999, Curr. Opin. Chem. Biol. 3:284-290; Stemmer, 1994, P.N.A.S. USA 91 : 10747-10751). This technique can be used to efficiently introduce multiple simultaneous changes in the protein. Nucleic acid molecule homologues or variants can be selected by hybridization with a gene or polynucleotide, or by screening for the function of a protein encoded by a nucleic acid molecule (i.e., biological activity).
[01136] The minimum size of a nucleic acid molecule of the present invention is a size sufficient to encode a protein (including a fragment, homologue, or variant of a full-length protein) having biological activity, sufficient to encode a protein comprising at least one epitope which binds to an antibody, or sufficient to form a probe or oligonucleotide primer that is capable of fomiing a stable hybrid with the complementary sequence of a nucleic acid molecule encoding a natural protein (e.g., under moderate, high, or high stringency conditions). As such, the size of the nucleic acid molecule encoding such a protein can be dependent on nucleic acid composition and percent homology or identity between the nucleic acid molecule and complementary sequence as well as upon hybridization conditions per se (e.g., temperature, salt concentration, and formamide concentration). The minimal size of a nucleic acid molecule that is used as an oligonucleotide primer or as a probe is typically at least about 12 to about 15 nucleotides in length if the nucleic acid molecules are GC-rich and at least about 15 to about 18 bases in length if they are AT -rich. There is no limit, other than a practical limit, on the maximal size of a nucleic acid molecule of the present invention, in that the nucleic acid molecule can include a portion of a protein encoding sequence, a nucleic acid sequence encoding a full-length protein (including a gene), including any length fragment between about 20 nucleotides and the number of nucleotides that make up the full length cDNA encoding a protein, in whole integers (e.g., 20, 21, 22, 23, 24, 25 nucleotides), or multiple genes, or portions thereof.
[01137] The phrase "consisting essentially of, when used with reference to a nucleic acid sequence herein, refers to a nucleic acid sequence encoding a specified amino acid sequence that can be flanked by from at least one, and up to as many as about 60, additional heterologous nucleotides at each of the 5' and/or the 3' end of the nucleic acid sequence encoding the specified amino acid sequence. The heterologous nucleotides are not naturally found (i.e., not found in nature, in vivo) flanking the nucleic acid sequence encoding the specified amino acid sequence as it occurs in the natural gene or do not encode a protein that imparts any additional function to the protein or changes the function of the protein having the specified amino acid sequence.
[01138] In one embodiment, the polynucleotide probes or primers of the invention are conjugated to detectable markers. Detectable labels suitable for use in the present invention include any composition detectable by spectroscopic, photochemical, biochemical, immunochemical, electrical, optical or chemical means. Useful labels in the present invention include biotin for staining with labeled streptavidin conjugate, magnetic beads (e.g., Dynabeads™), fluorescent dyes (e.g., fluorescein, texas red, rhodamine, green fluorescent protein, and the like),
3 125 35 14 32
radiolabels (e.g., H, I, S, C, or P), enzymes (e.g., horse radish peroxidase, alkaline phosphatase and others commonly used in an ELISA), and colorimetric labels such as colloidal gold or colored glass or plastic (e.g., polystyrene, polypropylene, latex, etc.) beads. Preferably, the polynucleotide probes are immobilized on a substrate such as: artificial membranes, organic supports, biopolymer supports and inorganic supports.
[01139] One embodiment of the present invention relates to a recombinant nucleic acid molecule which comprises the isolated nucleic acid molecule described above which is operatively linked to at least one expression control sequence. More particularly, according to the present invention, a recombinant nucleic acid molecule typically comprises a recombinant vector and any one or more of the isolated nucleic acid molecules as described herein. According to the present invention, a recombinant vector is an engineered (i.e., artificially produced) nucleic acid molecule that is used as a tool for manipulating a nucleic acid sequence of choice and/or for introducing such a nucleic acid sequence into a host cell. The recombinant vector is therefore suitable for use in cloning, sequencing, and/or otherwise manipulating the nucleic acid sequence of choice, such as by expressing and/or delivering the nucleic acid sequence of choice into a host cell to form a recombinant cell. Such a vector typically contains nucleic acid sequences that are not naturally found adjacent to nucleic acid sequence to be cloned or delivered, although the vector can also contain regulatory nucleic acid sequences (e.g., promoters, untranslated regions) which are naturally found adjacent to nucleic acid sequences of the present invention or which are useful for expression of the nucleic acid molecules of the present invention (discussed in detail below). The vector can be either R A or DNA, either prokaryotic or eukaryotic, and typically is a plasmid. The vector can be maintained as an extrachromosomal element (e.g., a plasmid) or it can be integrated into the chromosome of a recombinant host cell, although it is preferred if the vector remains separate from the genome for most applications of the invention. The entire vector can remain in place within a host cell, or under certain conditions, the plasmid DNA can be deleted, leaving behind the nucleic acid molecule of the present invention. An integrated nucleic acid molecule can be under chromosomal promoter control, under native or plasmid promoter control, or under a combination of several promoter controls. Single or multiple copies of the nucleic acid molecule can be integrated into the chromosome. A recombinant vector of the present invention can contain at least one selectable marker.
[01140] In one embodiment, a recombinant vector used in a recombinant nucleic acid molecule of the present invention is an expression vector. As used herein, the phrase "expression vector" is used to refer to a vector that is suitable for production of an encoded product (e.g., a protein of interest, such as an enzyme of the present invention). In this embodiment, a nucleic acid sequence encoding the product to be produced (e.g., the protein or homologue or variant thereof) is inserted into the recombinant vector to produce a recombinant nucleic acid molecule. The nucleic acid sequence encoding the protein to be produced is inserted into the vector in a manner that operatively links the nucleic acid sequence to regulatory sequences in the vector which enable the transcription and translation of the nucleic acid sequence within the recombinant host cell.
[01 141] Typically, a recombinant nucleic acid molecule includes at least one nucleic acid molecule of the present invention operatively linked to one or more expression control sequences (e.g., transcription control sequences or translation control sequences). As used herein, the phrase "recombinant molecule" or "recombinant nucleic acid molecule" primarily refers to a nucleic acid molecule or nucleic acid sequence operatively linked to a transcription control sequence, but can be used interchangeably with the phrase "nucleic acid molecule", when such nucleic acid molecule is a recombinant molecule as discussed herein. According to the present invention, the phrase "operatively linked" refers to linking a nucleic acid molecule to an expression control sequence in a manner such that the molecule is able to be expressed when transfected (i.e., transformed, transduced, transfected, conjugated or conduced) into a host cell. Transcription control sequences are sequences which control the initiation, elongation, or termination of transcription. Particularly important transcription control sequences are those which control transcription initiation, such as promoter, enhancer, operator and repressor sequences. Suitable transcription control sequences include any transcription control sequence that can function in a host cell or organism into which the recombinant nucleic acid molecule is to be introduced. Transcription control sequences may also include any combination of one or more of any of the foregoing.
[01 142] Recombinant nucleic acid molecules of the present invention can also contain additional regulatory sequences, such as translation regulatory sequences, origins of replication, and other regulatory sequences that are compatible with the recombinant cell. In one embodiment, a recombinant molecule of the present invention, including those which are integrated into the host cell chromosome, also contains secretory signals (i.e., signal segment nucleic acid sequences) to enable an expressed protein to be secreted from the cell that produces the protein. Suitable signal segments include a signal segment that is naturally associated with the protein to be expressed or any heterologous signal segment capable of directing the secretion of the protein according to the present invention. In another embodiment, a recombinant molecule of the present invention comprises a leader sequence to enable an expressed protein to be delivered to and inserted into the membrane of a host cell. Suitable leader sequences include a leader sequence that is naturally associated with the protein, or any heterologous leader sequence capable of directing the delivery and insertion of the protein to the membrane of a cell.
[01 143] According to the present invention, the term "transfection" is generally used to refer to any method by which an exogenous nucleic acid molecule (i.e., a recombinant nucleic acid molecule) can be inserted into a cell. The term "transformation" can be used interchangeably with the term "transfection" when such term is used to refer to the introduction of nucleic acid molecules into microbial cells or plants and describes an inherited change due to the acquisition of exogenous nucleic acids by the microorganism that is essentially synonymous with the term "transfection." Transfection techniques include, but are not limited to, transformation, particle bombardment, electroporation, microinjection, lipofection, adsorption, infection and protoplast fusion.
[01 144] One or more recombinant molecules of the present invention can be used to produce an encoded product (e.g., a protein) of the present invention. In one embodiment, an encoded product is produced by expressing a nucleic acid molecule as described herein under conditions effective to produce the protein. A preferred method to produce an encoded protein is by transfecting a host cell with one or more recombinant molecules to form a recombinant cell. Suitable host cells to transfect include, but are not limited to, any bacterial, fungal (e.g., filamentous fungi or yeast or mushrooms), algal, plant, insect, or animal cell that can be transfected. Host cells can be either untransfected cells or cells that are already transfected with at least one other recombinant nucleic acid molecule.
[01 145] Suitable cells (e.g., a host cell or production organism) may include any microorganism (e.g., a bacterium, a protist, an alga, a fungus, or other microbe), and is preferably a bacterium, a yeast or a filamentous fungus. Suitable bacterial genera include, but are not limited to, Escherichia, Bacillus, Lactobacillus, Pseudomonas and Streptomyces . Suitable bacterial species include, but are not limited to, Escherichia coli, Bacillus subtilis, Bacillus licheniformis, Bacillus Stearothermophilus, Lactobacillus brevis, Pseudomonas aeruginosa and Streptomyces lividans. Suitable genera of yeast include, but are not limited to, Saccharomyces, Schizosaccharomyces, Candida, Hansenula, Pichia, Kluyveromyces, and Phaffia. Suitable yeast species include, but are not limited to, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Candida albicans, Hansenula polymorpha, Pichia pastoris, P. canadensis, Kluyveromyces marxianus and Phaffia rhodozyma.
] Suitable fungal genera include, but are not limited to, Chrysosporium,
Thielavia, Neurospora, Aureobasidium, Filibasidium, Piromyces, Corynascus, Cryptococcus, Acremonium, Tolypocladium, Scytalidium, Schizophyllum, Sporotrichum, Penicillium, Gibberella, Myceliophthora, Mucor, Aspergillus, Fusarium, Humicola, and Trichoderma, and anamorphs and teleomorphs thereof. Suitable fungal species include, but are not limited to, Aspergillus niger, Aspergillus oryzae, Aspergillus nidulans, Aspergillus japonicus, Absidia coerulea, Rhizopus oryzae, Myceliophthora thermophila, Neurospora crassa, Neurospora intermedia, Trichoderma reesei, Trichoderma longibrachiatum, Penicillium canescens, Penicillium solitum, Penicillium funiculosum, Myceliophthora thermophila, Acremonium alabamense, Thielavia terrestris, Sporotrichum thermophile, Sporotrichum cellulophilum, Chaetomium globosum, Corynascus heterothallicus, and Talaromyces flavus. In another embodiment, a while (low cellulose) strain is sued. In one embodiment, the host cell is a fungal cell of Strain CI (VKM F-3500-D) or a mutant strain derived therefrom {e.g., UV13-6 (Accession No. VKM F-3632 D); NG7C-19 (Accession No. VKM F-3633 D); UV18-25 (VKM F-3631D), W1L (CBS122189), or W1L#100L (CBS122190)). The CI strain was initially classified as Myceliophthora thermophila based on morphological characteristics and was subsequently reclassified as M. thermophila based on genetic tests. Host cells can be either untransfected cells or cells that are already transfected with at least one other recombinant nucleic acid molecule. Additional embodiments of the present invention include any of the genetically modified cells described herein. [01147] In another embodiment, suitable host cells include insect cells (most particularly Drosophila melanogaster cells, Spodoptera frugiperda Sf9 and Sf21 cells and Trichoplusa High-Five cells), nematode cells (particularly C. elegans cells), avian cells, amphibian cells (particularly Xenopus laevis cells), reptilian cells, and mammalian cells (most particularly human, simian, canine, rodent, bovine, or sheep cells, e.g. NIH3T3, CHO (Chinese hamster ovary cell), COS, VERO, BHK, HEK, and other rodent or human cells).
[01148] In one embodiment, one or more protein(s) expressed by an isolated nucleic acid molecule of the present invention are produced by culturing a cell that expresses the protein (i.e., a recombinant cell or recombinant host cell) under conditions effective to produce the protein. In some instances, the protein may be recovered, and in others, the cell may be harvested in whole, either of which can be used in a composition.
[01149] Microorganisms used in the present invention (including recombinant host cells or genetically modified microorganisms) are cultured in an appropriate fermentation medium. An appropriate, or effective, fermentation medium refers to any medium in which a cell of the present invention, including a genetically modified microorganism (described below), when cultured, is capable of expressing enzymes useful in the present invention and/or of catalyzing the production of sugars from lignocellulosic biomass. The microorganisms can be cultured by any fermentation process which includes, but is not limited to, batch, fed-batch, cell recycle, and continuous fermentation. In general the fungal strains are grown in fermentors, optionally centrifuged or filtered to remove biomass, and optionally concentrated, formulated, and dried to produce an enzyme(s) or a multi-enzyme composition that is a crude fermentation product. Particularly suitable conditions for culturing filamentous fungi are described, for example, in U.S. Patent No. 6,015,707 and U.S. Patent No. 6,573,086, supra.
[01150] Depending on the vector and host system used for production, resultant proteins of the present invention may either remain within the recombinant cell; be secreted into the culture medium; be secreted into a space between two cellular membranes; or be retained on the outer surface of a cell membrane. The phrase "recovering the protein" refers to collecting the whole culture medium containing the protein and need not imply additional steps of separation or purification. Proteins produced according to the present invention can be purified using a variety of standard protein purification techniques, such as, but not limited to, affinity chromatography, ion exchange chromatography, filtration, electrophoresis, hydrophobic interaction chromatography, gel filtration chromatography, reverse phase chromatography, concanavalin A chromatography, chromato focusing and differential precipitation or solubilization.
[01151] Proteins of the present invention are preferably retrieved, obtained, and/or used in "substantially pure" form. As used herein, "substantially pure" refers to a purity that allows for the effective use of the protein in any method according to the present invention. For a protein to be useful in any of the methods described herein or in any method utilizing enzymes of the types described herein according to the present invention, it is substantially free of contaminants, other proteins and/or chemicals that might interfere or that would interfere with its use in a method disclosed by the present invention (e.g., that might interfere with enzyme activity), or that at least would be undesirable for inclusion with a protein of the present invention (including homologues and variants) when it is used in a method disclosed by the present invention (described in detail below). Preferably, a "substantially pure" protein, as referenced herein, is a protein that can be produced by any method (i.e., by direct purification from a natural source, recombinantly, or synthetically), and that has been purified from other protein components such that the protein comprises at least about 80% weight/weight of the total protein in a given composition (e.g., the protein of interest is about 80% of the protein in a solution/composition/buffer), and more preferably, at least about 85%, and more preferably at least about 90%, and more preferably at least about 91%, and more preferably at least about 92%, and more preferably at least about 93%, and more preferably at least about 94%, and more preferably at least about 95%, and more preferably at least about 96%, and more preferably at least about 97%, and more preferably at least about 98%>, and more preferably at least about 99%, weight/weight of the total protein in a given composition.
[01152] It will be appreciated by one skilled in the art that use of recombinant DNA technologies can improve control of expression of transfected nucleic acid molecules by manipulating, for example, the number of copies of the nucleic acid molecules within the host cell, the efficiency with which those nucleic acid molecules are transcribed, the efficiency with which the resultant transcripts are translated, and the efficiency of post-translational modifications. Additionally, the promoter sequence might be genetically engineered to improve the level of expression as compared to the native promoter. Recombinant techniques useful for controlling the expression of nucleic acid molecules include, but are not limited to, integration of the nucleic acid molecules into one or more host cell chromosomes, addition of vector stability sequences to plasmids, substitutions or modifications of transcription control signals (e.g., promoters, operators, enhancers), substitutions or modifications of translational control signals (e.g., ribosome binding sites), modification of nucleic acid molecules to correspond to the codon usage of the host cell, and deletion of sequences that destabilize transcripts.
[01153] Another aspect of the present invention relates to a genetically modified microorganism that has been transfected with one or more nucleic acid molecules of the present invention. As used herein, a genetically modified microorganism can include a genetically modified bacterium, alga, yeast, filamentous fungus, or other microbe. Such a genetically modified microorganism has a genome which is modified (i.e., mutated or changed) from its normal (i.e., wild-type or naturally occurring) form such that the desired result is achieved (i.e., increased or modified activity and/or production of at least one enzyme or a multi-enzyme composition for the conversion of lignocellulosic material to fermentable sugars). Genetic modification of a microorganism can be accomplished using classical strain development and/or molecular genetic techniques. Such techniques known in the art and are generally disclosed for microorganisms, for example, in Sambrook et al, 1989, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Labs Press or Molecular Cloning: A Laboratory Manual, third edition (Sambrook and Russel, 2001), (jointly referred to herein as "Sambrook"). A genetically modified microorganism can include a microorganism in which nucleic acid molecules have been inserted, deleted or modified (i.e., mutated; e.g., by insertion, deletion, substitution, and/or inversion of nucleotides), in such a manner that such modifications provide the desired effect within the microorganism.
[01154] In one embodiment, a genetically modified microorganism can endogenously contain and express an enzyme or a multi-enzyme composition and the genetic modification can be a genetic modification of one or more of such endogenous enzymes, whereby the modification has some effect on the amount and/or quality of enzyme mixtures produced by the organism of the microorganism (e.g., increased expression of the protein by introduction of promoters or other expression control sequences, or modification of the coding region by homologous recombination to increase the activity of the encoded protein).
[01 155] In another embodiment, a genetically modified microorganism can endogenously contain and express an enzyme for the catalysis of oxidation- reduction reactions, and the genetic modification can be an introduction of at least one exogenous nucleic acid sequence (e.g., a recombinant nucleic acid molecule), wherein the exogenous nucleic acid sequence encodes at least one additional enzyme useful for the catalysis of oxidation-reduction reactions and/or a protein that improves the efficiency of the target enzyme. In this aspect of the invention, the microorganism can also have at least one modification to a gene or genes comprising its endogenous enzyme(s) for the catalysis of oxidation-reduction reactions or an enzyme to aid in the conversion of lignocellulosic material.
[01 156] In yet another embodiment, the genetically modified microorganism does not necessarily endogenously (naturally) contain an enzyme for the catalysis of oxidation-reduction reactions, but is genetically modified to introduce at least one recombinant nucleic acid molecule encoding at least one enzyme or a multiplicity of enzymes for the catalysis of oxidation-reduction reactions. Such a microorganism can be used in a method of the invention, or as a production microorganism for crude fermentation products, partially purified recombinant enzymes, and/or purified recombinant enzymes, any of which can then be used in a method of the present invention.
[01 157] Once the proteins (enzymes) are expressed in a host cell, a cell extract that contains the activity to test can be generated. For example, a lysate from the host cell is produced, and the supernatant containing the activity is harvested and/or the activity can be isolated from the lysate. In the case of cells that secrete enzymes into the culture medium, the culture medium containing them can be harvested, and/or the activity can be purified from the culture medium. The extracts/activities prepared in this way can be tested using assays known in the art.
[01 158] The present invention is not limited to fungi and also contemplates genetically modified organisms such as algae, bacterial, and plants transformed with one or more nucleic acid molecules of the invention. The plants may be used for production of the enzymes, and/or as the lignocellulosic material used as a substrate in the methods of the invention. Methods to generate recombinant plants are known in the art. For instance, numerous methods for plant transformation have been developed, including biological and physical transformation protocols. See, for example, Miki et al, "Procedures for Introducing Foreign DNA into Plants" in Methods in Plant Molecular Biology and Biotechnology, Glick, B.R. and Thompson, J.E. Eds. (CRC Press, Inc., Boca Raton, 1993) pp. 67-88. In addition, vectors and in vitro culture methods for plant cell or tissue transformation and regeneration of plants are available. See, for example, Gruber et al, "Vectors for Plant Transformation" in Methods in Plant Molecular Biology and Biotechnology, Glick, B.R. and Thompson, J.E. Eds. (CRC Press, Inc., Boca Raton, 1993) pp. 89- 119.
[01159] The most widely utilized method for introducing an expression vector into plants is based on the natural transformation system of Agrobacterium. See, for example, Horsch et al, Science 227: 1229 (1985). Descriptions of Agrobacterium vector systems and methods for Agrobacterium-mediated gene transfer are provided by numerous references, including Gruber et al, supra, Miki et al, supra, Moloney et al, Plant Cell Reports 8:238 (1989), and U.S. Patents Nos. 4,940,838 and 5,464,763.
[01160] Another generally applicable method of plant transformation is microprojectile-mediated transformation, see e.gSanford et al, Part. Sci. Technol. 5:27 (1987), Sanford, J.C., Trends Biotech. 6:299 (1988), Sanford, J.C., Physiol. Plant 79:206 (1990), Klein et al, Biotechnology 10:268 (1992).
[01161] Another method for physical delivery of DNA to plants is sonication of target cells. Zhang et al, Bio/Technology 9:996 (1991). Alternatively, liposome or spheroplast fusion have been used to introduce expression vectors into plants. Deshayes et al, EMBO J., 4:2731 (1985), Christou et al, Proc Natl. Acad. Sci. USA 84:3962 (1987). Direct uptake of DNA into protoplasts using CaCl2 precipitation, polyvinyl alcohol or poly-L-ornithine have also been reported. Haiti et al, Mol. Gen. Genet. 199: 161 (1985) and Draper et al, Plant Cell Physiol. 23:451 (1982). Electroporation of protoplasts and whole cells and tissues have also been described. Donn et al, In Abstracts of Vllth International Congress on Plant Cell and Tissue Culture IAPTC, A2-38, p. 53 (1990); D'Halluin et al, Plant Cell 4: 1495-1505 (1992) and Spencer et al, Plant Mol. Biol. 24:51-61 (1994).
[01162] Some embodiments of the present invention include genetically modified organisms comprising at least one nucleic acid molecule encoding at least one enzyme of the present invention, in which the activity of the enzyme is downregulated. The downregulation may be achieved, for example, by introduction of inhibitors (chemical or biological) of the enzyme activity, by manipulating the efficiency with which those nucleic acid molecules are transcribed, the efficiency with which the resultant transcripts are translated, and the efficiency of post- translational modifications, or by "knocking out" the endogenous copy of the gene. A "knock out" of a gene refers to a molecular biological technique by which the gene in the organism is made inoperative, so that the expression of the gene is substantially reduced or eliminated. Alternatively, in some embodiments the activity of the enzyme may be upregulated. The present invention also contemplates downregulating activity of one or more enzymes while simultaneously upregulating activity of one or more enzymes to achieve the desired outcome.
[01163] Proteins of the present invention, at least one protein of the present invention, compositions comprising such protein(s) of the present invention, and multi-enzyme compositions (examples of which are described above) may be used in any method where it is desirable to hydro lyze glycosidic linkages in lignocellulosic material, or any other method wherein enzymes of the same or similar function are useful.
[01164] In one embodiment, the present invention includes the use of at least one protein of the present invention, compositions comprising at least one protein of the present invention, or multi-enzyme compositions in methods for hydrolyzing ligno cellulose and the generation of fermentable sugars therefrom. In one embodiment, the method comprises contacting the lignocellulosic material with an effective amount of one or more proteins of the present invention, composition comprising at least one protein of the present invention, or a multi-enzyme composition, whereby at least one fermentable sugar is produced (liberated). The lignocellulosic material may be partially or completely Icosts are contemplated.
[01165] Typically, the amount of enzyme or enzyme composition contacted with the ligno cellulose will depend upon the amount of glucan present in the ligno cellulose. In some embodiments, the amount of enzyme or enzyme composition contacted with the ligno cellulose may be from about 0.1 to about 200 mg enzyme or enzyme composition per gram of glucan; in other embodiments, from about 3 to about 20 mg enzyme or enzyme composition per gram of glucan. The invention encompasses the use of any suitable or sufficient amount of enzyme or enzyme composition between about 0.1 mg and about 200 mg enzyme per gram glucan, in increments of 0.05 mg (i.e., 0.1 mg, 0.15 mg, 0.2 mg... 199.9 mg, 199.95 mg, 200 mg).
[01166] In a further embodiment, the invention provides a method for degrading
DDG, preferably, but not limited to, DDG derived from corn, to sugars. The method comprises contacting the DDG with a protein of the present invention, a composition comprising at least one protein of the present invention, or a multi- enzyme composition. In certain embodiments, at least 10% of fermentable sugars are liberated. In other embodiment, the at least 15% of the sugars are liberated, or at least 20%> of the sugars are liberated, or at least 23% of the sugars are liberated, or at least 24% of the sugars are liberated, or at least 25% of the sugars are liberated, or at least 26% of the sugars are liberated, or at least 27% of the sugars are liberated, or at least 28% of the sugars are liberated.
[01167] In another embodiment, the invention provides a method for producing fermentable sugars comprising cultivating a genetically modified microorganism of the present invention in a nutrient medium comprising a ligno cellulo sic material, whereby fermentable sugars are produced.
[01168] Also provided are methods that comprise further contacting the ligno cellulo sic material with at least one accessory enzyme. Accessory enzymes have been described elsewhere herein. The accessory enzyme or enzymes may be added at the same time, prior to, or following the addition of a protein of the present invention, a composition comprising at least one protein of the present invention, or a multi-enzyme composition, or can be expressed (endogenously or overexpressed) in a genetically modified microorganism used in a method of the invention. When added simultaneously, the protein of the present invention, a composition comprising at least one protein of the present invention, or a multi- enzyme composition will be compatible with the accessory enzymes selected. When the enzymes are added following the treatment with the protein of the present invention, a composition comprising at least one protein of the present invention, or a multi-enzyme composition, the conditions (such as temperature and pH) may be altered to those optimal for the accessory enzyme before, during, or after addition of the accessory enzyme. Multiple rounds of enzyme addition are also encompassed. The accessory enzyme may also be present in the lignocellulosic material itself as a result of genetically modifying the plant. The nutrient medium used in a fermentation can also comprise one or more accessory enzymes.
[01169] In some embodiments, the method comprises a pretreatment process. In general, a pretreatment process will result in components of the ligno cellulose being more accessible for downstream applications or so that it is more digestible by enzymes following treatment in the absence of hydrolysis. The pretreatment can be a chemical, physical or biological pretreatment. The ligno cellulose may have been previously treated to release some or all of the sugars, as in the case of DDG. Physical treatments, such as grinding, boiling, freezing, milling, vacuum infiltration, and the like may also be used with the methods of the invention. In one embodiment, the heat treatment comprises heating the lignocellulosic material to 121°C for 15 minutes. A physical treatment such as milling can allow a higher concentration of ligno cellulose to be used in the methods of the invention. A higher concentration refers to about 20%, up to about 25%, up to about 30%>, up to about 35%), up to about 40%>, up to about 45%, or up to about 50%> ligno cellulose. The ligno cellulose may also be contacted with a metal ion, ultraviolet light, ozone, and the like. Additional pretreatment processes are known to those skilled in the art, and can include, for example, organosolv treatment, steam explosion treatment, lime impregnation with steam explosion treatment, hydrogen peroxide treatment, hydrogen peroxide/ozone (peroxone) treatment, acid treatment, dilute acid treatment, and base treatment, including ammonia fiber explosion (AFEX) technology. Details on pretreatment technologies and processes can be found in Wyman et al, Bioresource Tech. 96: 1959 (2005); Wyman et al, Bioresource Tech. 96:2026(2005); Hsu, "Pretreatment of biomass" In Handbook on Bioethanol: Production and Utilization, Wyman, Taylor and Francis Eds., p. 179- 212 (1996); and Mosier et al, Bioresource Tech. 96:673 (2005).
[01170] In some embodiments, the methods may be performed one or more times in whole or in part. That is, one may perform one or more pretreatments, followed by one or more reactions with a protein of the present invention, composition or product of the present invention and/or accessory enzyme. The enzymes may be added in a single dose, or may be added in a series of small doses. Further, the entire process may be repeated one or more times as necessary. Therefore, one or more additional treatments with heat and enzymes are contemplated.
[01171] The methods described above result in the production of fermentable sugars.
During, or subsequent to the methods described, the fermentable sugars may be recovered and/or purified by any method known in the art. The sugars can be subjected to further processing; e.g., they can also be sterilized, for example, by filtration.
[01172] In an additional embodiment, the invention provides a method for producing an organic substance, comprising saccharifying a lignocellulosic material with an effective amount of a protein of the present invention or a composition comprising at least one protein of the present invention, fermenting the saccharified lignocellulosic material obtained with one or more fermentating microorganisms, and recovering the organic substance from the fermentation. Sugars released from biomass can be converted to useful fermentation products including but not limited to amino acids, vitamins, pharmaceuticals, animal feed supplements, specialty chemicals, chemical feedstocks, plastics, solvents, fuels, or other organic polymers, lactic acid, and ethanol, including fuel ethanol. Specific products that may be produced by the methods of the invention include, but not limited to, biofuels (including ethanol); lactic acid; plastics; specialty chemicals; organic acids, including citric acid, succinic acid, itaconic and maleic acid; solvents; animal feed supplements; pharmaceuticals; vitamins; amino acids, such as lysine, methionine, tryptophan, threonine, and aspartic acid; industrial enzymes, such as proteases, cellulases, amylases, glucanases, lactases, lipases, lyases, oxidoreductases, and transferases; and chemical feedstocks. The methods of the invention are also useful to generate feedstocks for fermentation by fermenting microorganisms. In one embodiment, the method further comprises the addition of at least one fermenting organism.
[01173] As used herein, "fermenting organism" refers to an organism capable of fermentation, such as bacteria and fungi, including yeast. Such feedstocks have additional nutritive value above the nutritive value provided by the liberated sugars. [01174] In some embodiments the invention comprises, but is not limited to methods for oxidoreductases in the food industry, such as use as a disinfectant; cleaning/washing of vegetables; bleaching flour; improving the structure of baking products; treating bakery products, removing off-flavor from milk or beer, increasing shelf life of foodstuff and beverages and producing xylitol and other sugar alcohols such as sorbitol.
[01175] In some embodiments the invention comprises, but is not limited to methods for oxidoreductases in the printing and publising industry, such as bleaching pulp.
[01176] In some embodiments the invention comprises, but is not limited to methods for oxidoreductases in the biofuel industry, such as lignin degradation.
[01177] In some embodiments the invention comprises, but is not limited to methods for oxidoreductase in the medical industry, such as enzymatic absorbent materials such as bandages and pads for the production of hydrogen peroxide upon contact of the oxidoreductase with serum.
[01178] In some embodiments the invention comprises, but is not limited to methods for oxidoreductases in the synthesis of pharmaceuticals and other fine chemicals, such as the enantio selective production of lactones, esters and sulfoxides.
[01179] In some embodiments the invention comprises, but is not limited to additional methods for oxidoreductases, such as biosensors; diagnostic (analytical) kits; effective additives for refolding immunoglobulin-folded proteins in vitro; bleaching cotton; polymerizing phenols and aromatic amines; asymmetric syntheses of amino acids, steroids, pharmaceuticals and other fine chemicals; biocatalysis; pollution control, and oxygenation of hydrocarbons; treatment of industrial waste waters (detoxification); soil detoxification; manufacturing of adhesives, computer chips, car parts, and linings of drums and cans; whitening the skin/hair/teeth; and stimulating the immune system.
[01180] Exemplary methods according to the invention are presented below. Examples of the methods described above may also be found in the following references: Trichoderma & Gliocladium, Volume 2, Enzymes, biological control and commercial applications, Editors: Gary E. Harman, Christian P. Kubicek, Taylor & Francis Ltd. 1998, 393 (in particular, chapters 14, 15 and 16); Helmut Uhlig, Industrial enzymes and their applications, Translated and updated by Elfriede M. Linsmaier-Bednar, John Wiley & Sons, Inc 1998, p. 454 (in particular, chapters 5.1, 5.2, 5.3, 5.4, 5.5, 5.6, 5.7, 5.9, 5.10, 5.11, and 5.13). For saccharification applications: Hahn-Hagerdal, B., Galbe, M., Gorwa-Grauslund, M.F. Liden, Zacchi, G. Bio-ethanol - the fuel of tomorrow from the residues of today, Trends in Biotechnology, 2006, 24 (12), 549-556; Mielenz, J.R. Ethanol production from biomass: technology and commercialization status, Current Opinion in Microbiology, 2001, 4, 324-329; Himmel, M.E., Ruth, M.F., Wyman, C.E., Cellulase for commodity products from cellulosic biomass, Current Opinion in Biotechnology, 1999, 10, 358-364; Sheehan, J., Himmel, M. Enzymes, energy, and the environment: a strategic perspective on the U.S. Department of Energy's Research and Development Activities for Bioethanol, Biotechnology Progress. 1999, 15, 817-827. For textile processing applications: Galante, Y.M., Formantici, C, Enzyme applications in detergency and in manufacturing industries, Current Organic Chemistry, 2003, 7, 1399-1422. For pulp and paper applications: Bajpai, P., Bajpai, P.K Deinking with enzymes: a review. TAPPIJournal, 1998, 81(12), 111-117; Viikari, L., Pere, J., Suurnakki, A., Oksanen, T., Buchert, J. Use of cellulases in pulp and paper applications. In: "Carbohydrates from Trichoderma reesei and other microorganisms. Structure, Biochemistry, Genetics and Applications." Editors: Mark Claessens, Wim Nerinckx, and Kathleen Piens, The Royal Society of Chemistry 1998, 245-254. For food and beverage applications: Roller, S., Dea, I. CM. Biotechnology in the production and modification of biopolymers for foods, Critical Reviews in Biotechnology, 1992, 12(3), 261-277.
[01181] Additional references include, U.S. Patent No. 5,529,926; U.S. Patent No.
6,746,679; U.S. Patent No. 7,732,178; U.S. Patent No. 6,660,128; U.S. Patent No.6,093,436; U.S. Patent No. 5,691,193; U.S. Patent No. 5,785,811; U.S. Patent No. 7,329,424
[01182] Additional assays and methods for examining the activity of the enzymes are found in U.S. Patent Applications 60/806,876, 60/970,876, 11/487,547, 11/775,777, 11/833,133, and 12/205,694 and incorporated herein by reference. The following examples are provided for the purpose of illustration and are not intended to limit the scope of the present invention.
EXAMPLES
[01183] Example 1
[01184] Exemplary oxidase activity assay: [01185] An oxidase is any enzyme that catalyzes an oxidation-reduction reaction involving molecular oxygen (O2) as the electron acceptor. In these reactions, oxygen is reduced to water (H20) or hydrogen peroxide (H202). Activity of some oxidases can therefore be determined by measuring oxygen consumption, using a Clark electrode (Clark, L.C. Jnr. Ann. NY Acad. Sci. 102, 29-45, 1962) at a specific temperature in an air-saturated sample containing its substrate (e.g. glucose and galactose, for glucose oxidase and galactose oxidase, respectively). The reaction can be initiated by injection of a catalytic amount of oxidase in the oxygen electrode chamber. Kinetic parameters can be determined by measuring initial rates at different substrate concentrations.
[01186] Example 2
[01187] Exemplary peroxidase activity assay:
[01188] Peroxidase activity can be determined, based on the oxidation of 2, 2'-azino- di(3-ethylbenzthiazoline-6-sulphonate) (ABTS) obtained from Sigma-Aldrich (Gallati, V.H. J. Clin. Chem. Clin. Biochem. 17, 1, (1979). The absorbance increase of the oxidized form of ABTS, measured at 410 nm is proportional to the peroxidase activity. The method is sensitive, precise and linear up to 20 U/l.
[01189] The assay may also be used to indirectly measure oxidase activity. The formation of hydrogenperoxide, catalyzed by the oxidase, is coupled to the oxidation of ABTS by the addition of a peroxidase (e.g. horseradish peroxidase).
[01190] Example 3
[01191] Exemplary reductase activity assay:
[01192] Activity of some reductases activity, for example nitrate reductase activity, was determined as described by Garrett, R. H., and Cove, D. J. (1976) Mol. Gen. Genet. 149, 179-186.
[01193] Example 4
[01194] Exemplary for a dehydrogenase activity assay:
[01195] Activity of many dehydrogenases, can be monitored by measuring the decrease in absorbance at 340 nm resulting from the oxidation of the NADH or NADPH cofactor when incubated with a substrate. For example, the activity of glycerol 3 -phosphate dehydrogenase (GPDH), can be determined by measuring the decrease in absorbance at 340 nm when the enzyme was incubated with dihydroxyacetone phosphate as a substrate (Arst et al. Mol Gen Genet. 1990 Aug;223(l): 134-137).
* * * While various embodiments of the present invention have been described in detail, it is apparent that modifications and adaptations of those embodiments will occur to those skilled in the art. It is to be expressly understood, however, that such modifications and adaptations are within the scope of the present invention, as set forth in the following exemplary claims.

Claims

WHAT IS CLAIMED IS:
1. An isolated nucleic acid sequence selected from the group consisting of:
a) a nucleic acid sequence encoding a protein comprising an amino acid sequence selected from the amino acid sequences of SEQ ID NO: 2, SEQ ID No: 4, SEQ ID No: 6, SEQ ID No: 8, SEQ ID No: 10, SEQ ID No: 12, SEQ ID No: 14, SEQ ID No: 16, SEQ ID No: 18, SEQ ID No: 20, SEQ ID No: 22, SEQ ID No: 24, SEQ ID No: 26, SEQ ID No: 28, SEQ ID No: 30, SEQ ID No: 32, SEQ ID No: 34, SEQ ID No: 36, SEQ ID No: 38, SEQ ID No: 40, SEQ ID No: 42, SEQ ID No: 44, SEQ ID No: 46, SEQ ID No: 48, SEQ ID No: 50, SEQ ID No: 52, SEQ ID No: 54, SEQ ID No: 56, SEQ ID No: 58, SEQ ID No: 60, SEQ ID No: 62, SEQ ID No: 64, SEQ ID No: 66, SEQ ID No: 68, SEQ ID No: 70, SEQ ID No: 72, SEQ ID No: 74, SEQ ID No: 76, SEQ ID No: 78, SEQ ID No: 80, SEQ ID No: 82, SEQ ID No: 84, SEQ ID No: 86, SEQ ID No: 88, SEQ ID No: 90,
SEQ ID No: 92, SEQ ID No: 94, SEQ ID No: 96, SEQ ID No: 98, SEQ ID No: 100, SEQ
ID No: 102, SEQ ID No: 104, SEQ ID No: 106, SEQ ID No: 108, SEQ ID No: 110, SEQ
ID No: 112, SEQ ID No: 114, SEQ ID No: 116, SEQ ID No: 118, SEQ ID No: 120, SEQ
ID No: 122, SEQ ID No: 124, SEQ ID No: 126, SEQ ID No: 128, SEQ ID No: 130, SEQ
ID No: 132, SEQ ID No: 134, SEQ ID No: 136, SEQ ID No: 138, SEQ ID No: 140, SEQ
ID No: 142, SEQ ID No: 144, SEQ ID No: 146, SEQ ID No: 148, SEQ ID No: 150, SEQ
ID No: 152, SEQ ID No: 154, SEQ ID No: 156, SEQ ID No: 158, SEQ ID No: 160, SEQ
ID No: 162, SEQ ID No: 164, SEQ ID No: 166, SEQ ID No: 168, SEQ ID No: 170, SEQ
ID No: 172, SEQ ID No: 174, SEQ ID No: 176, SEQ ID No: 178, SEQ ID No: 180, SEQ
ID No: 182, SEQ ID No: 184, SEQ ID No: 186, SEQ ID No: 188, SEQ ID No: 190, SEQ
ID No: 192, SEQ ID No: 194, SEQ ID No: 196, SEQ ID No: 198, SEQ ID No: 200, SEQ
ID No: 202, SEQ ID No: 204, SEQ ID No: 206, SEQ ID No: 208, SEQ ID No: 210, SEQ
ID No: 212, SEQ ID No: 214, SEQ ID No: 216, SEQ ID No: 218, SEQ ID No: 220, SEQ
ID No: 222, SEQ ID No: 224, SEQ ID No: 226, SEQ ID No: 228, SEQ ID No: 230, SEQ
ID No: 232, SEQ ID No: 234, SEQ ID No: 236, SEQ ID No: 238, SEQ ID No: 240, SEQ
ID No: 242, SEQ ID No: 244, SEQ ID No: 246, SEQ ID No: 248, SEQ ID No: 250, SEQ
ID No: 252, SEQ ID No: 254, SEQ ID No: 256, SEQ ID No: 258, SEQ ID No: 260, SEQ
ID No: 262, SEQ ID No: 264, SEQ ID No: 266, SEQ ID No: 268, SEQ ID No: 270, SEQ
ID No: 272, SEQ ID No: 274, SEQ ID No: 276, SEQ ID No: 278, SEQ ID No: 280, SEQ
ID No: 282, SEQ ID No: 284, SEQ ID No: 286, SEQ ID No: 288, SEQ ID No: 290, SEQ
ID No: 292, SEQ ID No: 294, SEQ ID No: 296, SEQ ID No: 298, SEQ ID No: 300, SEQ ID No: 302, SEQ ID No: 304, SEQ ID No: 306, SEQ ID No: 308, SEQ ID No: 310, SEQ
ID No: 312, SEQ ID No: 314, SEQ ID No: 316, SEQ ID No: 318, SEQ ID No: 320, SEQ
ID No: 322, SEQ ID No: 324, SEQ ID No: 326, SEQ ID No: 328, SEQ ID No: 330, SEQ
ID No: 332, SEQ ID No: 334, SEQ ID No: 336, SEQ ID No: 338, SEQ ID No: 340, SEQ
ID No: 342, SEQ ID No: 344, SEQ ID No: 346, SEQ ID No: 348, SEQ ID No: 350, SEQ
ID No: 352, SEQ ID No: 354, SEQ ID No: 356, SEQ ID No: 358, SEQ ID No: 360, SEQ
ID No: 362, SEQ ID No: 364, SEQ ID No: 366, SEQ ID No: 368, SEQ ID No: 370, SEQ
ID No: 372, SEQ ID No: 374, SEQ ID No: 376, SEQ ID No: 378, SEQ ID No: 380, SEQ
ID No: 382, SEQ ID No: 384, SEQ ID No: 386, SEQ ID No: 388, SEQ ID No: 390, SEQ
ID No: 392, SEQ ID No: 394, SEQ ID No: 396, SEQ ID No: 398, SEQ ID No: 400, SEQ
ID No: 402, SEQ ID No: 404, SEQ ID No: 406, SEQ ID No: 408, SEQ ID No: 410, SEQ
ID No: 412, SEQ ID No: 414, SEQ ID No: 416, SEQ ID No: 418, SEQ ID No: 420, SEQ
ID No: 422, SEQ ID No: 424, SEQ ID No: 426, SEQ ID No: 428, SEQ ID No: 430, SEQ
ID No: 432, SEQ ID No: 434, SEQ ID No: 436, SEQ ID No: 438, SEQ ID No: 440, SEQ
ID No: 442, SEQ ID No: 444, SEQ ID No: 446, SEQ ID No: 448, SEQ ID No: 450, SEQ
ID No: 452, SEQ ID No: 454, SEQ ID No: 456, SEQ ID No: 458, SEQ ID No: 460, SEQ
ID No: 462, SEQ ID No: 464, SEQ ID No: 466, SEQ ID No: 468, SEQ ID No: 470, SEQ
ID No: 472, SEQ ID No: 474, SEQ ID No: 476, SEQ ID No: 478, SEQ ID No: 480, SEQ
ID No: 482, SEQ ID No: 484, SEQ ID No: 486, SEQ ID No: 488, SEQ ID No: 490, SEQ
ID No: 492, SEQ ID No: 494, SEQ ID No: 496, SEQ ID No: 498, SEQ ID No: 500, SEQ
ID No: 502, SEQ ID No: 504, SEQ ID No: 506, SEQ ID No: 508, SEQ ID No: 510, SEQ
ID No: 512, SEQ ID No: 514, SEQ ID No: 516, SEQ ID No: 518, SEQ ID No: 520, SEQ
ID No: 522, SEQ ID No: 524, SEQ ID No: 526, SEQ ID No: 528, SEQ ID No: 530, SEQ
ID No: 532, SEQ ID No: 534, SEQ ID No: 536, SEQ ID No: 538, SEQ ID No: 540, SEQ
ID No: 542, SEQ ID No: 544, SEQ ID No: 546, SEQ ID No: 548, SEQ ID No: 550, SEQ
ID No: 552, SEQ ID No: 554, SEQ ID No: 556, SEQ ID No: 558, SEQ ID No: 560, SEQ
ID No: 562, SEQ ID No: 564, SEQ ID No: 566, SEQ ID No: 568, SEQ ID No: 570, SEQ
ID No: 572, SEQ ID No: 574, SEQ ID No: 576, SEQ ID No: 578, SEQ ID No: 580, SEQ
ID No: 582, SEQ ID No: 584, SEQ ID No: 586, SEQ ID No: 588, SEQ ID No: 590, SEQ
ID No: 592, SEQ ID No: 594, SEQ ID No: 596, SEQ ID No: 598, SEQ ID No: 600, SEQ
ID No: 602, SEQ ID No: 604, SEQ ID No: 606, SEQ ID No: 608, SEQ ID No: 610, SEQ
ID No: 612, SEQ ID No: 614, SEQ ID No: 616, SEQ ID No: 618, SEQ ID No: 620, SEQ
ID No: 622, SEQ ID No: 624, SEQ ID No: 626, SEQ ID No: 628, SEQ ID No: 630, SEQ ID No: 632, SEQ ID No: 634, SEQ ID No: 636, SEQ ID No: 638, SEQ ID No: 640, SEQ
ID No: 642, SEQ ID No: 644, SEQ ID No: 646, SEQ ID No: 648, SEQ ID No: 650, SEQ
ID No: 652, SEQ ID No: 654, SEQ ID No: 656, SEQ ID No: 658, SEQ ID No: 660, SEQ
ID No: 662, SEQ ID No: 664, SEQ ID No: 666, SEQ ID No: 668, SEQ ID No: 670, SEQ
ID No: 672, SEQ ID No: 674, SEQ ID No: 676, SEQ ID No: 678, SEQ ID No: 680, SEQ
ID No: 682, SEQ ID No: 684, SEQ ID No: 686, SEQ ID No: 688, SEQ ID No: 690, SEQ
ID No: 692, SEQ ID No: 694, SEQ ID No: 696, SEQ ID No: 698, SEQ ID No: 700, SEQ
ID No: 702, SEQ ID No: 704, SEQ ID No: 706, SEQ ID No: 708, SEQ ID No: 710, SEQ
ID No: 712, SEQ ID No: 714, SEQ ID No: 716, SEQ ID No: 718, SEQ ID No: 720, SEQ
ID No: 722, SEQ ID No: 724, SEQ ID No: 726, SEQ ID No: 728, SEQ ID No: 730, SEQ
ID No: 732, SEQ ID No: 734, SEQ ID No: 736, SEQ ID No: 738, SEQ ID No: 740, SEQ
ID No: 742, SEQ ID No: 744, SEQ ID No: 746, SEQ ID No: 748, SEQ ID No: 750, SEQ
ID No: 752, SEQ ID No: 754, SEQ ID No: 756, SEQ ID No: 758, SEQ ID No: 760, SEQ
ID No: 762, SEQ ID No: 764, SEQ ID No: 766, SEQ ID No: 768, SEQ ID No: 770, SEQ
ID No: 772, SEQ ID No: 774, SEQ ID No: 776, SEQ ID No: 778, SEQ ID No: 780, SEQ
ID No: 782, SEQ ID No: 784, SEQ ID No: 786, SEQ ID No: 788, SEQ ID No: 790, SEQ
ID No: 792, SEQ ID No: 794, SEQ ID No: 796, SEQ ID No: SEQ ID No: 798, SEQ ID
No: 800, SEQ ID No: 802, SEQ ID No: 804, SEQ ID No: 806, SEQ ID No: 808, SEQ ID
No: 810, SEQ ID No: 812, SEQ ID No: 814, SEQ ID No: 816, SEQ ID No: 818, SEQ ID
No: 820, SEQ ID No: 822, SEQ ID No: 824, SEQ ID No: 826, SEQ ID No: 828, SEQ ID
No: 830, SEQ ID No: 832, SEQ ID No: 834, SEQ ID No: 836, SEQ ID No: 838, SEQ ID
No: 840, SEQ ID No: 842, SEQ ID No: 844, SEQ ID No: 846, SEQ ID No: 848, SEQ ID
No: 850, SEQ ID No: 852, SEQ ID No: 854, SEQ ID No: 856, SEQ ID No: 858, SEQ ID
No: 860, SEQ ID No: 862, SEQ ID No: 864, SEQ ID No: 866, SEQ ID No: 868, SEQ ID
No: 870, SEQ ID No: 872, SEQ ID No: 874, SEQ ID No: 876, SEQ ID No: 878, SEQ ID
No: 880, SEQ ID No: 882, SEQ ID No: 884, SEQ ID No: 886, SEQ ID No: 888, SEQ ID
No: 890, SEQ ID No: 892, SEQ ID No: 894, SEQ ID No: 896, SEQ ID No: 898, SEQ ID
No: 900, SEQ ID No: 902, SEQ ID No: 904, SEQ ID No: 906, SEQ ID No: 908, SEQ ID
No: 910, SEQ ID No: 912, SEQ ID No: 914, SEQ ID No: 916, SEQ ID No: 918, SEQ ID
No: 920, SEQ ID No: 922, SEQ ID No: 924, SEQ ID No: 926, SEQ ID No: 928, SEQ ID
No: 930, SEQ ID No: 932, SEQ ID No: 934, SEQ ID No: 936, SEQ ID No: 938, SEQ ID
No: 940, SEQ ID No: 942, SEQ ID No: 944, SEQ ID No: 946, SEQ ID No: 948, SEQ ID
No: 950, SEQ ID No: 952, SEQ ID No: 954, SEQ ID No: 956, SEQ ID No: 958, SEQ ID No: 960, SEQ ID No: 962, SEQ ID No: 964, SEQ ID No: 966, SEQ ID No: 968, SEQ ID No: 970, SEQ ID No: 972, SEQ ID No: 974, SEQ ID No: 976, SEQ ID No: 978, SEQ ID No: 980, SEQ ID No: 982, SEQ ID No: 984, SEQ ID No: 986, SEQ ID No: 988, SEQ ID No: 990, SEQ ID No: 992, SEQ ID No: 994, SEQ ID No: 996, SEQ ID No: 998, SEQ ID No: 1000, SEQ ID No: 1002, SEQ ID No: 1004, SEQ ID No: 1006, SEQ ID No: 1008, SEQ ID No: 1010, SEQ ID No: 1012, SEQ ID No: 1014, SEQ ID No: 1016, SEQ ID No: 1018, SEQ ID No: 1020, SEQ ID No: 1022, SEQ ID No: 1024, SEQ ID No: 1026, SEQ ID No: 1028, SEQ ID No: 1030, SEQ ID No: 1032, SEQ ID No: 1034, SEQ ID No: 1036, SEQ ID No: 1038, SEQ ID No: 1040, SEQ ID No: 1042, SEQ ID No: 1044, SEQ ID No: 1046, SEQ ID No: 1048, SEQ ID No: 1050, SEQ ID No: 1052, SEQ ID No: 1054, SEQ ID No: 1056, SEQ ID No: 1058, SEQ ID No: 1060, SEQ ID No: 1062, SEQ ID No: 1064, SEQ ID No: 1066, SEQ ID No: 1068, SEQ ID No: 1070, SEQ ID No: 1072, SEQ ID No: 1074, SEQ ID No: 1076, SEQ ID No: 1078, SEQ ID No: 1080, SEQ ID No: 1082, SEQ ID No: 1084, SEQ ID No: 1086, SEQ ID No: 1088, SEQ ID No: 1090, SEQ ID No: 1092, SEQ ID No: 1094, SEQ ID No: 1096, SEQ ID No: 1098, SEQ ID NO: 1100, SEQ ID No: 1102, SEQ ID No: 1104, SEQ ID No: 1106, SEQ ID No: 1108, SEQ ID No: 1110, SEQ ID No: 1112, SEQ ID No: 1114, SEQ ID No: 1116, SEQ ID No: 1118, SEQ ID No: 1120, SEQ ID No: 1122, SEQ ID No: 1124, SEQ ID No: 1126, SEQ ID No: 1128, SEQ ID No: 1130, SEQ ID No: 1132, SEQ ID No: 1134, SEQ ID No: 1136, SEQ ID No: 1138, SEQ ID No: 1140, SEQ ID No: 1142, SEQ ID No: 1144, SEQ ID No: 1146, SEQ ID No: 1148, SEQ ID No: 1150, SEQ ID No: 1152, SEQ ID No: 1154, SEQ ID No: 1156, SEQ ID No: 1158, SEQ ID No: 1160, SEQ ID No: 1162, SEQ ID No: 1164, SEQ ID No: 1166, SEQ ID No: 1168, SEQ ID No: 1170, SEQ ID No: 1172, SEQ ID No: 1174, SEQ ID No: 1176, SEQ ID No: 1178, SEQ ID No: 1180, SEQ ID No: 1182, SEQ ID No: 1184, SEQ ID No: 1186, SEQ ID No: 1188, SEQ ID No: 1190, SEQ ID No: 1192, SEQ ID No: 1194, SEQ ID No: 1196, SEQ ID No: 1198, SEQ ID No: 1200, SEQ ID No: 1202, SEQ ID No: 1204, SEQ ID No: 1206, SEQ ID No: 1208, SEQ ID No: 1210, SEQ ID No: 1212, SEQ ID No: 1214, SEQ ID No: 1216, SEQ ID No: 1218, SEQ ID No: 1220, SEQ ID No: 1222, SEQ ID No: 1224, SEQ ID No: 1226, SEQ ID No: 1228, SEQ ID No: 1230, SEQ ID No: 1232, SEQ ID No: 1234, SEQ ID No: 1236, SEQ ID No: 1238, SEQ ID No: 1240, SEQ ID No: 1242, SEQ ID No: 1244, SEQ ID No: 1246, SEQ ID No: 1248, SEQ ID No: 1250, SEQ ID No: 1252, SEQ ID No: 1254, SEQ ID No: 1256, SEQ ID No: 1258, SEQ ID No: 1260, SEQ ID No: 1262, SEQ ID No: 1264, SEQ ID No: 1266, SEQ ID No: 1268, SEQ ID No: 1270, SEQ ID No: 1272, SEQ ID No: 1274 , SEQ ID No: 1276, SEQ ID No: 1278, SEQ ID No: 1280, SEQ ID No: 1282, SEQ ID No: 1284, SEQ ID No: 1286, SEQ ID No: 1288, SEQ ID No: 1290, SEQ ID No: 1292 , SEQ ID No: 1294, SEQ ID No: 1296, SEQ ID No: 1298, SEQ ID No: 1300, SEQ ID No: 1302, SEQ ID No: 1304, SEQ ID No: 1306, SEQ ID No: 1308, SEQ ID No: 1310 , SEQ ID No: 1312, SEQ ID No: 1314, SEQ ID No: 1316, SEQ ID No: 1318, SEQ ID No: 1320, SEQ ID No: 1322, SEQ ID No: 1324, SEQ ID No: 1326, SEQ ID No: 1328 , SEQ ID No: 1330, SEQ ID No: 1332, SEQ ID No: 1334, SEQ ID No: 1336, SEQ ID No: 1338, SEQ ID No: 1340, SEQ ID No: 1342, SEQ ID No: 1344, SEQ ID No: 1346 , SEQ ID No: 1348, SEQ ID No: 1350, SEQ ID No: 1352, SEQ ID No: 1354, SEQ ID No: 1356, SEQ ID No: 1358, SEQ ID No: 1360, SEQ ID No: 1362, SEQ ID No: 1364 , SEQ ID No: 1366, SEQ ID No: 1368, SEQ ID No: 1370, SEQ ID No: 1372, SEQ ID No: 1374, SEQ ID No: 1376, SEQ ID No: 1378, SEQ ID No: 1380, SEQ ID No: 1382 , SEQ ID No: 1384, SEQ ID No: 1386, SEQ ID No: 1388, SEQ ID No: 1390, SEQ ID No: 1392, SEQ ID No: 1394, SEQ ID No: 1396, SEQ ID No: 1398, SEQ ID No: 1400 , SEQ ID No: 1402, SEQ ID No: 1404, SEQ ID No: 1406, SEQ ID No: 1408, SEQ ID No: 1410, SEQ ID No: 1412, SEQ ID No: 1414, SEQ ID No: 1416, SEQ ID No: 1418 , SEQ ID No: 1420, SEQ ID No: 1422, SEQ ID No: 1424, SEQ ID No: 1426, SEQ ID No: 1428, SEQ ID No: 1430, SEQ ID No: 1432, SEQ ID No: 1434, SEQ ID No: 1436 , SEQ ID No: 1438, SEQ ID No: 1440, SEQ ID No: 1442, SEQ ID No: 1444, SEQ ID No: 1446, SEQ ID No: 1448, SEQ ID No: 1450, SEQ ID No: 1452, SEQ ID No: 1454 , SEQ ID No: 1456, SEQ ID No: 1458, SEQ ID No: 1460, SEQ ID No: 1462, SEQ ID No: 1464, SEQ ID No: 1466, SEQ ID No: 1468, SEQ ID No: 1470, SEQ ID No: 1472 , SEQ ID No: 1474, SEQ ID No: 1476, SEQ ID No: 1478, SEQ ID No: 1480, SEQ ID No: 1482, SEQ ID No: 1484, SEQ ID No: 1486, SEQ ID No: 1488, SEQ ID No: 1490 , SEQ ID No: 1492, SEQ ID No: 1494, SEQ ID No: 1496, SEQ ID No: 1498, SEQ ID No: 1500, SEQ ID No: 1502, SEQ ID No: 1504, SEQ ID No: 1506, SEQ ID No: 1508 , SEQ ID No: 1510, SEQ ID No: 1512, SEQ ID No: 1514, SEQ ID No: 1516, SEQ ID No: 1518, SEQ ID No: 1520, SEQ ID No: 1522, SEQ ID No: 1524, SEQ ID No: 1526 , SEQ ID No: 1528, SEQ ID No: 1530, SEQ ID No: 1532, SEQ ID No: 1534, SEQ ID No: 1536, SEQ ID No: 1538, SEQ ID No: 1540, SEQ ID No: 1542, SEQ ID No: 1544 , SEQ ID No: 1546, SEQ ID No: 1548, SEQ ID No: 1550, SEQ ID No: 1552, SEQ ID No: 1554, SEQ ID No: 1556, SEQ ID No: 1558, SEQ ID No: 1560, SEQ ID No: 1562 , SEQ ID No: 1564, SEQ ID No: 1566, SEQ ID No: 1568, SEQ ID No: 1570, SEQ ID No: 1572, SEQ ID No: 1574, SEQ ID No: 1576, SEQ ID No: 1578, SEQ ID No: 1580 , SEQ ID No: 1582, SEQ ID No: 1584, SEQ ID No: 1586, SEQ ID No: 1588, SEQ ID No: 1590, SEQ ID No: 1592, SEQ ID No: 1594, SEQ ID No: 1596, SEQ ID No: 1598 , SEQ ID No: 1600, SEQ ID No: 1602, SEQ ID No: 1604, SEQ ID No: 1606, SEQ ID No: 1608, SEQ ID No: 1610, SEQ ID No: 1612, SEQ ID No: 1614, SEQ ID No: 1616 , SEQ ID No: 1618, SEQ ID No: 1620, SEQ ID No: 1622, SEQ ID No: 1624, SEQ ID No: 1626, SEQ ID No: 1628, SEQ ID No: 1630, SEQ ID No: 1632, SEQ ID No: 1634 , SEQ ID No: 1636, SEQ ID No: 1638, SEQ ID No: 1640, SEQ ID No: 1642, SEQ ID No: 1644, SEQ ID No: 1646, SEQ ID No: 1648, SEQ ID No: 1650, SEQ ID No: 1652 , SEQ ID No: 1654, SEQ ID No: 1656, SEQ ID No: 1658, SEQ ID No: 1660, SEQ ID No: 1662, SEQ ID No: 1664, SEQ ID No: 1666, SEQ ID No: 1668, SEQ ID No: 1670 , SEQ ID No: 1672, SEQ ID No: 1674, SEQ ID No: 1676, SEQ ID No: 1678, SEQ ID No: 1680, SEQ ID No: 1682, SEQ ID No: 1684, SEQ ID No: 1686, SEQ ID No: 1688 , SEQ ID No: 1690, SEQ ID No: 1692, SEQ ID No: 1694, SEQ ID No: 1696, SEQ ID No: 1698, SEQ ID No: 1700, SEQ ID No: 1702, SEQ ID No: 1704, SEQ ID No: 1706 , SEQ ID No: 1708, SEQ ID No: 1710, SEQ ID No: 1712, SEQ ID No: 1714, SEQ ID No: 1716, SEQ ID No: 1718, SEQ ID No: 1720, SEQ ID No: 1722, SEQ ID No: 1724 , SEQ ID No: 1726, SEQ ID No: 1728, SEQ ID No: 1730, SEQ ID No: 1732, SEQ ID No: 1734, SEQ ID No: 1736, SEQ ID No: 1738, SEQ ID No: 1740, SEQ ID No: 1742 , SEQ ID No: 1744, SEQ ID No: 1746, SEQ ID No: 1748, SEQ ID No: 1750, SEQ ID No: 1752, SEQ ID No: 1754, SEQ ID No: 1756, SEQ ID No: 1758, SEQ ID No: 1760 , SEQ ID No: 1762, SEQ ID No: 1764, SEQ ID No: 1766, SEQ ID No: 1768, SEQ ID No: 1770, SEQ ID No: 1772, SEQ ID No: 1774, SEQ ID No: 1776, SEQ ID No: 1778 , SEQ ID No: 1780, SEQ ID No: 1782, SEQ ID No: 1784, SEQ ID No: 1786, SEQ ID No: 1788, SEQ ID No: 1790, SEQ ID No: 1792, SEQ ID No: 1794, SEQ ID No: 1796 , SEQ ID No: 1798, SEQ ID No: 1800, SEQ ID No: 1802, SEQ ID No: 1804, SEQ ID No: 1806, SEQ ID No: 1808, SEQ ID No: 1810, SEQ ID No: 1812, SEQ ID No: 1814 , SEQ ID No: 1816, SEQ ID No: 1818, SEQ ID No: 1820, SEQ ID No: 1822, SEQ ID No: 1824, SEQ ID No: 1826, SEQ ID No: 1828, SEQ ID No: 1830, SEQ ID No: 1832 , SEQ ID No: 1834, SEQ ID No: 1836, SEQ ID No: 1838, SEQ ID No: 1840, SEQ ID No: 1842, SEQ ID No: 1844, SEQ ID No: 1846, SEQ ID No: 1848, SEQ ID No: 1850 , SEQ ID No: 1852, SEQ ID No: 1854, SEQ ID No: 1856, SEQ ID No: 1858, SEQ ID No: 1860, SEQ ID No: 1862, SEQ ID No: 1864, SEQ ID No: 1866, SEQ ID No: 1868, SEQ ID No: 1870, SEQ ID No: 1872, SEQ ID No: 1874, SEQ ID No: 1876, SEQ ID No: 1878, SEQ ID No: 1880, SEQ ID No: 1882, SEQ ID No: 1884, SEQ ID No: 1886, SEQ ID No: 1888, SEQ ID No: 1890, SEQ ID No: 1892, SEQ ID No: 1894, SEQ ID No: 1896, SEQ ID No: 1898, SEQ ID No: 1900, SEQ ID No: 1902, SEQ ID No: 1904, SEQ ID No: 1906, SEQ ID No: 1908, SEQ ID No: 1910, SEQ ID No: 1912, SEQ ID No: 1914, SEQ ID No: 1916, SEQ ID No: 1918, SEQ ID No: 1920, SEQ ID No: 1922, SEQ ID No: 1924, SEQ ID No: 1926, SEQ ID No: 1928, SEQ ID No: 1930, SEQ ID No: 1932, SEQ ID No: 1934, SEQ ID No: 1936, SEQ ID No: 1938, SEQ ID No: 1940, SEQ ID No: 1942, SEQ ID No: 1944, SEQ ID No: 1946, SEQ ID No: 1948, SEQ ID No: 1950, SEQ ID No: 1952, SEQ ID No: 1954, SEQ ID No: 1956, SEQ ID No: 1958, SEQ ID No: 1960, SEQ ID No: 1962, SEQ ID No: 1964, SEQ ID No: 1966, SEQ ID No: 1968, SEQ ID No: 1970, SEQ ID No: 1972, and SEQ ID No: 1974. b) a nucleic acid sequence encoding a fragment of the protein of (a), wherein the fragment has a biological activity of the protein of (a); and c) a nucleic acid sequence encoding an amino acid sequence that is at least about 70% identical to an amino acid sequence of (a) and has a biological activity of the protein comprising the amino acid sequence.
2. The isolated nucleic acid sequence of claim 1, wherein said nucleic acid sequence encodes an amino acid sequence that is at least about 80% identical to the amino acid sequence of (a) and has a biological activity of the protein comprising the amino acid sequence.
3. The isolated nucleic acid sequence of claim 1, wherein said nucleic acid sequence encodes an amino acid sequence that is at least about 90% identical to the amino acid sequence of (a) and has a biological activity of the protein comprising the amino acid sequence.
4. The isolated nucleic acid sequence of claim 1, wherein said nucleic acid sequence encodes an amino acid sequence that is at least about 95% identical to the amino acid sequence of (a) and has a biological activity of the protein comprising the amino acid sequence.
5. The isolated nucleic acid sequence of claim 1, wherein said nucleic acid sequence encodes an amino acid sequence that is at least about 97% identical to the amino acid sequence of (a) and has a biological activity of the protein comprising the amino acid sequence.
6. The isolated nucleic acid sequence of claim 1, wherein said nucleic acid sequence encodes an amino acid sequence that is at least about 99% identical to the amino acid sequence of (a) and has a biological activity of the protein comprising the amino acid sequence.
7. The isolated nucleic acid sequence of claim 1, wherein said nucleic acid sequence encodes a protein comprising an amino acid sequence selected from the group consisting of: the amino acid sequences of SEQ ID NO: 2, SEQ ID No: 4, SEQ ID No: 6, SEQ ID No: 8, SEQ ID No: 10, SEQ ID No: 12, SEQ ID No: 14, SEQ ID No: 16, SEQ ID No: 18, SEQ ID No: 20, SEQ ID No: 22, SEQ ID No: 24, SEQ ID No: 26, SEQ ID No: 28, SEQ ID No: 30, SEQ ID No: 32, SEQ ID No: 34, SEQ ID No: 36, SEQ ID No: 38, SEQ ID No: 40, SEQ ID No: 42, SEQ ID No: 44, SEQ ID No: 46, SEQ ID No: 48, SEQ ID No: 50, SEQ ID No: 52, SEQ ID No: 54, SEQ ID No: 56, SEQ ID No: 58, SEQ ID No: 60, SEQ ID No: 62, SEQ ID No: 64, SEQ ID No: 66, SEQ ID No: 68, SEQ ID No: 70, SEQ ID No: 72, SEQ ID No: 74, SEQ ID No: 76, SEQ ID No: 78, SEQ ID No: 80, SEQ ID No: 82, SEQ ID No: 84, SEQ ID No: 86, SEQ ID No: 88, SEQ ID No: 90, SEQ ID
No: 92, SEQ ID No: 94, SEQ ID No: 96 SEQ ID No : 98, SEQ ID No: 100, SEQ ID No:
102, SEQ ID No: 104, SEQ ID No: 106, SEQ ID No: 108, SEQ ID No: 110, SEQ ID No:
112, SEQ ID No: 114, SEQ ID No: 116, SEQ ID No: 118, SEQ ID No: 120, SEQ ID No:
122, SEQ ID No: 124, SEQ ID No: 126, SEQ ID No: 128, SEQ ID No: 130, SEQ ID No:
132, SEQ ID No: 134, SEQ ID No: 136, SEQ ID No: 138, SEQ ID No: 140, SEQ ID No:
142, SEQ ID No: 144, SEQ ID No: 146, SEQ ID No: 148, SEQ ID No: 150, SEQ ID No:
152, SEQ ID No: 154, SEQ ID No: 156, SEQ ID No: 158, SEQ ID No: 160, SEQ ID No:
162, SEQ ID No: 164, SEQ ID No: 166, SEQ ID No: 168, SEQ ID No: 170, SEQ ID No:
172, SEQ ID No: 174, SEQ ID No: 176, SEQ ID No: 178, SEQ ID No: 180, SEQ ID No:
182, SEQ ID No: 184, SEQ ID No: 186, SEQ ID No: 188, SEQ ID No: 190, SEQ ID No:
192, SEQ ID No: 194, SEQ ID No: 196, SEQ ID No: 198, SEQ ID No: 200, SEQ ID No:
202, SEQ ID No: 204, SEQ ID No: 206, SEQ ID No: 208, SEQ ID No: 210, SEQ ID No:
212, SEQ ID No: 214, SEQ ID No: 216, SEQ ID No: 218, SEQ ID No: 220, SEQ ID No:
222, SEQ ID No: 224, SEQ ID No: 226, SEQ ID No: 228, SEQ ID No: 230, SEQ ID No: 232, SEQ ID No: 234, SEQ ID No: 236, SEQ ID No: 238 SEQ ID No: 240, SEQ ID No
242, SEQ ID No: 244, SEQ ID No: 246, SEQ ID No: 248 SEQ ID No: 250, SEQ ID No
252, SEQ ID No: 254, SEQ ID No: 256, SEQ ID No: 258 SEQ ID No: 260, SEQ ID No
262, SEQ ID No: 264, SEQ ID No: 266, SEQ ID No: 268 SEQ ID No: 270, SEQ ID No
272, SEQ ID No: 274, SEQ ID No: 276, SEQ ID No: 278 SEQ ID No: 280, SEQ ID No
282, SEQ ID No: 284, SEQ ID No: 286, SEQ ID No: 288 SEQ ID No: 290, SEQ ID No
292, SEQ ID No: 294, SEQ ID No: 296, SEQ ID No: 298 SEQ ID No: 300, SEQ ID No
302, SEQ ID No: 304, SEQ ID No: 306, SEQ ID No: 308 SEQ ID No: 310, SEQ ID No
312, SEQ ID No: 314, SEQ ID No: 316, SEQ ID No: 318 SEQ ID No: 320, SEQ ID No
322, SEQ ID No: 324, SEQ ID No: 326, SEQ ID No: 328 SEQ ID No: 330, SEQ ID No
332, SEQ ID No: 334, SEQ ID No: 336, SEQ ID No: 338 SEQ ID No: 340, SEQ ID No
342, SEQ ID No: 344, SEQ ID No: 346, SEQ ID No: 348 SEQ ID No: 350, SEQ ID No
352, SEQ ID No: 354, SEQ ID No: 356, SEQ ID No: 358 SEQ ID No: 360, SEQ ID No
362, SEQ ID No: 364, SEQ ID No: 366, SEQ ID No: 368 SEQ ID No: 370, SEQ ID No
372, SEQ ID No: 374, SEQ ID No: 376, SEQ ID No: 378 SEQ ID No: 380, SEQ ID No
382, SEQ ID No: 384, SEQ ID No: 386, SEQ ID No: 388 SEQ ID No: 390, SEQ ID No
392, SEQ ID No: 394, SEQ ID No: 396, SEQ ID No: 398 SEQ ID No: 400, SEQ ID No
402, SEQ ID No: 404, SEQ ID No: 406, SEQ ID No: 408 SEQ ID No: 410, SEQ ID No
412, SEQ ID No: 414, SEQ ID No: 416, SEQ ID No: 418 SEQ ID No: 420, SEQ ID No
422, SEQ ID No: 424, SEQ ID No: 426, SEQ ID No: 428 SEQ ID No: 430, SEQ ID No
432, SEQ ID No: 434, SEQ ID No: 436, SEQ ID No: 438 SEQ ID No: 440, SEQ ID No
442, SEQ ID No: 444, SEQ ID No: 446, SEQ ID No: 448 SEQ ID No: 450, SEQ ID No
452, SEQ ID No: 454, SEQ ID No: 456, SEQ ID No: 458 SEQ ID No: 460, SEQ ID No
462, SEQ ID No: 464, SEQ ID No: 466, SEQ ID No: 468 SEQ ID No: 470, SEQ ID No
472, SEQ ID No: 474, SEQ ID No: 476, SEQ ID No: 478 SEQ ID No: 480, SEQ ID No
482, SEQ ID No: 484, SEQ ID No: 486, SEQ ID No: 488 SEQ ID No: 490, SEQ ID No
492, SEQ ID No: 494, SEQ ID No: 496, SEQ ID No: 498 SEQ ID No: 500, SEQ ID No
502, SEQ ID No: 504, SEQ ID No: 506, SEQ ID No: 508 SEQ ID No: 510, SEQ ID No
512, SEQ ID No: 514, SEQ ID No: 516, SEQ ID No: 518 SEQ ID No: 520, SEQ ID No
522, SEQ ID No: 524, SEQ ID No: 526, SEQ ID No: 528 SEQ ID No: 530, SEQ ID No
532, SEQ ID No: 534, SEQ ID No: 536, SEQ ID No: 538 SEQ ID No: 540, SEQ ID No
542, SEQ ID No: 544, SEQ ID No: 546, SEQ ID No: 548 SEQ ID No: 550, SEQ ID No
552, SEQ ID No: 554, SEQ ID No: 556, SEQ ID No: 558 SEQ ID No: 560, SEQ ID No 562, SEQ ID No 564, SEQ ID No 566, SEQ ID No 568, SEQ ID No 570, SEQ ID No 572, SEQ ID No 574, SEQ ID No 576, SEQ ID No 578, SEQ ID No 580, SEQ ID No 582, SEQ ID No 584, SEQ ID No 586, SEQ ID No 588, SEQ ID No 590, SEQ ID No 592, SEQ ID No 594, SEQ ID No 596, SEQ ID No 598, SEQ ID No 600, SEQ ID No 602, SEQ ID No 604, SEQ ID No 606, SEQ ID No 608, SEQ ID No 610, SEQ ID No 612, SEQ ID No 614, SEQ ID No 616, SEQ ID No 618, SEQ ID No 620, SEQ ID No 622, SEQ ID No 624, SEQ ID No 626, SEQ ID No 628, SEQ ID No 630, SEQ ID No 632, SEQ ID No 634, SEQ ID No 636, SEQ ID No 638, SEQ ID No 640, SEQ ID No 642, SEQ ID No 644, SEQ ID No 646, SEQ ID No 648, SEQ ID No 650, SEQ ID No 652, SEQ ID No 654, SEQ ID No 656, SEQ ID No 658, SEQ ID No 660, SEQ ID No 662, SEQ ID No 664, SEQ ID No 666, SEQ ID No 668, SEQ ID No 670, SEQ ID No 672, SEQ ID No 674, SEQ ID No 676, SEQ ID No 678, SEQ ID No 680, SEQ ID No 682, SEQ ID No 684, SEQ ID No 686, SEQ ID No 688, SEQ ID No 690, SEQ ID No 692, SEQ ID No 694, SEQ ID No 696, SEQ ID No 698, SEQ ID No 700, SEQ ID No 702, SEQ ID No 704, SEQ ID No 706, SEQ ID No 708, SEQ ID No 710, SEQ ID No 712, SEQ ID No 714, SEQ ID No 716, SEQ ID No 718, SEQ ID No 720, SEQ ID No 722, SEQ ID No 724, SEQ ID No 726, SEQ ID No 728, SEQ ID No 730, SEQ ID No 732, SEQ ID No 734, SEQ ID No 736, SEQ ID No 738, SEQ ID No 740, SEQ ID No 742, SEQ ID No 744, SEQ ID No 746, SEQ ID No 748, SEQ ID No 750, SEQ ID No 752, SEQ ID No 754, SEQ ID No 756, SEQ ID No 758, SEQ ID No 760, SEQ ID No 762, SEQ ID No 764, SEQ ID No 766, SEQ ID No 768, SEQ ID No 770, SEQ ID No 772, SEQ ID No 774, SEQ ID No 776, SEQ ID No 778, SEQ ID No 780, SEQ ID No 782, SEQ ID No 784, SEQ ID No 786, SEQ ID No 788, SEQ ID No 790, SEQ ID No 792, SEQ ID No 794, SEQ ID No 796, SEQ ID No SEQ ID No: 798 SEQ ID No: 800 SEQ ID No: 802 SEQ ID No: 804 SEQ ID No: 806 SEQ ID No: 808 SEQ ID No: 810 SEQ ID No: 812 SEQ ID No: 814 SEQ ID No: 816 SEQ ID No: 818 SEQ ID No: 820 SEQ ID No: 822 SEQ ID No: 824 SEQ ID No: 826 SEQ ID No: 828 SEQ ID No: 830 SEQ ID No: 832 SEQ ID No: 834 SEQ ID No: 836 SEQ ID No: 838 SEQ ID No: 840 SEQ ID No: 842 SEQ ID No: 844 SEQ ID No: 846 SEQ ID No: 848 SEQ ID No: 850 SEQ ID No: 852 SEQ ID No: 854 SEQ ID No: 856 SEQ ID No: 858 SEQ ID No: 860 SEQ ID No: 862 SEQ ID No: 864 SEQ ID No: 866 SEQ ID No: 868 SEQ ID No: 870 SEQ ID No: 872 SEQ ID No: 874 SEQ ID No: 876 SEQ ID No: 878 SEQ ID No: 880 SEQ ID No: 882 SEQ ID No: 884 SEQ ID No: 886 SEQ ID No: 888 SEQ ID No: 890 SEQ ID No: 892, SEQ ID No: 894, SEQ ID No: 896, SEQ ID No: 898, SEQ ID No: 900, SEQ ID No: 902, SEQ ID No: 904, SEQ ID No: 906, SEQ ID No: 908, SEQ ID No: 910, SEQ ID No: 912, SEQ ID No: 914, SEQ ID No: 916, SEQ ID No: 918, SEQ ID No: 920, SEQ ID No: 922, SEQ ID No: 924, SEQ ID No: 926, SEQ ID No: 928, SEQ ID No: 930, SEQ ID No: 932, SEQ ID No: 934, SEQ ID No: 936, SEQ ID No: 938, SEQ ID No: 940, SEQ ID No: 942, SEQ ID No: 944, SEQ ID No: 946, SEQ ID No: 948, SEQ ID No: 950, SEQ ID No: 952, SEQ ID No: 954, SEQ ID No: 956, SEQ ID No: 958, SEQ ID No: 960, SEQ ID No: 962, SEQ ID No: 964, SEQ ID No: 966, SEQ ID No: 968, SEQ ID No: 970, SEQ ID No: 972, SEQ ID No: 974, SEQ ID No: 976, SEQ ID No: 978, SEQ ID No: 980, SEQ ID No: 982, SEQ ID No: 984, SEQ ID No: 986, SEQ ID No: 988, SEQ ID No: 990, SEQ ID No: 992, SEQ ID No: 994, SEQ ID No: 996, SEQ ID No: 998, SEQ ID No: 1000, SEQ ID No: 1002, SEQ ID No: 1004, SEQ ID No: 1006, SEQ ID No: 1008, SEQ ID No: 1010, SEQ ID No: 1012, SEQ ID No: 1014, SEQ ID No: 1016, SEQ ID No: 1018, SEQ ID No: 1020, SEQ ID No: 1022, SEQ ID No: 1024, SEQ ID No: 1026, SEQ ID No: 1028, SEQ ID No: 1030, SEQ ID No: 1032, SEQ ID No: 1034, SEQ ID No: 1036, SEQ ID No: 1038, SEQ ID No: 1040, SEQ ID No: 1042, SEQ ID No: 1044, SEQ ID No: 1046, SEQ ID No: 1048, SEQ ID No: 1050, SEQ ID No: 1052, SEQ ID No: 1054, SEQ ID No: 1056, SEQ ID No: 1058, SEQ ID No: 1060, SEQ ID No: 1062, SEQ ID No: 1064, SEQ ID No: 1066, SEQ ID No: 1068, SEQ ID No: 1070, SEQ ID No: 1072, SEQ ID No: 1074, SEQ ID No: 1076, SEQ ID No: 1078, SEQ ID No: 1080, SEQ ID No: 1082, SEQ ID No: 1084, SEQ ID No: 1086, SEQ ID No: 1088, SEQ ID No: 1090, SEQ ID No: 1092, SEQ ID No: 1094, SEQ ID No: 1096, SEQ ID No: 1098, SEQ ID NO: 1100, SEQ ID No: 1102, SEQ ID No: 1104, SEQ ID No: 1106, SEQ ID No: 1108, SEQ ID No: 1110, SEQ ID No: 1112, SEQ ID No: 1114, SEQ ID No: 1116, SEQ ID No: 1118, SEQ ID No: 1120, SEQ ID No: 1122, SEQ ID No: 1124, SEQ ID No: 1126, SEQ ID No: 1128, SEQ ID No: 1130, SEQ ID No: 1132, SEQ ID No: 1134, SEQ ID No: 1136, SEQ ID No: 1138, SEQ ID No: 1140, SEQ ID No: 1142, SEQ ID No: 1144, SEQ ID No: 1146, SEQ ID No: 1148, SEQ ID No: 1150, SEQ ID No: 1152, SEQ ID No: 1154, SEQ ID No: 1156, SEQ ID No: 1158, SEQ ID No: 1160, SEQ ID No: 1162, SEQ ID No: 1164, SEQ ID No: 1166, SEQ ID No: 1168, SEQ ID No: 1170, SEQ ID No: 1172, SEQ ID No: 1174, SEQ ID No: 1176, SEQ ID No: 1178, SEQ ID No: 1180, SEQ ID No: 1182, SEQ ID No: 1184, SEQ ID No: 1186, SEQ ID No: 1188, SEQ ID No: 1190, SEQ ID No: 1192, SEQ ID No: 1194, SEQ ID No: 1196, SEQ ID No: 1198, SEQ ID No: 1200, SEQ ID No: 1202, SEQ ID No: 1204, SEQ ID No: 1206, SEQ ID No: 1208, SEQ ID No: 1210, SEQ ID No: 1212, SEQ ID No: 1214, SEQ ID No: 1216, SEQ ID No: 1218, SEQ ID No: 1220, SEQ ID No: 1222, SEQ ID No: 1224, SEQ ID No: 1226, SEQ ID No: 1228, SEQ ID No: 1230, SEQ ID No: 1232, SEQ ID No: 1234, SEQ ID No: 1236, SEQ ID No: 1238, SEQ ID No: 1240, SEQ ID No: 1242, SEQ ID No: 1244, SEQ ID No: 1246, SEQ ID No: 1248, SEQ ID No: 1250, SEQ ID No: 1252, SEQ ID No: 1254, SEQ ID No: 1256, SEQ ID No: 1258, SEQ ID No: 1260, SEQ ID No: 1262, SEQ ID No: 1264, SEQ ID No: 1266, SEQ ID No: 1268, SEQ ID No: 1270, SEQ ID No: 1272, SEQ ID No: 1274, SEQ ID No: 1276, SEQ ID No: 1278, SEQ ID No: 1280, SEQ ID No: 1282, SEQ ID No: 1284, SEQ ID No: 1286, SEQ ID No: 1288, SEQ ID No: 1290, SEQ ID No: 1292, SEQ ID No: 1294, SEQ ID No: 1296, SEQ ID No: 1298, SEQ ID No: 1300, SEQ ID No: 1302, SEQ ID No: 1304, SEQ ID No: 1306, SEQ ID No: 1308, SEQ ID No: 1310, SEQ ID No: 1312, SEQ ID No: 1314, SEQ ID No: 1316, SEQ ID No: 1318, SEQ ID No: 1320, SEQ ID No: 1322, SEQ ID No: 1324, SEQ ID No: 1326, SEQ ID No: 1328, SEQ ID No: 1330, SEQ ID No: 1332, SEQ ID No: 1334, SEQ ID No: 1336, SEQ ID No: 1338, SEQ ID No: 1340, SEQ ID No: 1342, SEQ ID No: 1344, SEQ ID No: 1346, SEQ ID No: 1348, SEQ ID No: 1350, SEQ ID No: 1352, SEQ ID No: 1354, SEQ ID No: 1356, SEQ ID No: 1358, SEQ ID No: 1360, SEQ ID No: 1362, SEQ ID No: 1364, SEQ ID No: 1366, SEQ ID No: 1368, SEQ ID No: 1370, SEQ ID No: 1372, SEQ ID No: 1374, SEQ ID No: 1376, SEQ ID No: 1378, SEQ ID No: 1380, SEQ ID No: 1382, SEQ ID No: 1384, SEQ ID No: 1386, SEQ ID No: 1388, SEQ ID No: 1390, SEQ ID No: 1392, SEQ ID No: 1394, SEQ ID No: 1396, SEQ ID No: 1398, SEQ ID No: 1400, SEQ ID No: 1402, SEQ ID No: 1404, SEQ ID No: 1406, SEQ ID No: 1408, SEQ ID No: 1410, SEQ ID No: 1412, SEQ ID No: 1414, SEQ ID No: 1416, SEQ ID No: 1418, SEQ ID No: 1420, SEQ ID No: 1422, SEQ ID No: 1424, SEQ ID No: 1426, SEQ ID No: 1428, SEQ ID No: 1430, SEQ ID No: 1432, SEQ ID No: 1434, SEQ ID No: 1436, SEQ ID No: 1438, SEQ ID No: 1440, SEQ ID No: 1442, SEQ ID No: 1444, SEQ ID No: 1446, SEQ ID No: 1448, SEQ ID No: 1450, SEQ ID No: 1452, SEQ ID No: 1454, SEQ ID No: 1456, SEQ ID No: 1458, SEQ ID No: 1460, SEQ ID No: 1462, SEQ ID No: 1464, SEQ ID No: 1466, SEQ ID No: 1468, SEQ ID No: 1470, SEQ ID No: 1472, SEQ ID No: 1474, SEQ ID No: 1476, SEQ ID No: 1478, SEQ ID No: 1480, SEQ ID No: 1482, SEQ ID No: 1484, SEQ ID No: 1486, SEQ ID No: 1488, SEQ ID No: 1490, SEQ ID No: 1492, SEQ ID No: 1494, SEQ ID No: 1496, SEQ ID No: 1498, SEQ ID No : 1500, SEQ ID No: 1502, SEQ ID No: 1504, SEQ ID No: 1506, SEQ ID No: 1508, SEQ ID No: 1510, SEQ ID No: 1512, SEQ ID No: 1514, SEQ ID No: 1516, SEQ ID No : 1518, SEQ ID No: 1520, SEQ ID No: 1522, SEQ ID No: 1524, SEQ ID No: 1526, SEQ ID No: 1528, SEQ ID No: 1530, SEQ ID No: 1532, SEQ ID No: 1534, SEQ ID No : 1536, SEQ ID No: 1538, SEQ ID No: 1540, SEQ ID No: 1542, SEQ ID No: 1544, SEQ ID No: 1546, SEQ ID No: 1548, SEQ ID No: 1550, SEQ ID No: 1552, SEQ ID No : 1554, SEQ ID No: 1556, SEQ ID No: 1558, SEQ ID No: 1560, SEQ ID No: 1562, SEQ ID No: 1564, SEQ ID No: 1566, SEQ ID No: 1568, SEQ ID No: 1570, SEQ ID No : 1572, SEQ ID No: 1574, SEQ ID No: 1576, SEQ ID No: 1578, SEQ ID No: 1580, SEQ ID No: 1582, SEQ ID No: 1584, SEQ ID No: 1586, SEQ ID No: 1588, SEQ ID No : 1590, SEQ ID No: 1592, SEQ ID No: 1594, SEQ ID No: 1596, SEQ ID No: 1598, SEQ ID No: 1600, SEQ ID No: 1602, SEQ ID No: 1604, SEQ ID No: 1606, SEQ ID No : 1608, SEQ ID No: 1610, SEQ ID No: 1612, SEQ ID No: 1614, SEQ ID No: 1616, SEQ ID No: 1618, SEQ ID No: 1620, SEQ ID No: 1622, SEQ ID No: 1624, SEQ ID No : 1626, SEQ ID No: 1628, SEQ ID No: 1630, SEQ ID No: 1632, SEQ ID No: 1634, SEQ ID No: 1636, SEQ ID No: 1638, SEQ ID No: 1640, SEQ ID No: 1642, SEQ ID No : 1644, SEQ ID No: 1646, SEQ ID No: 1648, SEQ ID No: 1650, SEQ ID No: 1652, SEQ ID No: 1654, SEQ ID No: 1656, SEQ ID No: 1658, SEQ ID No: 1660, SEQ ID No : 1662, SEQ ID No: 1664, SEQ ID No: 1666, SEQ ID No: 1668, SEQ ID No: 1670, SEQ ID No: 1672, SEQ ID No: 1674, SEQ ID No: 1676, SEQ ID No: 1678, SEQ ID No : 1680, SEQ ID No: 1682, SEQ ID No: 1684, SEQ ID No: 1686, SEQ ID No: 1688, SEQ ID No: 1690, SEQ ID No: 1692, SEQ ID No: 1694, SEQ ID No: 1696, SEQ ID No : 1698, SEQ ID No: 1700, SEQ ID No: 1702, SEQ ID No: 1704, SEQ ID No: 1706, SEQ ID No: 1708, SEQ ID No: 1710, SEQ ID No: 1712, SEQ ID No: 1714, SEQ ID No : 1716, SEQ ID No: 1718, SEQ ID No: 1720, SEQ ID No: 1722, SEQ ID No: 1724, SEQ ID No: 1726, SEQ ID No: 1728, SEQ ID No: 1730, SEQ ID No: 1732, SEQ ID No : 1734, SEQ ID No: 1736, SEQ ID No: 1738, SEQ ID No: 1740, SEQ ID No: 1742, SEQ ID No: 1744, SEQ ID No: 1746, SEQ ID No: 1748, SEQ ID No: 1750, SEQ ID No : 1752, SEQ ID No: 1754, SEQ ID No: 1756, SEQ ID No: 1758, SEQ ID No: 1760, SEQ ID No: 1762, SEQ ID No: 1764, SEQ ID No: 1766, SEQ ID No: 1768, SEQ ID No : 1770, SEQ ID No: 1772, SEQ ID No: 1774, SEQ ID No: 1776, SEQ ID No: 1778, SEQ ID No: 1780, SEQ ID No: 1782, SEQ ID No: 1784, SEQ ID No: 1786, SEQ ID No : 1788, SEQ ID No: 1790, SEQ ID No: 1792, SEQ ID No: 1794, SEQ ID No: 1796, SEQ ID No: 1798, SEQ ID No: 1800, SEQ ID No: 1802, SEQ ID No: 1804, SEQ ID No: 1806, SEQ ID No: 1808, SEQ ID No: 1810, SEQ ID No: 1812, SEQ ID No: 1814, SEQ ID No: 1816, SEQ ID No: 1818, SEQ ID No: 1820, SEQ ID No: 1822, SEQ ID No: 1824, SEQ ID No: 1826, SEQ ID No: 1828, SEQ ID No: 1830, SEQ ID No: 1832, SEQ ID No: 1834, SEQ ID No: 1836, SEQ ID No: 1838, SEQ ID No: 1840, SEQ ID No: 1842, SEQ ID No: 1844, SEQ ID No: 1846, SEQ ID No: 1848, SEQ ID No: 1850, SEQ ID No: 1852, SEQ ID No: 1854, SEQ ID No: 1856, SEQ ID No: 1858, SEQ ID No: 1860, SEQ ID No: 1862, SEQ ID No: 1864, SEQ ID No: 1866, SEQ ID No: 1868, SEQ ID No: 1870, SEQ ID No: 1872, SEQ ID No: 1874, SEQ ID No: 1876, SEQ ID No: 1878, SEQ ID No: 1880, SEQ ID No: 1882, SEQ ID No: 1884, SEQ ID No: 1886, SEQ ID No: 1888, SEQ ID No: 1890, SEQ ID No: 1892, SEQ ID No: 1894, SEQ ID No: 1896, SEQ ID No: 1898, SEQ ID No: 1900, SEQ ID No: 1902, SEQ ID No: 1904, SEQ ID No: 1906, SEQ ID No: 1908, SEQ ID No: 1910, SEQ ID No: 1912, SEQ ID No: 1914, SEQ ID No: 1916, SEQ ID No: 1918, SEQ ID No: 1920, SEQ ID No: 1922, SEQ ID No: 1924, SEQ ID No: 1926, SEQ ID No: 1928, SEQ ID No: 1930, SEQ ID No: 1932, SEQ ID No: 1934, SEQ ID No: 1936, SEQ ID No: 1938, SEQ ID No: 1940, SEQ ID No: 1942, SEQ ID No: 1944, SEQ ID No: 1946, SEQ ID No: 1948, SEQ ID No: 1950, SEQ ID No: 1952, SEQ ID No: 1954, SEQ ID No: 1956, SEQ ID No: 1958, SEQ ID No: 1960, SEQ ID No: 1962, SEQ ID No: 1964, SEQ ID No: 1966, SEQ ID No: 1968, SEQ ID No: 1970, SEQ ID No: 1972, and SEQ ID No: 1974.
8. The isolated nucleic acid sequence of claim 1, wherein said nucleic acid sequence comprises a nucleic acid sequence selected from the group consisting of: the nucleic acid sequences of SEQ ID No: 1, SEQ ID No: 3, SEQ ID No: 5, SEQ ID No: 7, SEQ ID No: 9, SEQ ID No: 11, SEQ ID No: 13, SEQ ID No: 15, SEQ ID No: 17, SEQ ID No: 19, SEQ ID No: 21, SEQ ID No: 23, SEQ ID No: 25, SEQ ID No: 27, SEQ ID No: 29, SEQ ID No: 31, SEQ ID No: 33, SEQ ID No: 35, SEQ ID No: 37, SEQ ID No: 39, SEQ ID No: 41, SEQ ID No: 43, SEQ ID No: 45, SEQ ID No: 47, SEQ ID No: 49, SEQ ID No: 51, SEQ ID No: 53, SEQ ID No: 55, SEQ ID No: 56, SEQ ID No: 57, SEQ ID No: 59, SEQ ID No: 61, SEQ ID No: 63, SEQ ID No: 65, SEQ ID No: 67, SEQ ID No: 69, SEQ ID No: 71, SEQ ID No: 73, SEQ ID No: 75, SEQ ID No: 77, SEQ ID No: 79, SEQ ID No: 81, SEQ ID No: 83, SEQ ID No: 85, SEQ ID No: 87, SEQ ID No: 89, SEQ ID No: 91, SEQ ID No: 93, SEQ ID No: 95, SEQ ID No: 97, SEQ ID No: 99, SEQ ID No: 101, SEQ ID No: 103, SEQ ID No: 105 SEQ ID No: 107 SEQ ID No: 109 SEQ ID No: 111 SEQ ID No: 113
SEQ ID No: 115 SEQ ID No: 117 SEQ ID No: 119 SEQ ID No: 121 SEQ ID No: 123
SEQ ID No: 125 SEQ ID No: 127, SEQ ID No: 129 SEQ ID No: 131 SEQ ID No: 133
SEQ ID No: 135 SEQ ID No: 137, SEQ ID No: 139 SEQ ID No: 141 SEQ ID No: 143
SEQ ID No: 145 SEQ ID No: 147 SEQ ID No: 149 SEQ ID No: 151 SEQ ID No: 153
SEQ ID No: 155 SEQ ID No: 157, SEQ ID No: 159 SEQ ID No: 161 SEQ ID No: 163
SEQ ID No: 165 SEQ ID No: 167 SEQ ID No: 169 SEQ ID No: 171 SEQ ID No: 173
SEQ ID No: 175 SEQ ID No: 177, SEQ ID No: 179 SEQ ID No: 181 SEQ ID No: 183
SEQ ID No: 185 SEQ ID No: 187 SEQ ID No: 189 SEQ ID No: 191 SEQ ID No: 193
SEQ ID No: 195 SEQ ID No: 197 SEQ ID No: 199 SEQ ID No: 201 SEQ ID No: 203
SEQ ID No: 205 SEQ ID No: 207 SEQ ID No: 209 SEQ ID No: 211 SEQ ID No: 213
SEQ ID No: 215 SEQ ID No: 217, SEQ ID No: 219 SEQ ID No: 221 SEQ ID No: 223
SEQ ID No: 225 SEQ ID No: 227, SEQ ID No: 229 SEQ ID No: 231 SEQ ID No: 233
SEQ ID No: 235 SEQ ID No: 237, SEQ ID No: 239 SEQ ID No: 241 SEQ ID No: 243
SEQ ID No: 245 SEQ ID No: 247, SEQ ID No: 249 SEQ ID No: 251 SEQ ID No: 253
SEQ ID No: 255 SEQ ID No: 257, SEQ ID No: 259 SEQ ID No: 261 SEQ ID No: 263
SEQ ID No: 265 SEQ ID No: 267, SEQ ID No: 269 SEQ ID No: 271 SEQ ID No: 273
SEQ ID No: 275 SEQ ID No: 277, SEQ ID No: 279, SEQ ID No: 281 SEQ ID No: 283
SEQ ID No: 285 SEQ ID No: 287, SEQ ID No: 289 SEQ ID No: 291 SEQ ID No: 293
SEQ ID No: 295 SEQ ID No: 297, SEQ ID No: 299 SEQ ID No: 301 SEQ ID No: 303
SEQ ID No: 305 SEQ ID No: 307 SEQ ID No: 309 SEQ ID No: 311 SEQ ID No: 313
SEQ ID No: 315 SEQ ID No: 317, SEQ ID No: 319 SEQ ID No: 321 SEQ ID No: 323
SEQ ID No: 325 SEQ ID No: 327, SEQ ID No: 329 SEQ ID No: 331 SEQ ID No: 333
SEQ ID No: 335 SEQ ID No: 337, SEQ ID No: 339 SEQ ID No: 341 SEQ ID No: 343
SEQ ID No: 345 SEQ ID No: 347, SEQ ID No: 349 SEQ ID No: 351 SEQ ID No: 353
SEQ ID No: 355 SEQ ID No: 357, SEQ ID No: 359 SEQ ID No: 361 SEQ ID No: 363
SEQ ID No: 365 SEQ ID No: 367, SEQ ID No: 369 SEQ ID No: 371 SEQ ID No: 373
SEQ ID No: 375 SEQ ID No: 377, SEQ ID No: 379, SEQ ID No: 381 SEQ ID No: 383
SEQ ID No: 385 SEQ ID No: 387, SEQ ID No: 389 SEQ ID No: 391 SEQ ID No: 393
SEQ ID No: 395 SEQ ID No: 397, SEQ ID No: 399 SEQ ID No: 401 SEQ ID No: 403
SEQ ID No: 405 SEQ ID No: 407 SEQ ID No: 409 SEQ ID No: 411 SEQ ID No: 413
SEQ ID No: 415 SEQ ID No: 417 SEQ ID No: 419 SEQ ID No: 421 SEQ ID No: 423
SEQ ID No: 425 SEQ ID No: 427, SEQ ID No: 429 SEQ ID No: 431 SEQ ID No: 433 SEQ ID No: 435 SEQ ID No: 437, SEQ ID No: 439 SEQ ID No: 441 SEQ ID No: 443
SEQ ID No: 445 SEQ ID No: 447 SEQ ID No: 449 SEQ ID No: 451 SEQ ID No: 453
SEQ ID No: 455 SEQ ID No: 457, SEQ ID No: 459 SEQ ID No: 461 SEQ ID No: 463
SEQ ID No: 465 SEQ ID No: 467 SEQ ID No: 469 SEQ ID No: 471 SEQ ID No: 473
SEQ ID No: 475 SEQ ID No: 477, SEQ ID No: 479 SEQ ID No: 481 SEQ ID No: 483
SEQ ID No: 485 SEQ ID No: 487, SEQ ID No: 489 SEQ ID No: 491 SEQ ID No: 493
SEQ ID No: 495 SEQ ID No: 497 SEQ ID No: 499 SEQ ID No: 501 SEQ ID No: 503
SEQ ID No: 505 SEQ ID No: 507 SEQ ID No: 509 SEQ ID No: 511 SEQ ID No: 513
SEQ ID No: 515 SEQ ID No: 517, SEQ ID No: 519 SEQ ID No: 521 SEQ ID No: 523
SEQ ID No: 525 SEQ ID No: 527, SEQ ID No: 529 SEQ ID No: 531 SEQ ID No: 533
SEQ ID No: 535 SEQ ID No: 537, SEQ ID No: 539 SEQ ID No: 541 SEQ ID No: 543
SEQ ID No: 545 SEQ ID No: 547, SEQ ID No: 549 SEQ ID No: 551 SEQ ID No: 553
SEQ ID No: 555 SEQ ID No: 557, SEQ ID No: 559 SEQ ID No: 561 SEQ ID No: 563
SEQ ID No: 565 SEQ ID No: 567, SEQ ID No: 569 SEQ ID No: 571 SEQ ID No: 573
SEQ ID No: 575 SEQ ID No: 577, SEQ ID No: 579, SEQ ID No: 581 SEQ ID No: 583
SEQ ID No: 585 SEQ ID No: 587, SEQ ID No: 589 SEQ ID No: 591 SEQ ID No: 593
SEQ ID No: 595 SEQ ID No: 597, SEQ ID No: 599 SEQ ID No: 601 SEQ ID No: 603
SEQ ID No: 605 SEQ ID No: 607 SEQ ID No: 609 SEQ ID No: 611 SEQ ID No: 613
SEQ ID No: 615 SEQ ID No: 617 SEQ ID No: 619 SEQ ID No: 621 SEQ ID No: 623
SEQ ID No: 625 SEQ ID No: 627, SEQ ID No: 629 SEQ ID No: 631 SEQ ID No: 633
SEQ ID No: 635 SEQ ID No: 637, SEQ ID No: 639 SEQ ID No: 641 SEQ ID No: 643
SEQ ID No: 645 SEQ ID No: 647 SEQ ID No: 649 SEQ ID No: 651 SEQ ID No: 653
SEQ ID No: 655 SEQ ID No: 657, SEQ ID No: 659 SEQ ID No: 661 SEQ ID No: 663
SEQ ID No: 665 SEQ ID No: 667 SEQ ID No: 669 SEQ ID No: 671 SEQ ID No: 673
SEQ ID No: 675 SEQ ID No: 677, SEQ ID No: 679 SEQ ID No: 681 SEQ ID No: 683
SEQ ID No: 685 SEQ ID No: 687, SEQ ID No: 689 SEQ ID No: 691 SEQ ID No: 693
SEQ ID No: 695 SEQ ID No: 697 SEQ ID No: 699 SEQ ID No: 701 SEQ ID No: 703
SEQ ID No: 705 SEQ ID No: 707 SEQ ID No: 709 SEQ ID No: 711 SEQ ID No: 713
SEQ ID No: 715 SEQ ID No: 717, SEQ ID No: 719 SEQ ID No: 721 SEQ ID No: 723
SEQ ID No: 725 SEQ ID No: 727, SEQ ID No: 729, SEQ ID No: 731 SEQ ID No: 733
SEQ ID No: 735 SEQ ID No: 737, SEQ ID No: 739, SEQ ID No: 741 SEQ ID No: 743
SEQ ID No: 745 SEQ ID No: 747, SEQ ID No: 749 SEQ ID No: 751 SEQ ID No: 753
SEQ ID No: 755 SEQ ID No: 757, SEQ ID No: 759, SEQ ID No: 761 SEQ ID No: 763 SEQ ID No: 765, SEQ ID No: 767, SEQ ID No: 769, SEQ ID No: 771, SEQ ID No: 773,
SEQ ID No: 775, SEQ ID No: 777, SEQ ID No: 779, SEQ ID No: 781, SEQ ID No: 783,
SEQ ID No: 785, SEQ ID No: 787, SEQ ID No: 789, SEQ ID No: 791, SEQ ID No: 793,
SEQ ID No: 795, SEQ ID No: 797, SEQ ID No: 799, SEQ ID No: 801, SEQ ID No: 803,
SEQ ID No: 805, SEQ ID No: 807, SEQ ID No: 809, SEQ ID No: 811, SEQ ID No: 813,
SEQ ID No: 815, SEQ ID No: 817, SEQ ID No: 819, SEQ ID No: 821, SEQ ID No: 823,
SEQ ID No: 825, SEQ ID No: 827, SEQ ID No: 829, SEQ ID No: 831, SEQ ID No: 833,
SEQ ID No: 835, SEQ ID No: 837, SEQ ID No: 839, SEQ ID No: 841, SEQ ID No: 843,
SEQ ID No: 845, SEQ ID No: 847, SEQ ID No: 849, SEQ ID No: 851, SEQ ID No: 853,
SEQ ID No: 855, SEQ ID No: 857, SEQ ID No: 859, SEQ ID No: 861, SEQ ID No: 863,
SEQ ID No: 865, SEQ ID No: 867, SEQ ID No: 869, SEQ ID No: 871, SEQ ID No: 873,
SEQ ID No: 875, SEQ ID No: 877, SEQ ID No: 879, SEQ ID No: 881, SEQ ID No: 883,
SEQ ID No: 885, SEQ ID No: 887, SEQ ID No: 889, SEQ ID No: 891, SEQ ID No: 893,
SEQ ID No: 895, SEQ ID No: 897, SEQ ID No: 899, SEQ ID No: 901, SEQ ID No: 903,
SEQ ID No: 905, SEQ ID No: 907, SEQ ID No: 909, SEQ ID No: 911, SEQ ID No: 913,
SEQ ID No: 915, SEQ ID No: 917, SEQ ID No: 919, SEQ ID No: 921, SEQ ID No: 923,
SEQ ID No: 925, SEQ ID No: 927, SEQ ID No: 929, SEQ ID No: 931, SEQ ID No: 933,
SEQ ID No: 935, SEQ ID No: 937, SEQ ID No: 939, SEQ ID No: 941, SEQ ID No: 943,
SEQ ID No: 945, SEQ ID No: 947, SEQ ID No: 949, SEQ ID No: 951, SEQ ID No: 953,
SEQ ID No: 955, SEQ ID No: 957, SEQ ID No: 959, SEQ ID No: 961, SEQ ID No: 963,
SEQ ID No: 965, SEQ ID No: 967, SEQ ID No: 969, SEQ ID No: 971, SEQ ID No: 973,
SEQ ID No: 975, SEQ ID No: 977, SEQ ID No: 979, SEQ ID No: 981, SEQ ID No: 983,
SEQ ID No: 985, SEQ ID No: 987, SEQ ID No: 989, SEQ ID No: 991, SEQ ID No: 993,
SEQ ID No: 995, SEQ ID No: 997, SEQ ID No: 999, SEQ ID No: 1001, SEQ ID No:
1003, SEQ ID Nc >: 1005, SEQ ID No: 1007, SEQ ID No: 1009, SEQ ID No: 1011, SEQ
ID No: 1013, SEQ ID No: 1015, SEQ ID No: 1017, SEQ ID No: 1019, SEQ ID No: 1021, SEQ ID No: 1023, SEQ ID No: 1025, SEQ ID No: 1027, SEQ ID No: 1029, SEQ ID No: 1031, SEQ ID No: 1033, SEQ ID No: 1035, SEQ ID No: 1037, SEQ ID No: 1039, SEQ ID No: 1041, SEQ ID No: 1043, SEQ ID No: 1045, SEQ ID No: 1047, SEQ ID No: 1049, SEQ ID No: 1051, SEQ ID No: 1053, SEQ ID No: 1055, SEQ ID No: 1057, SEQ ID No: 1059, SEQ ID No: 1061, SEQ ID No: 1063, SEQ ID No: 1065, SEQ ID No: 1067, SEQ ID No: 1069, SEQ ID No: 1071, SEQ ID No: 1073, SEQ ID No: 1075, SEQ ID No: 1077, SEQ ID No: 1079, SEQ ID No: 1081, SEQ ID No: 1083, SEQ ID No: 1085, SEQ ID No: 1087, SEQ ID No: 1089, SEQ ID No: 1091, SEQ ID No: 1093, SEQ ID No: 1095, SEQ ID No: 1097, SEQ ID No: 1099, SEQ ID No: 1101, SEQ ID No: 1103, SEQ ID No: 1105, SEQ ID No: 1107, SEQ ID No: 1109, SEQ ID No: 1111, SEQ ID No: 1113, SEQ ID No: 1115, SEQ ID No: 1117, SEQ ID No: 1119, SEQ ID No: 1121, SEQ ID No: 1123, SEQ ID No: 1125, SEQ ID No: 1127, SEQ ID No: 1129, SEQ ID No: 1131, SEQ ID No: 1133, SEQ ID No: 1135, SEQ ID No: 1137, SEQ ID No: 1139, SEQ ID No: 1141, SEQ ID No: 1143, SEQ ID No: 1145, SEQ ID No: 1147, SEQ ID No: 1149, SEQ ID No: 1151, SEQ ID No: 1153, SEQ ID No: 1155, SEQ ID No: 1157, SEQ ID No: 1159, SEQ ID No: 1161, SEQ ID No: 1163, SEQ ID No: 1165, SEQ ID No: 1167, SEQ ID No: 1169, SEQ ID No: 1171, SEQ ID No: 1173, SEQ ID No: 1175, SEQ ID No: 1177, SEQ ID No: 1179, SEQ ID No: 1181, SEQ ID No: 1183, SEQ ID No: 1185, SEQ ID No: 1187, SEQ ID No: 1189, SEQ ID No: 1191, SEQ ID No: 1193, SEQ ID No: 1195, SEQ ID No: 1197, SEQ ID No: 1199, SEQ ID No: 1201, SEQ ID No: 1203, SEQ ID No: 1205, SEQ ID No: 1207, SEQ ID No: 1209, SEQ ID No: 1211, SEQ ID No: 1213, SEQ ID No: 1215, SEQ ID No: 1217, SEQ ID No: 1219, SEQ ID No: 1221, SEQ ID No: 1223, SEQ ID No: 1225, SEQ ID No: 1227, SEQ ID No: 1229, SEQ ID No: 1231, SEQ ID No: 1233, SEQ ID No: 1235, SEQ ID No: 1237, SEQ ID No: 1239, SEQ ID No: 1241, SEQ ID No: 1243, SEQ ID No: 1245, SEQ ID No: 1247, SEQ ID No: 1249, SEQ ID No: 1251, SEQ ID No: 1253, SEQ ID No: 1255, SEQ ID No: 1257, SEQ ID No: 1259, SEQ ID No: 1261, SEQ ID No: 1263, SEQ ID No: 1265, SEQ ID No: 1267, SEQ ID No: 1269, SEQ ID No: 1271, SEQ ID No: 1273, SEQ ID No: 1275, SEQ ID No: 1277, SEQ ID No: 1279, SEQ ID No: 1281, SEQ ID No: 1283, SEQ ID No: 1285, SEQ ID No: 1287, SEQ ID No: 1289, SEQ ID No: 1291, SEQ ID No: 1293, SEQ ID No: 1295, SEQ ID No: 1297, SEQ ID No: 1299, SEQ ID No: 1301, SEQ ID No: 1303, SEQ ID No: 1305, SEQ ID No: 1307, SEQ ID No: 1309, SEQ ID No: 1311, SEQ ID No: 1313, SEQ ID No: 1315, SEQ ID No: 1317, SEQ ID No: 1319, SEQ ID No: 1321, SEQ ID No: 1323, SEQ ID No: 1325, SEQ ID No: 1327, SEQ ID No: 1329, SEQ ID No: 1331, SEQ ID No: 1333, SEQ ID No: 1335, SEQ ID No: 1337, SEQ ID No: 1339, SEQ ID No: 1341, SEQ ID No: 1343, SEQ ID No: 1345, SEQ ID No: 1347, SEQ ID No: 1349, SEQ ID No: 1351, SEQ ID No: 1353, SEQ ID No: 1355, SEQ ID No: 1357, SEQ ID No: 1359, SEQ ID No: 1361, SEQ ID No: 1363, SEQ ID No: 1365, SEQ ID No: 1367, SEQ ID No: 1369, SEQ ID No: 1371, SEQ ID No: 1373, SEQ ID No: 1375, SEQ ID No: 1377, SEQ ID No: 1379, SEQ ID No: 1381, SEQ ID No: 1383, SEQ ID No: 1385, SEQ ID No: 1387, SEQ ID No: 1389, SEQ ID No: 1391, SEQ ID No: 1393, SEQ ID No: 1395, SEQ ID No: 1397, SEQ ID No: 1399, SEQ ID No: 1401, SEQ ID No: 1403, SEQ ID No: 1405, SEQ ID No: 1407, SEQ ID No: 1409, SEQ ID No: 1411, SEQ ID No: 1413, SEQ ID No: 1415, SEQ ID No: 1417, SEQ ID No: 1419, SEQ ID No: 1421, SEQ ID No: 1423, SEQ ID No: 1425, SEQ ID No: 1427, SEQ ID No: 1429, SEQ ID No: 1431, SEQ ID No: 1433, SEQ ID No: 1435, SEQ ID No: 1437, SEQ ID No: 1439, SEQ ID No: 1441, SEQ ID No: 1443, SEQ ID No: 1445, SEQ ID No: 1447, SEQ ID No: 1449, SEQ ID No: 1451, SEQ ID No: 1453, SEQ ID No: 1455, SEQ ID No: 1457, SEQ ID No: 1459, SEQ ID No: 1461, SEQ ID No: 1463, SEQ ID No: 1465, SEQ ID No: 1467, SEQ ID No: 1469, SEQ ID No: 1471, SEQ ID No: 1473, SEQ ID No: 1475, SEQ ID No: 1477, SEQ ID No: 1479, SEQ ID No: 1481, SEQ ID No: 1483, SEQ ID No: 1485, SEQ ID No: 1487, SEQ ID No: 1489, SEQ ID No: 1491, SEQ ID No: 1493, SEQ ID No: 1495, SEQ ID No: 1497, SEQ ID No: 1499, SEQ ID No: 1501, SEQ ID No: 1503, SEQ ID No: 1505, SEQ ID No: 1507, SEQ ID No: 1509, SEQ ID No: 1511, SEQ ID No: 1513, SEQ ID No: 1515, SEQ ID No: 1517, SEQ ID No: 1519, SEQ ID No: 1521, SEQ ID No: 1523, SEQ ID No: 1525, SEQ ID No: 1527, SEQ ID No: 1529, SEQ ID No: 1531, SEQ ID No: 1533, SEQ ID No: 1535, SEQ ID No: 1537, SEQ ID No: 1539, SEQ ID No: 1541, SEQ ID No: 1543, SEQ ID No: 1545, SEQ ID No: 1547, SEQ ID No: 1549, SEQ ID No: 1551, SEQ ID No: 1553, SEQ ID No: 1555, SEQ ID No: 1557, SEQ ID No: 1559, SEQ ID No: 1561, SEQ ID No: 1563, SEQ ID No: 1565, SEQ ID No: 1567, SEQ ID No: 1569, SEQ ID No: 1571, SEQ ID No: 1573, SEQ ID No: 1575, SEQ ID No: 1577, SEQ ID No: 1579, SEQ ID No: 1581, SEQ ID No: 1583, SEQ ID No: 1585, SEQ ID No: 1587, SEQ ID No: 1589, SEQ ID No: 1591, SEQ ID No: 1593, SEQ ID No: 1595, SEQ ID No: 1597, SEQ ID No: 1599, SEQ ID No: 1601, SEQ ID No: 1603, SEQ ID No: 1605, SEQ ID No: 1607, SEQ ID No: 1609, SEQ ID No: 1611, SEQ ID No: 1613, SEQ ID No: 1615, SEQ ID No: 1617, SEQ ID No: 1619, SEQ ID No: 1621, SEQ ID No: 1623, SEQ ID No: 1625, SEQ ID No: 1627, SEQ ID No: 1629, SEQ ID No: 1631, SEQ ID No: 1633, SEQ ID No: 1635, SEQ ID No: 1637, SEQ ID No: 1639, SEQ ID No: 1641, SEQ ID No: 1643, SEQ ID No: 1645, SEQ ID No: 1647, SEQ ID No: 1649, SEQ ID No: 1651, SEQ ID No: 1653, SEQ ID No: 1655, SEQ ID No: 1657, SEQ ID No: 1659, SEQ ID No: 1661, SEQ ID No: 1663, SEQ ID No: 1665, SEQ ID No: 1667, SEQ ID No: 1669, SEQ ID No: 1671, SEQ ID No: 1673, SEQ ID No: 1675, SEQ ID No: 1677, SEQ ID No: 1679, SEQ ID No: 1681, SEQ ID No: 1683, SEQ ID No: 1685, SEQ ID No: 1687, SEQ ID No: 1689, SEQ ID No: 1691, SEQ ID No: 1693, SEQ ID No: 1695, SEQ ID No: 1697, SEQ ID No: 1699, SEQ ID No: 1701, SEQ ID No: 1703, SEQ ID No: 1705, SEQ ID No: 1707, SEQ ID No: 1709, SEQ ID No: 1711, SEQ ID No: 1713, SEQ ID No: 1715, SEQ ID No: 1717, SEQ ID No: 1719, SEQ ID No: 1721, SEQ ID No: 1723, SEQ ID No: 1725, SEQ ID No: 1727, SEQ ID No: 1729, SEQ ID No: 1731, SEQ ID No: 1733, SEQ ID No: 1735, SEQ ID No: 1737, SEQ ID No: 1739, SEQ ID No: 1741, SEQ ID No: 1743, SEQ ID No: 1745, SEQ ID No: 1747, SEQ ID No: 1749, SEQ ID No: 1751, SEQ ID No: 1753, SEQ ID No: 1755, SEQ ID No: 1757, SEQ ID No: 1759, SEQ ID No: 1761, SEQ ID No: 1763, SEQ ID No: 1765, SEQ ID No: 1767, SEQ ID No: 1769, SEQ ID No: 1771, SEQ ID No: 1773, SEQ ID No: 1775, SEQ ID No: 1777, SEQ ID No: 1779, SEQ ID No: 1781, SEQ ID No: 1783, SEQ ID No: 1785, SEQ ID No: 1787, SEQ ID No: 1789, SEQ ID No: 1791, SEQ ID No: 1793, SEQ ID No: 1795, SEQ ID No: 1797, SEQ ID No: 1799, SEQ ID No: 1801, SEQ ID No: 1803, SEQ ID No: 1805, SEQ ID No: 1807, SEQ ID No: 1809, SEQ ID No: 1811, SEQ ID No: 1813, SEQ ID No: 1815, SEQ ID No: 1817, SEQ ID No: 1819, SEQ ID No: 1821, SEQ ID No: 1823, SEQ ID No: 1825, SEQ ID No: 1827, SEQ ID No: 1829, SEQ ID No: 1831, SEQ ID No: 1833, SEQ ID No: 1835, SEQ ID No: 1837, SEQ ID No: 1839, SEQ ID No: 1841, SEQ ID No: 1843, SEQ ID No: 1845, SEQ ID No: 1847, SEQ ID No: 1849, SEQ ID No: 1851, SEQ ID No: 1853, SEQ ID No: 1855, SEQ ID No: 1857, SEQ ID No: 1859, SEQ ID No: 1861, SEQ ID No: 1863, SEQ ID No: 1865, SEQ ID No: 1867, SEQ ID No: 1869, SEQ ID No: 1871, SEQ ID No: 1873, SEQ ID No: 1875, SEQ ID No: 1877, SEQ ID No: 1879, SEQ ID No: 1881, SEQ ID No: 1883, SEQ ID No: 1885, SEQ ID No: 1887, SEQ ID No: 1889, SEQ ID No: 1891, SEQ ID No: 1893, SEQ ID No: 1895, SEQ ID No: 1897, SEQ ID No: 1899, SEQ ID No: 1901, SEQ ID No: 1903, SEQ ID No: 1905, SEQ ID No: 1907, SEQ ID No: 1909, SEQ ID No: 1911, SEQ ID No: 1913, SEQ ID No: 1915, SEQ ID No: 1917, SEQ ID No: 1919, SEQ ID No: 1921, SEQ ID No: 1923, SEQ ID No: 1925, SEQ ID No: 1927, SEQ ID No: 1929, SEQ ID No: 1931, SEQ ID No: 1933, SEQ ID No: 1935, SEQ ID No: 1937, SEQ ID No: 1939, SEQ ID No: 1941, SEQ ID No: 1943, SEQ ID No: 1945, SEQ ID No: 1947, SEQ ID No: 1949, SEQ ID No: 1951, SEQ ID No: 1953, SEQ ID No: 1955, SEQ ID No: 1957, SEQ ID No: 1959, SEQ ID No: 1961, SEQ ID No: 1963, SEQ ID No: 1965, SEQ ID No: 1967, SEQ ID No: 1969, SEQ ID No: 1971, SEQ ID No: 1973.
9. An isolated nucleic acid sequence comprising a nucleic acid sequence that is fully complementary to the nucleic acid sequence of the nucleic acid sequence of any one of Claims 1 to 8.
10. An isolated protein comprising an amino acid sequence encoded by the nucleic acid sequence of any one of Claims 1 to 8.
11. An isolated fusion protein comprising the isolated protein of Claim 10 fused to a protein comprising an amino acid sequence that is heterologous to the isolated protein of Claim 10.
12. An isolated antibody or antigen binding fragment thereof that selectively binds to the protein of Claim 10.
13. A kit for degrading a lignin containing material to fermentable sugars comprising at least one isolated protein of Claim 10.
14. A bleach comprising at least one isolated protein of Claim 10.
15. A composition for degrading a lignocellulosic material comprising at least one isolated protein of Claim 10.
16. A composition for the bleaching of a material comprising at least one isolated protein of Claim 10.
17. The composition of claim 16, wherein the material is cotton, flour, or pulp.
18. A composition for disinfecting a vegetable comprising at least one isolated protein of Claim 10.
19. A composition for the improving the structure of a baked good comprising at least one isolated protein of Claim 10.
20. A composition for the production of sugar alcohols comprising at least one isolated protein of Claim 10.
21. The composition of claims 20, wherein the sugar alcohols are xylitol or sorbitol.
22. A composition for the degradation of lignin comprising at least one isolated protein of Claim 10.
23. A composition for the polymerization of phenols and aromatic amines comprising at least one isolated protein of Claim 10.
24. A composition for the asymmetric synthesis of amino acids, steroids, or fine chemicals comprising at least one isolated protein of Claim 10.
25. A composition for pollution control comprising at least one isolated protein of Claim 10.
26. A composition for the soil detoxification comprising at least one isolated protein of Claim 10.
27. A composition for the whitening of teeth comprising at least one isolated protein of Claim 10.
28. A pharmaceutical composition for stimulating the immune system comprising at least one isolated protein of Claim 10.
29. A recombinant nucleic acid sequence comprising the isolated nucleic acid sequence of any one of Claims 1 to 8, operatively linked to at least one expression control sequence.
30. The recombinant nucleic acid sequence of Claim 29, wherein the recombinant nucleic acid sequence comprises an expression vector.
31. The recombinant nucleic acid sequence of Claim 29, wherein the recombinant nucleic acid sequence comprises a targeting vector.
32. An isolated host cell transfected with the nucleic acid sequence of any one of Claims 1 to 9.
33. The isolated host cell of Claim 32, wherein the host cell is selected from the group consisting of: a fungal cell, a plant cell, an algal cell, and a bacterium.
34. The isolated host cell of Claim 32, wherein the host cell is selected from the group consisting of: yeast, mushroom, or a filamentous fungus.
35. The isolated host cell of Claim 32, wherein the filamentous fungus is from a genus selected from the group consisting of: Chrysosporium, Thielavia, Neurospora,
Aureobasidium, Filibasidium, Piromyces, Corynascus, Cryplococcus, Acremonium, Tolypocladium, Scytalidium, Schizophyllum, Sporotrichum, Penicillium, Gibberella, Myceliophthora, Mucor, Aspergillus, Fusarium, Humicola, and Trichoderma, and anamorphs and teleomorphs thereof.
36. The isolated host cell of Claim 32, wherein the host cell is a bacterium.
37. An oligonucleotide consisting essentially of at least 12 consecutive nucleotides of a nucleic acid sequence selected from the group consisting of the nucleic acid sequence of SEQ ID No: 1, SEQ ID No: 3, SEQ ID No: 5, SEQ ID No: 7, SEQ ID No: 9, SEQ ID No: 11, SEQ ID No: 13, SEQ ID No: 15, SEQ ID No: 17, SEQ ID No: 19, SEQ ID No: 21, SEQ ID No: 23, SEQ ID No: 25, SEQ ID No: 27, SEQ ID No: 29, SEQ ID No: 31, SEQ ID No: 33, SEQ ID No: 35, SEQ ID No: 37, SEQ ID No: 39, SEQ ID No: 41, SEQ ID No: 43, SEQ ID No: 45, SEQ ID No: 47, SEQ ID No: 49, SEQ ID No: 51, SEQ ID No: 53, SEQ ID No: 55, SEQ ID No: 56, SEQ ID No: 57, SEQ ID No: 59, SEQ ID No: 61, SEQ ID No: 63, SEQ ID No: 65, SEQ ID No: 67, SEQ ID No: 69, SEQ ID No: 71, SEQ ID No: 73, SEQ ID No: 75, SEQ ID No: 77, SEQ ID No: 79, SEQ ID No: 81, SEQ ID No: 83, SEQ ID No: 85, SEQ ID No: 87, SEQ ID No: 89, SEQ ID No: 91, SEQ ID No: 93, SEQ ID No: 95, SEQ ID No: 97, SEQ ID No: 99, SEQ ID No: 101, SEQ ID No: 103,
SEQ ID No: 105, SEQ ID No: 107, SEQ ID No: 109, SEQ ID No: 111, SEQ ID No: 113,
SEQ ID No: 115, SEQ ID No: 117, SEQ ID No: 119, SEQ ID No: 121, SEQ ID No: 123,
SEQ ID No: 125, SEQ ID No: 127, SEQ ID No: 129, SEQ ID No: 131, SEQ ID No: 133,
SEQ ID No: 135, SEQ ID No: 137, SEQ ID No: 139, SEQ ID No: 141, SEQ ID No: 143,
SEQ ID No: 145, SEQ ID No: 147, SEQ ID No: 149, SEQ ID No: 151, SEQ ID No: 153,
SEQ ID No: 155, SEQ ID No: 157, SEQ ID No: 159, SEQ ID No: 161, SEQ ID No: 163,
SEQ ID No: 165, SEQ ID No: 167, SEQ ID No: 169, SEQ ID No: 171, SEQ ID No: 173,
SEQ ID No: 175, SEQ ID No: 177, SEQ ID No: 179, SEQ ID No: 181, SEQ ID No: 183,
SEQ ID No: 185, SEQ ID No: 187, SEQ ID No: 189, SEQ ID No: 191, SEQ ID No: 193,
SEQ ID No: 195, SEQ ID No: 197, SEQ ID No: 199, SEQ ID No: 201, SEQ ID No: 203,
SEQ ID No: 205, SEQ ID No: 207, SEQ ID No: 209, SEQ ID No: 211, SEQ ID No: 213,
SEQ ID No: 215, SEQ ID No: 217, SEQ ID No: 219, SEQ ID No: 221, SEQ ID No: 223,
SEQ ID No: 225, SEQ ID No: 227, SEQ ID No: 229, SEQ ID No: 231, SEQ ID No: 233,
SEQ ID No: 235. SEQ ID No: 237, SEQ ID No: 239, SEQ ID No: 241, SEQ ID No: 243,
SEQ ID No: 245, SEQ ID No: 247, SEQ ID No: 249, SEQ ID No: 251, SEQ ID No: 253,
SEQ ID No: 255, SEQ ID No: 257, SEQ ID No: 259, SEQ ID No: 261, SEQ ID No: 263,
SEQ ID No: 265, SEQ ID No: 267, SEQ ID No: 269, SEQ ID No: 271, SEQ ID No: 273,
SEQ ID No: 275, SEQ ID No: 277, SEQ ID No: 279, SEQ ID No: 281, SEQ ID No: 283,
SEQ ID No: 285, SEQ ID No: 287, SEQ ID No: 289, SEQ ID No: 291, SEQ ID No: 293,
SEQ ID No: 295, SEQ ID No: 297, SEQ ID No: 299, SEQ ID No: 301, SEQ ID No: 303,
SEQ ID No: 305, SEQ ID No: 307, SEQ ID No: 309, SEQ ID No: 311, SEQ ID No: 313,
SEQ ID No: 315, SEQ ID No: 317, SEQ ID No: 319, SEQ ID No: 321, SEQ ID No: 323,
SEQ ID No: 325, SEQ ID No: 327, SEQ ID No: 329, SEQ ID No: 331, SEQ ID No: 333,
SEQ ID No: 335, SEQ ID No: 337, SEQ ID No: 339, SEQ ID No: 341, SEQ ID No: 343, SEQ ID No: 345 SEQ ID No: 347, SEQ ID No: 349 SEQ ID No: 351 SEQ ID No: 353
SEQ ID No: 355 SEQ ID No: 357, SEQ ID No: 359 SEQ ID No: 361 SEQ ID No: 363
SEQ ID No: 365 SEQ ID No: 367, SEQ ID No: 369 SEQ ID No: 371 SEQ ID No: 373
SEQ ID No: 375 SEQ ID No: 377, SEQ ID No: 379, SEQ ID No: 381 SEQ ID No: 383
SEQ ID No: 385 SEQ ID No: 387, SEQ ID No: 389 SEQ ID No: 391 SEQ ID No: 393
SEQ ID No: 395 SEQ ID No: 397, SEQ ID No: 399 SEQ ID No: 401 SEQ ID No: 403
SEQ ID No: 405 SEQ ID No: 407 SEQ ID No: 409 SEQ ID No: 411 SEQ ID No: 413
SEQ ID No: 415 SEQ ID No: 417 SEQ ID No: 419 SEQ ID No: 421 SEQ ID No: 423
SEQ ID No: 425 SEQ ID No: 427, SEQ ID No: 429 SEQ ID No: 431 SEQ ID No: 433
SEQ ID No: 435 SEQ ID No: 437, SEQ ID No: 439 SEQ ID No: 441 SEQ ID No: 443
SEQ ID No: 445 SEQ ID No: 447 SEQ ID No: 449 SEQ ID No: 451 SEQ ID No: 453
SEQ ID No: 455 SEQ ID No: 457, SEQ ID No: 459 SEQ ID No: 461 SEQ ID No: 463
SEQ ID No: 465 SEQ ID No: 467 SEQ ID No: 469 SEQ ID No: 471 SEQ ID No: 473
SEQ ID No: 475 SEQ ID No: 477, SEQ ID No: 479 SEQ ID No: 481 SEQ ID No: 483
SEQ ID No: 485 SEQ ID No: 487, SEQ ID No: 489 SEQ ID No: 491 SEQ ID No: 493
SEQ ID No: 495 SEQ ID No: 497 SEQ ID No: 499 SEQ ID No: 501 SEQ ID No: 503
SEQ ID No: 505 SEQ ID No: 507 SEQ ID No: 509 SEQ ID No: 511 SEQ ID No: 513
SEQ ID No: 515 SEQ ID No: 517, SEQ ID No: 519 SEQ ID No: 521 SEQ ID No: 523
SEQ ID No: 525 SEQ ID No: 527, SEQ ID No: 529 SEQ ID No: 531 SEQ ID No: 533
SEQ ID No: 535 SEQ ID No: 537, SEQ ID No: 539 SEQ ID No: 541 SEQ ID No: 543
SEQ ID No: 545 SEQ ID No: 547, SEQ ID No: 549 SEQ ID No: 551 SEQ ID No: 553
SEQ ID No: 555 SEQ ID No: 557, SEQ ID No: 559 SEQ ID No: 561 SEQ ID No: 563
SEQ ID No: 565 SEQ ID No: 567, SEQ ID No: 569 SEQ ID No: 571 SEQ ID No: 573
SEQ ID No: 575 SEQ ID No: 577, SEQ ID No: 579, SEQ ID No: 581 SEQ ID No: 583
SEQ ID No: 585 SEQ ID No: 587, SEQ ID No: 589 SEQ ID No: 591 SEQ ID No: 593
SEQ ID No: 595 SEQ ID No: 597, SEQ ID No: 599 SEQ ID No: 601 SEQ ID No: 603
SEQ ID No: 605 SEQ ID No: 607 SEQ ID No: 609 SEQ ID No: 611 SEQ ID No: 613
SEQ ID No: 615 SEQ ID No: 617 SEQ ID No: 619 SEQ ID No: 621 SEQ ID No: 623
SEQ ID No: 625 SEQ ID No: 627, SEQ ID No: 629 SEQ ID No: 631 SEQ ID No: 633
SEQ ID No: 635 SEQ ID No: 637, SEQ ID No: 639 SEQ ID No: 641 SEQ ID No: 643
SEQ ID No: 645 SEQ ID No: 647 SEQ ID No: 649 SEQ ID No: 651 SEQ ID No: 653
SEQ ID No: 655 SEQ ID No: 657, SEQ ID No: 659 SEQ ID No: 661 SEQ ID No: 663
SEQ ID No: 665 SEQ ID No: 667 SEQ ID No: 669 SEQ ID No: 671 SEQ ID No: 673 SEQ ID No: 675 SEQ ID No: 677, SEQ ID No: 679 SEQ ID No: 681 SEQ ID No: 683
SEQ ID No: 685 SEQ ID No: 687, SEQ ID No: 689 SEQ ID No: 691 SEQ ID No: 693
SEQ ID No: 695 SEQ ID No: 697 SEQ ID No: 699 SEQ ID No: 701 SEQ ID No: 703
SEQ ID No: 705 SEQ ID No: 707 SEQ ID No: 709 SEQ ID No: 711 SEQ ID No: 713
SEQ ID No: 715 SEQ ID No: 717, SEQ ID No: 719 SEQ ID No: 721 SEQ ID No: 723
SEQ ID No: 725 SEQ ID No: 727, SEQ ID No: 729, SEQ ID No: 731 SEQ ID No: 733
SEQ ID No: 735 SEQ ID No: 737, SEQ ID No: 739, SEQ ID No: 741 SEQ ID No: 743
SEQ ID No: 745 SEQ ID No: 747, SEQ ID No: 749 SEQ ID No: 751 SEQ ID No: 753
SEQ ID No: 755 SEQ ID No: 757, SEQ ID No: 759, SEQ ID No: 761 SEQ ID No: 763
SEQ ID No: 765 SEQ ID No: 767, SEQ ID No: 769 SEQ ID No: 771 SEQ ID No: 773
SEQ ID No: 775 SEQ ID No: 777, SEQ ID No: 779, SEQ ID No: 781 SEQ ID No: 783
SEQ ID No: 785 SEQ ID No: 787, SEQ ID No: 789 SEQ ID No: 791 SEQ ID No: 793
SEQ ID No: 795 SEQ ID No: 797, SEQ ID No: 799 SEQ ID No: 801 SEQ ID No: 803
SEQ ID No: 805 SEQ ID No: 807 SEQ ID No: 809 SEQ ID No: 811 SEQ ID No: 813
SEQ ID No: 815 SEQ ID No: 817 SEQ ID No: 819 SEQ ID No: 821 SEQ ID No: 823
SEQ ID No: 825 SEQ ID No: 827, SEQ ID No: 829 SEQ ID No: 831 SEQ ID No: 833
SEQ ID No: 835 SEQ ID No: 837, SEQ ID No: 839 SEQ ID No: 841 SEQ ID No: 843
SEQ ID No: 845 SEQ ID No: 847, SEQ ID No: 849 SEQ ID No: 851 SEQ ID No: 853
SEQ ID No: 855 SEQ ID No: 857, SEQ ID No: 859 SEQ ID No: 861 SEQ ID No: 863
SEQ ID No: 865 SEQ ID No: 867, SEQ ID No: 869 SEQ ID No: 871 SEQ ID No: 873
SEQ ID No: 875 SEQ ID No: 877, SEQ ID No: 879 SEQ ID No: 881 SEQ ID No: 883
SEQ ID No: 885 SEQ ID No: 887, SEQ ID No: 889 SEQ ID No: 891 SEQ ID No: 893
SEQ ID No: 895 SEQ ID No: 897 SEQ ID No: 899 SEQ ID No: 901 SEQ ID No: 903
SEQ ID No: 905 SEQ ID No: 907 SEQ ID No: 909 SEQ ID No: 911 SEQ ID No: 913
SEQ ID No: 915 SEQ ID No: 917 SEQ ID No: 919 SEQ ID No: 921 SEQ ID No: 923
SEQ ID No: 925 SEQ ID No: 927, SEQ ID No: 929 SEQ ID No: 931 SEQ ID No: 933
SEQ ID No: 935 SEQ ID No: 937, SEQ ID No: 939 SEQ ID No: 941 SEQ ID No: 943
SEQ ID No: 945 SEQ ID No: 947 SEQ ID No: 949 SEQ ID No: 951 SEQ ID No: 953
SEQ ID No: 955 SEQ ID No: 957, SEQ ID No: 959 SEQ ID No: 961 SEQ ID No: 963
SEQ ID No: 965 SEQ ID No: 967 SEQ ID No: 969 SEQ ID No: 971 SEQ ID No: 973
SEQ ID No: 975 SEQ ID No: 977, SEQ ID No: 979 SEQ ID No: 981 SEQ ID No: 983
SEQ ID No: 985 SEQ ID No: 987 SEQ ID No: 989 SEQ ID No: 991 SEQ ID No: 993
SEQ ID No: 995 SEQ ID No: 997 SEQ ID No: 999 SEQ ID No: 1001 , SEQ ID No: 1003, SEQ ID No: 1005, SEQ ID No: 1007, SEQ ID No: 1009, SEQ ID No: 1011, SEQ ID No: 1013, SEQ ID No: 1015, SEQ ID No: 1017, SEQ ID No: 1019, SEQ ID No: 1021, SEQ ID No: 1023, SEQ ID No: 1025, SEQ ID No: 1027, SEQ ID No: 1029, SEQ ID No: 1031, SEQ ID No: 1033, SEQ ID No: 1035, SEQ ID No: 1037, SEQ ID No: 1039, SEQ ID No: 1041, SEQ ID No: 1043, SEQ ID No: 1045, SEQ ID No: 1047, SEQ ID No: 1049, SEQ ID No: 1051, SEQ ID No: 1053, SEQ ID No: 1055, SEQ ID No: 1057, SEQ ID No: 1059, SEQ ID No: 1061, SEQ ID No: 1063, SEQ ID No: 1065, SEQ ID No: 1067, SEQ ID No: 1069, SEQ ID No: 1071, SEQ ID No: 1073, SEQ ID No: 1075, SEQ ID No: 1077, SEQ ID No: 1079, SEQ ID No: 1081, SEQ ID No: 1083, SEQ ID No: 1085, SEQ ID No: 1087, SEQ ID No: 1089, SEQ ID No: 1091, SEQ ID No: 1093, SEQ ID No: 1095, SEQ ID No: 1097, SEQ ID No: 1099, SEQ ID No: 1101, SEQ ID No: 1103, SEQ ID No: 1105, SEQ ID No: 1107, SEQ ID No: 1109, SEQ ID No: 1111, SEQ ID No: 1113, SEQ ID No: 1115, SEQ ID No: 1117, SEQ ID No: 1119, SEQ ID No: 1121, SEQ ID No: 1123, SEQ ID No: 1125, SEQ ID No: 1127, SEQ ID No: 1129, SEQ ID No: 1131, SEQ ID No: 1133, SEQ ID No: 1135, SEQ ID No: 1137, SEQ ID No: 1139, SEQ ID No: 1141, SEQ ID No: 1143, SEQ ID No: 1145, SEQ ID No: 1147, SEQ ID No: 1149, SEQ ID No: 1151, SEQ ID No: 1153, SEQ ID No: 1155, SEQ ID No: 1157, SEQ ID No: 1159, SEQ ID No: 1161, SEQ ID No: 1163, SEQ ID No: 1165, SEQ ID No: 1167, SEQ ID No: 1169, SEQ ID No: 1171, SEQ ID No: 1173, SEQ ID No: 1175, SEQ ID No: 1177, SEQ ID No: 1179, SEQ ID No: 1181, SEQ ID No: 1183, SEQ ID No: 1185, SEQ ID No: 1187, SEQ ID No: 1189, SEQ ID No: 1191, SEQ ID No: 1193, SEQ ID No: 1195, SEQ ID No: 1197, SEQ ID No: 1199, SEQ ID No: 1201, SEQ ID No: 1203, SEQ ID No: 1205, SEQ ID No: 1207, SEQ ID No: 1209, SEQ ID No: 1211, SEQ ID No: 1213, SEQ ID No: 1215, SEQ ID No: 1217, SEQ ID No: 1219, SEQ ID No: 1221, SEQ ID No: 1223, SEQ ID No: 1225, SEQ ID No: 1227, SEQ ID No: 1229, SEQ ID No: 1231, SEQ ID No: 1233, SEQ ID No: 1235, SEQ ID No: 1237, SEQ ID No: 1239, SEQ ID No: 1241, SEQ ID No: 1243, SEQ ID No: 1245, SEQ ID No: 1247, SEQ ID No: 1249, SEQ ID No: 1251, SEQ ID No: 1253, SEQ ID No: 1255, SEQ ID No: 1257, SEQ ID No: 1259, SEQ ID No: 1261, SEQ ID No: 1263, SEQ ID No: 1265, SEQ ID No: 1267, SEQ ID No: 1269, SEQ ID No: 1271, SEQ ID No: 1273, SEQ ID No: 1275, SEQ ID No: 1277, SEQ ID No: 1279, SEQ ID No: 1281, SEQ ID No: 1283, SEQ ID No: 1285, SEQ ID No: 1287, SEQ ID No: 1289, SEQ ID No: 1291, SEQ ID No: 1293, SEQ ID No: 1295, SEQ ID No: 1297, SEQ ID No: 1299, SEQ ID No: 1301, SEQ ID No: 1303, SEQ ID No : 1305, SEQ ID No: 1307, SEQ ID No: 1309, SEQ ID No: 1311, SEQ ID No: 1313, SEQ ID No: 1315, SEQ ID No: 1317, SEQ ID No: 1319, SEQ ID No: 1321, SEQ ID No : 1323, SEQ ID No: 1325, SEQ ID No: 1327, SEQ ID No: 1329, SEQ ID No: 1331, SEQ ID No: 1333, SEQ ID No: 1335, SEQ ID No: 1337, SEQ ID No: 1339, SEQ ID No : 1341, SEQ ID No: 1343, SEQ ID No: 1345, SEQ ID No: 1347, SEQ ID No: 1349, SEQ ID No: 1351, SEQ ID No: 1353, SEQ ID No: 1355, SEQ ID No: 1357, SEQ ID No : 1359, SEQ ID No: 1361, SEQ ID No: 1363, SEQ ID No: 1365, SEQ ID No: 1367, SEQ ID No: 1369, SEQ ID No: 1371, SEQ ID No: 1373, SEQ ID No: 1375, SEQ ID No : 1377, SEQ ID No: 1379, SEQ ID No: 1381, SEQ ID No: 1383, SEQ ID No: 1385, SEQ ID No: 1387, SEQ ID No: 1389, SEQ ID No: 1391, SEQ ID No: 1393, SEQ ID No : 1395, SEQ ID No: 1397, SEQ ID No: 1399, SEQ ID No: 1401, SEQ ID No: 1403, SEQ ID No: 1405, SEQ ID No: 1407, SEQ ID No: 1409, SEQ ID No: 1411, SEQ ID No : 1413, SEQ ID No: 1415, SEQ ID No: 1417, SEQ ID No: 1419, SEQ ID No: 1421, SEQ ID No: 1423, SEQ ID No: 1425, SEQ ID No: 1427, SEQ ID No: 1429, SEQ ID No : 1431, SEQ ID No: 1433, SEQ ID No: 1435, SEQ ID No: 1437, SEQ ID No: 1439, SEQ ID No: 1441, SEQ ID No: 1443, SEQ ID No: 1445, SEQ ID No: 1447, SEQ ID No : 1449, SEQ ID No: 1451, SEQ ID No: 1453, SEQ ID No: 1455, SEQ ID No: 1457, SEQ ID No: 1459, SEQ ID No: 1461, SEQ ID No: 1463, SEQ ID No: 1465, SEQ ID No : 1467, SEQ ID No: 1469, SEQ ID No: 1471, SEQ ID No: 1473, SEQ ID No: 1475, SEQ ID No: 1477, SEQ ID No: 1479, SEQ ID No: 1481, SEQ ID No: 1483, SEQ ID No : 1485, SEQ ID No: 1487, SEQ ID No: 1489, SEQ ID No: 1491, SEQ ID No: 1493, SEQ ID No: 1495, SEQ ID No: 1497, SEQ ID No: 1499, SEQ ID No: 1501, SEQ ID No : 1503, SEQ ID No: 1505, SEQ ID No: 1507, SEQ ID No: 1509, SEQ ID No: 1511, SEQ ID No: 1513, SEQ ID No: 1515, SEQ ID No: 1517, SEQ ID No: 1519, SEQ ID No : 1521, SEQ ID No: 1523, SEQ ID No: 1525, SEQ ID No: 1527, SEQ ID No: 1529, SEQ ID No: 1531, SEQ ID No: 1533, SEQ ID No: 1535, SEQ ID No: 1537, SEQ ID No : 1539, SEQ ID No: 1541, SEQ ID No: 1543, SEQ ID No: 1545, SEQ ID No: 1547, SEQ ID No: 1549, SEQ ID No: 1551, SEQ ID No: 1553, SEQ ID No: 1555, SEQ ID No : 1557, SEQ ID No: 1559, SEQ ID No: 1561, SEQ ID No: 1563, SEQ ID No: 1565, SEQ ID No: 1567, SEQ ID No: 1569, SEQ ID No: 1571, SEQ ID No: 1573, SEQ ID No : 1575, SEQ ID No: 1577, SEQ ID No: 1579, SEQ ID No: 1581, SEQ ID No: 1583, SEQ ID No: 1585, SEQ ID No: 1587, SEQ ID No: 1589, SEQ ID No: 1591, SEQ ID No : 1593, SEQ ID No: 1595, SEQ ID No: 1597, SEQ ID No: 1599, SEQ ID No: 1601, SEQ ID No: 1603, SEQ ID No: 1605, SEQ ID No: 1607, SEQ ID No: 1609, SEQ ID No: 1611, SEQ ID No: 1613, SEQ ID No: 1615, SEQ ID No: 1617, SEQ ID No: 1619, SEQ ID No: 1621, SEQ ID No: 1623, SEQ ID No: 1625, SEQ ID No: 1627, SEQ ID No: 1629, SEQ ID No: 1631, SEQ ID No: 1633, SEQ ID No: 1635, SEQ ID No: 1637, SEQ ID No: 1639, SEQ ID No: 1641, SEQ ID No: 1643, SEQ ID No: 1645, SEQ ID No: 1647, SEQ ID No: 1649, SEQ ID No: 1651, SEQ ID No: 1653, SEQ ID No: 1655, SEQ ID No: 1657, SEQ ID No: 1659, SEQ ID No: 1661, SEQ ID No: 1663, SEQ ID No: 1665, SEQ ID No: 1667, SEQ ID No: 1669, SEQ ID No: 1671, SEQ ID No: 1673, SEQ ID No: 1675, SEQ ID No: 1677, SEQ ID No: 1679, SEQ ID No: 1681, SEQ ID No: 1683, SEQ ID No: 1685, SEQ ID No: 1687, SEQ ID No: 1689, SEQ ID No: 1691, SEQ ID No: 1693, SEQ ID No: 1695, SEQ ID No: 1697, SEQ ID No: 1699, SEQ ID No: 1701, SEQ ID No: 1703, SEQ ID No: 1705, SEQ ID No: 1707, SEQ ID No: 1709, SEQ ID No: 1711, SEQ ID No: 1713, SEQ ID No: 1715, SEQ ID No: 1717, SEQ ID No: 1719, SEQ ID No: 1721, SEQ ID No: 1723, SEQ ID No: 1725, SEQ ID No: 1727, SEQ ID No: 1729, SEQ ID No: 1731, SEQ ID No: 1733, SEQ ID No: 1735, SEQ ID No: 1737, SEQ ID No: 1739, SEQ ID No: 1741, SEQ ID No: 1743, SEQ ID No: 1745, SEQ ID No: 1747, SEQ ID No: 1749, SEQ ID No: 1751, SEQ ID No: 1753, SEQ ID No: 1755, SEQ ID No: 1757, SEQ ID No: 1759, SEQ ID No: 1761, SEQ ID No: 1763, SEQ ID No: 1765, SEQ ID No: 1767, SEQ ID No: 1769, SEQ ID No: 1771, SEQ ID No: 1773, SEQ ID No: 1775, SEQ ID No: 1777, SEQ ID No: 1779, SEQ ID No: 1781, SEQ ID No: 1783, SEQ ID No: 1785, SEQ ID No: 1787, SEQ ID No: 1789, SEQ ID No: 1791, SEQ ID No: 1793, SEQ ID No: 1795, SEQ ID No: 1797, SEQ ID No: 1799, SEQ ID No: 1801, SEQ ID No: 1803, SEQ ID No: 1805, SEQ ID No: 1807, SEQ ID No: 1809, SEQ ID No: 1811, SEQ ID No: 1813, SEQ ID No: 1815, SEQ ID No: 1817, SEQ ID No: 1819, SEQ ID No: 1821, SEQ ID No: 1823, SEQ ID No: 1825, SEQ ID No: 1827, SEQ ID No: 1829, SEQ ID No: 1831, SEQ ID No: 1833, SEQ ID No: 1835, SEQ ID No: 1837, SEQ ID No: 1839, SEQ ID No: 1841, SEQ ID No: 1843, SEQ ID No: 1845, SEQ ID No: 1847, SEQ ID No: 1849, SEQ ID No: 1851, SEQ ID No: 1853, SEQ ID No: 1855, SEQ ID No: 1857, SEQ ID No: 1859, SEQ ID No: 1861, SEQ ID No: 1863, SEQ ID No: 1865, SEQ ID No: 1867, SEQ ID No: 1869, SEQ ID No: 1871, SEQ ID No: 1873, SEQ ID No: 1875, SEQ ID No: 1877, SEQ ID No: 1879, SEQ ID No: 1881, SEQ ID No: 1883, SEQ ID No: 1885, SEQ ID No: 1887, SEQ ID No: 1889, SEQ ID No: 1891, SEQ ID No: 1893, SEQ ID No: 1895, SEQ ID No: 1897, SEQ ID No: 1899, SEQ ID No: 1901, SEQ ID No: 1903, SEQ ID No: 1905, SEQ ID No: 1907, SEQ ID No: 1909, SEQ ID No: 1911, SEQ ID No: 1913, SEQ ID No: 1915, SEQ ID No: 1917, SEQ ID No: 1919, SEQ ID No: 1921, SEQ ID No: 1923, SEQ ID No: 1925, SEQ ID No: 1927, SEQ ID No: 1929, SEQ ID No: 1931, SEQ ID No: 1933, SEQ ID No: 1935, SEQ ID No: 1937, SEQ ID No: 1939, SEQ ID No: 1941, SEQ ID No: 1943, SEQ ID No: 1945, SEQ ID No: 1947, SEQ ID No: 1949, SEQ ID No: 1951, SEQ ID No: 1953, SEQ ID No: 1955, SEQ ID No: 1957, SEQ ID No: 1959, SEQ ID No: 1961, SEQ ID No: 1963, SEQ ID No: 1965, SEQ ID No: 1967, SEQ ID No: 1969, SEQ ID No: 1971, or SEQ ID No: 1973, or the complement thereof.
38. A kit comprising at least one oligonucleotide of claim 37.
39. A method for producing the protein of Claim 10, comprising culturing a cell that has been transfected with a nucleic acid sequence comprising a nucleic acid sequence encoding the protein, and expressing the protein with the transfected cell.
40. The method of Claim 39, further comprising recovering the protein from the cell or from a culture comprising the cell.
41. A genetically modified organism comprising components suitable for degrading a lignocellulosic material to fermentable sugars, wherein the organism has been genetically modified to express at least one protein of Claim 10.
42. The genetically modified organism of Claim 41 , wherein the genetically modified organism is selected from the group consisting of: plants, algae, fungi, and bacteria.
43. The genetically modified organism of Claim 42, wherein the fungus is selected from the group consisting of: yeast, mushroom and filamentous fungus.
44. The genetically modified organism of Claim 43, wherein the filamentous fungus is from a genus selected from the group consisting of: Chrysosporium, Thielavia, Neurospora, Aureobasidium, Filibasidium, Piromyces, Corynascus, Cryplococcus, Acremonium, Tolypocladium, Scytalidium, Schizophyllum, Sporotrichum, Penicillium, Talaromyces, Gibber ella, Myceliophthora, Mucor, Aspergillus, Fusarium, Humicola, and Trichoderma.
45. The genetically modified organism of Claim 43, wherein the filamentous fungus is selected from the group consisting of: Myceliophthora thermophila, Trichoderma reesei, Chrysosporium lucknowense, Aspergillus niger, Aspergillus nidulans, Aspergillus oryzae, Aspergillus aculeatus, Aspergillus japonicus, Penicillium canescens, Penicillium solitum, Penicillium funiculosum, Talaromyces emersonii and Talaromyces flavus.
46. The genetically modified organism of Claim 41 , wherein the organism has been genetically modified to express at least one additional enzyme.
47. The genetically modified organism of Claim 46, wherein the additional enzyme is an enzyme selected from the group consisting of: cellulase, glucosidase, xylanase, xylosidase, ligninase, glucuronidase, arabinofuranosidase, arabinase, arabinogalactanase, ferulic acid esterase, lipase, pectinase, (gluco-) mannanase, amylase, laminarinase, xyloglucanase, galactanase, galactosidase, glucoamylase, pectate or pectin lyase, chitosanases, exo-β-ϋ- glucosaminidase, cellobiose dehydrogenase, glucuronyl esterase and acetylxylan esterase.
48. The genetically modified organism of Claim 41 , wherein the genetically modified organism is a plant.
49. A recombinant enzyme isolated from the genetically modified microorganism of any one of claims 41 to 48.
50. The recombinant enzyme of claim 49, wherein the enzyme has been subjected to a purification step.
51. A crude fermentation product produced by culturing the cells from the genetically modified organism of any one of claims 41 to 48, wherein the crude fermentation product contains the at least one protein of Claim 10.
52. A multi-enzyme composition comprising enzymes produced by the genetically modified organism of any one of Claims 41 to 48, and recovered therefrom.
53. A multi-enzyme composition comprising at least one protein of Claim 10, and at least one additional protein for degrading a lignocellulosic material or a fragment thereof that has biological activity.
54. A method for aiding in the degradation of a biomass material to fermentable sugars, comprising contacting the biomass material with at least one isolated protein of Claim 10.
55. The method of Claim 54, further comprising contacting the biomass material with at least one additional isolated protein comprising an amino acid sequence that is at least about 95% identical to an amino acid sequence selected from the group consisting of the amino acid sequences of SEQ ID NO: 2, SEQ ID No: 4, SEQ ID No: 6, SEQ ID No: 8, SEQ ID No: 10, SEQ ID No: 12, SEQ ID No: 14, SEQ ID No: 16, SEQ ID No: 18, SEQ ID No: 20, SEQ ID No: 22, SEQ ID No: 24, SEQ ID No: 26, SEQ ID No: 28, SEQ ID No: 30, SEQ ID No: 32, SEQ ID No: 34, SEQ ID No: 36, SEQ ID No: 38, SEQ ID No: 40, SEQ ID No: 42, SEQ ID No: 44, SEQ ID No: 46, SEQ ID No: 48, SEQ ID No: 50, SEQ ID No: 52, SEQ ID No: 54, SEQ ID No: 56, SEQ ID No: 58, SEQ ID No: 60, SEQ ID No: 62, SEQ ID No: 64, SEQ ID No: 66, SEQ ID No: 68, SEQ ID No: 70, SEQ ID No: 72, SEQ ID No: 74, SEQ ID No: 76, SEQ ID No: 78, SEQ ID No: 80, SEQ ID No: 82, SEQ ID No: 84, SEQ ID No: 86, SEQ ID No: 88, SEQ ID No: 90, SEQ ID No: 92,
SEQ ID No: 94, SEQ ID No: < ½, SEQ ID No: 98, SEQ ID No : 100, SEQ ID No : 102,
SEQ ID No: 104, SEQ ID No: 106, SEQ ID No: 108, SEQ ID No: 110, SEQ ID No: 112,
SEQ ID No: 114, SEQ ID No: 116, SEQ ID No: 118, SEQ ID No: 120, SEQ ID No: 122,
SEQ ID No: 124, SEQ ID No: 126, SEQ ID No: 128, SEQ ID No: 130, SEQ ID No: 132,
SEQ ID No: 134, SEQ ID No: 136, SEQ ID No: 138, SEQ ID No: 140, SEQ ID No: 142,
SEQ ID No: 144, SEQ ID No: 146, SEQ ID No: 148, SEQ ID No: 150, SEQ ID No: 152,
SEQ ID No: 154, SEQ ID No: 156, SEQ ID No: 158, SEQ ID No: 160, SEQ ID No: 162,
SEQ ID No: 164, SEQ ID No: 166, SEQ ID No: 168, SEQ ID No: 170, SEQ ID No: 172,
SEQ ID No: 174, SEQ ID No: 176, SEQ ID No: 178, SEQ ID No: 180, SEQ ID No: 182,
SEQ ID No: 184, SEQ ID No: 186, SEQ ID No: 188, SEQ ID No: 190, SEQ ID No: 192,
SEQ ID No: 194, SEQ ID No: 196, SEQ ID No: 198, SEQ ID No: 200, SEQ ID No: 202,
SEQ ID No: 204, SEQ ID No: 206, SEQ ID No: 208, SEQ ID No: 210, SEQ ID No: 212,
SEQ ID No: 214, SEQ ID No: 216, SEQ ID No: 218, SEQ ID No: 220, SEQ ID No: 222,
SEQ ID No: 224, SEQ ID No: 226, SEQ ID No: 228, SEQ ID No: 230, SEQ ID No: 232,
SEQ ID No: 234, SEQ ID No: 236, SEQ ID No: 238, SEQ ID No: 240, SEQ ID No: 242,
SEQ ID No: 244, SEQ ID No: 246, SEQ ID No: 248, SEQ ID No: 250, SEQ ID No: 252,
SEQ ID No: 254, SEQ ID No: 256, SEQ ID No: 258, SEQ ID No: 260, SEQ ID No: 262,
SEQ ID No: 264, SEQ ID No: 266, SEQ ID No: 268, SEQ ID No: 270, SEQ ID No: 272,
SEQ ID No: 274, SEQ ID No: 276, SEQ ID No: 278, SEQ ID No: 280, SEQ ID No: 282,
SEQ ID No: 284, SEQ ID No: 286, SEQ ID No: 288, SEQ ID No: 290, SEQ ID No: 292,
SEQ ID No: 294, SEQ ID No: 296, SEQ ID No: 298, SEQ ID No: 300, SEQ ID No: 302,
SEQ ID No: 304, SEQ ID No: 306, SEQ ID No: 308, SEQ ID No: 310, SEQ ID No: 312, SEQ ID No: 314, SEQ ID No: 316, SEQ ID No: 318, SEQ ID No: 320, SEQ ID No: 322,
SEQ ID No: 324, SEQ ID No: 326, SEQ ID No: 328, SEQ ID No: 330, SEQ ID No: 332,
SEQ ID No: 334, SEQ ID No: 336, SEQ ID No: 338, SEQ ID No: 340, SEQ ID No: 342,
SEQ ID No: 344, SEQ ID No: 346, SEQ ID No: 348, SEQ ID No: 350, SEQ ID No: 352,
SEQ ID No: 354, SEQ ID No: 356, SEQ ID No: 358, SEQ ID No: 360, SEQ ID No: 362,
SEQ ID No: 364, SEQ ID No: 366, SEQ ID No: 368, SEQ ID No: 370, SEQ ID No: 372,
SEQ ID No: 374, SEQ ID No: 376, SEQ ID No: 378, SEQ ID No: 380, SEQ ID No: 382,
SEQ ID No: 384, SEQ ID No: 386, SEQ ID No: 388, SEQ ID No: 390, SEQ ID No: 392,
SEQ ID No: 394, SEQ ID No: 396, SEQ ID No: 398, SEQ ID No: 400, SEQ ID No: 402,
SEQ ID No: 404, SEQ ID No: 406, SEQ ID No: 408, SEQ ID No: 410, SEQ ID No: 412,
SEQ ID No: 414, SEQ ID No: 416, SEQ ID No: 418, SEQ ID No: 420, SEQ ID No: 422,
SEQ ID No: 424, SEQ ID No: 426, SEQ ID No: 428, SEQ ID No: 430, SEQ ID No: 432,
SEQ ID No: 434, SEQ ID No: 436, SEQ ID No: 438, SEQ ID No: 440, SEQ ID No: 442,
SEQ ID No: 444, SEQ ID No: 446, SEQ ID No: 448, SEQ ID No: 450, SEQ ID No: 452,
SEQ ID No: 454, SEQ ID No: 456, SEQ ID No: 458, SEQ ID No: 460, SEQ ID No: 462,
SEQ ID No: 464, SEQ ID No: 466, SEQ ID No: 468, SEQ ID No: 470, SEQ ID No: 472,
SEQ ID No: 474, SEQ ID No: 476, SEQ ID No: 478, SEQ ID No: 480, SEQ ID No: 482,
SEQ ID No: 484, SEQ ID No: 486, SEQ ID No: 488, SEQ ID No: 490, SEQ ID No: 492,
SEQ ID No: 494, SEQ ID No: 496, SEQ ID No: 498, SEQ ID No: 500, SEQ ID No: 502,
SEQ ID No: 504, SEQ ID No: 506, SEQ ID No: 508, SEQ ID No: 510, SEQ ID No: 512,
SEQ ID No: 514, SEQ ID No: 516, SEQ ID No: 518, SEQ ID No: 520, SEQ ID No: 522,
SEQ ID No: 524, SEQ ID No: 526, SEQ ID No: 528, SEQ ID No: 530, SEQ ID No: 532,
SEQ ID No: 534, SEQ ID No: 536, SEQ ID No: 538, SEQ ID No: 540, SEQ ID No: 542,
SEQ ID No: 544, SEQ ID No: 546, SEQ ID No: 548, SEQ ID No: 550, SEQ ID No: 552,
SEQ ID No: 554, SEQ ID No: 556, SEQ ID No: 558, SEQ ID No: 560, SEQ ID No: 562,
SEQ ID No: 564, SEQ ID No: 566, SEQ ID No: 568, SEQ ID No: 570, SEQ ID No: 572,
SEQ ID No: 574, SEQ ID No: 576, SEQ ID No: 578, SEQ ID No: 580, SEQ ID No: 582,
SEQ ID No: 584, SEQ ID No: 586, SEQ ID No: 588, SEQ ID No: 590, SEQ ID No: 592,
SEQ ID No: 594, SEQ ID No: 596, SEQ ID No: 598, SEQ ID No: 600, SEQ ID No: 602,
SEQ ID No: 604, SEQ ID No: 606, SEQ ID No: 608, SEQ ID No: 610, SEQ ID No: 612,
SEQ ID No: 614, SEQ ID No: 616, SEQ ID No: 618, SEQ ID No: 620, SEQ ID No: 622,
SEQ ID No: 624, SEQ ID No: 626, SEQ ID No: 628, SEQ ID No: 630, SEQ ID No: 632,
SEQ ID No: 634, SEQ ID No: 636, SEQ ID No: 638, SEQ ID No: 640, SEQ ID No: 642, SEQ ID No: 644, SEQ ID No: 646, SEQ ID No: 648, SEQ ID No: 650, SEQ ID No: 652, SEQ ID No: 654, SEQ ID No: 656, SEQ ID No: 658, SEQ ID No: 660, SEQ ID No: 662, SEQ ID No: 664, SEQ ID No: 666, SEQ ID No: 668, SEQ ID No: 670, SEQ ID No: 672, SEQ ID No: 674, SEQ ID No: 676, SEQ ID No: 678, SEQ ID No: 680, SEQ ID No: 682, SEQ ID No: 684, SEQ ID No: 686, SEQ ID No: 688, SEQ ID No: 690, SEQ ID No: 692, SEQ ID No: 694, SEQ ID No: 696, SEQ ID No: 698, SEQ ID No: 700, SEQ ID No: 702, SEQ ID No: 704, SEQ ID No: 706, SEQ ID No: 708, SEQ ID No: 710, SEQ ID No: 712, SEQ ID No: 714, SEQ ID No: 716, SEQ ID No: 718, SEQ ID No: 720, SEQ ID No: 722, SEQ ID No: 724, SEQ ID No: 726, SEQ ID No: 728, SEQ ID No: 730, SEQ ID No: 732, SEQ ID No: 734, SEQ ID No: 736, SEQ ID No: 738, SEQ ID No: 740, SEQ ID No: 742, SEQ ID No: 744, SEQ ID No: 746, SEQ ID No: 748, SEQ ID No: 750, SEQ ID No: 752, SEQ ID No: 754, SEQ ID No: 756, SEQ ID No: 758, SEQ ID No: 760, SEQ ID No: 762, SEQ ID No: 764, SEQ ID No: 766, SEQ ID No: 768, SEQ ID No: 770, SEQ ID No: 772, SEQ ID No: 774, SEQ ID No: 776, SEQ ID No: 778, SEQ ID No: 780, SEQ ID No: 782, SEQ ID No: 784, SEQ ID No: 786, SEQ ID No: 788, SEQ ID No: 790, SEQ ID No: 792, SEQ ID No: 794, SEQ ID No: 796, SEQ ID No: SEQ ID No: 798, SEQ ID No: 800, SEQ ID No: 802, SEQ ID No: 804, SEQ ID No: 806, SEQ ID No: 808, SEQ ID No: 810, SEQ ID No: 812, SEQ ID No: 814, SEQ ID No: 816, SEQ ID No: 818, SEQ ID No: 820, SEQ ID No: 822, SEQ ID No: 824, SEQ ID No: 826, SEQ ID No: 828, SEQ ID No: 830, SEQ ID No: 832, SEQ ID No: 834, SEQ ID No: 836, SEQ ID No: 838, SEQ ID No: 840, SEQ ID No: 842, SEQ ID No: 844, SEQ ID No: 846, SEQ ID No: 848, SEQ ID No: 850, SEQ ID No: 852, SEQ ID No: 854, SEQ ID No: 856, SEQ ID No: 858, SEQ ID No: 860, SEQ ID No: 862, SEQ ID No: 864, SEQ ID No: 866, SEQ ID No: 868, SEQ ID No: 870, SEQ ID No: 872, SEQ ID No: 874, SEQ ID No: 876, SEQ ID No: 878, SEQ ID No: 880, SEQ ID No: 882, SEQ ID No: 884, SEQ ID No: 886, SEQ ID No: 888, SEQ ID No: 890, SEQ ID No: 892, SEQ ID No: 894, SEQ ID No: 896, SEQ ID No: 898, SEQ ID No: 900, SEQ ID No: 902, SEQ ID No: 904, SEQ ID No: 906, SEQ ID No: 908, SEQ ID No: 910, SEQ ID No: 912, SEQ ID No: 914, SEQ ID No: 916, SEQ ID No: 918, SEQ ID No: 920, SEQ ID No: 922, SEQ ID No: 924, SEQ ID No: 926, SEQ ID No: 928, SEQ ID No: 930, SEQ ID No: 932, SEQ ID No: 934, SEQ ID No: 936, SEQ ID No: 938, SEQ ID No: 940, SEQ ID No: 942, SEQ ID No: 944, SEQ ID No: 946, SEQ ID No: 948, SEQ ID No: 950, SEQ ID No: 952, SEQ ID No: 954, SEQ ID No: 956, SEQ ID No: 958, SEQ ID No: 960, SEQ ID No: 962, SEQ ID No: 964, SEQ ID No: 966, SEQ ID No: 968, SEQ ID No: 970, SEQ ID No: 972, SEQ ID No: 974, SEQ ID No: 976, SEQ ID No: 978, SEQ ID No: 980, SEQ ID No: 982, SEQ ID No: 984, SEQ ID No: 986, SEQ ID No: 988, SEQ ID No: 990, SEQ ID No: 992, SEQ ID No: 994, SEQ ID No: 996, SEQ ID No: 998, SEQ ID No: 1000, SEQ ID No: 1002, SEQ ID No: 1004, SEQ ID No: 1006, SEQ ID No: 1008, SEQ ID No: 1010, SEQ ID No: 1012, SEQ ID No: 1014, SEQ ID No: 1016, SEQ ID No: 1018, SEQ ID No: 1020, SEQ ID No: 1022, SEQ ID No: 1024, SEQ ID No: 1026, SEQ ID No: 1028, SEQ ID No: 1030, SEQ ID No: 1032, SEQ ID No: 1034, SEQ ID No: 1036, SEQ ID No: 1038, SEQ ID No: 1040, SEQ ID No: 1042, SEQ ID No: 1044, SEQ ID No: 1046, SEQ ID No: 1048, SEQ ID No: 1050, SEQ ID No: 1052, SEQ ID No: 1054, SEQ ID No: 1056, SEQ ID No: 1058, SEQ ID No: 1060, SEQ ID No: 1062, SEQ ID No: 1064, SEQ ID No: 1066, SEQ ID No: 1068, SEQ ID No: 1070, SEQ ID No: 1072, SEQ ID No: 1074, SEQ ID No: 1076, SEQ ID No: 1078, SEQ ID No: 1080, SEQ ID No: 1082, SEQ ID No: 1084, SEQ ID No: 1086, SEQ ID No: 1088, SEQ ID No: 1090, SEQ ID No: 1092, SEQ ID No: 1094, SEQ ID No: 1096, SEQ ID No: 1098, SEQ ID NO: 1100, SEQ ID No: 1102, SEQ ID No: 1104, SEQ ID No: 1106, SEQ ID No: 1108, SEQ ID No: 1110, SEQ ID No: 1112, SEQ ID No: 1114, SEQ ID No: 1116, SEQ ID No: 1118, SEQ ID No: 1120, SEQ ID No: 1122, SEQ ID No: 1124, SEQ ID No: 1126, SEQ ID No: 1128, SEQ ID No: 1130, SEQ ID No: 1132, SEQ ID No: 1134, SEQ ID No: 1136, SEQ ID No: 1138, SEQ ID No: 1140, SEQ ID No: 1142, SEQ ID No: 1144, SEQ ID No: 1146, SEQ ID No: 1148, SEQ ID No: 1150, SEQ ID No: 1152, SEQ ID No: 1154, SEQ ID No: 1156, SEQ ID No: 1158, SEQ ID No: 1160, SEQ ID No: 1162, SEQ ID No: 1164, SEQ ID No: 1166, SEQ ID No: 1168, SEQ ID No: 1170, SEQ ID No: 1172, SEQ ID No: 1174, SEQ ID No: 1176, SEQ ID No: 1178, SEQ ID No: 1180, SEQ ID No: 1182, SEQ ID No: 1184, SEQ ID No: 1186, SEQ ID No: 1188, SEQ ID No: 1190, SEQ ID No: 1192, SEQ ID No: 1194, SEQ ID No: 1196, SEQ ID No: 1198, SEQ ID No: 1200, SEQ ID No: 1202, SEQ ID No: 1204, SEQ ID No: 1206, SEQ ID No: 1208, SEQ ID No: 1210, SEQ ID No: 1212, SEQ ID No: 1214, SEQ ID No: 1216, SEQ ID No: 1218, SEQ ID No: 1220, SEQ ID No: 1222, SEQ ID No: 1224, SEQ ID No: 1226, SEQ ID No: 1228, SEQ ID No: 1230, SEQ ID No: 1232, SEQ ID No: 1234, SEQ ID No: 1236, SEQ ID No: 1238, SEQ ID No: 1240, SEQ ID No: 1242, SEQ ID No: 1244, SEQ ID No: 1246, SEQ ID No: 1248, SEQ ID No: 1250, SEQ ID No: 1252, SEQ ID No: 1254, SEQ ID No: 1256, SEQ ID No: 1258, SEQ ID No: 1260, SEQ ID No: 1262, SEQ ID No: 1264, SEQ ID No: 1266, SEQ ID No: 1268, SEQ ID No: 1270, SEQ ID No: 1272, SEQ ID No: 1274, SEQ ID No : 1276, SEQ ID No: 1278, SEQ ID No: 1280, SEQ ID No: 1282, SEQ ID No: 1284, SEQ ID No: 1286, SEQ ID No: 1288, SEQ ID No: 1290, SEQ ID No: 1292, SEQ ID No : 1294, SEQ ID No: 1296, SEQ ID No: 1298, SEQ ID No: 1300, SEQ ID No: 1302, SEQ ID No: 1304, SEQ ID No: 1306, SEQ ID No: 1308, SEQ ID No: 1310, SEQ ID No : 1312, SEQ ID No: 1314, SEQ ID No: 1316, SEQ ID No: 1318, SEQ ID No: 1320, SEQ ID No: 1322, SEQ ID No: 1324, SEQ ID No: 1326, SEQ ID No: 1328, SEQ ID No : 1330, SEQ ID No: 1332, SEQ ID No: 1334, SEQ ID No: 1336, SEQ ID No: 1338, SEQ ID No: 1340, SEQ ID No: 1342, SEQ ID No: 1344, SEQ ID No: 1346, SEQ ID No : 1348, SEQ ID No: 1350, SEQ ID No: 1352, SEQ ID No: 1354, SEQ ID No: 1356, SEQ ID No: 1358, SEQ ID No: 1360, SEQ ID No: 1362, SEQ ID No: 1364, SEQ ID No : 1366, SEQ ID No: 1368, SEQ ID No: 1370, SEQ ID No: 1372, SEQ ID No: 1374, SEQ ID No: 1376, SEQ ID No: 1378, SEQ ID No: 1380, SEQ ID No: 1382, SEQ ID No : 1384, SEQ ID No: 1386, SEQ ID No: 1388, SEQ ID No: 1390, SEQ ID No: 1392, SEQ ID No: 1394, SEQ ID No: 1396, SEQ ID No: 1398, SEQ ID No: 1400, SEQ ID No : 1402, SEQ ID No: 1404, SEQ ID No: 1406, SEQ ID No: 1408, SEQ ID No: 1410, SEQ ID No: 1412, SEQ ID No: 1414, SEQ ID No: 1416, SEQ ID No: 1418, SEQ ID No : 1420, SEQ ID No: 1422, SEQ ID No: 1424, SEQ ID No: 1426, SEQ ID No: 1428, SEQ ID No: 1430, SEQ ID No: 1432, SEQ ID No: 1434, SEQ ID No: 1436, SEQ ID No : 1438, SEQ ID No: 1440, SEQ ID No: 1442, SEQ ID No: 1444, SEQ ID No: 1446, SEQ ID No: 1448, SEQ ID No: 1450, SEQ ID No: 1452, SEQ ID No: 1454, SEQ ID No : 1456, SEQ ID No: 1458, SEQ ID No: 1460, SEQ ID No: 1462, SEQ ID No: 1464, SEQ ID No: 1466, SEQ ID No: 1468, SEQ ID No: 1470, SEQ ID No: 1472, SEQ ID No : 1474, SEQ ID No: 1476, SEQ ID No: 1478, SEQ ID No: 1480, SEQ ID No: 1482, SEQ ID No: 1484, SEQ ID No: 1486, SEQ ID No: 1488, SEQ ID No: 1490, SEQ ID No : 1492, SEQ ID No: 1494, SEQ ID No: 1496, SEQ ID No: 1498, SEQ ID No: 1500, SEQ ID No: 1502, SEQ ID No: 1504, SEQ ID No: 1506, SEQ ID No: 1508, SEQ ID No : 1510, SEQ ID No: 1512, SEQ ID No: 1514, SEQ ID No: 1516, SEQ ID No: 1518, SEQ ID No: 1520, SEQ ID No: 1522, SEQ ID No: 1524, SEQ ID No: 1526, SEQ ID No : 1528, SEQ ID No: 1530, SEQ ID No: 1532, SEQ ID No: 1534, SEQ ID No: 1536, SEQ ID No: 1538, SEQ ID No: 1540, SEQ ID No: 1542, SEQ ID No: 1544, SEQ ID No : 1546, SEQ ID No: 1548, SEQ ID No: 1550, SEQ ID No: 1552, SEQ ID No: 1554, SEQ ID No: 1556, SEQ ID No: 1558, SEQ ID No: 1560, SEQ ID No: 1562, SEQ ID No : 1564, SEQ ID No: 1566, SEQ ID No: 1568, SEQ ID No: 1570, SEQ ID No: 1572, SEQ ID No: 1574, SEQ ID No: 1576, SEQ ID No: 1578, SEQ ID No: 1580, SEQ ID No: 1582, SEQ ID No: 1584, SEQ ID No: 1586, SEQ ID No: 1588, SEQ ID No: 1590, SEQ ID No: 1592, SEQ ID No: 1594, SEQ ID No: 1596, SEQ ID No: 1598, SEQ ID No: 1600, SEQ ID No: 1602, SEQ ID No: 1604, SEQ ID No: 1606, SEQ ID No: 1608, SEQ ID No: 1610, SEQ ID No: 1612, SEQ ID No: 1614, SEQ ID No: 1616, SEQ ID No: 1618, SEQ ID No: 1620, SEQ ID No: 1622, SEQ ID No: 1624, SEQ ID No: 1626, SEQ ID No: 1628, SEQ ID No: 1630, SEQ ID No: 1632, SEQ ID No: 1634, SEQ ID No: 1636, SEQ ID No: 1638, SEQ ID No: 1640, SEQ ID No: 1642, SEQ ID No: 1644, SEQ ID No: 1646, SEQ ID No: 1648, SEQ ID No: 1650, SEQ ID No: 1652, SEQ ID No: 1654, SEQ ID No: 1656, SEQ ID No: 1658, SEQ ID No: 1660, SEQ ID No: 1662, SEQ ID No: 1664, SEQ ID No: 1666, SEQ ID No: 1668, SEQ ID No: 1670, SEQ ID No: 1672, SEQ ID No: 1674, SEQ ID No: 1676, SEQ ID No: 1678, SEQ ID No: 1680, SEQ ID No: 1682, SEQ ID No: 1684, SEQ ID No: 1686, SEQ ID No: 1688, SEQ ID No: 1690, SEQ ID No: 1692, SEQ ID No: 1694, SEQ ID No: 1696, SEQ ID No: 1698, SEQ ID No: 1700, SEQ ID No: 1702, SEQ ID No: 1704, SEQ ID No: 1706, SEQ ID No: 1708, SEQ ID No: 1710, SEQ ID No: 1712, SEQ ID No: 1714, SEQ ID No: 1716, SEQ ID No: 1718, SEQ ID No: 1720, SEQ ID No: 1722, SEQ ID No: 1724, SEQ ID No: 1726, SEQ ID No: 1728, SEQ ID No: 1730, SEQ ID No: 1732, SEQ ID No: 1734, SEQ ID No: 1736, SEQ ID No: 1738, SEQ ID No: 1740, SEQ ID No: 1742, SEQ ID No: 1744, SEQ ID No: 1746, SEQ ID No: 1748, SEQ ID No: 1750, SEQ ID No: 1752, SEQ ID No: 1754, SEQ ID No: 1756, SEQ ID No: 1758, SEQ ID No: 1760, SEQ ID No: 1762, SEQ ID No: 1764, SEQ ID No: 1766, SEQ ID No: 1768, SEQ ID No: 1770, SEQ ID No: 1772, SEQ ID No: 1774, SEQ ID No: 1776, SEQ ID No: 1778, SEQ ID No: 1780, SEQ ID No: 1782, SEQ ID No: 1784, SEQ ID No: 1786, SEQ ID No: 1788, SEQ ID No: 1790, SEQ ID No: 1792, SEQ ID No: 1794, SEQ ID No: 1796, SEQ ID No: 1798, SEQ ID No: 1800, SEQ ID No: 1802, SEQ ID No: 1804, SEQ ID No: 1806, SEQ ID No: 1808, SEQ ID No: 1810, SEQ ID No: 1812, SEQ ID No: 1814, SEQ ID No: 1816, SEQ ID No: 1818, SEQ ID No: 1820, SEQ ID No: 1822, SEQ ID No: 1824, SEQ ID No: 1826, SEQ ID No: 1828, SEQ ID No: 1830, SEQ ID No: 1832, SEQ ID No: 1834, SEQ ID No: 1836, SEQ ID No: 1838, SEQ ID No: 1840, SEQ ID No: 1842, SEQ ID No: 1844, SEQ ID No: 1846, SEQ ID No: 1848, SEQ ID No: 1850, SEQ ID No: 1852, SEQ ID No: 1854, SEQ ID No: 1856, SEQ ID No: 1858, SEQ ID No: 1860, SEQ ID No: 1862, SEQ ID No: 1864, SEQ ID No: 1866, SEQ ID No: 1868, SEQ ID No: 1870, SEQ ID No: 1872, SEQ ID No: 1874, SEQ ID No: 1876, SEQ ID No: 1878, SEQ ID No: 1880, SEQ ID No: 1882, SEQ ID No: 1884, SEQ ID No: 1886, SEQ ID No: 1888, SEQ ID No: 1890, SEQ ID No: 1892, SEQ ID No: 1894, SEQ ID No: 1896, SEQ ID No: 1898, SEQ ID No: 1900, SEQ ID No: 1902, SEQ ID No: 1904, SEQ ID No: 1906, SEQ ID No: 1908, SEQ ID No: 1910, SEQ ID No: 1912, SEQ ID No: 1914, SEQ ID No: 1916, SEQ ID No: 1918, SEQ ID No: 1920, SEQ ID No: 1922, SEQ ID No: 1924, SEQ ID No: 1926, SEQ ID No: 1928, SEQ ID No: 1930, SEQ ID No: 1932, SEQ ID No: 1934, SEQ ID No: 1936, SEQ ID No: 1938, SEQ ID No: 1940, SEQ ID No: 1942, SEQ ID No: 1944, SEQ ID No: 1946, SEQ ID No: 1948, SEQ ID No: 1950, SEQ ID No: 1952, SEQ ID No: 1954, SEQ ID No: 1956, SEQ ID No: 1958, SEQ ID No: 1960, SEQ ID No: 1962, SEQ ID No: 1964, SEQ ID No: 1966, SEQ ID No: 1968, SEQ ID No: 1970, SEQ ID No: 1972, SEQ ID No: 1974.
56. The method of Claim 54, wherein the isolated protein is part of a multi-enzyme composition.
57. A method for aiding in the degradation of a biomass material to fermentable sugars, comprising contacting the lignocellulosic material with at least one multi-enzyme composition of any one of Claims 52 to 53.
58. A method for producing an organic substance, comprising:
saccharifying a lignocellulosic material with a multi-enzyme composition of any one of Claims 52 to 53;
fermenting the saccharified lignocellulosic material obtained with one or more fermentating microoganisms; and
recovering the organic substance from the fermentation.
59. The method of claim 58, wherein the steps of saccharifying and fermenting are performed simultaneously.
60. The method of claim 58, wherein the organic substance is an alcohol, organic acid, ketone, amino acid, or gas.
61. The method of claim 58, wherein the organic substance is an alcohol.
62. The method of claim 60, wherein the alcohol is ethanol.
63. A method for bleaching a fabric, comprising contacting the fabric with at least one isolated protein of Claim 10.
64. A method for bleaching a fabric, comprising contacting the fabric with at least one multi-enzyme composition of any one of Claims 52 to 53.
65. A genetically modified organism comprising at least one nucleic acid sequence encoding al least one protein of Claim 10, in which the activity of one or more of the proteins of claim 10 is upregulated, the activity of one or more of the proteins of claim 10 downregulated, or the activity of one or more of the proteins of claim 10 is upregulated and the activity of one or more of the proteins of claim 10 is downregulated.
66. The method of Claim 54, further comprising contacting the biomass material in the presence of a CDH-like reductase
67. The method of Claim 54, further comprising contacting the biomass material in the presence of a CDH-like reductase comprising an amino acid sequence that is at least about 95% identical to an amino acid sequence selected from the group consisting of the amino acid sequences of SEQ ID NO: 234, SEQ ID NO: 1000, SEQ ID NO: 1774, SEQ ID NO: 1884, SEQ ID NO: 1886, SEQ ID NO: 1888 and SEQ ID NO: 1890.
68. The method of any of claims 66-67, further comprising at least one additional enzyme having either cellulase enhancing activity, hemicellulo lytic enhancing activity, chitino lytic enhancing activity, amylolytic enhancing activity, amylopectinolytic enhancing activity, pectinolytic enhancing activity, or ligninolytic enhancing activity.
69. The method of any of claims 68, where the enzyme having enhancing activity is comprising an amino acid sequence that is at least about 95% identical to an amino acid sequence selected from the group consisting of the amino acid sequences of SEQ ID No: 1892, SEQ ID No: 1894, SEQ ID No: 1896, SEQ ID No: 1898, SEQ ID No: 1900, SEQ ID No: 1902, SEQ ID No: 1904, SEQ ID No: 1906, SEQ ID No: 1908, SEQ ID No: 1910, SEQ ID No: 1912, SEQ ID No: 1914, SEQ ID No: 1916, SEQ ID No: 1918, SEQ ID No: 1920, SEQ ID No: 1922, SEQ ID No: 1924, SEQ ID No: 1926, SEQ ID No: 1928, SEQ ID No: 1930, SEQ ID No: 1932, SEQ ID No: 1934, SEQ ID No: 1936, SEQ ID No: 1938, SEQ ID No: 1940, SEQ ID No: 1942, SEQ ID No: 1944, SEQ ID No: 1946, SEQ ID No: 1948, SEQ ID No: 1950, SEQ ID No: 1952, SEQ ID No: 1954, SEQ ID No: 1956, SEQ ID No: 1958, SEQ ID No: 1960, SEQ ID No: 1962, SEQ ID No: 1964, SEQ ID No: 1966, SEQ ID No: 1968, SEQ ID No: 1970, SEQ ID No: 1972, or SEQ ID No: 1974.
70. The method of any of Claims 66-69 further comprising a cellobiose dehydrogenase
71. The method of any of Claim 66-70 further comprising a peroxidase.
72. The method of any of claims 66-71 where the CDH-like reductase has GH61 reducing activity.
PCT/US2011/060970 2010-11-16 2011-11-16 Novel fungal oxidoreductases Ceased WO2012068236A2 (en)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US41413710P 2010-11-16 2010-11-16
US61/414,137 2010-11-16

Publications (2)

Publication Number Publication Date
WO2012068236A2 true WO2012068236A2 (en) 2012-05-24
WO2012068236A3 WO2012068236A3 (en) 2012-08-16

Family

ID=46084614

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/US2011/060970 Ceased WO2012068236A2 (en) 2010-11-16 2011-11-16 Novel fungal oxidoreductases

Country Status (1)

Country Link
WO (1) WO2012068236A2 (en)

Cited By (26)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2013079533A1 (en) * 2011-12-02 2013-06-06 Novozymes A/S Polypeptides having peroxygenase activity and polynucleotides encoding same
WO2014056921A3 (en) * 2012-10-12 2014-06-05 Novozymes A/S Polypeptides having peroxygenase activity
WO2014056919A3 (en) * 2012-10-12 2014-06-12 Novozymes A/S Polypeptides having peroxygenase activity
WO2014056927A3 (en) * 2012-10-12 2014-06-12 Novozymes A/S Polypeptides having peroxygenase activity
WO2014090940A1 (en) * 2012-12-14 2014-06-19 Novozymes A/S Removal of skin-derived body soils
CN104342425A (en) * 2013-07-29 2015-02-11 瑞辰星生物技术（广州）有限公司 Fiber oxidase composition for improving whiteness of paper and papermaking method and application thereof
WO2015081139A1 (en) 2013-11-26 2015-06-04 Novozymes A/S Enzyme compositions and uses thereof
CN104694506A (en) * 2015-02-10 2015-06-10 江南大学 Method for producing heat-resistant superoxide dismutase (SOD) by using thermoleophilum album
CN104694510A (en) * 2015-02-10 2015-06-10 江南大学 Method for producing heat-resistant superoxide dismutase (SOD) by using sporotrichum thermophile
WO2015187935A1 (en) 2014-06-06 2015-12-10 Novozymes A/S Enzyme compositions and uses thereof
WO2016145358A1 (en) 2015-03-12 2016-09-15 Novozymes A/S Enzymatic hydrolysis with hemicellulolytic enzymes
WO2016145350A1 (en) 2015-03-12 2016-09-15 Novozymes A/S Multi-stage enzymatic hydrolysis of lignocellulosic biomass
WO2016142536A1 (en) * 2015-03-11 2016-09-15 Genencor International B.V. Enzymatic activity of lytic polysaccharide monooxygenase
WO2016145363A1 (en) 2015-03-12 2016-09-15 Novozymes A/S Multi-stage enzymatic hydrolysis of lignocellulosic biomass employing an oxidoreductase with an aa9 polypeptide
WO2016207351A3 (en) * 2015-06-24 2017-03-02 Genencor International B.V. Polypeptides having demethylating activity
WO2017040907A1 (en) 2015-09-04 2017-03-09 Novozymes A/S Methods of inhibiting aa9 lytic polysaccharide monooxygenase catalyzed inactivation of enzyme compositions
US9663806B2 (en) * 2012-03-31 2017-05-30 Novozymes A/S Expoxidation using peroxygenases
WO2018056351A1 (en) * 2016-09-21 2018-03-29 一般財団法人阪大微生物病研究会 Dendritic-cell-targeted peptide, fusion peptide utilizing said peptide, and vaccine utilizing said fusion peptide
WO2018060498A1 (en) * 2016-09-30 2018-04-05 Norwegian University Of Life Sciences Process for degrading a polysaccharide employing a lytic polysaccharide monooxygenase
EP3099706B1 (en) * 2014-01-29 2018-10-31 BioNTech AG Peptide mimotopes of claudin 18.2 and uses thereof
WO2018201050A1 (en) * 2017-04-28 2018-11-01 Board Of Trustees Of Michigan State University Tryptathionine biosynthesis by flavin mono-oxygenase 1 (fmo1)
CN109370995A (en) * 2018-12-11 2019-02-22 中国农业科学院饲料研究所 Manganese peroxidase CsMnP and its encoding gene and application
JPWO2021167011A1 (en) * 2020-02-21 2021-08-26
US20210373004A1 (en) * 2018-11-19 2021-12-02 Bioaster Methods and reagents for multiplex binding experiments
WO2023225459A2 (en) 2022-05-14 2023-11-23 Novozymes A/S Compositions and methods for preventing, treating, supressing and/or eliminating phytopathogenic infestations and infections
WO2024131880A3 (en) * 2022-12-23 2024-07-25 Novozymes A/S Detergent composition comprising catalase and amylase

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US6165761A (en) * 1997-12-22 2000-12-26 Novo Nordisk A/S Carbohydrate oxidase and use thereof in baking
AU771539C (en) * 1998-10-06 2005-01-13 Dyadic International (Usa), Inc. Transformation system in the field of filamentous fungal hosts
CN101379184B (en) * 2006-02-06 2011-12-14 帝斯曼知识产权资产管理有限公司 Novel oxidoreductases and uses thereof

Cited By (51)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2013079533A1 (en) * 2011-12-02 2013-06-06 Novozymes A/S Polypeptides having peroxygenase activity and polynucleotides encoding same
US9404093B2 (en) 2011-12-02 2016-08-02 Novozymes A/S Polypeptides having peroxygenase activity and polynucleotides encoding same
US10017483B2 (en) 2012-03-31 2018-07-10 Novozymes A/S Epoxidation using peroxygenase
US9663806B2 (en) * 2012-03-31 2017-05-30 Novozymes A/S Expoxidation using peroxygenases
US9908860B2 (en) 2012-03-31 2018-03-06 Novozymes A/S Epoxidation using peroxygenase
US10358429B2 (en) 2012-03-31 2019-07-23 Novozymes A/S Epoxidation using peroxygenase
US10155734B2 (en) 2012-03-31 2018-12-18 Novozymes A/S Epoxidation using peroxygenase
US9404094B2 (en) 2012-10-12 2016-08-02 Novozymes A/S Polypeptides having peroxygenase activity
CN104718286B (en) * 2012-10-12 2018-10-30 诺维信公司 With the active polypeptide of peroxygenases
CN104718286A (en) * 2012-10-12 2015-06-17 诺维信公司 Polypeptides having peroxygenase activity
CN104718287A (en) * 2012-10-12 2015-06-17 诺维信公司 Polypeptides having peroxygenase activity
US9920341B2 (en) 2012-10-12 2018-03-20 Novozymes A/S Polypeptides having peroxygenase activity
US9611459B2 (en) 2012-10-12 2017-04-04 Novozymes A/S Polypeptides having peroxygenase activity
WO2014056927A3 (en) * 2012-10-12 2014-06-12 Novozymes A/S Polypeptides having peroxygenase activity
WO2014056919A3 (en) * 2012-10-12 2014-06-12 Novozymes A/S Polypeptides having peroxygenase activity
US9719072B2 (en) 2012-10-12 2017-08-01 Novozymes A/S Polypeptides having peroxygenase activity
US9670468B2 (en) 2012-10-12 2017-06-06 Novozymes A/S Polypeptides having peroxygenase activity
WO2014056921A3 (en) * 2012-10-12 2014-06-05 Novozymes A/S Polypeptides having peroxygenase activity
WO2014090940A1 (en) * 2012-12-14 2014-06-19 Novozymes A/S Removal of skin-derived body soils
CN104342425B (en) * 2013-07-29 2017-11-28 瑞辰星生物技术（广州）有限公司 For improving fiber oxidation enzymatic compositions and papermaking process and the application of Paper White Degree
CN104342425A (en) * 2013-07-29 2015-02-11 瑞辰星生物技术（广州）有限公司 Fiber oxidase composition for improving whiteness of paper and papermaking method and application thereof
WO2015081139A1 (en) 2013-11-26 2015-06-04 Novozymes A/S Enzyme compositions and uses thereof
EP3099706B1 (en) * 2014-01-29 2018-10-31 BioNTech AG Peptide mimotopes of claudin 18.2 and uses thereof
US10858415B2 (en) 2014-01-29 2020-12-08 Tron—Translationale Onkologie An Der Universitatsmedizin Der Johannes Guttenberg-Universitat Mainz Gemeinnuizige Gmbh Peptide mimotopes of claudin 18.2 and uses thereof
WO2015187935A1 (en) 2014-06-06 2015-12-10 Novozymes A/S Enzyme compositions and uses thereof
CN104694510A (en) * 2015-02-10 2015-06-10 江南大学 Method for producing heat-resistant superoxide dismutase (SOD) by using sporotrichum thermophile
CN104694506A (en) * 2015-02-10 2015-06-10 江南大学 Method for producing heat-resistant superoxide dismutase (SOD) by using thermoleophilum album
US10266863B2 (en) * 2015-03-11 2019-04-23 Genencor International B.V. Enzymatic activity of lytic polysaccharide monooxygenase
CN108699578A (en) * 2015-03-11 2018-10-23 杰能科国际有限公司 Enzyme activity of lytic polysaccharide monooxygenase
US20180051305A1 (en) * 2015-03-11 2018-02-22 Genencor International B.V. Enzymatic activity of lytic polysaccharide monooxygenase
WO2016142536A1 (en) * 2015-03-11 2016-09-15 Genencor International B.V. Enzymatic activity of lytic polysaccharide monooxygenase
WO2016145363A1 (en) 2015-03-12 2016-09-15 Novozymes A/S Multi-stage enzymatic hydrolysis of lignocellulosic biomass employing an oxidoreductase with an aa9 polypeptide
WO2016145358A1 (en) 2015-03-12 2016-09-15 Novozymes A/S Enzymatic hydrolysis with hemicellulolytic enzymes
WO2016145350A1 (en) 2015-03-12 2016-09-15 Novozymes A/S Multi-stage enzymatic hydrolysis of lignocellulosic biomass
WO2016207351A3 (en) * 2015-06-24 2017-03-02 Genencor International B.V. Polypeptides having demethylating activity
WO2017040907A1 (en) 2015-09-04 2017-03-09 Novozymes A/S Methods of inhibiting aa9 lytic polysaccharide monooxygenase catalyzed inactivation of enzyme compositions
JPWO2018056351A1 (en) * 2016-09-21 2019-07-11 一般財団法人阪大微生物病研究会 Dendritic cell targeting peptide, peptide fusion using the peptide, and vaccine using the peptide fusion
WO2018056351A1 (en) * 2016-09-21 2018-03-29 一般財団法人阪大微生物病研究会 Dendritic-cell-targeted peptide, fusion peptide utilizing said peptide, and vaccine utilizing said fusion peptide
EP3517542A4 (en) * 2016-09-21 2020-05-13 The Research Foundation for Microbial Diseases of Osaka University PEPTIDE TARGETING DENDRITIC CELLS, FUSION PEPTIDE USING THE SAME, AND VACCINE USING THE SAME
US11186618B2 (en) 2016-09-21 2021-11-30 The Research Foundation For Microbial Diseases Of Osaka University Dendritic-cell-targeted peptide, fusion peptide utilizing said peptide, and vaccine utilizing said fusion peptide
WO2018060498A1 (en) * 2016-09-30 2018-04-05 Norwegian University Of Life Sciences Process for degrading a polysaccharide employing a lytic polysaccharide monooxygenase
WO2018201050A1 (en) * 2017-04-28 2018-11-01 Board Of Trustees Of Michigan State University Tryptathionine biosynthesis by flavin mono-oxygenase 1 (fmo1)
US20210373004A1 (en) * 2018-11-19 2021-12-02 Bioaster Methods and reagents for multiplex binding experiments
CN109370995A (en) * 2018-12-11 2019-02-22 中国农业科学院饲料研究所 Manganese peroxidase CsMnP and its encoding gene and application
CN109370995B (en) * 2018-12-11 2021-05-25 中国农业科学院北京畜牧兽医研究所 Manganese peroxidase CsMnP and its encoding gene and application
WO2021167011A1 (en) * 2020-02-21 2021-08-26 キッコーマン株式会社 Device for evaluating state of sample, system including same, method for evaluating state of sample, and lactate dehydrogenase used therefor
JPWO2021167011A1 (en) * 2020-02-21 2021-08-26
EP4108678A4 (en) * 2020-02-21 2024-03-27 Kikkoman Corporation DEVICE FOR EVALUATION OF THE CONDITION OF A SAMPLE, SYSTEM COMPRISING SAME, METHOD FOR EVALUATION OF THE CONDITION OF A SAMPLE AND LACTATE DEHYDROGENASE USED FOR THIS PURPOSE
JP7714520B2 (en) 2020-02-21 2025-07-29 キッコーマン株式会社 Device for assessing the condition of a specimen, system including the same, method for assessing the condition of a specimen, and lactate dehydrogenase used therein
WO2023225459A2 (en) 2022-05-14 2023-11-23 Novozymes A/S Compositions and methods for preventing, treating, supressing and/or eliminating phytopathogenic infestations and infections
WO2024131880A3 (en) * 2022-12-23 2024-07-25 Novozymes A/S Detergent composition comprising catalase and amylase

Also Published As

Publication number Publication date
WO2012068236A3 (en) 2012-08-16

Similar Documents

Publication Publication Date Title
WO2012068236A2 (en) Novel fungal oxidoreductases
EP2421965B1 (en) Carbohydrate degrading polypeptide and uses thereof
CA2657684C (en) Construction of highly efficient cellulase compositions for enzymatic hydrolysis of cellulose
US10266863B2 (en) Enzymatic activity of lytic polysaccharide monooxygenase
US20130280764A1 (en) Method of improving the activity of cellulase enzyme mixtures in the saccharification (ligno)cellulosic material
EP3318574B1 (en) Polypeptide having beta-glucosidase activity and uses thereof
US8802415B2 (en) Talaromyces transformants
MX2012009282A (en) Polypeptide having cellobiohydrolase activity and uses thereof.
KR20150113170A (en) Carbohydrate degrading polypeptide and uses thereof
WO2012027374A2 (en) Novel fungal carbohydrate hydrolases
WO2009138877A2 (en) Heterologous expression of fungal cellobiohydrolases in yeast
HUE030426T2 (en) Fungal xylanase
KR20140027154A (en) Glycosyl hydrolase enzymes and uses thereof for biomass hydrolysis
WO2009133036A1 (en) Cellobiohydrolase 1 from penicillium chysogenum and uses thereof
MX2012015144A (en) Polypeptide having acetyl xylan esterase activity and uses thereof.
WO2012021883A2 (en) Novel fungal enzymes
WO2009133035A1 (en) Cellobiohydrolase 1 from penicillium chysogenum and uses thereof
EP3313999B1 (en) Polypeptides having demethylating activity
MX2012014990A (en) Polypeptide having swollenin activity and uses thereof.
WO2009133034A1 (en) Carbohydrate modifying polypeptide and uses thereof
WO2012078741A2 (en) Novel fungal esterases
NZ597623A (en) Polypeptides having beta-glucosidase activity and polynucleotides encoding same
WO2009133039A1 (en) Carbohydrate modifying polypeptide and uses thereof
CN108368530A (en) β-glucosyl enzym and application thereof
CN108884481A (en) β-glucosyl enzym and application thereof

Legal Events

Date Code Title Description
121 Ep: the epo has been informed by wipo that ep was designated in this application

Ref document number: 11842196

Country of ref document: EP

Kind code of ref document: A2

NENP Non-entry into the national phase

Ref country code: DE

122 Ep: pct application non-entry in european phase

Ref document number: 11842196

Country of ref document: EP

Kind code of ref document: A2