RS20050804A - Novel glyphosate-n- acetyltransferase (gat) genes - Google Patents

Abstract

Novel proteins are provided herein, including proteins capable of catalyzing the acetylation of glyphosate and other structurally related proteins. Also provided are novel polynucleotides capable of encoding these proteins, compositions that include one or more of these novel proteins and/or polynucleotides, recombinant cells and transgenic plants comprising these novel compounds, diversification methods involving the novel compounds, and methods of using the compounds. Some of the novel methods and compounds provided herein can be used to render an organism, such as a plant, resistant to glyphosate.

Description

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KATARINA M. • V v'°'

PIONEER HI-BRED INTERNATIONAL, INC MAruanaVk^

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NEW GENES FOR GLYPHOSATE-N-ACETYLTRANSFERASE (GaIqo^ 2 -

COPYRIGHT NOTICE 37 C.F.R § 1.71(E)

The disclosure portion of this patent document contains copyrightable material. The copyright owner permits anyone to reproduce in facsimile form the patent document or patent disclosure as publicly available in the Patent and Trademark Office patent file or on file, but otherwise retains all copyright.

HISTORY OF THE INVENTION

Crop selectivity to specific herbicides can be ensured by constructing and inserting into the crop genes that code for the appropriate metabolic enzymes for herbicides. In some cases, these enzymes and the nucleic acids that encode them are of plant origin. In other cases, they are derived from other organisms, such as microorganisms. See, for example, Padgetteet al., (1996) "New weed control opportunities: Development of soybeans with Round UP Ready™ gene" and Vasil (1996) "Phosphinothricin-resistant crops", both published in Herbicide-Resistant Crops, ed. Duke (CRC Press, Boca Raton, FL) p. 54-84 and p. 85-91. Indeed, transgenic plants have been engineered to express different resistance/metabolism genes originating from different organisms. For example, acetohydroxy acid synthase has been introduced into various plants, and it has been shown that when plants express this enzyme, it confers resistance to various herbicides (see, for example, Hattoriet al., (1995) Mol. Gen. Genet. 246:419. Other genes that confer herbicide tolerance include: the gene encoding the rat cytochrome P4507A1 chimeric protein and the yeast NADPH-cytochrome P450 oxidoreductases (Shiota et al, (1994) Plant Physiol. 106:17), genes for glutathione reductase and superoxide dismutase (Aonoet al, (1995) Plant Cell Physiol. 36: 1687), and genes for various phosphotransferases (Datta et al, (1992) Plant Mol. Biol. 220:619).

One herbicide that has been the subject of much research in this regard is N-phosphomonomethylglycine, often called glyphosate. Glyphosate is the world's best-selling herbicide, with sales estimated to reach $5 billion by 2003. It is a broad-spectrum herbicide that kills both broadleaf and grass-type plants. A successful means of glyphosate resistance, at a commercial level in transgenic plants, is the insertion of a modified gene for Agrobacterium's CP4 5-enolpyruvylshikimate-3-phosphate synthase (hereafter referred to as EPSP synthase or EPSPS). The transgene is targeted to the chloroplast where it can continue EPSP synthesis from phosphoenolpyruvic acid (PEP) and shikimate-3-phosphate in the presence of glyphosate. In contrast, native EPSP synthase was inhibited by glyphosate. Without the transgene, plants sprayed with glyphosate die very quickly due to inhibition of EPSP synthase, which shuts down downstream pathways necessary for the biosynthesis of aromatic amino acids, hormones, and vitamins. CP4 glyphosate-resistant transgenic soybean plants are marketed, for example by Monsato under the name "Round UP Ready™".

In the natural environment, the predominant mechanism by which glyphosate is degraded is through the metabolism of soil microflora. The primary metabolite of glyphosate in the soil has been identified as aminomethylphosphonic acid (AMPK) which is ultimately converted to ammonia, phosphate and carbon dioxide. A proposed metabolic scheme describing the degradation of glyphosate in soil via the AMPK pathway is shown in Figure 8. An alternative metabolic pathway for the degradation of glyphosate by certain soil bacteria, the sarcosine pathway, takes place via the initial cleavage of the C-P bond to yield inorganic phosphate and sarcosine, as shown in Figure 9.

Another successful herbicide/transgenic harvest package is glufosinate (phosphinothricin) and the Libertv Link™ feature marketed, for example, by Aventis. Glufosinate is also a broad spectrum herbicide. His "target" ie. the target compound is the enzyme glutamate synthase in chloroplast. Resistant plants nosebargen from Streptomyces hygroscopius achieve resistance through the N-acetylation activity of bar- which modifies and detoxifies glufosinate.

An enzyme capable of acetylating the primary amine of AMPK is reported in PCT Application No. WO00/29596. The enzyme is not described to be able to acetylate a compound with a secondary amine (eg glyphosate).

While various strategies for herbicide resistance are available, as mentioned above, additional approaches would have significant commercial value. The present invention provides novel polynucleotides and polypeptides for conferring herbicide tolerance, as well as numerous other benefits that will become apparent upon review of the disclosure.

CONTENT OF THE INVENTION

The present invention provides methods and reagents for obtaining an organism, for example a plant, that is resistant to glyphosate using one or more embodiments described below.

One embodiment of the present invention provides novel polypeptides designated herein as glyphosate-N-acetyltransferase ("GAT") polypeptides. GAT polypeptides are characterized by their mutual structural similarity, for example, in terms of sequence similarity when GAT polypeptides are compared to each other. The GAT polypeptides of the present invention possess glycosate-N-acetyltransferase activity, that is, the ability to catalyze the acetylation of glyphosate. These GAT polypeptides transfer the acetyl group from acetyl CoA to the N of glyphosate. Additionally, some GAT polypeptides transfer the propionyl group from propionyl CoA to the N of glyphosate. Some GAT polypeptides are also capable of catalyzing acetylation of glyphosate analogs and/or glyphosate metabolites, for example, aminomethylphosphonic acid. Examples of GAT polypeptides correspond to SEQ ID NO: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597,598,599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 665, 667, 669, 671, 673, 675, 677, 679, 681, 683, 685, 687, 689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811,813, 815, 817, 819, 821, 823, 825, 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 929, 931, 953, 954, 955, 956, 957, 958, 959, 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971 and 972.

Also provided are novel polynucleotides designated herein as GAT polynucleotides, for example, SEQ ID NO: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 524, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 620, 622, 624, 626, 628, 630, 632, 634, 636, 638, 640, 642, 644, 646, 648, 650, 652, 654, 656, 658, 660, 662, 664, 666, 668, 670, 672, 674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726, 728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788, 790, 792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814, 816, 818, 820, 822, 824,832, 834, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916, 918, 920, 922, 924, 932, 933, 934, 935, 936, 937, 938, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952. GAT polynucleotides are characterized by their ability to encode GAT polypeptides. In some embodiments of the present invention, GAT polynucleotides are engineered to be better expressed in a plant by replacing one or more parental codons with synonymous codons preferentially used in plants over the parental codon. In another embodiment, the GAT polynucleotide is modified by inserting a nucleotide sequence encoding a chloroplast N-terminal transit peptide. In one embodiment, the GAT polynucleotide is modified by inserting one or more G+C-containing codons (such as GCG or GCT) immediately downstream of and adjacent to the Met initiation codon.

GAT polypeptides, GAT polynucleotides, and glyphosate-N-acetyltransferase activity are described in more detail below. The invention further includes certain fragments of the GAT polypeptides and GAT polynucleotides described herein.

The present invention includes non-native variants of the polypeptides and polynucleotides described herein, where one or more amino acids from the polypeptide have been mutated.

In certain preferred embodiments, the GAT polypeptides of the present invention are characterized as follows. When optionally aligning amino acid sequences selected from the group consisting of SEQ ID NOs: 300, 445, and 457 to obtain a similarity score of at least 460 using the BLOSUM62 matrix, a gap existence penalty of 11, and a gap extension penalty of 1, one or more of the following positions satisfy the following restrictions: (i) at positions 18 and 38, a Z5 amino acid residue; (ii) at position 62, a Z1 amino acid residue; (iii) at position 124, a Z6 amino acid residue; (iv) at position 144, a Z 2 amino acid residue wherein: Z 2 is an amino acid residue selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid residue selected from the group consisting of F, W and Y; Z5 is an amino acid residue selected from the group consisting of D and E; and Z6 is an amino acid residue selected from the group consisting of C, G and P.

The invention further provides an isolated or recombinant polypeptide comprising an amino acid sequence selected from the group consisting of: (a) an amino acid sequence that is at least 98% identical to SEQ ID NO: 577; (b) an amino acid sequence that is at least 97% identical to SEQ ID NO: 578; (c) an amino acid sequence that is at least 97% identical to SEQ ID NO: 621; (d) an amino acid sequence that is at least 98% identical to SEQ ID NO: 579; (e) an amino acid sequence that is at least 98% identical to SEQ ID NO: 602; (f) an amino acid sequence that is at least 95% identical to SEQ ID NO: 697; (g) an amino acid sequence that is at least 96% identical to SEQ ID NO: 712; (h) an amino acid sequence that is at least 97% identical to SEQ ID NO: 613; (i) an amino acid sequence that is at least 89% identical to SEQ ID NO: 677 (j) an amino acid sequence that is at least 96% identical to SEQ ID NO: 584 (k) an amino acid sequence that is at least 98% identical to SEQ ID NO: 707; (1) an amino acid sequence that is at least 98% identical to SEQ ID NO: 616; (m) an amino acid sequence that is at least 96% identical to SEQ ID NO: 612 (n) an amino acid sequence that is at least 98% identical to SEQ ID NO: 590.

The present invention further provides an isolated or recombinant polypeptide comprising an amino acid sequence selected from the group consisting of: (a) an amino acid sequence that is 96% identical to positions 2-146 of SEQ ID NO: 919 (such as SEQ ID NO: 917, 919, 921, 923, 925, 927, 833, 835, 839, 843, 845, 859, 863, 873, 877, 891, 895, 901, 905, 907, 913, 915 or 950); (b) an amino acid sequence that is 97% identical to position 2-146 of SEQ ID NO: 929 (such as SEQ ID NO: 929, 931, 835, 843, 849 or 867); (c) an amino acid sequence that is 98% identical to positions 2-146 of SEQ ID NO: 847 (such as SEQ ID NO: 845 or 847); (d) an amino acid sequence that is at least 98% identical to positions 2-146 of SEQ ID NO: 851; (e) an amino acid sequence that is at least 98% identical to positions 2-146 of SEQ ID NO: 853; (f) an amino acid sequence that is at least 98% identical to positions 2-146 of SEQ ID NO: 855 (such as SEQ ID NO:835 or 855); (g) an amino acid sequence that is at least 98% identical to positions 2-146 of SEQ ID NO: 857; (h) an amino acid sequence that is at least 98% identical to positions 2-146 of SEQ ID NO: 861 (such as SEQ ID NO: 839, 861 or 833); (i) an amino acid sequence that is at least 98% identical to positions 2-146 of SEQ ID NO: 875; (k) an amino acid sequence that is at least 98% identical to positions 2-146 of SEQ ID NO: 881; (1) an amino acid sequence that is at least 98% identical to positions 2-146 of SEQ ID NO: 885 (such as SEQ ID NO:845 or 885); (m) an amino acid sequence that is at least 98% identical to positions 2-146 of SEQ ID NO: 887; (n) an amino acid sequence that is at least 98% identical to positions 2-146 of SEQ ID NO: 889 (such as SEQ ID NO: 863, 889, 891 or 903); (o) an amino acid sequence that is at least 98% identical to positions 2-146 of SEQ ID NO: 893; (p) an amino acid sequence that is at least 98% identical to positions 2-146 of SEQ ID NO: 897; (q) an amino acid sequence that is at least 98% identical to positions 2-146 of SEQ ID NO: 899; (r) an amino acid sequence that is at least 98% identical to positions 2-146 of SEQ ID NO: 909 (such as SEQ ID NO:883 or 909; (s) an amino acid sequence that is at least 98% identical to positions 2-146 of SEQ ID NO: 911; (t) an amino acid sequence that is at least 99% identical to positions 2-146 of SEQ ID NO: 911 ID NO: 837; (u) an amino acid sequence that is at least 99% identical to positions 2-146 of SEQ ID NO: 865; and (x) an amino acid sequence which is at least 99% identical to positions 2-146 of SEQ ID NO: 879. In some embodiments of the invention, the amino acid sequence of the polypeptide comprises Met, Met-Ala, or Met-Ala-Ala at the N-terminal side of the amino acid corresponding to position 2 of the reference amino acid sequence.

The present invention further provides an isolated or recombinant polypeptide comprising an amino acid sequence that is at least 95% identical to positions 2-146 of SEQ DD NO:929 and that contains a Gly or Asn residue at amino acid position 33 of SEQ ID NO:929 (such as SEQ ID NOs: 837, 849, 893, 897, 905, 921, 927, 929, or 931). In some embodiments of the invention, the amino acid sequence of the polypeptide comprises Met, Met-Ala, or Met-Ala-Ala at the N-terminal side of the amino acid corresponding to position 2 of the reference amino acid sequence.

The invention further includes a nucleic acid construct comprising a polynucleotide of the invention. The construct can be a vector, such as a plant transformant vector. In some aspects, a vector of the invention will comprise a T-DNA sequence. The construct can optionally include a regulatory sequence (eg, a promoter) operably linked to the GAT polynucleotide, wherein the promoter is heterologous to the polynucleotide and is effective to induce sufficient expression of the encoded polypeptide to enhance glyphosate tolerance of a plant cell transformed with the nucleic acid construct.

In some aspects of the invention a GAT polynucleotide functions as a selectable marker, for example, in a plant, bacterium, actinomycete, yeast, or other fungus. For example, an organism transformed with a vector includes a GAT polynucleotide selectable marker that can be selected based on its ability to grow in the presence of glyphosate. The GAT marker gene can be used to select or screen transformed cells that express the gene.

The invention further encompasses vectors with complex properties, that is, vectors that encode GAT polypeptides and that also comprise a second polynucleotide sequence encoding a second polypeptide that exhibits a detectable phenotypic characteristic upon expression by a cell or organism of the second polypeptide in an effective amount, for example disease resistance or pest resistance. A detectable phenotypic trait can also function as a detectable marker, for example by showing resistance to a herbicide or by providing some type of marker that can be seen.

In one embodiment, the present invention provides a composition comprising two or more polynucleotides of the present invention. Preferably, the GAT polynucleotides encode GAT polypeptides that have different kinetic parameters, that is, a GAT variant having a lower Km can be combined with one that has a higher k<;at. In a further embodiment, different GAT polynucleotides can be combined with a chloroplast transit sequence or with another signal sequence and thus ensure the expression of GAT polypeptides in different parts of cells, organelles or the secretion of one or more GAT polypeptides.

Accordingly, compositions containing two or more polypeptides or coded polypeptides are objects of the invention. In some cases, these compositions are libraries of nucleic acids, for example, at least 3 or more such nucleic acids. Compositions obtained by digestion of the nucleic acids of the present invention with restriction endonucleases, DNAse or RNAse, or in other ways that lead to fragments of nucleic acids, for example, mechanical cleavage, chemical cleavage, and so on, are also subject of the invention, as well as compositions obtained by incubating the nucleic acid of the invention with deoxyribonucleotide triphosphate and a nucleic acid polymerase such as a thermostable nucleic acid polymerase.

Cells transduced with a vector of the invention, or cells otherwise having a nucleic acid of the invention, represent an aspect of the invention. In a preferred embodiment, cells expressing a polypeptide encoded by a nucleic acid of the invention.

In some embodiments, the cells in which the nucleic acids of the invention are incorporated are plant cells. Transgenic plants, transgenic plant cells, and transgenic plant explants incorporating nucleic acids of the present invention are also subject of the invention. In some embodiments, the transgenic plants, transgenic plant cells, and transgenic plant explants express an exogenous polypeptide with glyphosate-N-acetyltransferase activity encoded by a nucleic acid of the invention. The invention also provides transgenic seeds produced by a transgenic plant of the invention.

The invention further provides transgenic plants, transgenic plant cells and transgenic plant explants or transgenic seeds that have increased tolerance to glyphosate due to the expression of a polypeptide with glyphosate-N-acetyltransferase activity and a polypeptide that enables tolerance to glyphosate through another mechanism, such as glyphosate-tolerant 5-enolpyruvylshikimate-3-phosphate synthase and/or glyphosate-tolerant glyphosate oxido-reductase. In a further embodiment, the invention provides transgenic plants, transgenic plant cells, and transgenic plant explants that have increased tolerance to glyphosate, as well as tolerance to an additional herbicide due to the expression of a polypeptide with glyphosate-N-acetyltransferase activity, a polypeptide that enables tolerance to glyphosate through another mechanism, such as glyphosate-tolerant 5-enolpyruvylshikimate-3-phosphate synthase and/or glyphosate-tolerant glyphosate oxido-reductase and polypeptide that allows tolerance to additional herbicide, such as mutated hydroxyphenylpyruvate dioxygenase, sulfonamide-tolerant acetolactate synthase, sulfonamide-tolerant acetohydroxy acid synthase, imidazolinone-tolerant acetolactate synthase, imidazolinone-tolerant acetohydroxy acid synthase, phosphinothricin acetyltransferase and mutated protoporphyrinogen oxidase.

The invention also provides transgenic plants, transgenic plant cells and transgenic plant explants or transgenic seeds, which have increased tolerance to glyphosate as well as tolerance to an additional herbicide due to the expression of a polypeptide with glyphosate-N-acetyltransferase activity and a polypeptide that allows tolerance to an additional herbicide such as mutated hydroxyphenylpyruvate dioxygenase, sulfonamide-tolerant acetolactate synthase, sulfonamide-tolerant acetohydroxy acid synthase, imidazolinone-tolerant acetolactate synthase, imidazolinone-tolerant acetohydroxy acid synthase, phosphinothricin acetyltransferase and mutated protoporphyrinogen oxidase.

The present invention also provides transgenic plants, transgenic plant cells, and transgenic plant explants or transgenic seeds that have increased tolerance to glyphosate as well as additional desirable traits that may be provided by one or more transgenes.

Methods for the production of polypeptides of the invention - by introducing into the cells the nucleic acids that encode them and then express them and optionally the same are then obtained from the cells or the mind medium for growing cultures are also the subject of this invention. In preferred embodiments, the cells expressing the polypeptides of the present invention are transgenic plant cells.

Also objects of the present invention are methods for increasing the level of expression of a polypeptide of the invention in a plant or plant cell by inserting into the coding sequence for the polypeptide one or two G/C-rich codons (such as GCG or GCT) immediately adjacent to or downstream of the initial ATG codon, and/or by replacing in the polypeptide coding sequence one or more codons that are used in plants as codons for codons that code for the same amino acid(s) that are more commonly used in plants, and by introducing the modified coding sequence into a plant or plant cell and expressing the modified coding sequence.

Polypeptides specifically bound by a polyclonal antiserum reacting against an antigen derived from SEQ ID NO: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597, 598, 599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 665, 667, 669, 671, 673, 675, 677, 679, 681, 683, 685, 687, 689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811, 813, 815, 817, 819, 821, 823, 825, 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 929, 931, 953, 954, 955, 956, 957, 958, 959, 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971 and 972, but not sequences found in nature, such as the polypeptide represented by a sub-sequence of those of GenBank accession number CAA70664, as well as antibodies produced by delivery of an antigen derived from any one or more of SEQ ID NO: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597,598,599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 665, 667, 669, 671, 673, 675, 677, 679, 681, 683, 685, 687, 689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811, 813, 815, 817, 819, 821, 823, 825, 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 929, 931, 953, 954, 955, 956, 957, 958, 959, 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971 and 972 and/or which specifically binds to such antigens and which does not specifically bind to a naturally occurring polypeptide corresponding to those of GeneBank accession number CAA70664, all of which are subject of the invention.

Another aspect of the invention relates to methods of altering polynucleotides in order to produce new GAT polynucleotides and polypeptides by recombination or mutating nucleic acids of the invention in vitro or in vivo. In one embodiment, the recombination produces at least one library of recombinant GAT polynucleotides. Libraries so made are embodiments of the present invention as are the cells containing these libraries. Further, methods for producing a modified GAT polynucleotide by mutating a nucleic acid of the invention are embodiments of the present invention. Recombinant and mutant GAT polynucleotides and polypeptides produced by the methods of the invention are also embodiments of the present invention.

In some aspects of the invention, the alteration is achieved using recursive recombination which can be performed in vitro, in vivo, in silico or a combination thereof. Some examples of shuffling methods that are described in more detail in the following text are the "familv shuffling" method and the "svnthetic shuffling" method. The invention provides methods for producing glyphosate-resistant transgenic plants or plant cells, comprising transforming the plant or plant cell with a polynucleotide encoding glyphosate-N-acetyltransferase, and optionally regenerating the transgenic plant from the transformed plant cell. In some aspects the polynucleotide is a GAT polynucleotide, optionally a GAT polynucleotide derived from a bacterial source. In some aspects of the invention, the method may comprise growing the transformed plant or plant cell at concentrations of glyphosate that inhibit the growth of a wild-type plant of the same species without inhibiting the growth of the transformed plant. The method may comprise growing the transformed plant or plant cell or the progeny of the plant or plant cell in increasing concentrations of glyphosate and/or in a concentration of glyphosate that is lethal to a wild plant or plant cell of the same species. A glyphosate-resistant transgenic plant produced by this method can be propagated, for example by crossing with another plant, so that at least one part of the progeny of the cross shows tolerance to glyphosate.

The invention further provides methods for selective control of weeds in a field containing a crop, which include planting in the field seeds of crops or plants tolerant to glyphosate as a result of transformation with a gene encoding glyphosate N-acetyltransferase, and applying glyphosate to the crop and weeds in the field in an amount sufficient to control the weeds without significantly affecting the crop.

The invention further provides methods for controlling weeds in a field and preventing the emergence of weeds resistant to glyphosate in a field containing a crop, which include planting in the field seeds of crops or plants that are tolerant to glyphosate as a result of transformation with a gene encoding glyphosate N-acetyltransferase and a gene encoding a polypeptide that allows tolerance with another mechanism, such as glyphosate-tolerant 5-enolpyruvylshikimate-3-phosphate synthase and/or glyphosate-tolerant glyphosate oxido-reductase and application of glyphosate to the crop and weeds in the field in sufficient quantity to control weeds without significantly affecting the crop.

In further embodiments, the invention provides methods for controlling weeds in a field and preventing the emergence of herbicide-resistant weeds in a field containing a crop, which include planting in the field seeds of crops or plants that are glyphosate tolerant as a result of transformation with a gene encoding glyphosate N-acetyltransferase and a gene encoding a polypeptide that enables tolerance with another mechanism, such as glyphosate-tolerant 5-enolpyruvylshikimate-3-phosphate synthase and/or glyphosate-tolerant glyphosate oxido-reductase and a polypeptide that enables tolerance to additional herbicides, such as mutated hydroxyphenylpyruvate dioxygenase, sulfonamide-tolerant acetolactate synthase, sulfonamide-tolerant acetohydroxy acid synthase, imidazolinone-tolerant acetolactate synthase, imidazolinone-tolerant acetohydroxy acid synthase, phosphinothricin acetyltransferase and mutated protoporphyrinogen oxidase and applied to crops and weeds in the field in sufficient quantity glyphosate and additional herbicide as which is a hydroxyphenylpyruvate dioxygenase inhibitor, sulfonamide, imidazolone, bialphos, phosphinothricin, azafenidin, butafenacil, sulfosate, glufosinate, and protox inhibitor in order to control weeds without significant impact on the crop.

The invention further provides methods for producing a genetically transformed plant tolerant to glyphosate comprising inserting into the genome of a plant cell a recombinant double-stranded DNA molecule comprising: (i) a promoter that functions in the plant cell and enables the production of an RNA sequence; (ii) a structural DNA sequence that leads to the production of a GAT-encoding RNA sequence; and (iii) a 3' untranslated region that functions in plant cells and results in the addition of a series of polyadenylic nucleotides to the 3' end of the RNA sequence; wherein the promoter is heterologous to the structural DNA sequence and adapted to produce sufficient expression of the encoded polypeptide to enhance glyphosate tolerance of the plant cell transformed with the DNA molecule; obtaining a transformed plant cell; and regenerating from the transformed plant cell a genetically transformed plant having increased tolerance to glyphosate.

The invention further includes methods for producing a crop comprising growing a crop of a plant tolerant to glyphosate as a result of being transformed with a gene encoding glyphosate-N-acetyltransferase, under conditions that the crop plant produces a crop: and for harvesting the crop from the crop plant. These methods often involve applying glyphosate to the crop plant at a concentration effective to control the weed. Examples of crop plants include cotton, corn, and soybeans.

The invention also provides computers, computer-readable media and integrated systems, including databases consisting of recorded sequences including a sequence ("string") of characters corresponding to SEQ ID NO: 1-10, 16, 48, 190, 193, 196, 202, 205, 268, 300, 442, 445, 448, 454, 457, 515-830 and 832-972. Such integrated systems optionally include one or more sets of instructions for selecting, comparing, translating (translating), reverse translating, or displaying any one or more character strings corresponding to SEQ ID NO; 1-10, 16, 48, 190, 193, 196, 202, 205, 68, 300, 442, 445, 448, 454, 457, 515-830 and 832-972, with each other and/or with any additional nucleic acid or amino acid sequence.

SHORTCUT PICTURE

Figure 1 shows N-acetylation of glyphosate catalyzed by glyphosate-N-acetyltransferase ("GAT").

Figure 2 illustrates the detection of N-acetylglyphosate by mass spectrometry on the example of a Bacillus culture expressing native GAT activity.

Figure 3 is a table illustrating the relative identity between GAT sequences isolated from different strains of Bacillus subtilis bacteria.

Figure 4 is a map of plasmid pMAXY2120 for expression and purification of GAT enzymes from cultures

E. coli.

Figure 5 is a mass spectrometry result showing the increase in N-acetylglyphosate production over time in a typical GAR enzyme reaction mix.

Figure 6 is a graphical representation of the kinetic data of the GAT enzyme where the calculated Kmod is 2.9 mM for glyphosate.

Figure 7 is a graphical representation of the kinetic data taken from the data from Figure 6 from which the KM for 2uM for Acetyl CoA was calculated.

Figure 8 is a schematic diagram describing the degradation of glyphosate in soil via the AMPK pathway.

Figure 9 is a schematic diagram describing the sarcosine - glyphosate degradation pathway.

Figure 10 is the BLOSUM62 matrix.

Figure below is a map of plasmid pMAXY2190.

Figure 12 shows the T-DNA construct with a selective marker.

Figure 13 shows a yeast expression vector with a selective marker.

Figure 14 illustrates the effect of glyphosate on plant height during tassel development.

Figure 15A and 15B provide a comparison of the kinetic parameters Kmi kcat/Km, for various GAT enzymes assayed either in the absence of added KCl (unshaded columns) or in the presence of 20 mM KCl (shaded columns) as described in Example 18.

Figures 16A, 16B and 16C provide a comparison of the kinetic parameters Km, kcati kcat/Km for various GAT enzymes of the invention (shaded brackets) with the kinetic parameters of some GAT enzymes of the invention to be further developed (shaded brackets), as described in Example 9. "Error bars" represent, where available, the standard deviation from multiple essays.

Figure 17 represents the residual GAT activity after incubation at various temperatures as described in Example 16.

Figure 18 illustrates the effect of pH on kcati Km, as described in Example 30.

DETAILED DESCRIPTION OF THE INVENTION

This invention relates to a new class of enzymes exhibiting N-acetyltransferase activity. In one aspect, the invention relates to a new class of enzymes capable of acetylating glyphosate and glyphosate analogs, for example, enzymes possessing glyphosate-N-acetyltransferase ("GAT") activity. Such enzymes are characterized by the ability to acetylate a secondary amine from a compound. In some aspects of the invention, the compound is a herbicide, for example glyphosate, as illustrated schematically in Figure 1. The compound can also be a glyphosate analog or a metabolic degradation product of glyphosate, for example, aminomethylphosphonic acid. Although acetylation of glyphosate is a key catalytic step in one metabolic pathway for glyphosate catabolism, enzymatic acetylation of glyphosate by a natural, isolated or recombinant enzyme has not been previously described. Therefore, the nucleic acids and polypeptides of the invention provide a novel biochemical pathway for engineering herbicide resistance.

In one aspect the invention provides novel genes encoding GAT polypeptides. Isolated and recombinant GAT polynucleotides corresponding to polynucleotides found in nature, as well as recombinant and engineered, for example, altered, GAT polynucleotides are the subject of the invention. Examples of GAT polynucleotides are provided in SEQ ID NO: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 524, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550,551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 620, 622, 624, 626, 628, 630, 632, 634, 636, 638, 640, 642, 644, 646, 648, 650, 652, 654, 656, 658, 660, 662, 664, 666, 668, 670, 672, 674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726, 728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788, 790, 792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814, 816, 818, 820, 822, 824, 832, 834, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916, 918, 920, 922, 924, 932, 933, 934, 935, 936, 937, 938, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952. Specific GAT polynucleotide and polypeptide sequences are provided with examples to assist in illustrating the invention, and are not intended to limit the scope of the genus of GAT polynucleotides and polypeptides described and/or claimed herein.

The invention also provides methods for obtaining and selecting altered libraries to produce additional GAT polynucleotides, including polynucleotides encoding GAT polypeptides with improved and/or enhanced characteristics, e.g., altered Kmza glyphosate, enhanced rate of catalysis, increased stability, etc., based on the selection of a polynucleotide constituent from the library for new and improved activities described herein. It is particularly desirable to use such polynucleotides in the production of transgenic plants that are resistant to glyphosate.

The GAT polypeptides of the invention exhibit novel enzymatic activity. Specifically, enzymatic acetylation of the synthetic herbicide glyphosate has not been demonstrated until this invention. Therefore, the polopeptides described herein are exemplified by SEQ ID NOs: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597, 598, 599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 665, 667, 669, 671, 673, 675, 677, 679, 681, 683, 685, 687, 689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811, 813, 815, 817, 819, 821, 823, 825, 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 929, 931, 953, 954, 955, 956, 957, 958, 959, 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971 and 972 describe a novel biochemical pathway for glyphosate detoxification that is functional in vivo, for example in plants.

Accordingly, the nucleic acids and polypeptides of the invention have significant utility in the production of glyphosate-resistant plants by providing novel nucleic acids, polypeptides, and biochemical pathways for engineering herbicide selectivity in transgenic plants.

DEFINITIONS

Before describing the present invention in more detail, it should be understood that the present invention is not limited to particular compositions or biological systems, which of course may vary. It should be understood that the terminology used here is not used to describe only certain embodiments, - it is not intended to be limiting. As used in the specification and the appended claims, the singular forms "a", "an" and "the" include plural references unless the content indicates otherwise. So for example, a reference to a device (a device) includes a combination of two or more such devices, a reference to a gene fusion construct (a gene fusion construct) includes a mixture of constructs, and the like.

Unless otherwise defined, technical and scientific terms used herein have the same meaning as commonly used by scientists to whom this invention relates. Although methods and materials similar or equivalent to those described herein may be used to perform the tests of this invention, specific examples of suitable materials and methods are described herein. In describing and filing the patent claims of this invention, the following terminology will be used in accordance with the definitions shown below.

Accordingly, for purposes of this invention, the term "glyphosate" should be considered to include the herbicidally effective form of N-phosphomonomethylglycine (including its salt) and other forms that result in the production of glyphosate anionine planta. The term "glyphosate analog" refers to a structural analog of glyphosate that has the ability to inhibit EPSPS at levels such that the glyphosate analog is herbicidally effective.

As used herein, the term "glyphosate-N-acetyltransferase activity" or "GAT activity" refers to the ability to catalyze the acetylation of a secondary amino group of glyphosate, as illustrated for example in Figure 1. A "glyphosate-N-acetyltransferase" or "GAT" is an enzyme that catalyzes the acetylation of an amino group of glyphosate, a glyphosate analog, and/or a primary metabolite of glyphosate (ie, AMPK or sarcosine). In some preferred embodiments of the invention, GAT is capable of transferring an acetyl group from Acetyl CoA to the secondary amine of glyphosate and the primary amine of AMPK. Additionally, some GATs are also able to transfer the propionyl group of propionyl CoA to glyphosate, indicating that the GAT is also an acetyltransferase. Exemplary GATs described herein are active from about pH 5-9, with optimal activity in the range of about pH 6.5-8.0. Activity can be quantified using various kinetic parameters known in the art, for example, kcat, Kmi kcat/KM. These kinetic parameters can be determined as described in Example 7 or Example 19, below.

The terms "polynucleotide", "nucleotide sequence" and "nucleic acid", as used herein, refer to a polymer of nucleotides (A, C, T, U, G, etc., or those found in nature, or artificial nucleotide analogs), for example, DNA or RNA or descriptions thereof, for example, a character string (a character string), etc., depending on the relevant context. A given polynucleotide or complementary nucleotide can be determined from any specified nucleotide sequence.

Similarly, an "amino acid sequence" is a polymer of amino acids (protein, polypeptide, etc.) or a character string representing an amino acid polymer, depending on the context. The terms "protein", "polypeptide" and "peptide" as used herein are interchangeable.

A polynucleotide, polypeptide or other component is "isolated" when it is partially or completely separated from the components with which it is normally associated (other proteins, nucleic acids, cells, synthetic reagents, etc.). A nucleic acid or polypeptide is "recombinant" when it is artificial or engineered, or derived from an artificial or engineered protein or nucleic acid. For example, a polynucleotide that has been inserted into a vector or into any heterologous location, e.g., in the genome of a recombinant organism, so that it is not fused to a nucleotide sequence that normally flanks (flanks) a polynucleotide as found in nature is a recombinant polynucleotide. A protein expressed in vitro in vivo of a recombinant polynucleotide is an example of a recombinant polypeptide. Likewise, a polynucleotide sequence that is not found in nature, for example a naturally occurring variant of a gene, is a recombinant.

The terms "glyphosate-N-acetyltransferase polypeptide" and "GAT polypeptide" are used herein interchangeably and refer to any family of novel polypeptides provided herein.

The terms "glyphosate-N-acetyltransferase polynucleotide" and "GAT polynucleotide" are used interchangeably herein and refer to a polynucleotide encoding a GAT polypeptide.

A "subsequence" or "fragment" is any part of a complete sequence.

The assignment of numbers to amino acid or nucleotide polymers corresponds to the assignment of numbers to selected amino acid polymers or nucleic acids where the position of a given monomer component (amino acid residue, incorporated nucleotide, etc.) of the polymer corresponds to the same position of the residue in the selected reference polypeptide or polynucleotide.

A vector is a composition that facilitates cell transduction/transformation with a selected nucleic acid or expression of a nucleic acid in a cell. Vectors include, for example, plasmids, cosmids, viruses, YAC, bacteria, poly-lysine, chromosomal integration vectors, episomal vectors, etc.

"Substantially the complete length of the polynucleotide or amino acid sequence" refers to at least about 70%, generally at least about 80% or typically about 90% or more of the sequence.

As used herein, the term "antibody" refers to a protein comprising one or more polypeptides encoded substantially or in part by immunoglobulin genes or fragments of immunoglobulin genes. Commonly known immunoglobulin genes include kappa, lambda, alpha, delta, epsilon and mu genes for constant regions, as well as numerous immunoglobulin genes for variable regions. Light chains are classified as either lambda or kappa. The heavy chains are classified as gamma, mu, alpha, delta, or epsilon, which in turn define the immunoglobulin classes, IgG, IgM, IgA, IgD, and IgE. A typical immunoglobulin (antibody) structural unit contains a tetramer. Each tetramer is composed of two identical pairs of polypeptide chains, each pair having one "light" (about 25 kD) and one "heavy" chain (50-70 kD). The N-terminus (end) of each chain defines a variable region of about 100 to 110 or more amino acids primarily responsible for antigen recognition. The terms variable light chain (Vl) and variable heavy chain (VH) refer to these light and heavy chains. Antibodies exist as intact immunoglobulins or as numerous well-characterized fragments produced by digestion (cutting) with various peptidases. Therefore, for example, pepsin cleaves the antibody below the disulfide bonds in the hinge region and yields F(ab)'2, a dimer of Fab' which itself represents a light chain attached to VH-CH1 via a disulfide bond. F(ab)'2 can be reduced under mild conditions where the disulfide bond in the hinge region is broken and thus the F(ab)'2 dimer is converted to Fab' monomer. A Fab' monomer is essentially a Fab with part of a hinge region (see Paul, ed. (1998)Fundamentals! Immunology(4* Edition, Raven Press, NY) for a more detailed description of antibody fragments). While various antibody fragments are defined in terms of cleavage of an intact antibody, one skilled in the art will appreciate that such Fab' fragments can be synthesized de novo either chemically or using recombinant DNA methodology. Therefore, the term antibody as used herein also includes antibody fragments that are either produced by modification of whole antibodies or synthesized de novo using recombinant DNA methodologies. Antibodies include single chain antibodies, including single chain Fv (sFv) antibodies in which the variable heavy and variable light chains are joined together (directly or via a peptide linker) to form a continuous polypeptide. ;"Chloroplast transit peptide" is an amino acid sequence that is translated together with the protein and directs the protein to the chloroplast or other types of plastids present in the cell in which the protein is synthesized. "Chloroplast transit sequence" refers to a nucleotide sequence encoding a chloroplast transit peptide. A "signal peptide" is an amino acid sequence that is translated in conjunction with a protein and directs the protein to the secretory system (Chrispeels (\ 99\)Ann. Rev. Plant. Phuys. Plant Mol. Biol. 42: 21-53). If the protein is to be targeted to the vacuole, a vacuolar targeting signal can be further added, or if it is to be targeted to the endoplasmic reticulum, an endoplasmic reticulum retention signal can be added. If the protein is to be targeted to the nucleus, any signal present should be removed and replaced with a nuclear localization signal (Raikhel. (1992) Plant Phys. 100:1627-1632). The terms "diversification" and "diversity" as used herein for a polynucleotide refer to a plurality of modified forms of a parent polynucleotide or a plurality of parent polynucleotides. In the case where a polynucleotide encodes a polypeptide, diversity in the nucleotide sequence of the polynucleotide may result in diversity of the corresponding encoded polypeptide, for example a diverse pool of polynucleotides encoding multiple polypeptide variants. In some embodiments of the invention, sequence diversity is exploited by screening/selecting a library of diversified polynucleotides for variants with desired functional attributes, for example a polynucleotide encoding a GAT polypeptide with enhanced functional characteristics. The term "encodes" refers to the ability of a nucleotide sequence to encode one or more amino acids. The expression requires neither a start nor a stop codon. An amino acid sequence can be encoded in any of the six reading frames provided by the polynucleotide sequence and its complement. ;When used herein, the term "artificial variant" - refers to a polypeptide having GAT activity, which is encoded by a modified GAT polynucleotide, for example a modified form of any of SEQ ID NO: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 524, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 620, 622, 624, 626, 628, 630, 632, 634, 636, 638, 640, 642, 644, 646, 648, 650, 652, 654, 656, 658, 660, 662, 664, 666, 668, 670, 672, 674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726, 728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788, 790, 792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814, 816, 818, 820, 822, 824, 832, 834, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916, 918, 920, 922, 924, 932, 933, 934, 935, 936, 937, 938, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952 or natural GAT polynucleotide isolated from the organism. The modified polynucleotide from which the artificial variant is obtained when expressed in a suitable host is obtained by human intervention - modification of the GAT polynucleotide. ;The term "nucleic acid construct" or "polynucleotide construct" means a nucleic acid molecule, single-stranded or double-stranded, that has been isolated from a naturally occurring gene or that has been modified to contain nucleic acid segments in a way that does not normally exist in nature. The term nucleic acid construct is synonymous with the term "expression cassette", when the nucleic acid contains the control sequences required for the expression of the coding sequence of the present invention. The term "control sequence" is defined herein to include all components that are necessary or advantageous for the expression of the polypeptides of the present invention. Each control sequence may be native or foreign to the nucleotide sequence encoding the polypeptide. Such control sequences include, but are not limited to, a leader sequence, a polyadenylation sequence, a propeptide sequence, a promoter sequence, and a transcription termination sequence. At a minimum, control sequences include a promoter and transcriptional and translational stop signals. Control sequences can be provided with linkers for the purpose of inserting restriction sites that facilitate ligation of the control sequences with the coding region of the nucleotide sequence encoding the polypeptide. ;The term "operably linked" is defined herein as a configuration in which the control sequence is appropriately placed in a position relative to the coding sequence of the DNA sequence such that the control sequence directs the expression of the polypeptide. As used herein, the term "coding sequence" is intended to encompass nucleotide sequences that directly specify the amino acid sequence of its protein product. The boundaries of the coding sequence are generally determined by an open reading frame that usually begins with the ATG start codon. The coding sequence typically includes DNA, cDNA, and/or recombinant nucleotide sequence. In this context, the term "expression" includes any step in the production of a polypeptide including, but not limited to, transcription, post-transcriptional modification, translation, post-translational modification, and secretion. In this context, the term "expression vector" includes a DNA molecule, linear or circular, which includes a segment encoding a polypeptide of the invention and which is operably linked to additional segments that ensure its transcription. ;The term "host cell" as used herein includes any cell type that can be transformed with a nucleic acid construct. ;The term "plant" includes whole plants, shoots of vegetative organs/structures (for example, leaves, stems and bulbs), roots, flowers and floral organs/structures (for example, sepals, sepals, petals, stamens, pistils, stamens, unfertilized ovules), seeds (including embryo, endosperm, and seed coat) and fruit (mature ovule), plant tissue (for example, vascular tissue, ground tissue, and the like) and cells (for example, helper cells, ova, trichomes, and the like), and their progeny. The class of plants that can be used in the method of the present invention is generally as broad as the class of higher and lower plants that are amenable to transformation techniques, including angiosperms (monocots and dicots), gymnosperms, ferns, and multicellular algae. It includes plants of various ploidy levels, including aneuploid, polyploid, diploid, haploid and hemizygous. The term "heterologous" as used herein describes a relationship between two or more elements that indicates that the elements are not normally found in close proximity to each other in nature. Thus, for example, a polynucleotide sequence is "heterologous" to an organism or another polynucleotide sequence if it originates from a foreign species or from the same species and is modified from its original form. For example, a promoter operably linked to a heterologous coding sequence refers to a coding sequence originating from a species different from that from which the promoter is derived or originating from the same species, a coding sequence not naturally associated with the promoter (eg, a genetically engineered coding sequence or an allele from a different ecotype or variety). An example of a heterologous polypeptide is a polypeptide that is expressed from a recombinant polynucleotide in a transgenic organism. Heterologous polynucleotides and polypeptides are forms of recombinant molecules. ;Various additional terms are defined or otherwise characterized herein. ;GLYPHOSATE - N-ACETYLTRANSFERASES;In one aspect, the invention provides a novel family of isolated or recombinant enzymes designated herein as "glyphosate-N-acetyltransferases" "GATs" or "GAT enzymes". GATs are enzymes that possess GAT activity, preferably activity sufficient to cause some degree of tolerance to glyphosate after a transgenic plant has been engineered to express the GAT. Some examples of GAT activity, including GAT polypeptides, are described in more detail below. GAT-mediated tolerance to glyphosate is a complex function of GAT activity, GAT expression levels in the transgenic plant, the particular plant, and numerous other factors including, but not limited to, the nature and timing of herbicide application. One skilled in the art can determine without further experimentation the level of GAT activity required to manifest a glyphosate tolerance effect in a particular context. ;GAT activity can be characterized using conventional kinetic parameters kcat, Km, and kca/KM which can be measures of acetylation rate, especially at high substrate concentrations, KM is a measure of GAT affinity for substrates (for example acetyl CoA, propionylCoA, and glyphosate), and kcat/KM is a measure of catalytic efficiency that takes into account both substrate affinity and catalytic rate. kcat/Kmje is especially important in a situation where the concentration of the substrate is at least partially rate-limited. In general, GAT with higher kcatili kcJKM is a more efficient catalyst than long GAT with lower kcatili kcat/KM- GAT with lower Km is more efficient catalyst than other GAT with higher KM. Therefore, to determine whether one GAT is more efficient than the other, the kinetic parameters for the two enzymes can be compared. The relative importance of kcat, KM, and kcat/KM will vary depending on the context in which the GAT is expected to operate, for example, the predicted effective concentration of glyphosate relative to Kmza glyphosate. GAT activity can also be characterized in terms of any of a number of functional characteristics, including, but not limited to, stability, sensitivity to inhibition or activation by other molecules. ;GLYPHOSATE - N-ACETYLTRANSFERASE POLYPEPTIDES ;In one aspect, the invention provides a novel family of isolated or recombinant polypeptides designated herein as "glyphosate-N-acetyltransferase polypeptides" or "GAT polypeptides". GAT polypeptides are characterized by their structural similarity to the novel GAT family. Many but not all GAT polypeptides are GATs. The difference is that GATs are defined in terms of function, while GAT polypeptides are defined in terms of structure. A subset of GAT polypeptides consists of those GAT polypeptides that possess GAT activity, preferably at a level that will function and confer resistance to glyphosate after the transgenic plant expresses the protein at an effective level. Some preferred GAT polypeptides for use in conferring tolerance to glyphosate have a kcat of at least 1 min" <1>, or more preferably at least 10 min" <1>, 100 minutes" <1>or 1000 min" <1>. Other preferred GAT polypeptides for use in conferring tolerance to glyphosate have a KMne greater than 100 mM, or more preferably no greater than 10 mM, 1 mM, or 0.1 mM. Even more preferred GAT polypeptides for use in conferring glyphosate tolerance have a kcat/KM of at least 1 mM^min"1 or greater, preferably at least 10 mM^min"1, 100 mM"'min"', 1000 imVT'min"1, or 10000 mM^min"1. ;Examples of GAT polypeptides have been isolated and characterized from various bacterial strains. One example of a monomeric GAT polypeptide that has been isolated and characterized has a molecular radius of approximately 17 kD. Example for GAT enzyme isolated from strainB. licheniformis, SEQ ID NO:7, shows a Kmza glyphosate of approximately 2.9 mM and a Kmza acetyl CoA of approximately 2uM, with a kcat equal to 6 /minute. ;The term "GAT polypeptide" refers to any polypeptide comprising an amino acid sequence that can be optimally aligned ("aligned") with an amino acid sequence selected from the group consisting of SEQ ID NOs: 300, 445 and 457 to obtain a similarity score of at least 460 using the BLOSUM62 matrix, a break presence penalty of 11 and a break span penalty of 1, indicated at least one of the following positions fits the following restrictions: (i) there is a Z5 amino acid residue at positions 18 and 38; (ii) there is a Z1 amino acid residue at position 62; (iii) there is a Z6 amino acid residue at position 124; and (vi) at position 144 there is a Z2 amino acid residue, wherein: Z1 is an amino acid residue selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid residue selected from the group consisting of F, W and Y; Z5 is an amino acid residue selected from the group consisting of D and E; Z6 is an amino acid residue selected from the group consisting of C, G, and P. Some aspects of the present invention relate to GAT polypeptides comprising an amino acid sequence that can be optimally compared to an amino acid sequence selected from the group consisting of SEQ ID NOs: 300, 445, and 457 to obtain a similarity score of at least 440, 445, 450, 455, 460, 465, 470, 475, 480, 485, 490, 495, 500, 505, 510, 515, 520, 525, 530, 535, 540, 545, 550, 555, 560, 565, 570, 575, 580, 585, 590, 595, 600, 605, 610, 615, 620, 625, 630, 635, 640, 645, 650, 655, 660, 665, 670, 675, 680, 685, 690, 695, 700, 705, 710, 715, 720, 725, 730, 735, 740, 745, 750, 755 or 760 using the BLOSUM62 matrix, a break existence "penalty" of 11 and a break spread "penalty" of 1, indicated that at least one or more of the following positions fit the following restrictions: (i) at positions 18 and 38, Z5 amino acid residue; (ii) at position 62, a Z1 amino acid residue; (iii) at position 124, a Z6 amino acid residue; and (vi) at position 144, a Z2 amino acid residue, wherein: Z1 is an amino acid residue selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid residue selected from the group consisting of F, W and Y; Z5 is an amino acid residue selected from the group consisting of D and E; Z6 is an amino acid residue selected from the group consisting of C, G, and P. Two sequences are "optimally aligned" when compared for similarity scoring using an amino acid substitution matrix (eg, BLOSUM62), break existence penalty, and break spread penalty to reach the highest possible score (sum) for a pair of sequences. Amino acid substitution matrices and their use in quantifying the similarity between two sequences are known in the art and have already been described, for example in Davhoffet al., (1978) "A model of evolutionary change in proteins" in "Atlas of Protein Sequence and Structure," Vol. 5. Suppl. 3 (ed. M. O. Davhoff), p. 345-352. Natl. Biomed. Res. Found., Washington, DC and Henikoff et al., (1992) Proc. Nat' l. Acad. Sci. USA89: 10915-10919. The BLOSUM62 matrix (si. 10) is often used as a standard score substitution matrix in a sequence comparison protocol such as Gapped BLAST 2.0. A break existence "penalty" is set for introducing a single amino acid break into one of the sequences being compared, a break propagation "penalty" is set for each additional empty amino acid position inserted into an already open break. The comparison (comparison) is defined by the amino acid positions of each sequence where the comparison begins and ends, and optionally, based on the insertion of a break or multiple breaks in one or both sequences to obtain the highest possible sum (score). While optimal comparison and scoring can be done manually, the process is facilitated by the use of a computer-built comparison algorithm, for example "gapped" BLAST 2.0, described in Altschul et al., (1997)Nucl. Acids Res.25: 3389-3402, and is publicly available through the National Center for Biotechnology Information (NCBI) website (www.ncbi.nlm.nih.gov'). Optimal comparisons, including multiple comparisons, can be prepared using, for example, PSI-BLAST, available through the NCBI website and described in Altschul et al., (1997) Nucl. Acid. Res. 25:3389-3402. ;Relative to an amino acid sequence that is optimally compared to a reference sequence, the amino acid residue "matches" the position in the reference sequence to which the residue is paired during the comparison. "Position" is determined by the number of consecutive identifications of each amino acid in the reference sequence based on the position relative to the N-terminus. For example, in SEQ ID NO:300 position 1 is M, position 2 is I, position 3 is E, etc. When the test sequence optimally matches SEQ ID NO:300, the residue in the test sequence that matches E at position 3 is said to "match position 3" in SEQ ID NO:300. Due to deletions, insertions, truncations, fusions, etc., which must be taken into account when determining optimal alignment, generally the number of an amino acid residue in the test sequence as determined by simple counting from the N-terminus is not necessarily the same as the number of its corresponding position in the reference sequence. For example, in the case where there is a deletion in the test sequence being compared, there will be no amino acid matching the position in the reference sequence at the site of the deletion. Where there is an insertion in the reference sequence to which it is compared, that insertion will not correspond to any amino acid position in the reference sequence. In the case of truncations or in the case of fusions, there may be sequences of amino acids either in the reference sequence or the one being compared, which do not correspond to any amino acid in the corresponding sequence. ;The term "GAT polypeptide" further refers to any polypeptide comprising an amino acid sequence selected from the group consisting of: (a) an amino acid sequence that is at least 98% identical to SEQ ID NO: 577; (b) an amino acid sequence that is at least 97% identical to SEQ ID NO:578; (c) an amino acid sequence that is at least 97% identical to SEQ ID NO:621; (d) an amino acid sequence that is at least 98% identical to SEQ ID NO:579; (e) an amino acid sequence that is at least 98% identical to SEQ ID NO:602; (f) an amino acid sequence that is at least 95% identical to SEQ ID NO:697; (g) an amino acid sequence that is at least 96% identical to SEQ ID NO:721; (h) an amino acid sequence that is at least 97% identical to SEQ ID NO:613; (i) an amino acid sequence that is at least 89% identical to SEQ ID NO:677; (j) an amino acid sequence that is at least 96% identical to SEQ ID NO:584; (k) an amino acid sequence that is at least 98% identical to SEQ ID NO:707; (1) an amino acid sequence that is at least 98% identical to SEQ ID NO:616; (m) an amino acid sequence that is at least 96% identical to SEQ ID NO:612; and (n) an amino acid sequence that is at least 98%) identical to SEQ ID NO:590. ;The term "GAT polypeptide" further refers to any polypeptide comprising an amino acid sequence having at least 89% sequence identity to residues 1-96 of the amino acid sequence of SEQ ID NO:677; an amino acid sequence having at least 95% sequence identity to residues 1-96 of the amino acid sequence of SEQ ID NO:697; an amino acid sequence having at least 96% sequence identity to residues 1-96 of an amino acid sequence selected from the group consisting of SEQ ID NO:584, 612, 721; an amino acid sequence having at least 97% sequence identity to residues 1-96 of an amino acid sequence selected from the group consisting of SEQ ID NO:578, 613, 621; an amino acid sequence having at least 98% sequence identity to residues 1-96 of an amino acid sequence selected from the group consisting of SEQ ID NO:577, 579, 590, 603, 616 and 707. ;The term "GAT polypeptide" further refers to any polypeptide comprising an amino acid sequence having at least 89% sequence identity to residues 51-146 amino acid sequence of SEQ ID NO:677; an amino acid sequence having at least 95% sequence identity to residues 51-146 of the amino acid sequence of SEQ ID NO:697; an amino acid sequence having at least 96% sequence identity to residues 51-146 of an amino acid sequence selected from the group consisting of SEQ ID NO:584, 612, 721; an amino acid sequence having at least 97% sequence identity to residues 51-146 of an amino acid sequence selected from the group consisting of SEQ ID NO:578, 613, 621; an amino acid sequence having at least 98% sequence identity to residues 51-146 of an amino acid sequence selected from the group consisting of SEQ ID NO:577, 579, 590, 603, 616 and 707. ;The term "GAT polypeptide" further refers to any polypeptide comprising an amino acid sequence selected from the group consisting of: (a) amino acid an acid sequence that is at least 96% identical to residues 2-146 of SEQ ID NO:919; (b) an amino acid sequence that is at least 97% identical to residues 2-146 of SEQ ID NO:929; (c) an amino acid sequence that is at least 98% identical to residues 2-146 of SEQ ID NO:847; (d) an amino acid sequence that is at least 98% identical to residues 2-146 of SEQ ID NO:851; (e) an amino acid sequence that is at least 98% identical to residues 2-146 of SEQ ID NO:853; (f) an amino acid sequence that is at least 98% identical to residues 2-146 of SEQ ID NO:855; (g) an amino acid sequence that is at least 98% identical to residues 2-146 of SEQ ID NO:857; (h) an amino acid sequence that is at least 98% identical to residues 2-146 of SEQ ID NO:861; (i) an amino acid sequence that is at least 98% identical to residues 2-146 of SEQ ID NO:871; (j) an amino acid sequence that is at least 98% identical to residues 2-146 of SEQ ID NO:875; (k) an amino acid sequence that is at least 98% identical to residues 2-146 of SEQ ID NO:881; (1) an amino acid sequence that is at least 98% identical to residues 2-146 of SEQ ID NO:885; (m) an amino acid sequence that is at least 98% identical to residues 2-146 of SEQ ID NO:887; (n) an amino acid sequence that is at least 98% identical to residues 2-146 of SEQ ID NO:889; (o) an amino acid sequence that is at least 98% identical to residues 2-146 of SEQ ID NO:893; (p) an amino acid sequence that is at least 98% identical to residues 2-146 of SEQ ID NO:897; (q) an amino acid sequence that is at least 98% identical to residues 2-146 of SEQ ID NO:899; (r) an amino acid sequence that is at least 98% identical to residues 2-146 of SEQ ID NO:909; (s) an amino acid sequence that is at least 98% identical to residues 2-146 of SEQ ID NO:911; (t) an amino acid sequence that is at least 98% identical to residues 2-146 of SEQ ID NO:837; (u) an amino acid sequence that is at least 99% identical to residues 2-146 of SEQ ID NO:841; (v) an amino acid sequence that is at least 99% identical to residues 2-146 of SEQ ID NO:865; (w) an amino acid sequence that is at least 99% identical to residues 2-146 of SEQ ID NO:869; (x) an amino acid sequence that is at least 99% identical to residues 2-146 of SEQ ID NO:879. ;The term "GAT polypeptide" further refers to any polypeptide comprising an amino acid sequence having at least 95% sequence identity to residues 2-146 of the amino acid sequence of SEQ ID NO:929 and comprising a Gly and an Asn residue at the amino acid position corresponding to position 33 in SEQ ID NO:929. ;The term "GAT polypeptide" further refers to any polypeptide comprising an amino acid sequence having at least 60%, 65%, 70%, 75%, 80%, 881%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more sequence identity to a GAT polypeptide disclosed herein as an example (typical). Therefore, for example, GAT polypeptides of the present invention include polypeptides comprising an amino acid sequence having at least 60%, 65%, 70%, 75%, 80%, 881%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more sequence identity to any of SEQ ID NO:953, 954, 955, 956, 957, 958, 959 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971 and 972. ;As used herein - the term "identity" or "percent identity" - when used in relation to a particular pair of compared amino acid sequences, refers to the percentage amino acid sequence identity obtained by ClustalV/ analysis (version W 1.8 available from the European Bioinformatics Institute, Cambridge, UK), in which the number of identical matches is determined by comparing and dividing such number of identical matches greater than (i) the length of the compared sequences and (ii) 96, and using standard ClustalW parameters to obtain slow/accurate matching of matched pairs - gap open penalty: 10 (Gap Open Penalty); gap extension penalty: 0.10 (Gap Extension Penalty); protein weight matrix: "Gonnet" series; DNA weight matrix: IUB; "Toggle" slow/fast comparisons of matched pairs = SLOW or FULL comparison. ;In another aspect, the invention provides an isolated or recombinant polypeptide comprising at least 20, or alternatively at least 50, at least 75, at least 100, at least 125, at least 130, at least 135, at least 140, at least 141, at least 142, at least 143, at least 144 or at least 145 contiguous amino acids of an amino acid sequence selected from the group consisting of: (a) amino an acid sequence that is at least 98% identical to SEQ ID NO:577; (b) an amino acid sequence that is at least 97% identical to SEQ ID NO:578; (c) an amino acid sequence that is at least 97% identical to SEQ ID NO:621; (d) an amino acid sequence that is at least 98% identical to SEQ ID NO:579; (e) an amino acid sequence that is at least 98% identical to SEQ ID NO:602; (f) an amino acid sequence that is at least 95% identical to SEQ ID NO:697; (g) an amino acid sequence that is at least 96% identical to SEQ ID NO:721; (h) an amino acid sequence that is at least 97% identical to SEQ ID NO:613; (i) an amino acid sequence that is at least 89% identical to SEQ ID NO:677; (j) an amino acid sequence that is at least 96% identical to SEQ ID NO:584; (k) an amino acid sequence that is at least 98% identical to SEQ ID NO:707; (1) an amino acid sequence that is at least 98% identical to SEQ ID NO:616; (m) an amino acid sequence that is at least 96% identical to SEQ ID NO:612; and (n) an amino acid sequence that is at least 98% identical to SEQ ID NO:590. ;In another embodiment, the invention provides a polypeptide comprising residues 2-146 of an amino acid sequence selected from the group consisting of SEQ ID NO: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597, 598, 599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 665, 667, 669, 671, 673, 675, 677, 679, 681, 683, 685, 687, 689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811, 813, 815, 817, 819, 821, 823 and 825. In some embodiments of the invention, the amino acid sequence of the polypeptide comprises Met, Met-Ala, or Met-Ala-Ala at the N-terminal end of an amino acid that corresponds to position 2 of the reference amino acid sequence. ;Some preferred GAT polypeptides of the invention can be optimally compared to a reference amino acid sequence selected from the group consisting of SEQ ID NO:300, 445 and 457 to obtain a similarity score of at least 460 using the BLOSUM62 matrix, a break existence "penalty" of 11 and a break span "penalty" of 1, indicated that at least one of the following positions fits the restrictions that are as follows: (i) there is a Z5 amino acid residue at positions 18 and 38; (ii) there is a Z1 amino acid residue at position 62; (iii) there is a Z6 amino acid residue at position 124; and (vi) at position 144 there is a Z2 amino acid residue, wherein: Z1 is an amino acid residue selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid residue selected from the group consisting of F, W and Y; Z5 is an amino acid residue selected from the group consisting of D and E; Z6 is an amino acid residue selected from the group consisting of C, G and P, and further indicated that the amino acid residues in the amino acid sequence correspond to the following positions, and at least 90% fit the following restrictions: (a) at positions 2, 4, 15, 19, 26, 28, 31, 45, 51, 54, 86, 90, 91, 97, 103, 105, 106, 114, 123, 129, 139 and/or 145 amino acid residue is B1; and (b) at positions 3, 5, 8, 10, 11, 14, 17, 24,27, 32,37,47, 48,49, 52,57,58,61,63,68, 69, 79, 80, 82, 83, 89, 92, 100, 101, 104, 119, 120, 125, 126, 128, 131 and/or 143 amino acid residue is B2; wherein BI is an amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S, and T. When used to designate an amino acid or amino acid residue, the single letter designations A, C, D, E, F, G, H, I, K, L, M, N, P, Q, R, S, T, V, W, and Y have their standard meanings as used in science and as shown in the table herein 1. ;Some preferred GAT polypeptides of the invention can be optimally compared to a reference amino acid sequence selected from the group consisting of SEQ ID NO:300, 445 and 457 to obtain a similarity score of at least 460 using the BLOSUM62 matrix, a break presence "penalty" of 11 and a break spread "penalty" of 1, indicated that at least one of the following positions fits in the following restrictions: (i) on positions 18 and 38 there is a Z5 amino acid residue; (ii) there is a Z1 amino acid residue at position 62; (iii) there is a Z6 amino acid residue at position 124; and (vi) at position 144 there is a Z2 amino acid residue, wherein: Z1 is an amino acid residue selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid residue selected from the group consisting of F, W and Y; Z5 is an amino acid residue selected from the group consisting of D and E; Z6 is an amino acid residue selected from the group consisting of C, G and P, and further indicated that the amino acid residues in the amino acid sequence corresponding to the following positions and at least 80% fit the following restrictions: (a) at positions 2, 4, 15, 19, 26, 28, 51, 54, 86, 90, 91, 97, 103, 105, 106, 114, 129, 139 and/or 145 amino acid residue is Z1; (b) at positions 31 and/or 45 the amino acid residue is Z2; (c) at position 8 the amino acid residue is Z3; (d) at position 89 the amino acid residue is Z3 or Z6; (e) at positions 82, 92, 101 and/or 120 the amino acid residue is Z4; (f) at positions 3, 11, 27 and/or 79 the amino acid residue is Z5; (g) at position 18 the amino acid residue is Z4 or Z5; (h) at position 123 the amino acid residue is Z1 or Z2; (i) at positions 12, 33, 35, 39, 53, 59, 112, 132, 135, 140 and/or 146 the amino acid residue is Z1 or Z3; (j) at position 30 the amino acid residue is Z1; (k) at position 6 the amino acid residue is Z6; (1) at position 81 the amino acid residue is Z2 or Z4; (m) at position 113 the amino acid residue is Z3; (n) at position 138 the amino acid residue is Z4; (o) at position 142 the amino acid residue is Z2; (p) at positions 57 and/or 126 the amino acid residue is Z3 or Z4; (q) at positions 5, 17 and/or 61 the amino acid residue is Z4; (r) at position 24 the amino acid residue is Z3; (s) at position 104 the amino acid residue is Z5; (t) at positions 52 and/or 69 the amino acid residue is Z3; (u) at positions 14 and/or 119 the amino acid residue is Z5; (v) at positions 10, 32, 63 and/or 83 the amino acid residue is Z5; (w) at positions 48 and/or 80 the amino acid residue is Z6; (x) at position 40 the amino acid residue is Z1 or Z2; (y) at position 96 the amino acid residue is Z3 or Z5; (z) at position 65 the amino acid residue is Z3, Z4 or Z6; (aa) at positions 84 and/or 115 the amino acid residue is Z3; (ab) at position 93 the amino acid residue is Z4; (ac) at position 130 the amino acid residue is Z2; (ad) at position 58 the amino acid residue is Z3, Z4 or Z6; (ae) at position 47 the amino acid residue is Z4 or Z6; (af) at positions 49 and/or 100 the amino acid residue is Z3 or Z4; (ag) at position 68 the amino acid residue is Z4 or Z5; (ah) at position 143 the amino acid residue is Z4; (ai) at position 131 the amino acid residue is Z5; (aj) at positions 125 and/or 128 the amino acid residue is Z5; (ak) at position 67 the amino acid residue is Z3 or Z4; (al) at position 60 the amino acid residue is Z5; and (am) at position 37 the amino acid residue is Z4 or Z6; wherein Z1 is an amino acid selected from the group consisting of A, I, L, M, and V; Z 2 is an amino acid selected from the group consisting of F, W and Y; Z3 is an amino acid selected from the group consisting of N, Q, S and T; Z4 is an amino acid selected from the group consisting of R, H and K; Z5 is an amino acid selected from the group consisting of D and E; and Z6 is an amino acid selected from the group consisting of C, G and P. Some preferred GAT polypeptides of the invention further comprise amino acid residues and amino acid sequences corresponding to the positions specified in (a) - (am), indicated that at least 90% fit within the amino acid residue restrictions specified in (a) - (am). ;Some preferred GAT polypeptides of the invention additionally contain amino acid residues in the amino acid sequence corresponding to the following positions, indicated that at least 90% fit the following restrictions: (a) at positions 1, 7, 9, 13, 20, 36, 42, 46, 50, 56, 64, 70, 72, 75, 76, 78, 94, 98, 107, 110, 117, 118, 121 and/or 141 amino acid residues is BI; and (b) at positions 16, 21, 22, 23, 25, 29, 34, 41, 43, 44, 55, 66, 71, 73, 74, 77, 85, 87, 88, 95, 99, 102, 108, 109, 111, 116, 122, 127, 133, 134, 136 and/or 137 amino acid residue is B2; wherein BI is an amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S, and T. ;Some preferred GAT polypeptides of the invention additionally comprise amino acid residues in the amino acid sequence corresponding to the following positions, indicated that at least 90% fit the following restrictions: (a) at positions 1, 7, 9, 13, 20, 42, 46, 50, 56, 64, 70, 72, 75, 76, 78, 94, 98, 107, 110, 117, 118, 121 and/or 141 amino acid residue is BI; and (b) at positions 16, 21, 22, 23, 25, 29, 34, 36, 41, 43, 44, 55, 66, 71, 73, 74, 77, 85, 87, 88, 95, 99, 102, 108, 109, 111, 116, 122, 127, 133, 134, 136 and/or 137 amino acid residue is B2; wherein BI is an amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S and T. ;Some preferred GAT polypeptides of the invention additionally contain amino acid residues in the amino acid sequence corresponding to the following positions, indicated that at least 90% fit the restrictions: (a) at positions 1, 7, 9, 20, 42, 50, 72, 75, 76, 78, 94, 98, 110, 121 and/or 141 amino acid residue is Z1; (b) at positions 13, 46, 56, 70, 107, 117 and/or 118 the amino acid residue is Z2; (c) at positions 23, 55, 71, 77, 88 and/or 109 the amino acid residue is Z3; (d) at positions 16, 21, 41, 73, 85, 99 and/or 111 the amino acid residue is Z4; (e) at positions 34 and/or 95 the amino acid residue is Z5; (f) at positions 22, 25, 29, 43, 44, 66, 74, 87, 102, 108, 116, 122, 127, 133, 134, 136 and/or 137 the amino acid residue is Z6; characterized in that Z1 is an amino acid selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid selected from the group consisting of F, W and Y; Z3 is an amino acid selected from the group consisting of N, Q, S and T; Z4 is an amino acid selected from the group consisting of R, H and K; Z5 is an amino acid selected from the group consisting of D and E; Z6 is an amino acid selected from the group consisting of C, G and P. Certain preferred GAT polypeptides of the invention further comprise an amino acid residue at position 36 selected from the group consisting of Z1 and Z3. Some preferred GAT polypeptides of the invention further comprise an amino acid residue at position 64 selected from the group consisting of Z1 and Z2. Some preferred GAT polypeptides of the invention additionally contain amino acid residues in the amino acid sequence corresponding to the following positions, indicated that at least 80% fit the following restrictions: (a) at position 2 the amino acid residue is I or L; (b) at position 3 the amino acid residue is E; (c) at position 4 the amino acid residue is V or I; (d) at position 5 the amino acid residue is K; (e) at position 6 the amino acid residue is P; (f) at position 8 the amino acid residue is N; (g) at position 10 the amino acid residue is E; (h) at position 11 the amino acid residue is D or E; (i) at position 12 the amino acid residue is T; (j) at position 14 the amino acid residue is E or D; (k) at position 15 the amino acid residue is L; (1) at position 17 the amino acid residue is H; (m) at position 18 the amino acid residue is R, E or K; (n) at position 19 the amino acid residue is I or V; (o) at position 24 the amino acid residue is Q; (p) at position 26 the amino acid residue is M, L, V or I; (q) at position 27 the amino acid residue is E; (r) at position 28 the amino acid residue is A or V; (s) at position 30 the amino acid residue is M; (t) at position 31 the amino acid residue is Y or F; (u) at position 32 the amino acid residue is E or D; (v) at position 33 the amino acid residue is T or S; (w) at position 35 the amino acid residue is L; (x) at position 37 the amino acid residue is R, G, E or Q; (y) at position 39 the amino acid residue is A or S; (z) at position 40 the amino acid residue is F or L; (aa) at position 45 the amino acid residue is Y or F; (ab) at position 47 the amino acid residue is R or G; (ac) at position 48 the amino acid residue is G; (ad) at position 49 the amino acid residue is K, R or Q; (ae) at position 51 the amino acid residue is I or V; (af) at position 52 the amino acid residue is S; (ag) at position 53 the amino acid residue is I or V; (ah) at position 54 the amino acid residue is A; (ai) at position 57 the amino acid residue is H or N; (aj) at position 58 the amino acid residue is Q, K, R or P; (ak) at position 59 the amino acid residue is A; (al) at position 60 the amino acid residue is E; (am) at position 61 the amino acid residue is H or R; (an) at position 63 the amino acid residue is E or D; (ao) at position 65 the amino acid residue is E, P or Q; (ap) at position 67 the amino acid residue is Q or R; (aq) at position 68 the amino acid residue is K or E; (ar) at position 69 the amino acid residue is Q; (as) at position 79 the amino acid residue is E; (at) at position 80 the amino acid residue is G; (au) at position 81 the amino acid residue is Y, H or F; (av) at position 82 the amino acid residue is R; (aw) at position 83 the amino acid residue is E or D; (ax) at position 84 the amino acid residue is Q; (ay) at position 86 the amino acid residue is A; (az) at position 89 the amino acid residue is G, T or S; (ba) at position 90 the amino acid residue is L; (bb) at position 91 the amino acid residue is L, I or V; (bc) at position 92 the amino acid residue is R or K; (bd) at position 93 the amino acid residue is H; (be) at position 96 the amino acid residue is E or Q; (bf) at position 97 the amino acid residue is I; (bg) at position 100 the amino acid residue is K or N; (bh) at position 101 the amino acid residue is K or R; (bi) at position 103 the amino acid residue is A or V; (bj) at position 104 the amino acid residue is D; (bk) at position 105 the amino acid residue is M, L or I; (bi) at position 106 the amino acid residue is L; (bm) at position 112 the amino acid residue is T or A; (bn) at position 113 the amino acid residue is S or T; (bo) at position 114 the amino acid residue is A; (bp) at position 115 the amino acid residue is S; (bq) at position 119 the amino acid residue is K or R; (br) at position 120 the amino acid residue is K or R; (bs) at position 123 the amino acid residue is F or L; (bt) at position 125 the amino acid residue is E; (bu) at position 126 the amino acid residue is Q or H; (bv) at position 128 the amino acid residue is E or D; (bw) at position 129 the amino acid residue is V or I; (bx) at position 130 the amino acid residue is F; (by) at position 131 the amino acid residue is D or E; (bz) at position 132 the amino acid residue is T; (ca) at position 135 the amino acid residue is V; (cb) at position 138 the amino acid residue is H; (cc) at position 139 the amino acid residue is I; (cd) at position 140 the amino acid residue is L or M; (ce) at position 142 the amino acid residue is Y; (cf) at position 143 the amino acid residue is K or R; (cg) at position 145 the amino acid residue is L or I; and (ch) at position 146 the amino acid residue is T. Certain preferred GAT polypeptides of the invention further comprise amino acid residues in the amino acid sequence corresponding to the positions specified in (a) - (ch) above, indicated that at least 90% fit within the amino acid residue restrictions specified in (a) - (ch). ;Some preferred GAT polypeptides of the invention can be optimally compared to a reference amino acid sequence selected from the group consisting of SEQ ID NO: 300, 445 and 457 to obtain a similarity score of at least 460 using the BLOSUM62 matrix, a break presence "penalty" of 11 and a break span "penalty" of 1, indicated that at least one of the following positions fits the restrictions which follow: (i) there is a Z5 amino acid residue at positions 18 and 38; (ii) there is a Z1 amino acid residue at position 62; (iii) there is a Z6 amino acid residue at position 124; and (vi) at position 144 there is a Z2 amino acid residue, wherein Z1 is an amino acid residue selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid residue selected from the group consisting of F, W and Y; Z5 is an amino acid residue selected from the group consisting of D and E; and Z6 is an amino acid residue selected from the group consisting of C, G and P, and further indicated that the amino acid residues in the amino acid sequence correspond to the following positions, and at least 80% fit the following restrictions: (a) at positions 9, 76, 94 and 110 the amino acid residue is A; (b) at positions 29 and 108 the amino acid residue is C; (c) at position 34 the amino acid residue is D; (d) at position 95 the amino acid residue is E; (e) at position 56 the amino acid residue is F; (f) at positions 43, 44, 66, 74, 87, 102, 116, 122, 127 and 136 the amino acid residue is G; (g) at position 41 the amino acid residue is H; (h) at position 7 the amino acid residue is I; (i) at position 85 the amino acid residue is K; (j) at positions 20, 42, 50, 78 and 121 the amino acid residue is L; (k) at position 1 and 141 the amino acid residue is M; (1) at position 23 and 109 the amino acid residue is N; (m) at positions 22, 25, 133, 134 and 137 the amino acid residue is P; (n) at position 71 the amino acid residue is Q; (o) at positions 16, 21, 73, 99 and 111 the amino acid residue is R; (p) at position 55 the amino acid residue is S; (q) at position 77 the amino acid residue is T; (r) at position 107 the amino acid residue is W; (s) at positions 13, 46, 70 and 118 the amino acid residue is Y. Some preferred GAT polypeptides of the invention further comprise amino acid sequences, wherein the amino acid residues satisfy at least one of the following restrictions: (a) at position 36 the amino acid residue is M, L or T; (b) at position 72 the amino acid residue is L or I; (c) at position 75 the amino acid residue is M or V; (d) at position 64 the amino acid residue is L, I or F; (e) at position 88 the amino acid residue is T or F; and (f) at position 117 the amino acid residue is Y or F. Certain preferred GAT polypeptides of the invention further comprise an amino acid sequence wherein the amino acid residues satisfy at least one of the following additional restrictions: (a) at position 14 the amino acid residue is D; (b) at position 18 the amino acid residue is E; (c) at position 26 the amino acid residue is M or V; (e) at position 30 the amino acid residue is I; (f) at position 32 the amino acid residue is D; (g) at position 36 the amino acid residue is M or T; (h) at position 37 the amino acid residue is C; (i) at position 38 the amino acid residue is D; (j) at position 53 the amino acid residue is V; (k) at position 58 the amino acid residue is R; (1) at position 61 the amino acid residue is R; (m) at position 62 the amino acid residue is L; (n) at position 64 the amino acid residue is I or F; (o) at position 65 the amino acid residue is P; (p) at position 72 the amino acid residue is I; (q) at position 75 the amino acid residue is V; (r) at position 88 the amino acid residue is T; (s) at position 89 the amino acid residue is G; (t) at position 91 the amino acid residue is L; (u) at position 98 the amino acid residue is 1; (v) at position 105 the amino acid residue is I; (w) at position 112 the amino acid residue is A; (x) at position 124 the amino acid residue is G or C; (y) at position 128 the amino acid residue is D; (z) at position 140 the amino acid residue is M; (aa) at position 143 the amino acid residue is R; and (ab) at position 144 the amino acid residue is W. Some preferred GAT polypeptides of the invention contain an amino acid sequence, characterized in that the amino acid residues corresponding to the positions specified in (a) to (ab), as described above in the text - at least 80% fit within the amino acid residue restrictions specified in (a) to (ab). Certain preferred GAT polypeptides of the invention have an amino acid sequence comprising amino acid residues at least one of which satisfies the following additional restrictions: (a) at position 41 the amino acid residue is H; (b) at position 138 the amino acid residue is H; (c) at position 34 the amino acid residue is N; and (d) at position 55 the amino acid residue is ;S. ;Some preferred GAT polypeptides of the invention further comprise an amino acid sequence selected from the group consisting of: (a) an amino acid sequence that is at least 98% identical to SEQ ID NO:577; (b) an amino acid sequence that is at least 97% identical to SEQ ID NO:578; (c) an amino acid sequence that is at least 97% identical to SEQ ID NO:621; (d) an amino acid sequence that is at least 98% identical to SEQ ID NO:579; (e) an amino acid sequence that is at least 98% identical to SEQ ID NO:602; (f) an amino acid sequence that is at least 95% identical to SEQ ID NO:697; (g) an amino acid sequence that is at least 96% identical to SEQ ID NO:721; (h) an amino acid sequence that is at least 97% identical to SEQ ID NO:613; (i) an amino acid sequence that is at least 89% identical to SEQ ID NO:677; (j) an amino acid sequence that is at least 96% identical to SEQ ID NO:584; (k) an amino acid sequence that is at least 98% identical to SEQ ID NO:707; (1) an amino acid sequence that is at least 98% identical to SEQ ID NO:616; (m) an amino acid sequence that is at least 96% identical to SEQ ID NO:612; and (n) an amino acid sequence that is at least 98% identical to SEQ ID NO:590. ;Some preferred GAT polypeptides of the invention further comprise an amino acid sequence selected from the group consisting of: (a) an amino acid sequence that is at least 98% identical to SEQ ID NO:577; (b) an amino acid sequence that is at least 97% identical to SEQ ID NO:578; (c) an amino acid sequence that is at least 97% identical to SEQ ID NO:621; (d) an amino acid sequence that is at least 98% identical to SEQ ID NO:579; (e) an amino acid sequence that is at least 98% identical to SEQ ID NO:602; (f) an amino acid sequence that is at least 95% identical to SEQ ID NO:697; (g) an amino acid sequence that is at least 96% identical to SEQ ID NO:721; (h) an amino acid sequence that is at least 97% identical to SEQ ID NO:613; (i) an amino acid sequence that is at least 89% identical to SEQ ID NO:677; (j) an amino acid sequence that is at least 96% identical to SEQ ID NO:584; (k) an amino acid sequence that is at least 98% identical to SEQ ID NO:707; (1) an amino acid sequence that is at least 98% identical to SEQ ID NO:616; (m) an amino acid sequence that is at least 96% identical to SEQ ID NO:612; and (n) an amino acid sequence that is at least 98% identical to SEQ ID NO:590, wherein at least one of the following positions further fits the following restrictions: (i) at positions 18 and 38, a Z5 amino acid residue; (ii) at position 62, a Z1 amino acid residue; (iii) at position 124, a Z6 amino acid residue; and (Iv) at position 144, a Z2 amino acid residue, wherein Z1 is an amino acid residue selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid residue selected from the group consisting of F, W and Y; Z5 is an amino acid residue selected from the group consisting of D and E; Z6 is an amino acid residue selected from the group consisting of C, G and P. Certain preferred GAT polypeptides of the invention comprise an amino acid sequence selected from the group consisting of: (a) an amino acid sequence that is at least 98% identical to SEQ ID NO:577; (b) an amino acid sequence that is at least 97% identical to SEQ ID NO:578; (c) an amino acid sequence that is at least 97% identical to SEQ ID NO:621; (d) an amino acid sequence that is at least 98% identical to SEQ ID NO:579; (e) an amino acid sequence that is at least 98% identical to SEQ ID NO:602; (f) an amino acid sequence that is at least 95% identical to SEQ ID NO:697; (g) an amino acid sequence that is at least 96% identical to SEQ ID NO:721; (h) an amino acid sequence that is at least 97% identical to SEQ ID NO:613; (i) an amino acid sequence that is at least 89% identical to SEQ ID NO:677; (j) an amino acid sequence that is at least 96% identical to SEQ ID NO:584; (k) an amino acid sequence that is at least 98% identical to SEQ ID NO:707; (1) an amino acid sequence that is at least 98% identical to SEQ ID NO:616; (m) an amino acid sequence that is at least 96% identical to SEQ ID NO:612; and (n) an amino acid sequence that is at least 98% identical to SEQ ID NO:590, indicated that the amino acid residues in the amino acid sequence corresponding to the following positions are at least 90% compatible with the following additional restrictions: (a) at positions 2, 4, 15, 19, 26, 28, 31, 45, 51, 54, 86, 90, 91, 97, 103, 105, 106, 114, 129, 139 and/or 145 amino acid residue is BI; and (b) at positions 3, 5, 8, 10, 11, 14, 17, 24, 27, 32, 37, 47, 48, 49, 52, 57, 58, 61, 63, 68, 69, 79, 80, 82, 83, 89, 92, 100, 101, 104, 119, 120, 125, 126, 128, 131 and/or 143 amino acid residue is B2; wherein BI is an amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S and T. Certain preferred GAT polypeptides of the invention comprise an amino acid sequence selected from the group consisting of: (a) an amino acid sequence that is at least 98% identical to SEQ ID NO:577; (b) an amino acid sequence that is at least 97% identical to SEQ ID NO:578; (c) an amino acid sequence that is at least 97% identical to SEQ ID NO:621; (d) an amino acid sequence that is at least 98% identical to SEQ ID NO:579; (e) an amino acid sequence that is at least 98%> identical to SEQ ID NO:602; (f) an amino acid sequence that is at least 95% identical to SEQ ID NO:697; (g) an amino acid sequence that is at least 96% identical to SEQ ID NO:721; (h) an amino acid sequence that is at least 97% identical to SEQ ID NO:613; (i) an amino acid sequence that is at least 89% identical to SEQ ID NO:677; (j) an amino acid sequence that is at least 96% identical to SEQ ID NO:584; (k) an amino acid sequence that is at least 98% identical to SEQ ID NO:707; (1) an amino acid sequence that is at least 98%> identical to SEQ ID NO:616; (m) an amino acid sequence that is at least 96% identical to SEQ ID NO:612; and (n) an amino acid sequence that is at least 98% identical to SEQ ID NO:590; indicated that the amino acid residues in the amino acid sequence corresponding to the following positions are at least 80% compatible with the following additional restrictions: (a) at positions 2, 4, 15, 19, 26, 28, 51, 54, 86, 90, 91, 97, 103, 105, 106, 114, 129, 139 and/or the 145 amino acid residue is Z1; (b) at positions 31 and/or 45 the amino acid residue is Z2; (c) at position 8 the amino acid residue is Z3; (d) at position 89 the amino acid residue is Z3 or Z6; (e) at positions 82, 92, 101 and/or 120 the amino acid residue is Z4; (f) at positions 3, 11, 27 and/or 79 the amino acid residue is Z5; (g) at position 18 the amino acid residue is Z4 or Z5; (h) at position 123 the amino acid residue is Z1 or Z2; (i) at positions 12, 33, 35, 39, 53, 59, 112, 132, 135, 140 and/or 146 the amino acid residue is Z1 or Z3; (j) at position 30 the amino acid residue is Z1; (k) at position 6 the amino acid residue is Z6; (1) at position 81 the amino acid residue is Z2 or Z4; (m) at position 113 the amino acid residue is Z3; (n) at position 138 the amino acid residue is Z4; (o) at position 142 the amino acid residue is Z2; (p) at positions 57 and/or 126 the amino acid residue is Z3 or Z4; (q) at positions 5, 17 and/or 61 the amino acid residue is Z4; (r) at position 24 the amino acid residue is Z3; (s) at position 104 the amino acid residue is Z5; (t) at positions 52 and/or 69 the amino acid residue is Z3; (u) at positions 14 and/or 119 the amino acid residue is Z5; (v) at positions 10, 32, 63 and/or 83 the amino acid residue is Z5; (w) at positions 48 and/or 80 the amino acid residue is Z6; (x) at position 40 the amino acid residue is Z1 or Z2; (y) at position 96 the amino acid residue is Z3 or Z5; (z) at position 65 the amino acid residue is Z3, Z4 or Z6; (aa) at positions 84 and/or 115 the amino acid residue is Z3; (ab) at position 93 the amino acid residue is Z4; (ac) at position 130 the amino acid residue is Z2; (ad) at position 58 the amino acid residue is Z3, Z4 or Z6; (ae) at position 47 the amino acid residue is Z4 or Z6; (af) at positions 49 and/or 100 the amino acid residue is Z3 or Z4; (ag) at position 68 the amino acid residue is Z4 or Z5; (ah) at position 143 the amino acid residue is Z4; (ai) at position 131 the amino acid residue is Z5; (aj) at positions 125 and/or 128 the amino acid residue is Z5; (ak) at position 67 the amino acid residue is Z3 or Z4; (al) at position 60 the amino acid residue is Z5; and (am) at position 37 the amino acid residue is Z4 or Z6; characterized in that Z1 is an amino acid selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid selected from the group consisting of F, W and Y; Z3 is an amino acid selected from the group consisting of N, Q, S and T; Z4 is an amino acid selected from the group consisting of R, H and K; Z5 is an amino acid selected from the group consisting of D and E; Z6 is an amino acid selected from the group consisting of C, G and P. Certain preferred GAT polypeptides of the invention further comprise amino acid residues in the amino acid sequence corresponding to the positions specified in (a) - (am), indicated that at least 90% fit within the amino acid residue restrictions specified in (a) - (am). ;Some preferred GAT polypeptides of the invention further comprise amino acid residues in the amino acid sequence corresponding to the following positions, indicated that at least 90% fit the following additional restrictions: (a) at positions 1, 7, 9, 13, 20, 36, 42, 46, 50, 56, 64, 70, 72, 75, 76, 78, 94, 98, 107, 110, 117, 118, 121 and/or 141 amino acid residues is BI; and (b) at positions 16, 21, 22, 23, 25, 29, 34, 41, 43, 44, 55, 66, 71, 73, 74, 77, 85, 87, 88, 95, 99, 102, 108, 109, 111, 116, 122, 127, 133, 134, 136 and/or 137 amino acid residue is B2; wherein BI is an amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, ;D, C, Q, E, G, H, K, P, S and T. ;Some preferred GAT polypeptides of the invention comprise amino acid residues in the amino acid sequence corresponding to the following positions, indicated that at least 90% fit the following additional restrictions: (a) at positions 1, 7, 9, 13, 20, 42, 46, 50, 56, 64, 70, 72, 75, 76, 78, 94, 98, 107, 110, 117, 118, 121 and/or 141 amino acid residue is BI; and (b) at positions 16, 21, 22, 23, 25, 29, 34, 36, 41, 43, 44, 55, 66, 71, 73, 74, 77, 85, 87, 88, 95, 99, 102, 108, 109, 111, 116, 122, 127, 133, 134, 136 and/or 137 amino acid residue is B2; indicated that BI is an amino acid selected from the group consisting of A, I, L, ;M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, ;E, G, H, K, P, S and T. ;Some preferred GAT polypeptides of the invention comprise amino acid residues in the amino acid sequence corresponding to the following positions, indicated that at least 90% fit the following additional restrictions: (a) at positions 1, 7, 9, 20, 42, 50, 72, 75, 76, 78, 94, 98, 110, 121 and/or 141 amino acid residue is Z1; (b) at positions 13, 46, 56, 70, 107, 117 and/or 118 the amino acid residue is Z2; (c) at positions 23, 55, 71, 77, 88 and/or 109 the amino acid residue is Z3; (d) at positions 16, 21, 41, 73, 85, 99 and/or 111 the amino acid residue is Z4; (e) at positions 34 and/or 95 the amino acid residue is Z5; (f) at positions 22, 25, 29, 43, 44, 66, 74, 87, 102, 108, 116, 122, 127, 133, 134, 136 and/or 137 the amino acid residue is Z6; characterized in that Z1 is an amino acid selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid selected from the group consisting of F, W and Y; Z3 is an amino acid selected from the group consisting of N, Q, S and T; Z4 is an amino acid selected from the group consisting of R, H and K; Z5 is an amino acid selected from the group consisting of D and E; Z6 is an amino acid selected from the group consisting of C, G and P. Certain preferred GAT polypeptides of the invention further comprise an amino acid sequence wherein the amino acid residue at position 36 is selected from the group consisting of Z1 and Z3. Some preferred GAT polypeptides of the invention further comprise an amino acid sequence wherein the amino acid residue at position 64 is selected from the group consisting of Z1 and Z2. Some preferred GAT polypeptides of the invention comprise an amino acid sequence wherein the amino acid residues corresponding to the following positions are at least 80% compatible with the following additional restrictions: (a) at position 2 the amino acid residue is I or L; (b) at position 3 the amino acid residue is E; (c) at position 4 the amino acid residue is V or I; (d) at position 5 the amino acid residue is K; (e) at position 6 the amino acid residue is P; (f) at position 8 the amino acid residue is N; (g) at position 10 the amino acid residue is E; (h) at position 11 the amino acid residue is D or E; (i) at position 12 the amino acid residue is T; (j) at position 14 the amino acid residue is E or D; (k) at position 15 the amino acid residue is L; (1) at position 17 the amino acid residue is H; (m) at position 18 the amino acid residue is R, E or K; (n) at position 19 the amino acid residue is I or V; (o) at position 24 the amino acid residue is Q; (p) at position 26 the amino acid residue is M, L, V, or I; (q) at position 27 the amino acid residue is E; (r) at position 28 the amino acid residue is A or V; (s) at position 30 the amino acid residue is M; (t) at position 31 the amino acid residue is Y or F; (u) at position 32 the amino acid residue is E or D; (v) at position 33 the amino acid residue is T or S; (w) at position 35 the amino acid residue is L; (x) at position 37 the amino acid residue is R, G, E or Q; (y) at position 39 the amino acid residue is A or S; (z) at position 40 the amino acid residue is F or L; (aa) at position 45 the amino acid residue is Y or F; (ab) at position 47 the amino acid residue is R or G; (ac) at position 48 the amino acid residue is G; (ad) at position 49 the amino acid residue is K, R or Q; (ae) at position 51 the amino acid residue is I or V; (af) at position 52 the amino acid residue is S; (ag) at position 53 the amino acid residue is I or V; (ah) at position 54 the amino acid residue is A; (ai) at position 57 the amino acid residue is H or N; (aj) at position 58 the amino acid residue is Q, K, R or P; (ak) at position 59 the amino acid residue is A; (al) at position 60 the amino acid residue is E; (am) at position 61 the amino acid residue is H or R; (an) at position 63 the amino acid residue is E or D; (ao) at position 65 the amino acid residue is E, P or Q; (ap) at position 67 the amino acid residue is Q or R; (aq) at position 68 the amino acid residue is K or E; (ar) at position 69 the amino acid residue is Q; (as) at position 79 the amino acid residue is E; (at) at position 80 the amino acid residue is G; (au) at position 81 the amino acid residue is Y, H or F; (av) at position 82 the amino acid residue is R; (aw) at position 83 the amino acid residue is E or D; (ax) at position 84 the amino acid residue is Q; (ay) at position 86 the amino acid residue is A; (az) at position 89 the amino acid residue is G, T or S; (ba) at position 90 the amino acid residue is L; (bb) at position 91 the amino acid residue is L, I or V; (bc) at position 92 the amino acid residue is R or K; (bd) at position 93 the amino acid residue is H; (be) at position 96 the amino acid residue is E or Q; (bf) at position 97 the amino acid residue is I; (bg) at position 100 the amino acid residue is K or N; (bh) at position 101 the amino acid residue is K or R; (bi) at position 103 the amino acid residue is A or V; (bj) at position 104 the amino acid residue is D; (bk) at position 105 the amino acid residue is M, L or I; (bi) at position 106 the amino acid residue is L; (bm) at position 112 the amino acid residue is T or A; (bn) at position 113 the amino acid residue is S or T; (bo) at position 114 the amino acid residue is A; (bp) at position 115 the amino acid residue is S; (bq) at position 119 the amino acid residue is K or R; (br) at position 120 the amino acid residue is K or R; (bs) at position 123 the amino acid residue is F or L; (bt) at position 125 the amino acid residue is E; (bu) at position 126 the amino acid residue is Q or H; (bv) at position 128 the amino acid residue is E or D; (bw) at position 129 the amino acid residue is V or I; (bx) at position 130 the amino acid residue is F; (by) at position 131 the amino acid residue is D or E; (bz) at position 132 amino acid residues T; (ca) at position 135 amino acid residues V; (cb) at position 138 amino acid residues H; (cc) at position 139 amino acid residues I; (cd) at position 140 amino acid residues L or M; (ce) at position 142 amino acid residues Y; (cf) at position 143 amino acid residues K or R; (cg) at position 145 amino acid residues L or I; and (ch) at position 146 amino acid residues T. Some preferred GAT polypeptides of the invention comprise an amino acid sequence in which the residues corresponding to the positions specified in (a) - (ch) in the text above fit at least 90% within the amino acid residue restrictions specified in (a) - (ch). ;Some preferred GAT polypeptides of the invention comprise an amino acid sequence selected from the group consisting of: (a) an amino acid sequence that is at least 98% identical to SEQ ID NO:577; (b) an amino acid sequence that is at least 97% identical to SEQ ID NO:578; (c) an amino acid sequence that is at least 97% identical to SEQ ID NO:621; (d) an amino acid sequence that is at least 98% identical to SEQ ID NO:579; (e) an amino acid sequence that is at least 98% identical to SEQ ID NO:602; (f) an amino acid sequence that is at least 95% identical to SEQ ID NO:697; (g) an amino acid sequence that is at least 96% identical to SEQ ID NO:721; (h) an amino acid sequence that is at least 97% identical to SEQ ID NO:613; (i) an amino acid sequence that is at least 89% identical to SEQ ID NO:677; (j) an amino acid sequence that is at least 96% identical to SEQ ID NO:584; (k) an amino acid sequence that is at least 98% identical to SEQ ID NO:707; (1) an amino acid sequence that is at least 98% identical to SEQ ID NO:616; (m) an amino acid sequence that is at least 96% identical to SEQ ID NO:612; and (n) an amino acid sequence that is at least 98% identical to SEQ ID NO:590, further indicated that of the amino acid residues in the amino acid sequence corresponding to the following positions, at least 80% fit the following restrictions: (a) at positions 9, 76, 94 and 110 amino acid residues A; (b) at positions 29 and 108 amino acid residues C; (c) at position 34 amino acid residues D; (d) at position 95 amino acid residues E; (e) at position 56 amino acid residues F; (f) at positions 43, 44, 66, 74, 87, 102, 116, 122, 127 and 136 amino acid residues G; (g) at position 41 amino acid residues H; (h) at position 7 amino acid residues I; (i) at position 85 amino acid residues K; (j) at position 20, 42, 50, 78 and 121 amino acid residues L; (k) at position 1 and 141 the amino acid residue is M; (1) at position 23 and 109 the amino acid residue is N; (m) at positions 22, 25, 133, 134 and 137 amino acid residues P; (n) at position 71 amino acid residues Q; (o) at positions 16, 21, 73, 99 and 111 amino acid residues R; (p) at position 55 amino acid residues S; (q) at position 77 amino acid residues T; (r) at position 107 amino acid residues W; (s) at positions 13, 46, 70 and 118 the amino acid residues are Y. Certain preferred GAT polypeptides of the invention further comprise an amino acid sequence in which at least one of the following criteria is met: (a) at position 14 the amino acid residue is D; (b) at position 18 the amino acid residue is E; (c) at position 26 amino acid residues M or V; (e) at position 30 amino acid residues I; (f) at position 32 the amino acid residue is D; (g) at position 36 the amino acid residue is M or T; (h) at position 37 amino acid residues C; (i) at position 38 amino acid residues D; (j) at position 53 amino acid residues V; (k) at position 58 amino acid residues R; (1) at position 61 amino acid residues R; (m) at position 62 amino acid residues L; (n) at position 64 amino acid residues I or F; (o) at position 65 the amino acid residue is P; (p) at position 72 amino acid residues I; (q) at position 75 the amino acid residue is V; (r) at position 88 the amino acid residue is T; (s) at position 89 the amino acid residue is G; (t) at position 91 the amino acid residue is L; (u) at position 98 amino acid residues I; (v) at position 105 amino acid residues I; (w) at position 112 the amino acid residue is A; (x) at position 124 amino acid residues G or C; (y) at position 128 amino acid residues D; (z) at position 140 amino acid residues M; (aa) at position 143 the amino acid residue is R; (ab) at position 144 amino acid residues W. Some preferred GAT polypeptides of the invention further contain an amino acid sequence characterized in that the amino acid residues corresponding to the positions specified in (a) to (ab), as described above in the text - at least 80% fit within the restrictions of the amino acid residues specified in (a) to (ab). Certain preferred GAT polypeptides of the invention further comprise an amino acid sequence wherein the following conditions are also met: (a) at position 41 the amino acid residue is H; (b) at position 138 the amino acid residue is H; (c) at position 34 amino acid residues N; and (f) at position 55 amino acid residues S. ;Some preferred GAT polypeptides of the invention when optimally matched to a reference amino acid sequence selected from the group consisting of SEQ ID NOs: 300, 445 and 457 to obtain a similarity score of at least 460 using the BLOSUM62 matrix, a break presence penalty of 11 and a break spread penalty of 1, have amino acid sequences such that one or more of the following positions satisfy the following restrictions: (i) at positions 18 and 38, there is a Z5 amino acid residue; (ii) at position 62, there is a Z1 amino acid residue; (iii) at position 124, there is a Z6 amino acid residue; and (iv) at position 144, there is a Z2 amino acid residue, characterized in that: a Z1 amino acid residue selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid residue selected from the group consisting of F, W and Y; Z5 is an amino acid residue selected from the group consisting of D and E; Z6 is an amino acid residue selected from the group consisting of C, G, and P. In the ordered GAT polypeptides mentioned in the preceding section, the amino acid residue in the polypeptide corresponding to position 28 is V, I, or A. Valine or isoleucine at position 28 generally correlates with reduced KM, while alanine at that position generally correlates with increased kcat. Threonine at position 89 and arginine at position 58 generally correlate with reduced Km. Other GAT polypeptides are characterized by having 127 (ie, I at position 27), M30, D34, S35, R37, S39, H41, G48, K49, N57, Q58, P62, T62, Q65, Q67, K68, V75, E83, S89, A96, E96, R101, TI 12, A114, Kl 19, K120, E128, V129, D131, T131, V132, V134, V135, H138, R144,1145 or T146 or any combination thereof. ;Some preferred GAT polypeptides of the invention comprise an amino acid sequence selected from the group consisting of SEQ ID NO: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597, 598, 599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 665, 667, 669, 671, 673, 675, 677, 679, 681, 683, 685, 687, 689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811, 813, 815, 817, 819, 821, 823 and 825. ;In another aspect, the invention provides an isolated or recombinant polypeptide comprising at least 20, or alternatively, at least 50, 75, at least 100, at least 125, at least 130, at least 135, at least 140, at least 141, at least 142, at least 143, at least 144, or at least 145 contiguous amino acids of an amino acid sequence selected from the group consisting of: (a) an amino acid sequence that is at least 96% identical to SEQ ID NO:919 (such as SEQ ID NO:919 NO: 917, 919, 921, 923, 925, 927, 833, 835, 839, 843, 845, 859, 863, 873, 877, 891, 895, 901, 905, 907, 913, 915 or 950); (b) an amino acid sequence that is at least 97% identical to SEQ ID NO:929 (such as SEQ ID NO: 929, 931, 835, 843, 849 or 867); (c) an amino acid sequence that is at least 98% identical to SEQ ID NO:847 (such as SEQ ID NO: 845 or 847); (d) an amino acid sequence that is at least 98% identical to SEQ ID NO:851; (e) an amino acid sequence that is at least 98% identical to SEQ ID NO:853; (f) an amino acid sequence that is at least 98% identical to SEQ ID NO:855 (such as SEQ ID NO: 835 or 855); (g) an amino acid sequence that is at least 98% identical to SEQ ID NO:857; (h) an amino acid sequence that is at least 98% identical to SEQ ID NO:861 (such as SEQ ID NO: 839, 861 or 883); (i) an amino acid sequence that is at least 98% identical to SEQ ID NO:871; (j) an amino acid sequence that is at least 98% identical to SEQ ID NO:875; (k) an amino acid sequence that is at least 98% identical to SEQ ID NO:881; ;(1) an amino acid sequence that is at least 98% identical to SEQ ID NO:885 (such as SEQ ID NO: 845 or 885); (m) an amino acid sequence that is at least 98% identical to SEQ ID NO:887; (n) an amino acid sequence that is at least 98%> identical to SEQ ID NO:889 (such as SEQ ID NO: 863, 889, 891 or 903); (o) an amino acid sequence that is at least 98% identical to SEQ ID NO:893; (p) an amino acid sequence that is at least 98% identical to SEQ ID NO:897; (q) an amino acid sequence that is at least 98%> identical to SEQ ID NO:899; (r) an amino acid sequence that is at least 98% identical to SEQ ID NO:909 (such as SEQ ID NO: 883 or 909); (s) an amino acid sequence that is at least 98% identical to SEQ ID NO:911; (t) an amino acid sequence that is at least 99% identical to SEQ ID NO: 837; (u) an amino acid sequence that is at least 99% identical to SEQ ID NO:841; (v) an amino acid sequence that is at least 99% identical to SEQ ID NO:865; (w) an amino acid sequence that is at least 99% identical to SEQ ID NO:869; (x) an amino acid sequence that is at least 99% identical to SEQ ID NO:879. In another aspect, the invention provides an isolated or recombinant polypeptide comprising at least 20 or alternatively at least 50, at least 75, at least 100, at least 125, at least 130, at least 135, at least 140, at least 141, at least 142, at least 143, at least 144 or at least 145 contiguous amino acids of an amino acid sequence that is at least 95% identical to SEQ ID NO: 929 and comprising Gly or Asn at an amino acid position corresponding to position 33 in SEQ ID NO: 929 (such as SEQ ID NO: 837, 849, 893, 897, 905, 921, 927, 929, or 931. In another embodiment, the invention provides a polypeptide comprising amino acid residues 2-146 acid sequences selected from the group consisting of of SEQ ID NO: 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905,907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 929, 931, 953, 954, 955, 956, 957, 958, 959, 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971 and 972. In some embodiments of the invention amino the polypeptide acid sequence contains Met, Met-Ala, or Met-Ala-Ala at the N-terminal end of the amino acid corresponding to position 2 of the reference amino acid sequence. ;Some preferred GAT polypeptides of the invention comprise an amino acid sequence selected from the group consisting of SEQ ID NO: 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905,907, 909, 911, 913, 915, 917, 919,921, 923, 925,927, 929, 931,946, 948 and 950. The invention further provides preferred GAT polypeptides characterized by a combination of the aforementioned restriction for positions of amino acid residues. Additionally, the invention provides GAT polynucleotides encoding the preferred GAT polypeptides described above, and their complementary nucleotide sequences. Certain aspects of the invention particularly relate to a subset of any of the above-described categories of GAT polypeptides that possess GAT activity, as described herein. These GAT polypeptides are desirable, for example for use as agents for conferring resistance to glyphosate when found in a plant. Examples of desired levels of GAT activity are described herein. ;In one embodiment, GAT polypeptides comprise an amino acid sequence encoded by recombinant or isolated forms of naturally occurring nucleic acids isolated from a natural source, for example, a bacterial strain. Wild-type polynucleotides encoding such GAT polypeptides can be specifically screened by standard techniques known in the art. Polypeptides defined by SEQ ID NO: 6-10 for example, were discovered by expression cloning of sequences from Baccilus strains exhibiting GAT activity, as described in more detail in the text that follows. ;The invention also includes isolated or recombinant polypeptides encoded by an isolated or recombinant polynucleotide comprising a nucleotide sequence that hybridizes under strict (stringend) conditions with almost the entire length of a nucleotide sequence selected from the group consisting of SEQ ID NO: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 534, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 620, 622, 624, 626, 628, 630, 632, 634, 636, 638, 640, 642, 644, 646, 648, 650, 652, 654, 656, 658, 660, 662, 664, 666, 668, 670, 672, 674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726, 728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788, 790, 792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814, 816, 818, 820, 822 and 824, their complements and nucleotide sequences encoding an amino acid sequence selected from the group consisting of SEQ ID NO: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597, 598, 599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 665, 667, 669, 671, 673, 675, 677, 679, 681, 683, 685, 687, 689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811, 813, 815, 817, 819, 821, 823 and 825, including their complements. The invention also includes isolated or recombinant polypeptides encoded by an isolated or recombinant polynucleotide comprising a nucleotide sequence that hybridizes under stringency conditions with nearly full length nucleotide sequence selected from the group consisting of SEQ ID NO: 32, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916, 918, 920, 922, 924, 926, 928 and 930, their complements and nucleotide sequences encoding an amino acid sequence selected from the group consisting of SEQ ID NO: 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 929, 931, 953, 954, 955, 956, 957, 958, 959, 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971 and 972. The invention further includes any polypeptide possessing GAT activity that is encoded by a fragment of any GAT-encoding polynucleotide described herein. The present invention also provides GAT polypeptide fragments that can be spliced together to form a functional GAT polypeptide. Primary processing splicing can be performed in vitro or in vivo, and can include cis- and trans-primary processing of the transcript (that is, intramolecular or intermolecular primary processing of the transcript). The fragments themselves may or may not possess GAT activity. For example, two or more segments of a GAT polypeptide can be separated by inteins; removal of the intein sequence via cis primary processing of the transcript results in a functional polypeptide. In another example, the written GAT polypeptide can be expressed as two or more separate segments; trans-primary processing of the transcript of these segments results in the return of a functional GAT polypeptide. Various aspects of cis- and trans primary transcript processing, gene encoding, and introduction of altered sequences are described in detail in U.S. Pat. Patent Application Serial Nos. (U.S. Patent Application Serial Nos.) 09/517,933 and 09/710,686, both of which are fully incorporated herein by reference. In general, the invention includes any polypeptide that is encoded by a modified polynucleotide obtained by mutation, recursive sequence recombination, and/or diversification of the polynucleotide sequence described herein. In some aspects of the invention, the GAT polypeptide is modified by a single or multiple amino acid substitution, deletion, insertion, or a combination of one or more of these types of modifications. Substitutions can be conservative or non-conservative, they can change function or not, and they can provide (add) new function. Insertions or deletions may be complete, as in the case of truncation of a significant fragment of sequence, or in fusion with additional sequence, either internal or at the N or C terminus. In some embodiments of the invention, the GAT polypeptide is part of a fusion protein comprising a functional addition, such as, for example, a secretion signal, a chloroplast transit peptide, a purification tag, or any of a number of other functional groups that will be known and apparent to those skilled in the art and that are described in more detail elsewhere in this specification. The polypeptides of the present invention may contain one or more amino acids. The presence of modified amino acids can be advantageous, for example for (a) increasing the half-life of the polypeptide in vivo, (b) reducing or increasing the antigenicity of the polypeptide (b) reducing the storage stability of the polypeptide. The amino acid(s) are modified, for example co-translationally or post-translationally during recombinant production (for example, N-linked glycosylation at N-X-S/T motifs during expression in mammalian cells) or modified by synthetic routes. Non-limiting examples of a modified amino acid include a glycosylated amino acid, a sulfonated amino acid, a pronylated amino acid, a pronylated amino acid, a carboxylated amino acid, a phosphorylated amino acid, and the like. References which adequately guide experts from this field of science in the modification of amino acids are numerous in the literature. Examples of protocols can also be found in the literature. Examples of protocols are found in Walker (1998) Protein Protocols on CD-ROM (HumanaPress, Towata, NJ). ;Recombination methods for the production and isolation of GAT polypeptides of the invention are described herein. In addition to recombinant production, polypeptides can be produced by direct peptide synthesis using solid-phase techniques (eg, Stewart et al., (1969) Solid-Phase Peptide Synthesis (WH Freeman Co, San Francisco); and Merrifield (1963) J. Am. Chem. Soc. 85:2149-2154). Peptide synthesis can be carried out by manual techniques or by automation. Automated synthesis can be accomplished, for example, using an Applied Biosystems 431A Peptide Synthesizer (Perkin Elmer, Foster City, CA) according to instructions provided by the manufacturer. For example, subsequences can be chemically synthesized separately and combined using chemical methods to provide full-length GAT polypeptides. Peptides can also be ordered from various sources (ie, manufacturers). In another aspect of the invention, the GAT polypeptide of the invention is used to produce antibodies that have, for example, diagnostic uses, for example, related to the activity, distribution and expression of the GAT polypeptide, for example in various tissues of the transgenic plant. GAT homologous polypeptides do not require biological activity to induce antibodies; however, the polypeptide or oligopeptide must have an antigenic function. Peptides used to induce antibodies may have an amino acid sequence consisting of at least ten amino acids, preferably 15 or 20 amino acids. Short strings of GAT polypeptides can be fused to another protein, such as hemocyanin from sticklebacks (orderFissuralidae), and an antibody produced against the chimeric molecule. Methods for producing polyclonal and monoclonal antibodies are known to those skilled in the art, and many antibodies are available. See, for example, Holigan (1991) Current Protocols in Immunobiology (Wiley/Green, NY), Harlow and Lane (1989) Antibodies: A Laboratory Manual (Cold Spring Harbor Press, NY); Stites et al. (eds) Basic and Clinical Immunology, 4 <th>ed. (Lange Medical Publications, los Altos, CA) and references cited therein; Golding (19986) Monocial Antibodies: Principles and Practice, 2 <nd>ed. (Academic Press, New York, NY); and Kohler and Milstein (1975) Nature 256:495-497. Other suitable techniques for antibody preparation include selection of recombinant antibody libraries in phage or similar vectors. See, Huseet al. (1989) Science 246:1275-1281; and Wardet al. (1989) Nature 341: 544-546. Specific monoclonal and polyclonal antibodies and antisera will most often bind to Kdod at least about 0.1 µM, preferably at least about 0.01 µM or better, and most typically and preferably 0.01 µM or better. Additional details on antibody production and construction techniques can be found in Borrebaeck, ed. (1995) Antibody Engineering, 2 <nd>ed. (Freeman and Company, NY); McCaffertyet al.; (1996) Antibody Engineering, A Practical Approach (IRL at Oxford Press, Oxford, England); and Paul (1995) Antibody Engineering Protocols (Humana Press, Towata, NJ). ;Sequence Variations ;The GAT polypeptides of the present invention include conservatively modified sequence variations disclosed herein as SEQ ID NO: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597,598,599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 665, 667, 669, 671, 673, 675, 677, 679, 681, 683, 685, 687, 689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811, 813, 815, 817, 819, 821, 823, 825, 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 929, 931, 953, 954, 955, 956, 957, 958, 959, 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971, and 972. Such conservatively modified variations include substitutions, additions, or deletions that change, add, or delete a single amino acid or a small percentage of amino acids (typically less than about 5%, more typically less than about 4%, 2% or 1%) in any of SEQ ID NO: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597,598,599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 665, 667, 669, 671, 673, 675, 677, 679, 681, 683, 685, 687, 689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811, 813, 815, 817, 819, 821, 823, 825, 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 929, 931, 953, 954, 955, 956, 957, 958, 959, 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971 and 972. ;For example, conservatively modified variants (eg, by deletion) of the 146 amino acid polypeptide identified herein as SEQ ID NO:6 will have a length of at least 140 amino acids, preferably at least 141 amino acids, more preferably at least 144 amino acids, and even more preferably at least 145 amino acids, which correspond to the deletion that is less than about 5%, 4%, 2%, or 1% or less of the polypeptide sequence. ;Another example of a conservatively modified variation (eg a "conservatively substituted variation") of the polypeptide identified herein as SEQ ID NO:6 will contain "conservative substitutions", based on the 6 substitution groups shown in Table 2 in about 7 residues (ie, less than 5%) of the 146 amino acid polypeptide. ;GAT polypeptide sequence homologues of the invention, including conservatively substituted sequences, may be present as part of larger polypeptide sequences, as occurs in a GAT polypeptide in a GAT fusion with a signal sequence, e.g., a chloroplast targeting sequence, or after addition of one or more protein purification domains (e.g., poly-his segments, FLAG "tag" segments, etc.). In another case, the additional functional domains have little or no effect on the activity of the GAT portion of the protein or where the additional domains can be removed by a post-synthesis processing step such as protease treatment. ;Defined Polypeptides by Immunoreactivity ;Because the polypeptides of the invention provide a new class of enzymes with defined activity, ie by acetylation and acylation of glyphosate, the polypeptides also provide new structural features that can be detected in, for example, immunoassays. Obtaining an antiserum that specifically binds to polypeptides from the invention, as well as polypeptides that are bound by such an antiserum, are the subject of this invention. ;The invention includes GAT polypeptides that specifically bind or are specifically immunoreactive with an antibody or antiserum raised against an immunogen comprising an amino acid sequence selected from one or more of SEQ ID NOs: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597,598,599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 665, 667, 669, 671, 673, 675, 677, 679, 681, 683, 685, 687, 689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811, 813, 815, 817, 819, 821, 823, 825, 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921,923, 925, 927, 929, 931, 953, 954,955, 956, 957, 958, 959, 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971 and 972. To eliminate cross-reactivity with other GAT homologs, the antibody or antiserum was isolated with available related proteins, such as those represented by proteins or peptides corresponding to GenBank accession numbers available as of the filing date of this application and exemplified by CAA700664, Z99109, and Y09476. Where the accession number corresponds to the nucleic acid, a polypeptide is obtained which is encoded by the nucleic acid and is used for antibody/antisera extraction purposes. Figure 3 presents a table of relative identity between the GAT sequences used as an example and the most closely related sequence available in GenBank, Yitl. The function of native Yitl has not yet been elucidated, but the enzyme has been shown to possess detectable GAT activity. ;In one typical form, the immunoassay uses a polyclonal antiserum raised against one or more polypeptides containing one or more sequences corresponding to one or more SEQ ID NOs: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597,598,599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 665, 667, 669, 671, 673, 675, 677, 679, 681, 683, 685, 687, 689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811, 813, 815, 817, 819, 821, 823, 825, 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 929, 931, 953, 954, 955, 956, 957,958, 959, 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971, and 972, or substantial subsequences thereof (ie, at least about 30% of the complete sequence length provided). A complete panel of potential polypeptide immunogens derived from SEQ ID NO: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597,598,599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 665, 667, 669, 671, 673, 675, 677, 679, 681, 683, 685, 687, 689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811, 813, 815, 817, 819, 821, 823, 825, 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 929, 931, 953, 954, 955, 956, 957, 958, 959, 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971 and 972, are collectively referred to below as "immunogenic polypeptide(s)". The resulting antisera are optionally selected to have low cross-reactivity against other related sequences and any cross-reactivity is removed by immunoabsorption with one or more related sequences before using the polyclonal antisera in the immunoassay. ;In order to produce antisera for use in an immunoassay, one or more immunogenic polypeptides are produced and purified, as described herein. For example, a recombinant protein can be produced in a bacterial cell line. An inbred mouse line (used in this essay because the results are more easily reproduced due to the virtual genetic identity of the mouse) is immunized with the immunogenic polypeptide(s) in combination with a standard adjuvant, such as Freund's adjuvant, using a standard mouse immunization protocol (see Harlow and Lane (1988) Antibodies, A Laboratory Manual, (Cold Spring Harbor Publications, New York), for a standard description of obtaining antibodies, immunoassay formats and conditions that can be used to determine specific immunoreactivity). Alternatively, one or more recombinant polypeptides derived from the sequences disclosed herein were conjugated to a protein carrier and used as an immunogen. Polyclonal sera are collected and titrated against immunogenic polypeptides in an immunoassay, for example a solid phase immunoassay with one or more immunogenic proteins immobilized on a solid support. Polyclonal antisera with a titer of 106 or greater are selected, pooled, and separated with related polypeptides, for example those identified in GENEBANK as described, to obtain pooled, titrated polyclonal antisera. ;Raised, pooled, titrated polyclonal antisera were tested for cross-reactivity against related polypeptides. Preferably at least two of the immunogenic GATs are used in this assay, preferably in conjunction with at least two polypeptides in order to identify antibodies that specifically bind to the immunogenic polypeptide(s). ;In this comparative assay, conditions for discriminatory binding are determined for isolated, titrated polyclonal antisera that result in at least a 5-10-fold higher signal-to-noise ratio for binding of titrated polyclonal antisera to immunogenic GAT polypeptides when compared to binding to cognate polypeptides. This means that the restrictiveness of the binding reaction is adjusted by adding non-specific competitors such as albumin or skimmed milk powder or by adjusting the conditions of salt concentration, temperature or the like. These binding conditions are used in further assays to determine whether the polypeptide specifically binds to pooled isolated polyclonal antisera. In particular, a tested polypeptide that exhibits at least a 2-5 times higher signal-to-noise ratio than a control polypeptide under discriminatory binding conditions and that exhibits at least about a !4 signal-to-noise ratio when compared to the immunogenic polypeptide(s), shares a significant degree of structural similarity with the immunogenic polypeptide(s) as compared to a known GAT and therefore represents a polypeptide of the present invention. In another example, an immunoassay in a competitive binding format is used to detect a test polypeptide. For example, as noted, cross-reacting antibodies are removed from the pooled antisera mixture by immunoabsorption with control GAT polypeptides. The immunogenic polypeptide(s) are then immobilized on a solid support which is exposed to the subtracted pooled antisera. Test proteins are added to the assay to compete for binding to the pooled antisera. The ability of the test proteins to compete for binding to the pooled antisera when compared to the immobilized protein(s) is compared to the ability of the immunogenic polypeptide(s) added to the assay to compete for binding (the immunogenic polypeptide(s) compete effectively with the immobilized immunogenic polypeptide(s) for binding to the pooled antisera). The percentage of cross-reactivity for test proteins is calculated by standard calculations. In a parallel assay, the ability of the control proteins to compete for binding to the pooled subtracted antisera is optionally determined as the ability of the immunogenic polypeptide(s) to compete for binding to the antisera. Again, percent cross-activity for control polypeptides is calculated by standard calculations. Where the cross-reactivity is at least 5-10 times greater for the test polypeptides, the test polypeptides are said to specifically bind the pooled antisera. ;Generally, immunoabsorbed and pooled antisera can be used in a competitive binding immunoassay, as described herein, to compare any test peptide with an immunogenic polypeptide(s). To make such a comparison, a wide concentration range assay is performed for each polypeptide and the amount of each polypeptide required to inhibit 50% binding of the pooled antiserum to the immobilized protein is determined using standard techniques. If the amount of test polypeptide required is less than 2 x the amount of immunogenic polypeptide(s) required, then the test polypeptide is said to bind specifically to the antibody generated to the immunogenic polypeptide(s), with the amount being at least 5-10 times greater for the control polypeptide. ;For final determination of specificity, pooled antisera are optionally fully immunoabsorbed with immunogen polypeptide(s) (rather than control polypeptides) until little or no binding of pooled antisera to immunogen and polypeptide(s) is detected. Antisera thus immunoabsorbed are then tested for reactivity with the test polypeptide. If little or no reactivity is detected (ie, no greater than 2 x the signal-to-noise ratio detected for binding of fully immunoabsorbed antisera to the immunogenic polypeptide(s)), then the test polypeptide is specifically bound by the antisera elicited by the immunogenic polypeptide(s). ;GLYPHOSATE-N-ACETYLTRANSFERASE POLYNULKEOTIDES ;In one aspect the invention provides a novel family of isolated or recombinant polynucleotides designated herein as "glyphosate-N-acetyltransferase polynucleotides" or "GAT polynucleotides". GAT polynucleotide sequences are characterized by the ability to encode a GAT polypeptide. In general, the invention includes any nucleotide sequence encoding any novel GAT polypeptide described herein. In some aspects of the invention, a GAT polynucleotide encoding a GAT polypeptide with GAT activity is preferred. ;In one aspect, GAT polynucleotides comprise recombinant or isolated forms of natural nucleic acids isolated from an organism, for example from a bacterial strain. Examples of GAT polynucleotides, for example SEQ ID NO: 1-5, were discovered by expression of cloned sequences from Bacillus strains exhibiting GAT activity. Briefly, a collection of approximately 500 strains of Bacillus- and Pseudomonas- were screened for their native ability to N-acetylate glyphosate. Strains were grown in LB overnight, collected by centrifugation, permeabilized in dilute toluene and then washed and resuspended in a reaction mixture containing buffer, 5 mM glyphosate and 200 µM acetyl-CoA. Cells were incubated in the reaction mixture for between 1-48 hours when an equal volume of methanol was added to the reaction. Cells were then pelleted by centrifugation and the supernatant was filtered before analysis by "parent ion mode" mass spectrometry. The product of the reaction was positively identified as N-acetyl glyphosate by comparing the reaction mixture profile obtained by mass spectrometry with an N-acetyl glyophosate standard, as shown in Figure 2. Product detection was dependent on the inclusion of both substrates (acetyl CoA and glyphosate) and was terminated by heat denaturation of the bacterial cells. ;Individual GAT polynucleotides were then cloned from the identified strains by functional screening. Genomic DNA was prepared and partially digested with Sau3Al enzyme. Fragments of approximately 4 kb were cloned into the expression vector E. coli transformed into electro-competent E. coli. Individual clones that exhibited GAT activity were identified by mass spectrometry in the reaction described previously, except that the toluene wash was replaced by PMBS permeabilization. Genomic fragments were sequenced and the putative GAT polypeptide-encoding open reading frame was identified. The identity of the GAT gene was confirmed by expression of the uE open reading frame. colii by detecting high levels of N-acetyl glyphosate produced from the reaction mixtures. ;In another aspect of the invention GAT polynucleotides are produced by diversification, for example by recombination and/or mutating one or more naturally isolated or recombinant GAT polynucleotides. As described in more detail in other parts of the application, it is often possible to obtain diversified GAT polynucleotides that encode GAT polypeptides with superior functional attributes, for example enhanced catalytic function, increased stability or higher expression level, than the GAT polynucleotide used as a substrate or output polynucleotide in the diversification (modification) process. ;The polynucleotides of the invention can be used for various purposes, for example the recombinant production (that is, the expression) of the GAT polypeptides of the invention, as transgenes (for example, to provide herbicide resistance in transgenic plants); as selective markers for plasmid transformation and maintenance; as immunogens; as tests for diagnosing the presence of complementary or partially complementary nucleic acids (including the detection of natural GAT-encoding nucleic acids); as substrates for further diversification, for example, for recombination or mutation reactions to produce new and/or improved GAT homologues, and the like. It is important to note that certain specific, significant and plausible uses of GAT polynucleotides do not require that the polynucleotide encodes a polypeptide with significant GAT activity. For example, GAT polynucleotides that do not encode active enzymes can be important sources of parent nucleotides (parent) polynucleotides for use in diversification procedures, to obtain polynucleotide variants of GAT, or non-GAT polynucleotides, with desirable functional characteristics (for example, high kcat or kcat /Km, low Km, high resistance to heat (in terms of stability) or to other environmental factors, high level of transcription or translation, resistance to proteolytic cleavage, reduced antigenicity, etc.). For example, nucleotide sequences encoding protease variants with little or no detectable activity have been used as parent polynucleotides in DNA "shuffling" experiments to produce progeny encoding highly active proteases (Nesset al.(1999)Nature Biotech.17:893-96). Polynucleotide sequences produced by diversity generation methods or recursive sequence recombination ("RSR") methods, (for example DNA "shuffling") are a feature of the present invention. The methods of mutation and recombination using nucleic acids described herein are a feature of the present invention. For example, one method of the present invention includes recursively recombining one or more nucleotide sequences of the invention, as described above and below, with one or more additional nucleotides. The recombination steps are optionally performed in vivo, ex vivo, in silico or in vitro. Diversity generation or recursive sequence recombination produces at least one library of recombinant modified GAT polynucleotides. Polypeptides encoded by members of this library are encompassed by the present invention. Also contemplated are the uses of polynucleotides designated herein as oligonucleotides typically having at least 12 bases, preferably at least 15, more preferably at least 20, 30, or 50 or more bases, which hybridize under restrictive or highly restrictive conditions to a GAT polynucleotide sequence. Polynucleotides can be used as probes, primers, sense and anti-sense agents (coding and non-coding agents), and the like, according to the methods described herein. In accordance with the present invention, GAT polynucleotides, including nucleotide sequences encoding GAT polypeptides, fragments of GAT polypeptides, related fusion proteins, or functional equivalents thereof, are used in recombinant DNA molecules that direct the expression of GAT polypeptides in appropriate host cells such as bacterial or plant cells. Due to the inherent nature of the genetic code, other nucleic acid sequences that encode substantially the same or functionally equivalent amino acid sequences may also be used for cloning and expression of GAT polynucleotides. The invention provides GAT polynucleotides that encode transcription and/or translation products that are substantially processed (spliced) to ultimately yield functional GAT polypeptides. Processing of the primary transcript (splicing) can be achieved in vitro or in vivo and may involve cis- or trans-processing of the primary transcript. The substrate for the primary processing of transcripts can be polynucleotides (eg RNA transcripts) or polypeptides. An example of cis-primary processing of a polynucleotide transcript is when an intron inserted into a coding sequence is removed and the two exon regions surrounding it are joined, to give the GAT polypeptide coding sequence. An example of trans-primary processing of a transcript would be one where a GAT polynucleotide encoded with a coding sequence is split into two or more fragments, which can be transcribed separately and then after processing, form the full-length GAT coding sequence. The use of an enhancer sequence for primary processing of the transcript (which can be introduced into the construct of the invention) can facilitate splicing in both cis- and trans-. Cis- and trans-processing of the primary polypeptide transcript is described in more detail elsewhere in the text and in U.S. Pat. Patent Application Serial Nos. 09/517,933 and 09/710,686. ;Therefore, some GAT polynucleotides do not directly encode a full-length GAT polypeptide, but instead encode a fragment or fragments of a GAT polypeptide. These GAT polynucleotides can be used to express a functional GAT polypeptide through a mechanism involving primary processing of the transcript, where this processing can take place at the polynucleotide (eg intron/exon) and/or polypeptide (eg intein/extein) level. This can be useful for, for example, controlling the expression of GAT activity, since a functional GAT polypeptide will only be expressed if all the required fragments are expressed in an environment that allows for primary processing (splicing) to yield a functional product. In another example, introducing one or more insertion sequences into a GAT polynucleotide can facilitate recombination with a polynucleotide having low homology; the use of an intron or intein for the insertion sequence facilitates removal of the intervening sequence, thereby reestablishing the function of the coding variant. Scientists will appreciate that modification of the coding sequence to increase its expression in a particular host may be advantageous. The genetic code is rich and defined by 64 possible codons, although most organisms preferentially use only a subset of these codons. Codons that are most frequently used in a species are called optimal codons, and those that are not frequently used are classified as rare or infrequently used codons (see, for example, Zhang et al. (1991) Gene105:61-72). Codons can be replaced to reflect the preferred codon usage of the host - a process sometimes called "codon optimization" or "species codon usage tendency control". Optimized coding sequences containing codons that are desirable for a particular prokaryotic or eukaryotic host (see also, Murravat et al. (1989) Nucl. Acids. Res. 17:477-508) can be prepared, for example to increase the level of translation or to produce recombinant RNA transcripts that have desired properties such as a longer half-life, when compared to transcripts produced by unoptimized sequence. Translational stop codons can also be modified to reflect host preference. For example, the preferred stop codons for S. cerevisiae mammals are UAA and UGA. The preferred stop codon for monocots is UGA, while insects and E. coli use UAA as a preferred stop codon (Dalphinet al. (1996) Nucl. Acids. Res. 24:216-218). A methodology for optimizing a nucleotide sequence for expression in a plant is provided, for example in U.S. Pat. Patent No. 6,015,891 and references are incorporated herein by reference. One embodiment of the invention includes a GAT polynucleotide having optimal codons for expression in a relevant host, for example a transgenic plant host. This is particularly desirable when a GAT polynucleotide of bacterial origin is introduced into a transgenic plant, for example to provide glyphosate resistance in the plant. Polynucleotide sequences of the present invention can be engineered to alter GAT polynucleotides for a variety of reasons, including, but not limited to, alterations that modify the cloning, processing, and/or expression of the gene product. For example, changes can be made using techniques well known in the art, for example, "site-directed" mutagenesis (site-directed mutagenesis), to insert new restriction sites, change the glycosylation pattern, change codon preferences, introduce processing sites (splice sites), etc. As described in more detail herein, the polynucleotides of the invention include sequences encoding novel GAT polypeptides and sequences complementary to the coding sequences and novel fragments of the coding sequences and their complements. Polynucleotides can be in the form of RNA or in the form of DNA, and include mRNA, cRNA and DNA, synthetic RNA and DNA, genomic DNA and cDNA. Polynucleotides can be double-stranded or single-stranded, and if they are single-stranded, they can be a coding strand or a non-coding (anti-sense, complementary) strand. The polynucleotides optionally include the coding sequence of a GAT polypeptide (i) in isolation, (ii) in combination with an additional coding sequence, which may encode, for example, a fusion protein, pre-protein, prepro-protein or the like, (iii) in combination with non-coding sequences, such as introns or inteins, control elements such as a promoter, enhancer, terminator, or 5' and/or 3' untranslated regions effective in expression of the coding sequence in a suitable host, and/or (iv) in a vector or host environment in which the GAT polynucleotide is a heterologous gene. The sequences may also be found in combination with typical compositions of nucleic acid formulations, including the presence of carriers, buffers, adjuvants, excipients, and the like. Polynucleotides and oligonucleotides of the invention can be prepared by standard solid phase methods, according to known synthetic methods. Typically, fragments of up to about 100 bases are individually synthesized then joined (for example by enzymatic or chemical ligation methods, or polymerase mediated methods) to obtain essentially any desired continuous sequence. For example, the polynucleotides and oligonucleotides of the present invention can be prepared by chemical synthesis using, for example, the classical "phosphoramidite" method described by Beaucageet al. (1981) Tetrahedron Letters 22:1859-69, or by the method described by Mattheset al. (1984) EMBO J.3:801-05, for example, as commonly practiced in automated synthetic methods. Based on the "phosphoramidite" method, oligonucleotides are synthesized, for example in an automatic DNA synthesizer, purified, connected, ligated and cloned into appropriate vectors. Additionally, essentially any nucleic acid can be ordered at will from any of the existing commercial manufacturers, such as The Midland Certified Reagent Companv ( mcrc@oligos. com), The Great American Gene Companv ( www. genco. com), ExpressGen Ine ( www. expressgen. inc), Operon Technologies Inc. (Alameida, CA) and many others. Similarly, peptides and antibodies can be ordered as desired from any of a number of existing commercial manufacturers, such as PeptidoGenic (pkim@ccnet.com), HTI Bio-products, Inc. (www.htibio.com), BMA Biomedicals Ltd. (U.K.), Bio. Svthesis Inc., and many others. Polynucleotides can also be synthesized by well-known techniques as described in the technical literature. See, for example, Carrutherset al, Cold Spring Harbor Symp. Quant. Biol. 47:411-418 (1982), and Adamet al. (1983) J. Am. Chem Soc. 105:661. Double-stranded DNA fragments can then be obtained either by synthesizing the complementary strand and ligating them under appropriate conditions or by adding the complementary strand using DNA polymerase with the appropriate primer sequence. General texts describing molecular biological techniques useful for this invention, including mutagenesis, include Berger and Kimmel, Guide to Molecular Cloning Techniques, Methods in Enzymology, Volume 152 (Academic Press, Inc., San Diego, CA); Sambrook et al. (1989jMolecular Cloning - A Laboratory Manual, 2d ed, Vol. 1-3, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York); and Ausubelet al., eds. (2000) Current Protocols in Molecular Biology (Greene Publishing Associates, Inc. and John Wiley & Sons, Inc.). Examples of techniques sufficient to guide one skilled in the art through in vitro amplification methods include polymerase chain reaction (PCR), Ugase chain reaction (LCR), QP-replicase amplification, and other RNA polymerase-mediated techniques (eg NASBA) can be found in Berger, Sambrook, and Ausubel, as well as in Mullis et al. (1987) U.S. Patent No. 4,683,202; Innisset al, eds. (1990) PCR Protocols: A Guide to Methods and Applications (Academic Press Inc. San Diego, CA); ("Innis"; Arnheim & Levinson (October 1, 1990) Chemical and Engineering News36-47; Journal of NIH Research(1991) 3: 81-94; Kwohet al.(1989)Proc. Nat' l. Acad. Sci. USA86: 1173; Guatelliet al.(1990) Proc. Nat' l. Acad. Sci. USA87: 1874; Lomellet et al. (1989) Chem35: 1077-1080; (1995) Biotechnology 13: 563-564. Improved methods for cloning in vitro amplified nucleic acids are described in Wallace et al, U.S. Pat. No. 5,426,039. Improved methods for amplification of large nucleic acids using PCR are summarized in Chengat al. (1994) Nature 369:684-685 and references cited therein, which generate amplicons up to 40 kb. One skilled in the art will appreciate that essentially any RNA can be converted into double-stranded DNA suitable for restriction digestion, amplification by PCR, and sequencing using reverse transcriptase and polymerase. See, Ausbel, Sambrook, and Berger, supra. ;One aspect of the present invention provides an isolated or recombinant polynucleotide selected from the group consisting of SEQ ID NO: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 534, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 620, 622, 624, 626, 628, 630, 632, 634, 636, 638, 640, 642, 644, 646, 648, 650, 652, 654, 656, 658, 660, 662, 664, 666, 668, 670, 672, 674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726, 728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788, 790, 792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814, 816, 818, 820, 822, 824, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916, 918, 920, 922, 924, 926, 928, 930, 932, 933, 934, 935, 936, 937, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952. Preferred polynucleotides of the present invention include an isolated or recombinant polynucleotide sequence encoding an amino acid sequence that can be optimally compared to a reference amino acid sequence selected from the group consisting of SEQ ID NOs: 300, 445 and 457 to obtain a similarity score of at least 460 using the BLOSUM62 matrix, a break presence "penalty" of 11 and a break spread "penalty" of 1, indicated that at least one of of the following positions fits into the following restrictions: (i) there is a Z5 amino acid residue at positions 18 and 38; (ii) there is a Z1 amino acid residue at position 62; (iii) there is a Z6 amino acid residue at position 124; and (vi) at position 144 there is a Z2 amino acid residue, wherein: Z1 is an amino acid residue selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid residue selected from the group consisting of F, W and Y; Z5 is an amino acid residue selected from the group consisting of D and E; Z6 is an amino acid residue selected from the group consisting of C, G and P, and further indicated that the amino acid residues in the amino acid sequence corresponding to the following positions are at least 90% compatible with the following restrictions: (a) at positions 2, 4, 15, 19, 26, 28, 31, 45, 51, 54, 86, 90, 91, 97, 103, 105, 106, 114, 123, 129, 139 and/or 145 amino acid residues BI; and (b) at positions 3, 5, 8, 10, 11, 14, 17, 24, 27, 32, 37, 47, 48, 49, 52, 57, 58, 61, 63, 68, 69, 79, 80, 82, 83, 89, 92, 100, 101, 104, 119, 120, 125, 126, 128, 131 and/or 143 amino acid residues B2; wherein BI is an amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S, and T. When used to designate an amino acid or amino acid residue, the single letter designations A, C, D, E, F, G, H, I, K, L, M, N, P, Q, R, S, T, V, W, and Y have their standard meanings as used in science and as shown in the table herein 1. ;Some preferred isolated or recombinant polynucleotides of the invention which encode an amino acid sequence such that when the sequence is optimally compared to a reference amino acid sequence selected from the group consisting of SEQ ID NO: 300, 445 and 457 to obtain a similarity score of at least 460 using the BLOSUM62 matrix, a "penalty" of having a break of 11 and a "penalty" of a break span of 1, one or more of the following positions fits the following restrictions: (i) there is a Z5 amino acid residue at positions 18 and 38; (ii) there is a Z1 amino acid residue at position 62; (iii) there is a Z6 amino acid residue at position 124; and (vi) at position 144 there is a Z2 amino acid residue, wherein: Z1 is an amino acid residue selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid residue selected from the group consisting of F, W and Y; Z5 is an amino acid residue selected from the group consisting of D and E; Z6 is an amino acid residue selected from the group consisting of C, G and P, and further indicated that the amino acid residues in the amino acid sequence corresponding to the following positions, and at least 80% fit into the following restrictions: (a) at positions 2, 4, 15, 19, 26, 28, 51, 54, 86, 90, 91, 97, 103, 105, 106, 114, 129, 139 and/or 145 amino acid residues Zl; (b) at positions 31 and/or 45 the amino acid residue is Z2; (c) at position 8 the amino acid residue is Z3; (d) at position 89 amino acid residues Z3 or Z6; (e) at positions 82, 92, 101 and/or 120 amino acid residues Z4; (f) at positions 3, 11, 27 and/or 79 amino acid residues Z5; (g) at position 18 the amino acid residue is Z4 or Z5; (h) at position 123 amino acid residues Z1 or Z2; (i) at positions 12, 33, 35, 39, 53, 59, 112, 132, 135, 140 and/or 146 are amino acid residues Z1 or Z3; (j) at position 30 amino acid residues Zl; (k) at position 6 amino acid residues Z6; (1) at position 81 amino acid residues Z2 or Z4; (m) at position 113 amino acid residues Z3; (n) at position 138 amino acid residues Z4; (o) at position 142 amino acid residues Z2; (p) at positions 57 and/or 126 amino acid residues Z3 or Z4; (q) at positions 5, 17 and/or 61 amino acids the remainder is Z4; (r) at position 24 amino acid residues Z3; (s) at position 104 amino acid residues Z5; (t) at positions 52 and/or 69 amino acid residues Z3; (u) at positions 14 and/or 119 amino acid residues Z5; (v) at positions 10, 32, 63 and/or 83 amino acid residues Z5; (w) at positions 48 and/or 80 amino acid residues Z6; (x) at position 40 amino acid residues Z1 or Z2; (y) at position 96 amino acid residues Z3 or Z5; (z) at position 65 amino acid residues Z3, Z4 or Z6; (aa) at positions 84 and/or 115 the amino acid residue is Z3; (ab) at position 93 amino acid the remainder is Z4; (ac) at position 130 amino acid residues Z2; (ad) at position 58 amino acid residues Z3, Z4 or Z6; (ae) at position 47 amino acid residues Z4 or Z6; (af) at positions 49 and/or 100 amino acid residues Z3 or Z4; (ag) at position 68 amino acid residues Z4 or Z5; (ah) at position 143 amino acid residues Z4; (ai) at position 131 amino acid residues Z5; (aj) at positions 125 and/or 128 amino acid residues Z5; (ak) at position 67 amino acid residues Z3 or Z4; (al) at position 60 amino acid residues Z5; and (am) at position 37 the amino acid residue is Z4 or Z6; indicated that the Z1 amino acid is selected from groups consisting of A, I, L, M, and V; Z 2 is an amino acid selected from the group consisting of F, W and Y; Z3 is an amino acid selected from the group consisting of N, Q, S and T; Z4 is an amino acid selected from the group consisting of R, H and K; Z5 is an amino acid selected from the group consisting of D and E; and Z6 is an amino acid selected from the group consisting of C, G and P. Certain preferred isolated or recombinant polynucleotides of the invention encoding an amino acid sequence further comprise amino acid residues in the amino acid sequence corresponding to the positions specified in (a) - (am), indicated that at least 90% fit within the amino acid residue restrictions specified in (a) - (am). ;Some preferred isolated or recombinant polynucleotides of the invention which encode an amino acid sequence such that when the sequence is optimally compared to SEQ ID NO: 300, 445 and 457, at least 90% of the amino acid residues in the amino acid sequence fit within the following constraints: (a) at positions 1, 7, 9, 13, 20, 36, 42, 46, 50, 56, 64, 70, 72, 75, 76, 78, 94, 98, 107, 110, 117, 118, 121 and/or 141 amino acid residues BI; and (b) at positions 16, 21,22,23,25,29, 34,41,43,44, 55,66,71,73,74, 77, 85,87, 88, 95,99, 102, 108, 109, 111, 116, 122, 127, 133, 134, 136 and/or 137 are amino acid residues B2; wherein BI is an amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S and T. ;Some preferred isolated or recombinant polynucleotides of the invention which encode an amino acid sequence such that when the sequence is optimally compared to SEQ ID NO: 300, 445 and 457, at least 90% of the amino acid residues in the amino acid sequence match the following restrictions: (a) at positions 1, 7, 9, 13, 20, 42, 46, 50, 56, 64, 70, 72, 75, 76, 78, 94, 98, 107, 110, 117, 118, 121 and/or 141 amino acid residues BI; and (b) at positions 16, 21, 22, 23, 25, 29, 34, 36, 41, 43, 44, 55, 66, 71, 73, 74, 77, 85, 87, 88, 95, 99, 102, 108, 109, 111, 116, 122, 127, 133, 134, 136 and/or 137 amino acid residues B2; indicated that the BI amino acid is selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S and T. ;Some preferred isolated or recombinant polynucleotides of the invention which encode an amino acid sequence such that when the sequence is optimally compared to SEQ ID NO: 300, 445 and 457, at least 90% of the amino acid residues in the amino acid sequence match the following additional restrictions: (a) at positions 1, 7, 9, 20, 42, 50, 72, 75, 76, 78, 94, 98, 110, 121 and/or 141 amino acid residues Z1; (b) at positions 13, 46, 56, 70, 107, 117 and/or the 118 amino acid residue is Z2; (c) at positions 23, 55, 71, 77, 88 and/or 109 amino acid residues Z3; (d) at positions 16, 21, 41, 73, 85, 99 and/or 111 amino acid residues Z4; (e) at positions 34 and/or 95 amino acid residues Z5; (f) at positions 22, 25, 29, 43, 44, 66, 74, 87, 102, 108, 116, 122, 127, 133, 134, 136 and/or 137 amino acid residues Z6; characterized in that Z1 is an amino acid selected from the group consisting of A, I, L, M and V; Z2 is an amino acid selected from the group consisting of F, W and Y; Z3 is an amino acid selected from the group consisting of N, Q, S and T; Z4 is an amino acid selected from the group consisting of R, H and K; Z5 is an amino acid selected from the group consisting of D and E; Z6 is an amino acid selected from the group consisting of C, G and P. Certain preferred isolated or recombinant polynucleotides of the invention encoding the amino acid sequence further comprise at position 36 an amino acid residue selected from the group consisting of Z1 and Z3. Some preferred isolated or recombinant polynucleotides of the invention encoding the amino acid sequence further comprise at position 64 an amino acid residue selected from the group consisting of Z1 and Z2. ;Some preferred isolated or recombinant polynucleotides of the invention which encode an amino acid sequence such that when the sequence is optimally compared to SEQ ID NOs: 300, 445 and 457, at least 80% of the amino acid residues in the amino acid sequence fit the following additional restrictions: (a) at position 2 amino acid residues I or L; (b) at position 3 the amino acid residue is E; (c) at position 4 the amino acid residue is V or I; (d) at position 5 amino acid residues K; (e) at position 6 amino acid residues P; (f) at position 8 amino acid residues N; (g) at position 10 amino acid residues E; (h) at position 11 amino acid residues D or E; (i) at position 12 amino acid residues T; (j) at position 14 amino acid residues E or D; (k) at position 15 the amino acid residue is L; (1) at position 17 amino acid residues H; (m) at position 18 amino acid residues R, E or K; (n) at position 19 amino acid residues I or V; (o) at position 24 amino acid residues Q; (p) at position 26 amino acid residues M, L, V, or I; (q) at position 27 amino acid residues E; (r) at position 28 amino acid residues A or V; (s) at position 30 amino acid residues M; (t) at position 31 the amino acid residue is Y or F; (u) at position 32 the amino acid residue is E or D; (v) at position 33 amino acid residues T or S; (w) at position 35 amino acid residues L; (x) at position 37 amino acid residues R, G, E or Q; (y) at position 39 amino acid residues A or S; (z) at position 40 the amino acid residue is F or L; (aa) at position 45 amino acid residues Y or F; (ab) at position 47 amino acid residues R or G; (ac) at position 48 amino acid residues G; (ad) at position 49 amino acid residues K, R or Q; (ae) at position 51 amino acid residues I or V; (af) at position 52 amino acid residues S; (ag) at position 53 amino acid residues I or V; (ah) at position 54 amino acid residues A; (ai) at position 57 amino acid residues H or N; (aj) at position 58 are amino acid residues Q, K, R or P; (ak) at position 59 amino acid residues A; (al) at position 60 amino acid residues E; (am) at position 61 amino acid residues H or R; (an) at position 63 amino acid residues E or D; (ao) in position 65 amino acid residues E, P or Q; (ap) at position 67 amino acid residues Q or R; (aq) at position 68 the amino acid residue is K or E; (ar) at position 69 the amino acid residue is Q; (as) at position 79 amino acid residues E; (at) at position 80 amino acid residues G; (au) at position 81 the amino acid residue is Y, H or F; (av) at position 82 amino acid residues R; (aw) at position 83 amino acid residues E or D; (ax) at position 84 the amino acid residue is Q; (ay) at position 86 the amino acid residue is A; (az) at position 89 amino acid residues G, T or S; (ba) at position 90 amino acid residues L; (bb) at position 91 amino acid residues L, I or V; (bc) in position 92 amino acid residues R or K; (bd) at position 93 amino acid residues H; (be) at position 96 amino acid residues E or Q; (bi) at position 97 amino acid residues I; (bg) at position 100 amino acid residues K or N; (bh) at position 101 amino acid residues K or R; (bi) at position 103 amino acid residues A or V; (bj) at position 104 amino acid residues D; (bk) at position 105 the amino acid residue is M, L or I; (bi) at position 106 the amino acid residue is L; (bm) at position 112 the amino acid residue is T or A; (bn) at position 113 amino acid residues S or T; (bo) at position 114 amino acid residues A; (bp) at position 115 amino acid residues of S; (bq) at position 119 amino acid residues K or R; (br) at position 120 amino acid residues K or R; (bs) at position 123 amino acid residues F or L; (bt) at position 125 amino acid residues E; (bu) at position 126 amino acid residues Q or H; (bv) at position 128 the amino acid residue is E or D; (bw) at position 129 amino acid residues V or I; (bx) at position 130 amino acid residues F; (by) at position 131 amino acid residues D or E; (bz) at position 132 amino acid residues T; (ca) at position 135 amino acid residues V; (cb) at position 138 amino acid residues H; (cc) at position 139 amino acid residues I; (cd) in position 140 amino acid residues L or M; (ce) at position 142 the amino acid residue is Y; (cf) at position 143 the amino acid residue is K or R; (cg) at position 145 amino acid residues L or I; and (ch) at position 146 amino acid residues T. ;Some preferred isolated or recombinant polynucleotides of the invention that encode an amino acid sequence such that when the sequence is optimally compared to SEQ ID NO: 300, 445 and 457, at least 90% of the amino acid residues in the amino acid sequence fit within the amino acid residue restrictions specified in (a) - (ch) in the text above. ;Some preferred isolated or recombinant polynucleotides of the invention encode an amino acid sequence that when optimally compared to a reference amino acid sequence selected from the group consisting of SEQ ID NO: 300, 445 and 457 to obtain a similarity score of at least 460 using the BLOSUM62 matrix, a break existence "penalty" of 11 and a break spread "penalty" of One or more of the following positions fit the following restrictions: (i) at positions 18 and 38 there is a Z5 amino acid residue; (ii) there is a Z1 amino acid residue at position 62; (iii) there is a Z6 amino acid residue at position 124; and (vi) at position 144 there is a Z2 amino acid residue, wherein: Z1 is an amino acid residue selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid residue selected from the group consisting of F, W and Y; Z5 is an amino acid residue selected from the group consisting of D and E; Z6 is an amino acid residue selected from the group consisting of C, G, and P, and further indicated that amino acid residues in the amino acid sequence corresponding to the following positions, at least 80% fit the following restrictions: (a) at positions 9, 76, 94 and 110 amino acid residues A; (b) at positions 29 and 108 amino acid residues C; (c) at position 34 the amino acid residue is D; (d) at position 95 the amino acid residue is E; (e) at position 56 amino acid residues F; (f) at positions 43, 44, 66, 74, 87, 102, 116, 122, 127 and 136 amino acid residues G; (g) at position 41 amino acid residues H; (h) at position 7 amino acid residues I; (i) at position 85 amino acid residues K; (j) in position 20, 42, 50, 78 and 121 amino acid residues of L; (k) at position 1 and 141 amino acid residues M; (1) at position 23 and 109 amino acid residues N; (m) at positions 22, 25, 133, 134 and 137 are amino acid residues P; (n) at position 71 amino acid residues Q; (o) at positions 16, 21, 73, 99 and 111 the amino acid residue is R; (p) at position 55 the amino acid residue is S; (q) at position 77 the amino acid residue is T; (r) at position 107 amino acid residues W; (s) at positions 13, 46, 70 and 118 are amino acid residues ;Y. ;Some desirable isolated or the recombinant polynucleotides of the invention encode an amino acid sequence that fits at least one of the following additional restrictions: (a) at position 36 amino acid residues M, L or T; (b) at position 72 amino acid residues L or I; (c) at position 75 the amino acid residue is M or V; (d) at position 64 the amino acid residue is L, I or F; (e) at position 88 the amino acid residue is T or S; (f) at position 117 is an amino acid residue Y or F. Some preferred isolated or recombinant polynucleotides of the invention encode an amino acid sequence in which at least one of the following additional conditions is met: (a) at position 14 is an amino acid residue D; (b) at position 18 amino acid residues E; (c) at position 26 amino acid residues M or V; (e) at position 30 amino acid residues I; (f) at position 32 amino acid residues D; (g) at position 36 amino acid residues M or T; (h) at position 37 the amino acid residue is C; (i) at position 38 the amino acid residue is D; (j) at position 53 the amino acid residue is V; (k) at position 58 the amino acid residue is R; (1) at position 61 the amino acid residue is R; (m) at position 62 the amino acid residue is L; (n) at position 64 the amino acid residue is I or F; (o) at position 65 amino acid residues P; (p) at position 72 amino acid residues I; (q) at position 75 amino acid residues V; (r) at position 88 amino acid residues T; (s) at position 89 amino acid residues G; (t) at position 91 amino acid residues L; (u) at position 98 amino acid residues I; (v) at position 105 amino acid residues I; (w) at position 112 amino acid residues A; (x) at position 124 amino acid residues G or C; (y) at position 128 amino acid residues D; (z) at position 140 the amino acid residue is M; (aa) at position 143 the amino acid residue is R; and (ab) at position 144 amino acid residues W. Some preferred isolated or recombinant polynucleotides of the invention encode an amino acid sequence characterized in that the amino acid residues of the amino acid sequence corresponding to the positions specified in (a) to (ab), as described in the text above, at least 80% fit within the restrictions of the amino acid residues specified in (a) to (ab). Certain preferred isolated or recombinant polynucleotides of the invention encode an amino acid sequence that fits at least one of the following additional restrictions: (a) at position 41 amino acid residues H; (b) at position 138 amino acid residues H; (c) at position 34 amino acid residues N; and (f) at position 55 amino acid residues S. Some preferred isolated or recombinant polynucleotides of the invention are selected from the group consisting of: (a) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 577; (b) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO: 578; (c) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO: 621; (d) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 579; (e) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 602; (f) a nucleotide sequence encoding an amino acid sequence that is at least 95% identical to SEQ ID NO: 697; (g) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO: 721; (h) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO: 613; (i) a nucleotide sequence encoding an amino acid sequence that is at least 89% identical to SEQ ID NO: 677; (j) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO: 584; (k) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 707; (1) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 616; (m) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO: 612; (n) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 590. Some preferred isolated or recombinant polynucleotides of the invention are selected from the group consisting of: (a) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 577; (b) a nucleotide sequence encoding an amino acid sequence that is at least 97%> identical to SEQ ID NO: 578; (c) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO: 621; (d) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 579; (e) a nucleotide sequence encoding an amino acid sequence that is at least 98%> identical to SEQ ID NO: 602; (f) a nucleotide sequence encoding an amino acid sequence that is at least 95% identical to SEQ ID NO: 697; (g) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO: 721; (h) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO: 613; (i) a nucleotide sequence encoding an amino acid sequence that is at least 89% identical to SEQ ID NO: 677; (j) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO: 584; (k) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 707; (1) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 616; (m) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO: 612; (n) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 590, provided that the following positions fit the following restrictions: (i) at positions 18 and 38 there is a Z5 amino acid residue; (ii) there is a Z1 amino acid residue at position 62; (iii) there is a Z6 amino acid residue at position 124; and (vi) at position 144 there is a Z2 amino acid residue, wherein: Z1 is an amino acid residue selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid residue selected from the group consisting of F, W and Y; Z5 is an amino acid residue selected from the group consisting of D and E; Z6 is an amino acid residue selected from the group consisting of C, G and P. Some preferred isolated or recombinant polynucleotides of the invention are selected from the group consisting of: (a) a nucleotide sequence encoding an amino acid sequence that is at least 98%> identical to SEQ ID NO: 577; (b) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO: 578; (c) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO: 621; (d) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 579; (e) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 602; (f) a nucleotide sequence encoding an amino acid sequence that is at least 95% identical to SEQ ID NO: 697; (g) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO: 721; (h) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO: 613; (i) a nucleotide sequence encoding an amino acid sequence that is at least 89% identical to SEQ ID NO: 677; (j) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO: 584; (k) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 707; (1) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 616; (m) a nucleotide sequence encoding an amino acid sequence that is at least 96%> identical to SEQ ID NO: 612; (n) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 590, further indicated that the amino acid residues in the amino acid sequence corresponding to the following positions, at least 90% fit the following restrictions: (a) at positions 2, 4, 15, 19, 26, 28, 31, 45, 51, 54, 86, 90, 91, 97, 103, 105, 106, 114, 129, 139, and/or 145 amino acid residues of BI; and (b) at positions 3, 5, 8, 10, 11, 14, 17, 24, 27, 32, 37, 47, 48, 49, 52, 57, 58, 61, 63, 68, 69, 79, 80, 82, 83, 89, 92, 100, 101, 104, 119, 120, 125, 126, 128, 131 and/or 143 amino acid residues B2; characterized in that: a BI amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S and T. ;Some preferred isolated or recombinant polynucleotides of the invention are selected from the group consisting of: (a) a nucleotide sequence encoding an amino acid sequence that is at least 98%> identical to SEQ ID NO: 577; (b) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO: 578; (c) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO: 621; (d) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 579; (e) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 602; (f) a nucleotide sequence encoding an amino acid sequence that is at least 95% identical to SEQ ID NO: 697; (g) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO: 721; (h) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO: 613; (i) a nucleotide sequence encoding an amino acid sequence that is at least 89% identical to SEQ ID NO: 677; (j) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO: 584; (k) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 707; (1) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 616; (m) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO: 612; (n) a nucleotide sequence that encodes an amino acid sequence that is at least 98% identical to SEQ ID NO: 590, further indicated that the amino acid residues in the amino acid sequence corresponding to the following positions, at least 90% fit the following restrictions: (a) at positions 2,4, 15, 19, 26, 28, 51, 54, 86, 90, 91, 97, 103, 105, 106, 114, 129, 139, and/or 145 amino acid residues Z1; (b) at positions 31 and/or 45 the amino acid residue is Z2; (c) at position 8 the amino acid residue is Z3; (d) at position 89 the amino acid residue is Z3 or Z6; (e) at positions 82, 92, 101 and/or 120 amino acid residues Z4; (f) at positions 3, 11, 27 and/or 79 amino acid residues Z5; (g) at position 18 amino acid residues Z4 or Z5; (h) at position 123 amino acid residues Z1 or Z2; (i) at positions 12, 33, 35, 39, 53, 59, 112, 132, 135, 140 and/or 146 are amino acid residues Z1 or Z3; (j) at position 30 the amino acid residue is Z1; (k) at position 6 the amino acid residue is Z6; (1) at position 81 amino acid residues Z2 or Z4; (m) at position 113 amino acid residues Z3; (n) at position 138 amino acid residues Z4; (o) at position 142 amino acid residues Z2; (p) at positions 57 and/or 126 amino acid residues Z3 or Z4; (q) at positions 5, 17 and/or 61 the amino acid residue is Z4; (r) at position 24 the amino acid residue is Z3; (s) at position 104 the amino acid residue is Z5; (t) at positions 52 and/or 69 amino acid residues Z3; (u) at positions 14 and/or 119 amino acid residues Z5; (v) at positions 10, 32, 63 and/or 83 the amino acid residue is Z5; (w) at positions 48 and/or 80 amino acid residues Z6; (x) at position 40 amino acid residues Z1 or Z2; (y) at position 96 amino acid residues Z3 or Z5; (z) at position 65 amino acid residues Z3, Z4 or Z6; (aa) at positions 84 and/or 115 amino acid residues Z3; (ab) at position 93 amino acid residues Z4; (ac) at position 130 amino acid residues Z2; (ad) at position 58 amino acid residues Z3, Z4 or Z6; (ae) at position 47 amino acid residues Z4 or Z6; (af) at positions 49 and/or 100 amino acid residues Z3 or Z4; (ag) at position 68 amino acid residues Z4 or Z5; (ah) at position 143 amino acid residues Z4; (ai) at position 131 the amino acid residue is Z5; (aj) at positions 125 and/or 128 the amino acid residue is Z5; (ak) at position 67 the amino acid residue is Z3 or Z4; (al) at position 60 amino acid residues Z5; and (am) at position 37 amino acid residues Z4 or Z6; characterized in that: Zl amino acid selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid selected from the group consisting of F, W and Y; Z3 is an amino acid selected from the group consisting of N, Q, S and T; Z4 is an amino acid selected from the group consisting of R, H and K; Z5 is an amino acid selected from the group consisting of D and E; Z6 is an amino acid selected from the group consisting of C, G and P. Some preferred isolated or recombinant polynucleotides of the invention encode an amino acid sequence further characterized in that the amino acid residues in the amino acid sequence corresponding to the positions specified in (a) - (am), at least 90% fit within the amino acid residue restrictions specified in (a) - (am). ;Some preferred isolated or recombinant polynucleotides of the invention encode an amino acid sequence in which the amino acid residues in the amino acid sequence corresponding to the following positions are at least 90% compatible with the following additional restrictions: (a) at positions 1, 7, 9, 13, 20, 36, 42, 46, 50, 56, 64, 70, 72, 75, 76, 78, 94, 98, 107, 110, 117, 118, 121 and/or 141 amino acid residues BI; and (b) at positions 16, 21, 22, 23, 25, 29, 34, 41, 43, 44, 55, 66, 71, 73, 74, 77, 85, 87, 88, 95, 99, 102, 108, 109, 111, 116, 122, 127, 133, 134, 136 and/or 137 are amino acid residues B2; wherein BI is an amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S and T. ;Some preferred isolated or recombinant polynucleotides of the invention encode an amino acid sequence such that when the sequence is optimally compared to SEQ ID NO: 300, 445 or 457, at least 90% of the SEQ ID NO: residues in the amino acid sequence match the following restrictions: (a) at positions 1, 7, 9, 13, 20, 42, 46, 50, 56, 64, 70, 72, 75, 76, 78, 94, 98, 107, 110, 117, 118, 121 and/or 141 amino acid residues BI; and (b) at positions 16, 21, 22, 23, 25, 29, 34, 36, 41, 43, 44, 55, 66, 71, 73, 74, 77, 85, 87, 88, 95, 99, 102, 108, 109, 111, 116, 122, 127, 133, 134, 136 and/or 137 amino acid residues B2; wherein BI is an amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S and T. ;Some preferred isolated or recombinant polynucleotides of the invention encode an amino acid sequence such that when the sequence is optimally matched to SEQ ID NO: 300, 445 or 457, at least 90% of the amino acid residues in the amino acid sequence match the following restrictions: (a) at positions 1, 7, 9, 20, 42, 50, 72, 75, 76, 78, 94, 98, 110, 121 and/or 141 amino acid residues Z1; (b) at positions 13, 46, 56, 70, 107, 117 and/or 118 amino acid residues Z2; (c) at positions 23, 55, 71, 77, 88 and/or 109 the amino acid residue is Z3; (d) at positions 16, 21, 41, 73, 85, 99 and/or 111 amino acid residues Z4; (e) at positions 34 and/or 95 amino acid residues Z5; (f) at positions 22, 25, 29, 43, 44, 66, 74, 87, 102, 108, 116, 122, 127, 133, 134, 136 and/or 137 amino acid residues Z6; characterized in that: Zl amino acid selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid selected from the group consisting of F, W and Y; Z3 is an amino acid selected from the group consisting of N, Q, S and T; Z4 is an amino acid selected from the group consisting of R, H and K; Z5 is an amino acid selected from the group consisting of D and E; Z6 is an amino acid selected from the group consisting of C, G and P. Certain preferred isolated or recombinant polynucleotides of the invention encode an amino acid sequence further comprising at position 36 an amino acid residue selected from the group consisting of Z1 and Z3. Certain preferred isolated or recombinant polynucleotides of the invention encode an amino acid sequence further comprising at position 64 an amino acid residue selected from the group consisting of Z1 and Z2. Some preferred isolated or recombinant polynucleotides of the invention encode an amino acid sequence such that when the sequence is optimally matched to SEQ ID NO: 300, 445 or 457, at least 80% of the amino acid residues in the amino acid sequence fit within the following restrictions: (a) at position 2 amino acid residues I or L; (b) at position 3 amino acid residues E; (c) at position 4 amino acid residues V or I; (d) at position 5 amino acid residues K; (e) at position 6 amino acid residues P; (f) at position 8 amino acid residues N; (g) at position 10 amino acid residues E; (h) at position 11 amino acid residues D or E; (i) at position 12 amino acid residues T; (j) at position 14 amino acid residues E or D; (k) at position 15 amino acid residues L; (1) at position 17 amino acid residues H; (m) at position 18 amino acid residues R, E or K; (n) at position 19 the amino acid residue is I or V; (o) at position 24 the amino acid residue is Q; (p) at position 26 the amino acid residue is M, L, V, or I; (q) at position 27 amino acid residues E; (r) at position 28 amino acid residues A or V; (s) at position 30 amino acid residues M; (t) at position 31 amino acid residues Y or F; (u) at position 32 the amino acid residue is E or D; (v) at position 33 amino acid residues T or S; (w) at position 35 amino acid residues L; (x) at position 37 amino acid residues R, G, E or Q; (y) at position 39 amino acid residues A or S; (z) at position 40 the amino acid residue is F or L; (aa) at position 45 amino acid residues Y or F; (ab) at position 47 amino acid residues R or G; (ac) at position 48 amino acid residues G; (ad) at position 49 amino acid residues K, R or Q; (ae) at position 51 amino acid residues I or V; (af) at position 52 amino acid residues S; (ag) at position 53 amino acid residues I or V; (ah) at position 54 amino acid residues A; (ai) at position 57 amino acid residues H or N; (aj) at position 58 are amino acid residues Q, K, R or P; (ak) at position 59 amino acid residues A; (al) at position 60 amino acid residues E; (am) at position 61 amino acid residues H or R; (an) at position 63 amino acid residues E or D; (ao) at position 65 amino acid residues E, P or Q; (ap) at position 67 amino acid residues Q or R; (aq) at position 68 amino acid residues K or E; (ar) at position 69 amino acid residues Q; (as) at position 79 amino acid residues E; (at) at position 80 amino acid residues G; (au) at position 81 the amino acid residue is Y, H or F; (av) at position 82 amino acid residues R; (aw) at position 83 amino acid residues E or D; (ax) at position 84 amino acid residues Q; (ay) at position 86 amino acid residues A; (az) at position 89 amino acid residues G, T or S; (ba) at position 90 amino acid residues L; (bb) at position 91 amino acid residues L, I or V; (bc) at position 92 amino acid residues R or K; (bd) at position 93 amino acid residues H; (be) at position 96 amino acid residues E or Q; (bf) at position 97 amino acid residues I; (bg) at position 100 amino acid residues K or N; (bh) at position 101 amino acid residues K or R; (bi) at position 103 amino acid residues A or V; (bj) at position 104 amino acid residues D; (bk) at position 105 amino acid residues M, L or I; (bi) at position 106 the amino acid residue is L; (bm) at position 112 the amino acid residue is T or A; (bn) at position 113 amino acid residues S or T; (bo) at position 114 amino acid residues A; (bp) at position 115 amino acid residues S; (bq) at position 119 amino acid residues K or R; (br) at position 120 amino acid residues K or R; (bs) at position 123 amino acid residues F or L; (bt) at position 125 amino acid residues E; (bu) at position 126 amino acid residues Q or H; (bv) at position 128 the amino acid residue is E or D; (bw) at position 129 amino acid residues V or I; (bx) at position 130 amino acid residues F; (by) at position 131 amino acid residues D or E; (bz) at position 132 amino acid residues T; (ca) at position 135 amino acid residues V; (cb) at position 138 amino acid residues H; (cc) at position 139 amino acid residues I; (cd) at position 140 amino acid residues L or M; (ce) at position 142 the amino acid residue is Y; (cf) at position 143 the amino acid residue is K or R; (cg) at position 145 amino acid residues L or I; and (ch) at position 146 amino acid residues T. Some preferred isolated or recombinant polynucleotides of the invention encode an amino acid sequence such that when the sequence is optimally compared to SEQ ID NO: 300, 445 and 457, at least 90% of the amino acid residues in the amino acid sequence fit within the amino acid residue restrictions specified in (a) - (ch) in to the text above. ;Some preferred isolated or recombinant polynucleotides of the invention are selected from the group consisting of: (a) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 577; (b) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO: 578; (c) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO: 621; (d) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 579; (e) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 602; (f) a nucleotide sequence encoding an amino acid sequence that is at least 95% identical to SEQ ID NO: 697; (g) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO: 721; (h) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO: 613; (i) a nucleotide sequence encoding an amino acid sequence that is at least 89% identical to SEQ ID NO: 677; (j) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO: 584; (k) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 707; (1) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO: 616; (m) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO: 612; (n) a nucleotide sequence that encodes an amino acid sequence that is at least 98% identical to SEQ ID NO: 590, and further indicated that the amino acid residues in the amino acid sequence corresponding to the following positions at least 80% fit the following restrictions: (a) at positions 9, 76, 94 and 110 amino acid residues A; (b) at positions 29 and 108 amino acid residues C; (c) at position 34 amino acid residues D; (d) at position 95 the amino acid residue is E; (e) at position 56 amino acid residues F; (f) at positions 43, 44, 66, 74, 87, 102, 116, 122, 127 and 136 amino acid residues G; (g) at position 41 the amino acid residue is H; (h) at position 7 the amino acid residue is I; (i) at position 85 the amino acid residue is K; (j) at position 20, 42, 50, 78 and 121 amino acid residues L; (k) at position 1 and 141 amino acid residues M; (1) at position 23 and 109 amino acid residues N; (m) at positions 22, 25, 133, 134 and 137 are amino acid residues P; (n) at position 71 amino acid residues Q; (o) at positions 16, 21, 73, 99 and 111 amino acid residues R; (p) at position 55 amino acid residues S; (q) at position 77 amino acid residues T; (r) at position 107 amino acid residues W; (s) at positions 13, 46, 70 and 118 the amino acid residues are Y. Some preferred isolated or recombinant polynucleotides of the invention encode an amino acid sequence that further comprises at least one amino acid residue that meets the following criteria: (a) at position 14 the amino acid residue is D; (b) at position 18 amino acid residues E; (c) at position 26 amino acid residues M or V; (e) at position 30 amino acid residues I; (f) at position 32 amino acid residues D; (g) at position 36 the amino acid residue is M or T; (h) at position 37 amino acid residues C; (i) at position 38 amino acid residues D; (j) at position 53 the amino acid residue is V; (k) at position 58 the amino acid residue is R; (1) at position 61 the amino acid residue is R; (m) at position 62 the amino acid residue is L; (n) at position 64 the amino acid residue is I or F; (o) at position 65 the amino acid residue is P; (p) at position 72 amino acid residues I; (q) at position 75 amino acid residues V; (r) at position 88 amino acid residues T; (s) at position 89 amino acid residues G; (t) at position 91 amino acid residues L; (u) at position 98 amino acid residues I; (v) at position 105 amino acid residues I; (w) at position 112 amino acid residues A; (x) at position 124 amino acid residues G or C; (y) at position 128 the amino acid residue is D; (z) at position 140 the amino acid residue is M; (aa) at position 143 amino acid residues R; and (ab) at position 144 amino acid residues W. ;Some preferred isolated or recombinant polynucleotides of the invention encode an amino acid sequence such that when the sequence is optimally compared to SEQ ID NO: 300, 445 and 457, at least 80% of the amino acid residues in the amino acid sequence fit within the amino acid residue restrictions specified in (a) through (ab) in the text. above. ;Some preferred isolated or recombinant polynucleotides of the invention comprise a nucleotide sequence encoding an amino acid sequence selected from the group consisting of: (a) an amino acid sequence that is at least 96% identical to SEQ ID NO: 919 (such as SEQ ID NO: 917, 919, 921, 923, 925, 927, 833, 835, 839, 843, 845, 859, 863, 873, 877, 891, 895, 901, 905, 907, 913, 915 or 950); (b) an amino acid sequence that is at least 97% identical to SEQ ID NO: 929 (such as SEQ ID NO: 929, 931, 835, 843, 849 or 867); (c) an amino acid sequence that is at least 98% identical to SEQ ID NO: 847 (such as SEQ ID NO: 845 or 847); (d) an amino acid sequence that is at least 98% identical to SEQ ID NO: 851; (e) an amino acid sequence that is at least 98% identical to SEQ ID NO: 853; (f) an amino acid sequence that is at least 98%> identical to SEQ ID NO: 855 (such as SEQ ID NO: 835 or 855); (g) an amino acid sequence that is at least 98% identical to SEQ ID NO: 857; (h) an amino acid sequence that is at least 98% identical to SEQ ID NO: 861 (such as SEQ ID NO: 839, 861 or 883); (i) an amino acid sequence that is at least 98% identical to SEQ ID NO: 871; (j) an amino acid sequence that is at least 98% identical to SEQ ID NO: 875; (k) an amino acid sequence that is at least 98% identical to SEQ ID NO: 881; (1) an amino acid sequence that is at least 98% identical to SEQ ID NO: 885 (such as SEQ ID NO: 845 or 885); (m) an amino acid sequence that is at least 98% identical to SEQ ID NO: 887; (n) an amino acid sequence that is at least 98% identical to SEQ ID NO: 889 (such as SEQ ID NO: 863, 889, 891 or 903); (o) an amino acid sequence that is at least 98% identical to SEQ ID NO: 893; (p) an amino acid sequence that is at least 98% identical to SEQ ID NO: 897; (q) an amino acid sequence that is at least 98% identical to SEQ ID NO: 899; (r) an amino acid sequence that is at least 98% identical to SEQ ID NO: 909 (such as SEQ ID NO: 883 or 909); (s) an amino acid sequence that is at least 98% identical to SEQ ID NO: 911; (t) an amino acid sequence that is at least 99% identical to SEQ ID NO: 837; (u) an amino acid sequence that is at least 99% identical to SEQ ID NO:841; (v) an amino acid sequence that is at least 99% identical to SEQ ID NO: 865; (w) an amino acid sequence that is at least 99% identical to SEQ ID NO: 869; (x) an amino acid sequence that is at least 99% identical to SEQ ID NO: 879. ; Some preferred isolated or recombinant polynucleotides of the invention are selected from the group consisting of: (a) an amino acid sequence that is at least 96% identical to SEQ ID NO: 919 (such as a nucleotide sequence such as SEQ ID NO: 916, 918, 920, 922, 924, 926, 832, 834, 838, 842, 844, 858, 862, 872, 876, 890, 894, 900, 904,906,912,914,939, 940, 941, 942, 943, 944, 949, 951 or 952); (b) an amino acid sequence that is at least 97% identical to SEQ ID NO: 929 (such as a nucleotide sequence such as SEQ ID NO: 928, 930, 834, 842, 848, 866, 936 or 937); (c) an amino acid sequence that is at least 98% identical to SEQ ID NO: 847 (such as a nucleotide sequence such as SEQ ID NO: 844 or 846); (d) an amino acid sequence that is at least 98% identical to SEQ ID NO: 851 (such as a nucleotide sequence such as SEQ ID NO: 852); (e) an amino acid sequence that is at least 98% identical to SEQ ID NO: 853 (for example a nucleotide sequence such as SEQ ID NO: 852); (f) an amino acid sequence that is at least 98% identical to SEQ ID NO: 855 (such as a nucleotide sequence such as SEQ ID NO: 834 or 854); (g) an amino acid sequence that is at least 98% identical to SEQ ID NO: 857 (such as a nucleotide sequence such as SEQ ID NO: 856); (h) an amino acid sequence that is at least 98% identical to SEQ ID NO: 861 (such as a nucleotide sequence such as SEQ ID NO: 838, 860 or 882); (i) an amino acid sequence that is at least 98% identical to SEQ ID NO: 871 (such as a nucleotide sequence such as SEQ ID NO: 870); (j) an amino acid sequence that is at least 98% identical to SEQ ID NO: 875 (such as a nucleotide sequence such as SEQ ID NO: 874); (k) an amino acid sequence that is at least 98% identical to SEQ ID NO: 881 (such as a nucleotide sequence such as SEQ ID NO: 880); (1) an amino acid sequence that is at least 98% identical to SEQ ID NO: 885 (such as a nucleotide sequence such as SEQ ID NO: 844 or 884); (m) an amino acid sequence that is at least 98% identical to SEQ ID NO: 887 (such as a nucleotide sequence such as SEQ ID NO: 886); (n) an amino acid sequence that is at least 98% identical to SEQ ID NO: 889 (such as a nucleotide sequence such as SEQ ID NO: 862, 888, 890 or 902); (o) an amino acid sequence that is at least 98% identical to SEQ ID NO: 893 (such as a nucleotide sequence such as SEQ ID NO: 892); (p) an amino acid sequence that is at least 98% identical to SEQ ID NO: 897 (such as a nucleotide sequence such as SEQ ID NO: 896); (q) an amino acid sequence that is at least 98% identical to SEQ ID NO: 899 (such as a nucleotide sequence such as SEQ ID NO: 898); (r) an amino acid sequence that is at least 98% identical to SEQ ID NO: 909 (such as a nucleotide sequence such as SEQ ID NO: 882 or 908); (s) an amino acid sequence that is at least 98% identical to SEQ ID NO: 911 (such as a nucleotide sequence such as SEQ ID NO: 910); (t) an amino acid sequence that is at least 99% identical to SEQ ID NO: 837 (such as a nucleotide sequence such as SEQ ID NO: 836; (u) an amino acid sequence that is at least 99% identical to SEQ ID NO: 841 (such as a nucleotide sequence such as SEQ ID NO: 840); (v) an amino acid sequence that is at least 99% identical to SEQ ID NO: 865 (such as a nucleotide sequence such as SEQ ID NO:864); (w) an amino acid sequence that is at least 99% identical to SEQ ID NO: 869 (such as a nucleotide sequence such as SEQ ID NO: 868); (x) an amino acid sequence that is at least 99% identical to SEQ ID NO: 879 a sequence such as SEQ ID NO:878). ;Some preferred isolated or recombinant polynucleotides of the invention comprise a nucleotide sequence encoding an amino acid sequence that is at least 95% identical to SEQ ID NO:929 and that contains a Gly or ASN residue at the amino acid position corresponding to position 33 of SEQ ID NO:929 (such as, for example, a nucleotide sequence encoding SEQ ID NO: 837, 849, 893, 897, 905, 921, 927, 929 or 931). Some preferred isolated or recombinant polynucleotides of the invention comprise a nucleotide sequence that encodes an amino acid sequence that is at least 95% identical to SEQ ID NO:929 and that contains a Gly or ASN residue at the amino acid position corresponding to position 33 of SEQ ID NO:929 (such as, for example, a nucleotide sequence as SEQ ID NO:929 NO: 836, 848, 892, 896, 904, 920, 926, 928, 930, 938). Some preferred isolated or recombinant polynucleotides of the invention encode an amino acid sequence that further contains one or more amino acid residues that meet the following criteria: (a) at position 41 an amino acid residue H, (b) at position 138 an amino acid residue H, (c) at position 34 an amino acid residue N, and (d) at position 55 an amino acid residue S. ;While the description polypeptide of the invention is sometimes presented here as a list of possible restrictions on which amino acid residues are located at certain positions, in some embodiments the polypeptide of the invention satisfies all possible restrictions of a certain group of restrictions. ;This means that in some places here - the list of possible restrictions is expressed as a list of options associated with a conjunction "and/or" and in some embodiments each of these conjunctions functions as "and" rather than "or". In some embodiments, possible restrictions expressed as fallbacks are found in the polypeptide of the invention; this is true only for fallbacks that are not mutually exclusive. ;Sequence Variations ;Those of ordinary skill in the art will appreciate that the inherent nature of the genetic code can produce numerous nucleotide sequences encoding the GAT polypeptides of the invention, some of which bear substantial identity to the nucleic acid sequences explicitly disclosed herein. For example, a look at the codon table (Table 1) indicates that the codons AGA, AGG, CGA, CGC, CGG, and CGU all code for the amino acid arginine. Therefore, at each position of the nucleic acids of the present invention in which arginine is designated by a codon, the codon may be changed to any of the corresponding codons, as described above, without a change in the coding polypeptide. It is understood that "U" in The RNA sequence corresponds to the "T" in the DNA sequence. Using as an example, a nucleic acid sequence corresponding to nucleotides 1-15 of SEQ ID NO:1 (ATG ATT GAA GTC AAA (SEQ ID NO:862)), silent variations of these sequences include ATG ATC GAG GTG AAG (SEQ ID NO:827); both sequences encode the amino acid sequence MIEVK (SEQ ID NO:828) corresponding to amino acids 1-5; SEQ ID NO:6. Such "silent variations" are one type of "conservatively modified variation" discussed below. Those skilled in the art will recognize that any codon in a nucleic acid (except AUG, which is usually the only codon for methionine) can be modified by standard techniques to encode a functionally identical polypeptide. Accordingly, any silent variation of the polypeptide-encoding nucleic acid is implicit in any described sequence. The present invention provides for every possible variation of the nucleic acid sequence encoding the polypeptide of the invention that can be made by selecting combinations based on possible codon choices. These combinations are made according to the standard "triplet" genetic code (eg, as shown in Table 1), as applied to the nucleic acid sequence encoding the GAT homologous polypeptide of the invention. All such variations for each nucleic acid are specifically provided herein and described by reference to the sequence in combination with the genetic code. Any variant may be produced as described herein. ;A group of two or more different codons which, when translated in the same context, encode the same amino acid are referred to herein as "synonymous codons". As described herein, in some aspects of the invention a GAT polynucleotide is engineered to optimize codon usage in a desired host organism, for example a plant host. The term "optimized" or "optimal" is not intended to restrict to the best possible combination of codons but simply indicate that the coding sequence as a whole has improved codon usage compared to the precursor polynucleotide from which it was derived. Therefore, in one aspect, the invention provides a method for producing a variant GAT polynucleotide by replacing at least one parental codon in a nucleotide sequence with a synonymous codon that is preferentially used in a desired host organism, for example a plant, over the parental codon. ;"Conservatively modified variations" or simply "conservative variations" of a particular nucleic acid sequence, refers to those nucleic acids that encode identical or substantially identical amino acid sequences, or where the nucleic acid does not encode an amino acid sequence to substantially identical sequences. The skilled artisan will recognize that single substitutions, deletions or additions that change, add, or delete a single amino acid or a small percentage of amino acids (typically less than 5%, more typically less than 4%, 2%, or 1%, or less) in the coding sequence represent "conservatively modified variations", where the changes result in the deletion of an amino acid, the addition of an amino acid, or the replacement of an amino acid with a chemically similar amino acid. Tables of conservative substitutions that provide functionally similar amino acids are well known in the art. Table 2 shows six groups containing amino acids that represent "conservative substitutions" for each other. Therefore, "conservative substitution variations" of the polypeptide sequence listed in this invention include substitutions with a small percentage, typically less than 5%, more typically less than 2% and most often less than 1% - of an amino acid of the polypeptide sequence, with a conservatively selected amino acid of the same conservative substitution group. Therefore, a conservatively substituted variation of the polypeptide of the invention may contain 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 substitutions with a conservatively substituted variation of the same conservatively substituted group. ;For example, a conservatively substituted variation of the polypeptide identified herein as SEQ ID NO:6 will contain "conservative substitutions" in accordance with the 6 groups defined above, in as many as 7 residues (ie, 5% amino acids) in a polypeptide consisting of 146 amino acids. ;In a further example, if the four conservative substitutions are located in the region corresponding to amino acids 21-30 of SEQ ID NO:6, examples of conservatively substituted variations of this region, ;RPN QPL EAC M (SEQ ID NO:829), include: ;KPQ QPV ESC M (SEQ ID NO:830) and ;KPN NPL DAC V (SEQ ID NO:831) and the like, according to the conservative substitutions shown in Table 2 (in the example above, conservative substitutions are underlined). The protein sequence listing shown here in conjunction with the substitution table shown above provides an express listing of all conservatively substituted proteins. ;Finally, adding non-changing sequences an encoded activity of a nucleic acid molecule, such as the addition (addition) of a non-functional or non-coding sequence, is a conservative variation of the basic nucleic acid. The skilled artisan will recognize that many conservative variations of the nucleic acid constructs described herein result in the creation of a functionally identical construct. For example, as discussed above, by virtue of the innateness of the genetic code "silent substitutions" (ie, substitutions in a nucleic acid sequence that do not result in a change in the coding polypeptide) are traits encompassed within each nucleic acid sequence that encodes an amino acid. Similarly, "conservative amino acid substitutions" in one or more amino acids in the amino acid sequence are replaced with different amino acids having very similar properties, also simply identified as those that are remarkably similar to the disclosed construct. Such conservative variations of each disclosed sequence are a feature of the present invention. ;Non-conservative modifications of a particular nucleic acid are those that replace any amino acid that is not characterized as a conservative substitution, for example any substitution that exceeds the limit of 6 groups shown in Table 2. This includes substitutions of basic or acidic amino acids with neutral amino acids (for example, Asp, Glu, Asn or Gln for Val, Ile, Leu or Met), aromatic amino acids for basic or acidic amino acids (for example, Phe, Tyr or Trp for Asp, Asn, Glu or Gln), or any substitution that does not replace an amino acid with a similar amino acid. ;Hybridization of Nucleic Acids ;Nucleic acids "hybridize" when linked typically in solution. Nucleic acids hybridize due to various well-characterized physical and chemical forces such as hydrogen bonding, solvent exclusion, base lag, and the like. Detailed instructions for hybridization can be found in Tijssen (1993) Laboratory Techniques in Biochemistry and Molecular Biology — Hybridization with Nucleic Acid Probes, Part I, Chapter 2, "Overview of principles of hybridization and the strategy of nucleic acid probe assays," (Elsevier, New York (Tijssen")), as well as in Ausubel, cited above, Hames and Higgins (1995) Gene Probes I, IRL Press at Oxford University Press, Oxford, England (" Hames and Higgins 1") (1995) Gene Probes 2, IRL Press at Oxford University Press, Oxford, England (" Hames and Higgins 2") and provide details of synthesis, labeling, detection and quantification of DNA and RNA, including oligonucleotides. "Restrictive washing conditions during hybridization" in the context of nucleic acid hybridization experiments such as Southern and Northern hybridizations are sequence dependent and vary in different environmental parameters. Detailed instructions for nucleic acid hybridization are found in Tijsenn (1993), supra, and Hames and Higgins 1 and Hames and Higgins 2, supra. ;For the purposes of this of the invention generally "highly restrictive" hybridization and elution conditions are selected to be approximately 5°C or less lower than the thermal melting point (Tm) for a specific sequence at a defined ionic strength and Ph (as noted in the text below), highly restrictive conditions may also be designated in comparative terms. Dark temperature (at a defined ionic strength and pH) at which 50% of the tested sequence hybridizes with a probe that fully matches the sequence. Highly restrictive conditions were chosen to be equal to the Tm of the respective probe. The temperature of a nucleic acid duplex indicates the temperature at which 50% of the duplex is denatured, under given conditions, and is a direct measure of the stability of the nucleic acid hybrid. Therefore, Tmod refers to the temperature corresponding to the middle point in the transition from the helix structure to the random coil structure ("random coil") and depends on the length of the nucleotide composition and the ionic strength for long sequences of nucleotides. ;After hybridization unhybridized nucleic acid material can be removed by a series of washes, where the stringency can be adjusted depending on the desired results. Less restrictive washing conditions (for example, using high salt concentration and lower temperature) increase sensitivity, but may produce atypical hybridization signals and high background signals (noise). Highly restrictive conditions (for example, using a lower salt concentration and a higher temperature closer to the hybridization temperature) reduce the background signal, and typically only the specific signal remains. See Raplev, R and Walker, J.M. eds., Molecular Biomethods Handbook (Humana Press, Inc. 1998) (hereinafter referred to as "Raplev and Walker") which is hereby incorporated by reference in its entirety for all purposes. ;Tmod of the DNA-DNA duplex can be estimated using Equation 1, as follows: ;Tm(°C) = 82.5°C + 16.6 (logi0M) + 0.41 (%G + C) - 0.72 (%f) - 500/n ; Where M is the molarity of the monovalent cation (most often Na+), (%G + C) is the percentage of guanosine (G) and cytosine (C) nucleotides, (%f) is the percentage of formalized (formalization) and the number of nucleotide bases (length) of the hybrid. See Raplev and Walker, already cited. ;Tmod of the RNA-DNA duplex can be estimated using Equation 2, as follows: ;Tm(°C) = 79.8°C + 18.5 (log10M) + 0.58 (%G +C) - 11.8 (%G + C) <2>- 0.56 (%f) - 820/n, Where M is the molarity of the monovalent cation (most often Na+), (%G + C) is the percentage of guanosine (G) and cytosine (C) nucleotides, (%f) is the percentage of formalized (formalization) and the number of nucleotide bases (length) of the hybrid. The same. ;Equations 1 and 2 are typically only true for hybrid duplexes greater than approximately 100-200 nucleotides in length. The same ;Tm for nucleic acid sequences shorter than 50 nucleotides can be calculated as follows: ;Tm (°C) = 4(G + C) + 2(A + T), ;Where A (adenine), C, T (thymine) and G (guanosine) are the numbers of the corresponding nucleotides. An example of restrictive hybridization conditions for hybridization of complementary nucleic acids possessing more than 100 complementary residues on a Southern or Northern blot filter is 50% formalin with lmg heparin at 42°C, with hybridization performed overnight. An example of restrictive washing conditions is washing in 0.2 x SSC at 65°C for 15 minutes (see Sambrook, supra, for a description of SSC buffer). ;Often, a high-restriction wash is performed after a low-restriction wash, to remove the background probe signal. An example of a low restriction wash is 2 x SSC at 40°C for 15 minutes. ;Generally, a signal-to-noise ratio of 2.5x - 5x (or higher) than that detected for an unrelated probe in a particular hybridization assay indicates detection of specific hybridization. Detection of at least restriction hybridization between two sequences in the context of the present invention indicates relatively strong structural similarity or homology to, for example, the nucleic acids of the present invention provided herein in the sequence listings. As noted "highly restrictive" conditions are selected to be about 5°C or less lower than the thermal melting point (Tm) for a specific sequence at a defined ionic strength and pH. Target sequences that are closely related or identical to the nucleotide sequence of interest (eg "probes") can be identified under highly restrictive conditions. Lower restriction conditions are suitable for sequences that are less complementary. See, for example, Raplev and Walker, supra. Comparative hybridization can be used to identify nucleic acids of the invention and this method of comparative hybridization is a preferred method for distinguishing nucleic acids of the invention. Detection of highly restrictive hybridization between two nucleotide sequences, in the context of the present invention, indicates relatively strong structural similarity/homology to, for example, the nucleic acids provided herein in the sequence listing. Highly restrictive hybridization between two nucleotide sequences demonstrates a degree of structural similarity or homology of the nucleotide base composition of the arrangement or ordering that is greater than that detected by restrictive hybridization conditions. In particular, high restriction hybridization detection in the context of the present invention indicates strong structural similarity or structural homology (eg, nucleotide structure, base composition, arrangement, or arrangement) to, for example, nucleic acids provided herein in the sequence listing. For example, it is desirable to identify a test nucleic acid that hybridizes to the exemplary nucleic acids herein, under restrictive conditions. ;Therefore, one measure of restriction hybridization is the ability to hybridize to one of the nucleic acids listed (for example nucleic acid sequences SEQ ID NO: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 534, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 620, 622, 624, 626, 628, 630, 632, 634, 636, 638, 640, 642, 644, 646, 648, 650, 652, 654, 656, 658, 660, 662, 664, 666, 668, 670, 672, 674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726, 728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788, 790, 792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814, 816, 818, 820, 822, 824, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916, 918, 920, 922, 924, 926, 928, 930, 932, 933, 934, 935, 936, 937, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952, and their complementary polynucleotide sequences under highly restrictive conditions (or under extremely restrictive conditions, or ultra highly restrictive hybridization conditions or ultra-ultra highly restrictive hybridization conditions). Restrictive hybridization (as well as highly restrictive, ultra highly restrictive, or ultra-ultra highly restrictive hybridization conditions) and washing conditions can be easily determined empirically for any nucleic acid being tested. For example, in determining the conditions for highly restrictive hybridization and washing, the hybridization and washing conditions are gradually increased (for example, by increasing the temperature, decreasing the salt concentration, increasing the detergent concentration, and/or increasing the concentration of organic solvents such as formalin in the hybridization or washing), until a selected set of criteria is satisfied. For example, hybridization and washing conditions are gradually increased until a probe containing one or more nucleic acid sequences selected from SEQ ID NO: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 534, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 620, 622, 624, 626, 628, 630, 632, 634, 636, 638, 640, 642, 644, 646, 648, 650, 652, 654, 656, 658, 660, 662, 664, 666, 668, 670, 672, 674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726, 728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788, 790, 792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814, 816, 818, 820, 822, 824, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916, 918, 920, 922, 924, 926, 928, 930, 932, 933, 934, 935, 936, 937, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952, and their complementary polynucleotide sequences do not bind to their complementary target sequence (perfect match) (again, a nucleic acid comprising one or more nucleic acid sequences selected from SEQ ID NOs: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 534, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 620, 622, 624, 626, 628, 630, 632, 634, 636, 638, 640, 642, 644, 646, 648, 650, 652, 654, 656, 658, 660, 662, 664, 666, 668, 670, 672, 674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726, 728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788, 790, 792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814,816,818,820,822,824, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916, 918, 920, 922, 924, 926, 928, 930, 932, 933, 934, 935, 936, 937, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952, and their complementary polynucleotide sequences with a signal-to-noise ratio of at least about 2.5x, and optionally about 5x or more - as big as the one that is being tested for hybridization a target sequence that does not correspond to it (unmatched target). In this case, the non-matching target sequence is a nucleic acid that matches a nucleic acid (other than that in the accompanying sequence list) that is present in a public database such as GenBank™ at the time this application is filed. Such sequences can be identified by an expert in GenBank. Examples include accession numbers Z99109 and Y09476. Additional such sequences may be identified in, for example, GenBank by the ordinary scientific researcher. ;A test nucleic acid is said to hybridize specifically to a nucleic acid probe when it hybridizes at least Vi to both the probe and a perfectly matching complementary target sequence, ie. with a signal-to-noise ratio that is at least as high as that ratio for hybridization of a probe to a target sequence under conditions in which a perfectly matched probe binds to a complementary perfect-matched target sequence with a signal-to-noise ratio of at least 2x to 10x, and occasionally 20x, 50x, or more than that recorded for hybridization for mismatched polynucleotides from accession numbers Z99109 and Y09476. ;Ultra highly restrictive hybridization and wash conditions are those in which the stringency of the hybridization and wash conditions is increased until a signal-to-noise ratio is obtained that is at least 10x greater than that obtained for hybridization with any mismatched target nucleic sequence, from GenBank accession numbers Z99109 and Y09476. A target nucleic acid that hybridizes to a probe under these conditions, with a signal-to-noise ratio of at least Viu relative to that observed with a perfectly matched complementary target nucleic acid, is said to bind to the probe under ultra-high-stringency conditions. Similarly, even higher levels of stringency can be determined by stepwise amplification of hybridization conditions and/or washing of the relevant hybridization assay. For example, those in which the hybridization and washing conditions are intensified up to the ratio the signal-to-noise for probe binding to the completed matched complementary target nucleic acid is at least 10x, 20x, 50x, 100x, or 500x or more as high as that obtained for hybridization to any mismatched target nucleic acid from GenBank accession numbers Z99109 and Y09476. A target nucleic acid that hybridizes to a probe under these conditions, with a signal-to-noise ratio of at least Vi relative to that of a perfectly matched complementary target nucleic acid, is said to bind to the probe under ultra-ultra highly restrictive conditions. ;Target nucleic acids that hybridize to nucleic acids represented by SEQ ID NO: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 534, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556,557,558,559,560,561,562,563,564,565,566, 567,620,622, 624, 626, 628, 630, 632, 634, 636, 638, 640, 642, 644, 646, 648, 650, 652, 654, 656, 658, 660, 662, 664, 666, 668, 670, 672, 674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706,708,710,712,714,716,718,720, 722,724, 726, 728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788, 790, 792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814, 816, 818, 820, 822, 824, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916, 918, 920, 922, 924, 926, 928, 930, 932, 933, 934, 935, 936, 937, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951, and 952 under high, ultra-high, and ultra-ultra high restriction conditions are a feature of this invention. Examples of such nucleic acids include those with one or more silent or conservative nucleic acid substitutions when compared to a given nucleic acid sequence. Nucleic acids that do not hybridize to each other under restrictive conditions are still substantially identical if the polypeptides they encode are substantially identical. This occurs, for example, when a nucleic acid copy is created using the maximum genetic codon abundance allowed by the genetic code, or when an antiserum or antisera are raised against one or more of SEQ ID NOs: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597, 598, 599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 665, 667, 669, 671, 673, 675, 677, 679, 681, 683, 685, 687, 689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811, 813, 815, 817, 819, 821, 823, 825, 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 929,931,953,954,955,956,957,958,959,960,961,962,963,964, 965, 966, 967, 968, 969, 970, 971 and 972, which were isolated using polypeptides encoded by known nucleotide sequences, including those of GenBank accession number CAA70664. Further details on the immunological identification of polypeptides of the invention are provided in the text that follows. Additionally, to distinguish between duplexes with sequences of less than about 100 nucleotides, the TMAC1 hybridization procedure known to those skilled in the art can be used. See for example Sorg. U, et al. Nucleic Acids, Res.(Sept 11, 1991) 19(17), incorporated herein for all purposes in its entirety with by reference. ;In one aspect the invention provides a nucleic acid comprising a unique subsequence in a nucleic acid selected from SEQ ID NO: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 534, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 620, 622, 624, 626, 628, 630, 632, 634, 636, 638, 640, 642, 644, 646, 648, 650, 652, 654, 656, 658, 660, 662, 664, 666, 668, 670, 672, 674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726, 728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788, 790, 792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814, 816, 818, 820, 822, 824, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902,904, 906, 908,910, 912, 914, 916, 918,920, 922, 924, 926, 928, 930, 932, 933, 934, 935, 936, 937, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952. The unique subsequence is unique when compared to the nucleic sequence corresponding to any of GenBank accession numbers Z99109 and Y09476. Such unique subsequences can be determined by comparing any of SEQ ID NOs: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 534, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 620, 622, 624, 626, 628, 630, 632, 634, 636, 638, 640, 642, 644, 646, 648, 650, 652, 654, 656, 658, 660, 662, 664, 666, 668,670, 672, 674, 676, 678, 680, 682, 684, 686, 688,690,692, 694,696,698, 700, 702, 704, 706, 708, 710, 712, 714,716,718, 720, 722, 724, 726, 728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788,790,792,794, 796, 798, 800, 802, 804, 806, 808, 810,812,814, 816, 818, 820, 822, 824, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904,906, 908,910,912,914, 916, 918, 920, 922, 924, 926, 928, 930,932,933, 934, 935, 936, 937, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952 with the complete nucleic acid pool represented by GenBank accession numbers Z99109 and Y09476 or with other related sequences available in public databases as of the filing date of the application in question. The comparison can be performed using the BLAST algorithm with set standard parameters. Each unique subsequence is useful, for example, as a probe for identifying nucleic acids of the invention. ;Similarly, the invention includes a polypeptide comprising a unique subsequence in the polypeptide selected from SEQ ID NO: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597, 598, 599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 665, 667, 669, 671, 673, 675, 677, 679, 681, 683, 685, 687, 689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711,713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811, 813, 815, 817, 819, 821, 823, 825, 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 929, 931, 953, 954, 955, 956, 957, 958, 959, 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971 and 972. Here, the unique subsequence is unique when compared to the polypeptide corresponding to GenBank accession number CAA70664. Here again the polypeptide is compared to the sequences represented by accession number CAA70664. It should be noted that if the sequence corresponds to a non-translating sequence such as a pseudo gene, the corresponding polypeptide is obtained simply by in silico translation of the nucleic acid sequence into an amino acid sequence, in which the reading frame is selected to match the reading frame of homologous GAT polynucleotides. ;The invention also provides target nucleic acids that hybridize under restrictive (stringent) conditions with a uniquely encoding oligonucleotide encoding a unique subsequence in a polypeptide selected from SEQ ID NO: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597, 598, 599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 665, 667, 669, 671, 673, 675, 677, 679, 681, 683, 685, 687, 689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811, 813, 815, 817, 819, 821, 823, 825, 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 929, 931, 953, 954, 955, 956, 957, 958, 959, 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971 and 972 indicated that a unique subsequence is unique when compared to the corresponding polypeptide of any of the control polypeptides. Unique sequences were determined as described above in the text. ;In one example, the restriction conditions are selected so that the perfectly complementary oligonucleotide to the coding oligonucleotide hybridizes to the coding oligonucleotide with at least about 2.5x-10x higher, preferably at least about 5-10x higher signal-to-noise ratio than for hybridization of the perfectly complementary oligonucleotide to the control nucleic acid corresponding to any of the control polypeptides. Conditions can be chosen so that higher signal-to-noise ratios are detected in the particular assay being used, for example 15x, 20x, 30x, 50x or more. In this example, the target nucleic acid hybridizes to the unique coding oligonucleotide with at least a 2x higher signal-to-noise ratio when compared to hybridization of the control nucleic acid to the coding oligonucleotide. Again, a higher signal-to-noise ratio can be chosen for example, about 2.5x, 5x, 10x, 20x, 30x, 50x, or more - The specific signal will depend on the label used in the assay, for example, fluorescent label (dye), colorimetric label, radioactive label or the like. ;Vectors, Promoters and Expression Systems ;The present invention also includes recombinant constructs containing one or more of the nucleic acid sequences described in detail above. Constructs include a vector such as a plasmid, cosmid, phage, virus, bacterial artificial chromosome (VHB), yeast artificial chromosome (VHC) and the like into which a nucleic acid sequence of the invention has been inserted in a forward or reverse orientation. In a preferred aspect of this embodiment, the construct further comprises regulatory sequences, including for example a promoter operably linked to the sequence. A large number of suitable vectors and promoters are known to those skilled in the art and are available from commercial sources. As previously discussed, general texts describing molecular biology techniques useful for this invention including the use of vectors, promoters, and many other relevant techniques include Berger and Kimmel, Guide to molecular CloningTechniques, Methods in Enzymology Volume 152, (Academic Press, Inc., San Diego, CA) (Berger; Sambrook et al, molecular Cloning - A Laboratory Manual, 2d ed, Vol. 1-3, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, 1989 ("Sambrook") and Current Protocols in Molecular Biology, F.M. Ausubel, eds., a joint publication by Greene Publishing Associates, Inc. and John Wiley & Sons, Inc., (Supplement to 1999) Examples of protocols sufficient to guide those skilled in the art through in vitro amplification methods, ligase chain reaction (LCR), amplification by Qp replicase and other RNA polymerase (eg NASBA) mediated techniques, for example for the production of homologous nucleic acids of the invention, can be found in Berger, Sambrook, and Ausubel, as well as in Mullisat al. (1987) U.S. Patent No. 4,683,202; Innisset al, eds. (1990). (1990) Proc. Nat'l. Sci. USA 87: 1874; 1989) J. Clin. Chem35: 1826; Landegrenet al. (1988) Science 241: 1077-1080; Van Brunt (1990) Biotechnology8: 291-294; Wu and Wallace (1989) Gene4:560; Barringer et al. (1990) Gene89:117; and Sooknanan and Malek (1995) Biotechnology 13: 563-564. Improved methods for cloning in vitro amplified nucleic acids are described in Wallace et al, U.S. Pat. Pat. No. 5,426,039. Improved methods for amplification of large nucleic acids by PCR are described in Chenget al. (1994) Nature 369:684-685 and references cited therein, wherein PCR amplified products (amplicons) up to 40 kb. One skilled in the art will appreciate that essentially any RNA can be converted to double-stranded DNA amenable to restriction digestion, PCR amplification and sequencing by reverse transcriptase and polymerase. Also, see for example Ausubel, Sambrook and Berger - all mentioned earlier in the text. The present invention also relates to engineered host cells transduced (transformed or transfected) with a vector of the invention (for example a cloning vector of the invention or an expression vector of the invention), as well as to the production of polypeptides of the invention by recombination techniques. A vector can be, for example, a plasmid, a viral particle, a phage, etc. Engineered host cells can be cultured in a conventional nutrient medium that has been modified in order to activate the promoter, select transformants, or amplify the GAT homologous gene. The culture conditions, such as temperature, pH, and the like, are those already used for the host cell selected for expression and will be apparent to those skilled in the art as well as in the references cited herein including, for example, Sambrook, Ausubel and Berger, as well as, for example, Freshnell (1994)Culture of Animal Cells: A manual of Basic Technique,3 <rd>ed. (Willey-Liss New York) and references cited therein. ;GAT Polypeptides of the invention can be produced in non-animal cells such as plant cells, yeast cells, fungal cells, bacterial cells and the like. In addition to Sambrook, Berger and Ausubel, details regarding non-animal cell cultures can be found in Payneet al.; (1992) Plant Cell and Tissue Culture in Liquid Systems (John Wiley & Sons, Inc. New York, NY); Gamborg and Philips, eds. (1995) Plant Cell, Tissue and Organ Culture: Fundamental Methods/ Springer Lab Manual (Springer-Verlag, Verlin); and Atlas and Parks, eds., The Handbook of Microbiological Media (1993) CRC Press, Boca Raton, FL. The polynucleotides of the present invention can be inserted into any of a number of expression vectors suitable for expressing the polypeptide. Suitable vectors include chromosomal, non-chromosomal and synthetic DNA sequences, for example derivatives of SV40; bacterial plasmids; phagnum DNA; baculovirus; yeast plasmids; vectors obtained by combining plasmid and phage DNA; viral DNA such as vaccinium, adenovirus, fowlpox virus, pseudorabies, adenovirus, adeno-associated viruses, retroviruses and many others. Any vector which serves to transduce genetic material into a cell and (if replication is necessary), which can replicate and survive in the relevant host - can be used. ;When incorporated into an expression vector, a polynucleotide of the invention is operably linked to an appropriate transcriptional control sequence (promoter) to direct mRNA synthesis. Examples of such transcriptional control sequences that are particularly suitable for use in transgenic plants include the promoters of cauliflower mosaic virus (CaMV), downy mildew mosaic virus (field plant Scropulariae) (FMV), and strawberry vein banding virus, which are described in U.S. Pat. Provisional Application No. 60/245,354. Other promoters known to control gene expression in prokaryotic or eukaryotic cells or their viruses and which may be used in some embodiments of the invention include the SV40 promoter, E. colilac or trp promoter and lambda Plpromoter of FAG. The expression vector optionally contains a ribosome binding site for translation initiation and a transcription terminator such as Pinll. The vector also optionally includes appropriate sequences to enhance expression, for example, an enhancer. Additionally, the expression vectors of the present invention contain one or more selectable genetic markers to provide a phenotypic trait for selection of the transformed host cell. Most often, a selectable gene marker will encode resistance to an antibiotic or herbicide. Suitable genes include those encoding resistance to the antibiotic spectinomycin or streptomycin (for example), the streptomycin phosphotransferase (SPT) gene encoding resistance to streptomycin, the neomycin phosphotransferase (NPTII) gene encoding resistance to kanamycin or geneticin, the hygromycin phosphotransferase (HPT) gene encoding resistance to hygromycin. Additional selectable genetic markers include dihydrofolate reductase or neomycin resistance for eukaryotic cell cultures and tetracycline or ampicillin resistance in E. coli.; Suitable genes encoding resistance to herbicides include those that act by inhibiting the action of acetolactate synthase (ALS), especially sulfonylurea herbicides (for example, the acetolactate synthase (ALS) gene containing mutations that lead to such resistance, (especially S4 and/or Hra mutations), those that act by inhibiting the action of glutamine synthase, such as phosphinothricin or "basta" (for example, bargen), or the like genes that encode resistance to the herbicide "basta" and the ALS gene encode resistance to chlorsulfuron. In some cases, the vectors of the present invention can be used to transform the host to express the new protein or polypeptide. Examples of suitable expression hosts include: E. coli, B. subtilis, and Salmonella typhimurium; cells of fungi such as Saccharomyces cerevisiae, Pichia pastoris, and Neurospora crassa; insect cells such as Drosophila and Spodoptera frugiperda; mammalian cells such as CHO, COS, BHK, HEK 293 and Browes melanoma; or plant cells or explants, etc. Clearly, it is not necessary that all cells or cell lines have the ability to produce fully functional polypeptides; for example, antigenic fragments of GAT polypeptides can be produced. This invention is not limited to the use of a host cell. In bacterial systems, the number of expression vectors can be chosen depending on the intended use for the GAT polypeptide. For example, when large amounts of GAT polypeptides or fragments thereof are required for commercial production or antibody induction, vectors that direct high-level expression of fusion proteins that have already been previously purified may be desirable. Such vectors include, but are not limited to, multifunctional expression vectors and cloning vectorsE. coli, such as BLUESCRIPT (Stratagene), in which the GAT polypeptide coding sequence can be ligate with the vector in-frame reading (in-frame) with sequences for the amino-terminal Met and the next seven residues of beta-galactosidase, so that a hybrid protein is produced; pIN vectors (Van Heeke & Schuster (1989) J. Biol. Chem. 264: 5503-5509); pET vectors (Novagen, Madison WI) and the like. Similarly, numerous vectors containing constitutive or inducible promoters such as alpha-factor, alcohol oxidase and PGH can be used in the yeast Saccharomyces cervisae to produce the GAT polypeptide of the invention. For review papers, see Ausubel (already cited) and Grantet al. (1987) Methods in Enzymology 153: 516-544. A number of different expression systems can be used in mammalian host cells, including virus-based systems. In cases where an adeno virus is used as an expression vector, coding sequence, for example for a GAT polypeptide, is optionally ligated to an adenoviral transcription/translation complex consisting of a late promoter and a tripartite leader sequence. Insertion of the GAT polypeptide coding region into a non-essential E1 or E3 region of the viral genome will result in a viable virus capable of expressing GAT in infected host cells (Logan and Shenk (1984) Proc. Nat'l. Acad. Sci USA81:3655-3659). Additionally, transcriptional enhancers such as the Rous sarcoma virus (RSV) enhancer can be used to enhance expression in mammalian host cells. Similarly, in plant cells expression can be directed by a transgene integrated into the plant chromosome, or cytoplasmically by episomal or viral nucleic acid. In the case of stably integrated transgenes it is often necessary to provide sequences capable of directing constitutive or inducible GAT expression polynucleotides of the invention, for example, using viral eg CaMV or plant-derived regulatory sequences. A number of plant-derived regulatory sequences have been described, including sequences that direct expression in a tissue-specific manner, for example, TobRB7, patatin B33, GRP, gene promoters, rbcS-3A promoters, and the like. Alternatively, high level expression can be achieved by transient expression of exogenous plant viral vector sequences, for example TMV, BMV, etc. Typically, transgenic plants constitutively expressing a GAT polynucleotide of the invention will be preferred, and regulatory sequences are selected to ensure constitutive stable expression of the GAT polypeptide. Typical vectors useful for the expression of nucleic acids in higher plants are well known in the art and include vectors derived from the tumor-inducing (Ti) plasmid of Agrobacterium tumefaciens described by Rogers et al. (1987) Meth. Enzymol. 153:253-277. Examples of vectorsA. tumefaciens useful for the invention are plasmids pKYLX6 and pKYLX7 described by Schardlet al. (1987) Gene61:1-11 and Bergeret al. (1989) Proc. Nat' l. Acad. Sci. USA86: 8402-8406. Another useful vector for the invention is plasmid pBI101.2 available from Contech Laboratories, Inc. (Paolo Alto, CA). Various plant viruses that can be used as vectors are known in the art and include cauliflower mosaic virus (CaMV), "gemini" virus, grass mosaic virus of the genus Bromusi and tobacco mosaic virus. In some embodiments of the present invention, a GAT polynucleotide construct suitable for plant cell transformation is prepared. For example, a desired GAT polynucleotide can be incorporated into a recombinant expression cassette to facilitate gene insertion into a plant and thereafter, expression of the encoded polypeptide. The expression cassette will typically contain a GAT polynucleotide, or a functional fragment thereof, operably linked to a promoter sequence and other transcriptional and translational initiation regulatory sequences that will direct expression of the sequence in the desired tissue (eg whole plant, leaf, seed) of the transformed plant. For example, a strong or weak constitutive plant promoter can be used to direct the expression of a GAT polypeptide in all plant tissues. Such promoters are active in most environmental conditions and stages of development or cell differentiation. Examples of constitutive promoters include the 35S transcription initiation region of Cauliflower mosaic virus (CaMV), the 1'—or 2'-promoter derived from T-DNKAgrobacterium tumefaciens, the ubiquitin 1 promoter, the Smas promoter, the cinnamyl (cvnnamyl) alcohol dehydrogenase promoter (U.S. Patent. No. 5,683,439), the Nos promoter, the pEmu promoter, rubisco, the GRP-1 promoter, and other transcription initiation regions from various plant genes known to those skilled in the art. In situations where overexpression of a GAT polynucleotide is undesirable or otherwise harmful to a plant, scientists upon review of this disclosure will appreciate that weak constitutive promoters can be used for low levels of expression. In cases where high levels of expression are not harmful to the plant, a strong promoter, for example, a t-RNA or other pol III promoter, or a strong pol II promoter, such as the cauliflower mosaic virus promoter, can be used. ;Alternatively, the plant promoter may be under environmental control. Such promoters are referred to herein as "inducible" promoters. Examples of environmental conditions that can affect the transcription of inducible promoters include attack by pathogens, anaerobic conditions, or the presence of light. In particular, examples of inducible promoters are the Adh 1 promoter which is inducible under conditions of hypoxia or cold stress, the Hsp70 promoter which is inducible under conditions of heat stress and the PPDK promoter which is induced by light. Also useful are promoters that are chemically inducible. The promoters used in the present invention may be "tissue specific" and as such are under developmental control in the sense that the polynucleotide is expressed only in certain tissues such as leaves, roots, fruit, inflorescences and/or seeds. An example of a promoter is the anther-specific promoter 5126 (U.S. Patent Nos. 5,689,049 and 5,689,051). Examples of seed-preferring promoters include, but are not limited to, the 27kD gamma zein promoter and the waxy promoter, Boronatet al. (1986) Plant Sci. 47, 95-102; Reina et al. (1990) Nucleid Acids Res. (18-21): 6426; and Klosgenet al. (1986) Mol. Gen. Genet.203: 237-244. Promoters expressed in the embryo, pericarp and endosperm were discovered in U.S. Pat. Patent Application Ser. The nose. 60/097,233 filed Aug. 20, 1998 and 60/098,230 filed Aug. 28, 1998. The disclosures of both applications are incorporated herein by reference in their entirety. In embodiments where one or more nucleic acid sequences that are endogenous to the plant system are incorporated into the construct, endogenous promoters (or variants thereof) from these genes can be used to direct gene expression in the transfected plants. Tissue-specific promoters can also be used to direct the expression of heterologous polynucleotides. In general, the particular promoter used in an expression cassette in plants depends on the intended application. Both heterologous and non-heterologous (that is, endogenous) promoters can be used to direct expression nucleic acids of this invention. These promoters can also be used, for example, in expression cassettes to cause the expression of "anti sense" (non-coding) nucleic acids in order to reduce, increase or change the concentration and/or composition of the proteins of this invention in the desired tissue. Any of the many promoters that direct transcription in plant cells are suitable. A promoter can be constitutive or inducible. In addition to the promoters described above, promoters of bacterial origin that function in plants include the octopine synthase promoter, the nopaline synthase promoter, and other promoters derived from native Ti plasmids. (See Herrara-Estrella et al. (1983) Nature 303: 209-213). Viral promoters include the 35S and 19S RNA promoters of cauliflower mosaic virus (Odellet al. (1985) Nature 313: 810-812). Deikman and Fischer (1988) EMBO J.7: 3315-3327. Other plant promoters include the ribulose-1,3-bisphosphate carboxylase small subunit promoter and the phaseolin promoter. The promoter sequence from the E8 gene and other genes can also be used. The isolation and sequence of the E8 promoter is described in detail in Deikmai and Fischer (1988) EMBOJ.7:3315-3327. In order to identify candidate promoters, the 5' parts of the genomic clone are analyzed in order to search for sequences that are characteristic of promoter sequences. For example, promoter sequence elements include a "TATA box" consensus sequence (TATAAT) that is typically located 20-30 base pairs upstream of the strata transcription site. In plants further upstream of the "TATA" box at positions -80 to -100, there is typically a promoter element with a series of adenines surrounding the trinucleotide G (or T), as described by Messinget al. (1983) Genetic Engineering in Plant, eds. Kosage, et al, pp. 221-227. In the process of preparing polynucleotide constructs, for example vectors of the invention, other sequences can also be used in relation to the promoter and the polynucleotides associated with it. If normal expression of the polypeptide is required, a polyadenylation region at the 3'-end of the GAT coding region can be included. The polyadenylation region can be derived, for example, from various plant genes, or from T-DNA. The 3' end of the sequence to be added can be obtained from, for example, a gene for nopaline synthase or octopine synthase, or alternatively from another plant gene or from any other eukaryotic gene - whichever is less preferred. An intronic sequence can be added to the 5' untranslated region of the coding sequence or part of the coding sequence to increase the amount of mature information (message) that accumulates. See, for example, Buchman and Berg (1988) Mol. Cell Biol. 8: 4395-4405 and Calliset al. (1987) Genes Dev. 1: 1183-1200. The use of maize Adhl introns, introns 1,2 and 6, and the Bronze-1 intron is known in the art. See generally Freeling and Walbot, eds. (1994) The Maize Handbook (Springer, New York), Chapter 116. The construct may also include a genetic marker that provides a selectable plant cell phenotype. For example, a marker can encode biocide tolerance, especially antibiotic tolerance such as tolerance to kanamycin, G418, bleomycin, hygromycin or herbicide tolerance such as tolerance to chlorsulfuron or phosphinothricin (the active ingredient in the herbicides biolaphos and Basta). ;Specific initiation signals can assist in the efficient translation of the coding sequence for the GAT polynucleotide of the present invention. These signals can turn on example ATG initiation codon and adjacent sequence. In cases where the GAT polypeptide-coding sequence, its initiation codon and upstream sequences are inserted into the appropriate expression vector, there is no need for additional translational control signals. However, in cases where only the coding sequence (eg the coding sequence for mature portein), or part thereof, is inserted, exogenous transcriptional control signals including the initiation codon must be provided. Furthermore, the initiation codon must be in the correct orientation (reading frame) to ensure transcription of the entire inserted sequence. Exogenous transcriptional elements and initiation codons can be of different origin, both natural and synthetic. Expression efficiency can be increased by including enhancers appropriate to the cell system used (Scharf et al. (1994) Results Probi. Cell Dijfer. 20: 125-62 and Bittner et al. ( 1987; Methods in Enzymol 153: 516-544. ; Secretion/localization of sequences ; Polynucleotides of the invention can also be spliced, for example in the same direction) reads (infrared) with nucleic acids encoding a secretion/localization sequence, to direct the expression of the target polypeptide to a desired cellular compartment, membrane, or organelle of the host cell, or to direct secretion of the polypeptide into the periplasmic space or into the cell culture medium. Such sequences are known to scientists and include secretory leader peptides, organelle targeting sequences (eg, nuclear localization sequences, retention signals, and ER, transit mitochondrial sequences and transit chloroplast sequences), membrane localization/anchor sequences (eg stop transfer sequences, GPI anchor sequences) and the like. In a preferred embodiment, a polynucleotide of the invention is fused read-through to an N-terminal chloroplast transit sequence (or to a chloroplast transit peptide sequence) derived from a gene encoding a polypeptide normally targeted to the chloroplast. Such sequences are typically rich in serine and threonine; they are deficient in aspartate, glutamate and tyrosine; and generally have a central domain that is rich in positively charged amino acids. ;Expression Hosts ;In a further embodiment, this invention relates to host cells containing the constructs described above. The host cell may be a eukaryotic cell, such as a mammalian cell, a yeast cell, or a plant cell; or a host cell which may be a prokaryotic cell such as a bacterial cell. Introduction of the construct into the host cell can be performed by calcium phosphate, DEAE-dextran-mediated transfection. by transfection, electroporation or other commonly used techniques (Davishet al., Basic Methods in Molecular Biology).;The host cell is optionally selected based on its ability to modulate the expression of the inserted sequences or to process the expressed protein in the desired manner. Such protein modifications include, but are not limited to, acetylation, carboxylation, glycosylation, phosphorylation, lipidation, and acylation. Post-translational processing, in which the "pre" or "pre-pro" form of the protein is cut, may also play an important role in proper insertion, folding, and/or function. Different host cells such as E. coli, Bacillus sp., yeast cells or mammalian cells such as CHO, HeLa, BHK MDCK, 293, W138, and so on, possess specific cellular machinery and characteristic mechanisms, for example for post-translational activities, and can be selected to ensure the desired modification and processing of the inserted foreign protein. ;For long-term production with high yield of recombinant protein, stable expression systems can be used. For example, plant cells, explants or tissues, for example, shoots or leaf discs, which stably express a polypeptide of the invention, are transduced using expression vectors containing a viral origin ("origin") of replication or endogenous expression elements and a selectable gene marker. After vector injection, the cells can be allowed to grow for a period of time appropriate for the particular cell type, for example 1 or more hours for bacterial cells, 1-4 days for plant cells, 2-4 weeks for some plant cells - in enriched medium - before being switched to selective medium. The purpose of the selectable marker is to provide resistance to selection and its presence allows the growth and recovery of cells that successfully express the inserted sequences. For example, transgenic plants expressing polypeptides of the invention can be directly selected for resistance to the herbicide, glyphosate. Resistant embryos obtained from stably transformed explants can proliferate se), for example, by using tissue culture techniques that are appropriate for that type of cells. Host cells transformed with a nucleotide sequence encoding a polypeptide of the invention are optionally grown under conditions suitable for expression and recovery of the encoded protein from cell culture. The protein or its fragment, which is produced in the recombinant cell, can be secreted, bound to the membrane or located intracellularly (in the cell) depending on the sequence and/or the vector used. As will be appreciated by those skilled in the art, expression vectors containing the GAT polynucleotides of the invention can be designed with signal sequences that direct secretion of the mature polypeptide across a prokaryotic or eukaryotic cell membrane. ;Additional polypeptide sequences ;Polynucleotides of the present invention may also contain a coding sequence fused in-frame with a marker sequence that, for example, facilitates purification of the encoded polypeptide. Such domains to facilitate purification include, but are not limited to, metal chelating (chelating) peptides such as histidine-tryptophan modules that allow purification on immobilized metals, a glutathione-binding sequence (eg, GST), a hemagglutinin (HA) "tag" tag (corresponding to an epitope derived from hemagglutinin influenza protein; Wilson et al. (1984)Cell37: 767), protein sequences for maltose binding, the FLAG epitope used in the FLAGS extension/affinity purification system (Immunex Corp, Seattle, WA), and the like. To facilitate the purification process, it is useful to insert a "linker" sequence of the protease-cut polypeptide between the purification domain and the GAT homologous sequence. One expression vector contemplated for use in the compositions and methods described herein provides for expression a fusion protein comprising a polypeptide of the invention fused to polyhistidine region and separated by an enterokinase cleavage site. The histidine residues facilitate purification by IMAIC (affinity chromatography with immobilized metal ions, as described by Porathet al. (1992)Protein Expression and Purification3:263-281) while the enterokinase cleavage site provides a means to separate the GAT homologous polypeptide from the fusion protein. pGEX vectors (Promega, Madison, WI) can also be used to express foreign polypeptides as fusion proteins with glutathione-S-transferase (GST). Generally, such fusion proteins are soluble and can be readily purified from lysed cells by adsorption to ligand-agarose beads (eg, glutathione-agarose in the case of GST-fusions) followed by elution in the presence of free Uganda. ;Production and production of polypeptides ;After transduction of a suitable host and growth of host cells to an appropriate density, the selected promoter is induced at in an appropriate way (for example by temperature change or chemical induction) and the cells are grown for an additional period. Cells are typically harvested by centrifugation, disrupted physically or chemically, and the resulting crude extract retained for further purification. Bacterial cells used for protein expression can be disrupted by any conventional method, including alternating freezing and thawing, sonication, mechanical disruption, or the use of lysing agents, or other methods well known in the art. As mentioned, many references are available for the cultivation and production of various cells, including bacterial cells, plant cells, animal cells (especially mammalian) and cells of archaebacterial origin. See e.g., Sambrook, Ausubel and Berger (all already mentioned) as well as Freshnev (1994) Culture of Animal Cells: A Manual of Basic Technique, 3 <rd>ed. (Wiley-Liss, New York) and references cited therein; Doyle and Griffiths (1997) Mammalian Cell Culture: Essential Techniques (John Wiley and Sons, NY); Humason (1979JAnimal Tissue Techniques, 4 <th>ed. (W:H: Freeman and Company); and Ricciardelli, et al. (1989) In Vitro Cell Dev. Biol. 25: 1016-1024. For plant cell culture and regeneration, see Payneet al. (1992) Plant Cell and Tissue Culture in Liquid Systems (John Wiley & Sons, Inc., New York, NY); Ganborg and Phillips, eds. (1995) Plant Cell, Tissue and Organ Culture: Fundamental Methods Springer Lab Manual (Springer-Verlag, Berlin); Jones, ed. (1984) Plant Gene Transfer and Expression Protocols (Humana Press, Totowa, New Jersey); and Croy, ed. ;(1993)Plant Molecular Biology (Bios Scintific Publishers, Oxford, U.K.), ISBN 0 12 198370 6. Cell culture media are generally described in Atlas and Parks, eds. (1993) The Handbook of Microbiological Media (CRC Press, Boca Raton, FL). Additional information on cell culture can be found in available commercial literature such as the Life Science Research Cell Culture Catalog (1998) from Sigma-Aldrich, Inc. (St Louis, MO) ("Sigma-LSRCCC") and, e.g., The Plant Culture Catalog and Supplement (1997) also by Sigma-Aldrich, Inc. (St Louis, MO) ("Sigma-PCCS"). Further details related to the transformation of plant cells and the production of transgenic plants can be found in the text that follows. Polypeptides of the invention can be obtained and purified from recombinant cell cultures by any of a number of methods known in the art, including ethanol precipitation or ammonium sulfate precipitation, casein extraction, anion or cation exchange chromatography, phosphocellulose chromatography, hydrophobic interaction chromatography, affinity chromatography (for example, using the tag system described herein), hydroxyapatite chromatography and lecithin chromatography. Protein repackaging steps can be used, if necessary, to allow the formation of the final configuration of the mature protein. Finally, high performance liquid chromatography (HPLC) can be used for the final purification steps. In addition to the references cited above, various purification methods are well known in the art including for example those disclosed in Sandana (1997) Bioseparation of Proteins (Academic Press, Inc.; Bollaget al. (1996) Protein Methods, 2nd ed. (Wiley-Liss, NY); Walker (1996) The Protein Protocols Handbook (Humana Press NJ), Harris and Angal (1990) Protein Purification Applications: A Practical Approach(IRL Press at Oxford, England); Harris and AngalProtein Purification Methods: A Practical Approach(IRL Press at Oxford, England); Scopes (1993)Protein Purification: Principles and Practice,3 <rd>ed. (Spring Verlag, NY); Janson and Ryden (1998) Protein Purification: Principles, High Resolution Methods and Applications, 2 <nd>ed. (Wiley-VCH, NY); and Walker (1998) Protein Protocols on CD-ROM (HumanaPress, NJ). In some cases, it is desirable to produce the GAT polypeptide of the invention, on a large scale, suitable for industrial and/or commercial applications. In such cases, large-scale fermentation procedures are used. Briefly, a GAT polynucleotide, for example, a polynucleotide comprising any of SEQ ID NO: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 534, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563,564, 565, 566, 567,620,622,624,626, 628,630,632, 634,636, 638,640,642, 644, 646, 648, 650, 652, 654, 656, 658,660, 662, 664, 666,668, 670, 672,674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726, 728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788, 790, 792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814, 816, 818, 820, 822, 824, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916, 918, 920, 922, 924, 926, 928, 930, 932, 933, 934, 935, 936, 937, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952, or other nucleic acids encoding GAT polypeptides of the invention can be cloned into an expression vector. For example, U.S. Patent No. 5,955,310 to Widneret al., "METHODS FOR PRODUCING A POLYPEPTIDE IN A BACILLUS CELL", describes a vector with tandem promoters and stabilizing sequences operably linked to the polypeptide coding sequence. After inserting the polynucleotide of interest into the vector, the vector is transformed into a bacterial host, for example strain Bacillus subtilisPL1801IIE (amyE, apr, eg, spoIIE:Tn917). Introduction of the expression vector into Bacillus cells can, for example, be performed by protoplast transformation (see, for example, Chang and Cohen (1979) Mol. Gen Genet. 168:111), using competent cells (see, for example, Young and Spizizin (196 UBacteriol. 81:823, or Dubnau and Davidoff-Abelson (1971JJ. Mol. Biol. 56:56). 209), by electroporation (see, for example, Shigekava and Dower (1988) Biotechniques 6:742), or by conjugation (see, for example, Koehler and Thorne (1987) J. Bacteriol, 169: 5271), see also, Ausubel, Sambrook and Berger, all previously cited. Transformed cells are grown in nutrient medium suitable for polypeptide production using methods that are known in science. For example, cells can grown in shake flasks, small-scale or large-scale fermentations (including continuous, "batch", "fed-batch" fermentations or solid-state fermentations) in the laboratory or in industrial fermenters, taking place in a suitable medium under conditions that allow the expression of the polypeptide and/or its isolation. Cultivation takes place in a suitable nutrient medium containing sources of carbon and nitrogen and inorganic salts, using procedures known in science. Suitable media are available from commercial suppliers or can be prepared from published compositions (eg, in the American Type Culture Collection catalogs). The secreted polypeptide can be obtained directly from the medium. The resulting polypeptide can be isolated by methods known in the art. For example, a polypeptide can be isolated from a nutrient medium by conventional procedures including, but not limited to, centrifugation, filtration, extraction, spray-drying, evaporation, or precipitation. The isolated polypeptide can be further purified by various procedures known in the art sciences, including, but not limited to, chromatography (eg, ion exchange, affinity, hydrophobic, chromatofocusing, and size exclusion), electrophoretic procedures (eg, preparative isoelectric focusing), differential solubility (eg, ammonium sulfate precipitation), or extraction (see, for example, Bollaget al.;(1996;Protein Methods,2 <nd>ed. (Wiley-Liss, NY) and Walker (1996) The Protein Protocols Handbook (Humana Press, NJ). Cell-free transcription/translation systems can also be used to produce polypeptides using the DNA and RNA of the present invention. Several such systems are commercially available. A general guide to in vitro transcription and translation protocols can be found in Tymms (1995) In Vitro Transcription and Translation Protocols Methods in Molecular Biology (Garland Publishing, NY), vol. 37. ;SEQUENCE RECOMBINATION SUBSTRATES AND FORMATS ;Polynucleotides of the invention are optionally used as substrates for various diversity generation procedures, for example mutation, recombination and recursive recombination reactions, in addition to their use in standard cloning methods as shown in, for example, Ausubel, Berger and Sambrook, to produce additional GAT polynucleotides with desired properties. Various protocols for generating biodiversity are available and described in science. The procedures may be used separately and/or in combination to produce one or more variant polynucleotides or sets of polynucleotides, as well as variants of encoded proteins. Individually and collectively, these procedures provide robust, broadly applicable ways to generate diversified polynucleotides and sets of polynucleotides (including, for example, polynucleotide libraries) that are useful for, for example, the construction or rapid evolution of polynucleotides, proteins, pathways, cells, and/or organs with new and/or improved characteristics. A sequence alteration process can result in, for example, a single nucleotide substitution, multiple nucleotide substitutions, insertion or deletion of a region of a nucleic acid sequence. While distinctions and classifications are made to ensure clarity of discussion, it will be clear that the techniques are often not mutually exclusive. Indeed, different methods can be used individually or in combination, in parallel or in series, to provide different sequence variants. The result of any of the diversity generation procedures described herein can be one or more polynucleotides that can be selected or screened for polynucleotides that encode proteins or that provide desired traits. After diversification by one or more of the methods described herein or otherwise available to the skilled artisan, any polynucleotides produced can be selected for a desired activity or trait, for example, altered Kmza glyphosate, altered Kmza acetylCoA, use of an alternative cofactor (eg, propionyl CoA), increased kcat, etc. This may include the identification of any detectable activity, for example, in an automated or automated format, through any science essay. For example, GAT homologues with increased specific activity can be detected via a glyphosate to N-acetylglyphosate conversion assay, for example by mass spectrometry. Alternatively, assays can be performed for improved abilities to confer resistance to glyphosate by growing bacteria transformed with the nucleic acid of the invention on agar containing increasing concentrations of glyphosate or by spraying transgenic plants incorporating the nucleic acid of the invention with glyphosate. Numerous related (or even unrelated) traits can be assessed, serially or in parallel, which is left to the practitioner to choose. Additional details relating to recombination and selection for herbicide tolerance can be found, for example, in "DNA SHUFFLING TO PRODUCE HERBICIDE RESISTANT CROPS" (U:S: ;Pub. No. 2002/0058249), filed Aug. 12, 1999. ;Descriptions of various procedures for generating diversity, including shuffling multiple genes and methods for generating modified nucleic acid sequences that encode a number of enzyme domains, can be found in the following publications and references cited therein: Soong, N. et al. (2000) Nat. Genet.25(4): 436-39; Stemmer, et al. (1999) Tumor Targeting 4:1-4; Nesset al. (1999) Nature Biotech. 17:893-896; Changet al. (1999) Nature Biotech. 17: 793-797; Minshull and Stemmer (1999) Current Opinion in Chemical Biology 3:284-290; Christinianset al. (1999) Nature Biotech. 17: 259-264; Crameri at el. (1998) Nature 391: 288-291; Crameriet al. (1997) Nature Biotech. 15; 436-438; Zhang et al. (1997) Proc. Nat' l. Acad. Sci. USA94: 4504-4509; Pattenet al. (1997) Current Opinion in Biotech. 8: 724-733; Crameriet al. (1996) Nature Med. 2:100-103, Crameriet al. (1996) Nature Biotech, 14:315-319; Gateset al. (1996) J. Mol. Biol. 255: 373-386; Stemmer (1996) "Sexual PCR and Assembly PCR" in The Encyclopedia of Molecular Biology (VCH Publishers, New York) pp. 447-457; Crameri and Stemmer (1995) BioTechniques 18: 194-195; Stemmer et al., (1995) Gene 164: 49-53; Stemmer (1995) Science 270: 1510; Stemmer (1995) BioTechnology 13: 549-553; Stemmer (1994) Nature 370: 389-391; and Stemmer (1994) Proc. Nat' l. Acad. Sci. USA 91: 10747-10751. Mutational methods for generating diversity include, for example, site-directed mutagenesis (Linget al.( 1997) "Approaches to DNA mutagenesis: an overview" Anal Biochem 254(2): 157-178; Daleet al.( 1996) "Oligonucleotide-directed random mutagenesis using the Phosphorothioate method" Methods Mol. Biol. 57: 369-374; Smith (1985) "In vitromutagenesis" (1985) "Site-directed mutagenesis" and Kunkel (1987) mutagenesis" in Nucleic Acids & Molecular Bilology (Eckstein, F, and Lillev, D:M:J: eds., Springer Verlag, Berlin)); mutagenesis using matrices containing uracil (Kunkel; (1985) "Rapid and efficient site-specific mutagenesis without phenotypic selection" Proc. Nat' l. Acad. Sci. USA82:488-492; Kunkelet al. (1987) "Rapid and efficient site-specific mutagenesis without phenotypic selection" Methods in Enzymol. 154, 367-382; and Basset al.; (1998) "Mutant Trp repressors with new DNA-binding specificities" Science242:240-245); Oligonucleotide-directed mutagenesis using M13-derived vectors: an efficient and general procedure for the production of point mutations in any DNA fragment" Nucleic Acids Res.10:6487-6500: Zoller &Smith; (1983) "Oligonucleotide-directed mutagenesis of DNA fragments cloned into M13 vectors" Methods in Enzymol.100:468-500; and Zoller & Smith (1987) "Oligonucleotide-directed mutagenesis: a simple method using teo oligonucleotide primers and a single-stranded DNA template" Enzymol. 154:329-350); DNA mutagenesis modified with phosphorothioate (Tavloret al.( 1985) "The use of phosphorothioate-modified DNA in restriction enzyme reactions to prepare nicked DNA" Nucl. Acids Res.13: 8749-8764; Tavloret al.( 1985) "The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate-modified DNA" Nucl. Acid Res.13: 8765-8787; Nakamaye & Eckstein (1986) "Inhibition of restriction endonuclease I by phosphorothioate groups and its application to oligonucleotide-directed mutagenesis" Nucl. Acids Res. 16:791-802; bromides"Nucl. Acids Res.16:803-814); mutagenesis using gapped duplex DNA (Krameret al.( 1984) "The gapped duplex DNA approach to oligonucleotide-directed mutation construction"Nucl. Acids Res.12:9441-9456; Kramer & Fritz (1987)Methods in Enzymol. "Oligonucleotide-directed construction of mutations via gapped duplex DNA" 154:350-367; (1988) "Improved enzymatic in vitro reactions to oligonucleotide-directed construction of mutations" Nucl. Acids Res. 16:7207; 6987-6999). Additional suitable methods include point mismatched repair (Kramer et al. (1984) "Point Mismatch Repair" Cell 38:879-887), mutagenesis using repair-deficient host strains (Charter et al. (1985) "Improved oligonucleotide site-directed mutagenesis using M13 vectors" Nucl. Acids Res.13:4431-4443, Charter (1987) "Improved oligonucleotide-directed mutagenesis using Ml3 vectors" Methods in Enzymol.154:382-403), deletion mutagenesis (Eghtedarzadeh & Henikoff (1986) "Use of oligonucleotides to generate large detections" Nucl. Acids Res: 14:5115), restriction selection and restriction purification (Wellset al.( 1986) "Importance of hydrogen-bond formation in stabilizing the transition state of subtilisin" Phil. trans. R. Soc. Lond.A 317: 415-423), mutagenesis by total gene synthesis (Nambiaret al.( 1984) "Total synthesis and cloning of a gene coding for the ribonuclease S protein" Science223: 1299-1301; Sakamar and Khorana (1988) "Total synthesis and expression of a gene for the a-subunit of bovine rod outer segment guanine nucleotide-binding protein (tranducin)"Nucl. Acid Res.14: 6361-6372; Wellset al.( 1985) "Cassette mutagenesis: an efficient method for generation of multiple mutations at defined sites"Gene34: 315-323; and Grunstromet al.( 1985) "Oligonucleotide-directed mutagenesis 'shot-gun' gene synthesis" Nucl. Acid Res. 13: 3305-3316; repair of breaks in both chains (Mandecki (1986), Arnold (1993) "Protein engineering for unusual environments" Current Opinion in Biotechnology4: 450-455; and "Oligonucleotide-directed double-strand break repair in plasmids of Escherichia coli: a method for site-specific mutagenesis" Proc. Nat' l. Acad. Sci.USA, 83:7181).Additional details for many of the above-mentioned methods can be found in "Methods in Enzymology" Volume 154, which also describes the various methods for generating diversity in the following U.S. Pat. 5,605,793 to Stemmer (February 25, 1977), "Methods for in vitroRecombination;" U.S. Pat. No. 5,811,238 to Stemmer et al. (September 22, 1988) "Methods for Generating Polynucleotides having Desired Characteristics by Iterative Selection and Recombination;" U.S. Pat. No. 5,830,721 to Stemmer et al. (November 3, 1998), "DNA Mutagenesis by Random Fragmentation and Reassembly;" U.S. Pat. No. 5,834,252 to Stemmer, et al. (November 10, 1998) "End-Complementary Polymerase Reaction;" U.S. Pat. No. 5,837,458 to Minshull, et al. (November 17, 1998), "Methods and Compositions for Cellular and Metabolic Engineering;" WO 95/22625, Stemmer and Crameri, "Mutagenesis by Random Fragmentation and Reassembly;" WO 96/33207 by Stemmer and Lipxxhutz "End Complementary Polymerase Chain Reaction;" WO 97/20078 by Stemmer and Crameri "Methods for Generating Polynucleotides having Desired Characteristics by Iterative Selection and Recombination;" WO 97/35966 by Minshull and Stemmer, "Methods and Compositions for Cellular and Metabolic Engineering;" WO 99/41402 by Punnonenet al. "Targeting of Genetic Vaccine Vectors;" WO 99/41383 by Punnonenet al. "Antigen Library Immunization;" WO 99/41369 by Punnonenet al. "Genetic Vaccine Vector Engineering;" WO 99/41368 by Punnonenet al. "Optimization of Immunomodulatory Properties of Genetic Vaccines;" EP 752008 by Stemmer and Crameri, "DNA Mutagenesis by Random Fragmentation and Reassembly;" EP 0932670 by Stemmer "Evolving Cellular DNA Uptake by Recursive Sequence Recombination;" WO 99/23107 by Stemmeret al,"Modification of Virus Tropism and Host Range by Viral Genome Shuffling;" WO 99/21979 by Aptet al,"Human Papilloma virus Vectors;" WO 98/31837 by del Cardayreet al. "Evolution of Whole Cells and Organisms by Recursive Sequence Recombination;" WO 98/27230 by Patten and Stemmer, "Methods and Compositions for Polypeptide Engineering;" WO 98/13487 by Stemmeret al,"Methods for Optimization of Gene Therapy by Recursive Sequence Shuffling and Selection;" WO 00/00632, "Methods for Generating Highly Diverse Libraries;" WO 00/09679, "Methods for Obtaining in vitro Recombined Polynucleotide Sequence Banks and Resulting Sequences;" WO 98/42832 by Arnoldet al,"Recombination of Plynucleotide Sequence Using Random or defined Primers;" WO 99/29902 by Arnoldet al,"Method for Creating Polynucleotide and Polypeptide Sequences;" WO 98/41653 by Vind, "An in vitro Method for Constructing a DNA Library;" WO 98/41622 by Borchertet al,"Method for Constructing a Library Using DNA Shuffling;" WO 00/18906 by Pattenet al,"Evolution of Whole Cells and Organisms by Recursive Recombination;" 00/42561 by Crameriet al,"Oligonucleotide Mediated Nucleic Acid Recombination;" WO 00/42559 by Selifonov and Stemmer "Methods for Populating Data Structures for Use in Evolutionary Simulations;" WO 00/42560 by Selifonovet al,"Methods for Making Character Strings, Polynucleotides & Polypeptides Having Desired Characteristics;" WO 01/23401 by Weltchet al,"Use of Codon-Varied Oligonucleotide Synthesis for Synthetic Shuffling;" and WO 01/64864 "Single-Strained Nucleic Acid Template-Mediated Recombination and Nucleic Acid Fragment Isolation", Affholter. ;Some U.S. applications provide additional details regarding various methods for generating diversity including "SHUFFLING OF CODON ALTERED GENES" by Pattenet al. filed Sep. 28, 1999, (USSN 09/407,800); "EVOLUTION OF ;WHOLE CELLS AND ORGANISMS BY RECURSIVE SEQUENCE RECOMBINATION", ;by del Cardavreet al. filed July 15, 1998 (USSN 09/166,188) and July 15, 1999 (US Patent No 6,379,964); "OLIGONUCLEOTIDE MEDIATED NUCLEIC ACID RECOMBINATION" by Crameriet al., filed September 28, 1999 (US Patent No. 6,376,246); "OLIGONUCLEOTIDE MEDIATED NUCLEIC ACID RECOMBINATION" by Crameriet al, filed January 18, 2000 (WO 00/42561); September, 1999 (U:S: Pat No. 6,436,675); "METHODS FOR MAKING CHARACTER STRING, POLYNUCLEOTIDES & POLYPEPTIDES HAVING DESIRED CHARACTERISTICS", Selifonovet al, filed Jan. 18, 2000, (WO 00/42560); ;"METHODS FOR MAKING CHARACTER STRING, POLYNUCLEOTIDES &;POLYPEPTIDES HAVING DESIRED CHARACTERISTICS", Selifonovet al, filed July 18, 2000, (USSN 09/618,579); "METHODS OF POPULATING DATA STRUCTURES FOR USE IN EVOLUTIONARY SIMULATIONS", Selifonov and Stemmer (WO 00/42559), filed January 18, 2000; and "SINGLE-STRANDED NUCLEIC ACID TEMPLATE-MEDIATED RECOMBINATION AND NUCLEIC ACID FRAGMENT ISOLATION", ;Affholter (USSN 60/186,482, filed Mar. 22, 2000). ;Briefly, several different general classes of methods for sequence modifications such as mutation, recombination, etc., are applicable to the present invention and shown in the above references. That is, component changes in nucleic acid sequences to produce modified gene fusion constructs can be carried out using any of the protocols described, either prior to the ligation step, or after the ligation step. The following exemplifies the various types of diversity generation formats in the context of the present invention, including, for example, certain recombination-based diversity generation formats. assembly of nucleic acids by PCR. For example, sexual PCR mutagenesis can be used in which random (or pseudo-random, or even non-random) fragmentation of DNA molecules is followed by recombination based on sequence similarity, between DNA molecules with different but related sequences, in vitro, followed by fixation of crossovers by extension in the polymerase chain reaction. The process, as well as many variants of this process, are described in several references already listed above, for example in Stemmer (1994) Proc. Nat' l. Acad. Sci. USA 91: 10747-10751. Similarly, nucleic acids can recombine recursively in vivo, for example, if recombination is allowed to occur between nucleic acids in cells. Many such in vivo recombination formats are shown in the references mentioned above. Such formats optionally provide direct recombination between the nucleic acids of interest, or provide recombination between vectors, viruses, plasmids, etc., which include the nucleic acids of interest, as well as other formats. Details relating to such procedures can be found in the above references. Whole genome recombination methods may also be used, wherein the entire genomes of cells or other organisms are recombined and optionally include "spiking" (local intensification) of genomic recombination mixtures with desired library components (eg, genes corresponding to the pathways of the present invention). These methods have many applications, including those where the identity of the target gene is unknown. Details of such methods can be found in, for example, WO 98/31837 by Cardavreet al. "Evolution of Whole Cells and Organisms by Recursive Sequence Recombination;" and in e.g. WO 00/04190 by del Cardayra also entitled "Evolution of Whole Cells and Organisms by Recursive Recombination". Therefore, any of these processes and techniques for recombination, recursive recombination, alone or in combination, can be used to generate modified nucleic acid sequences and/or modified gene fusion constructs of the present invention. Synthetic recombination methods can also be used, in which oligonucleotides corresponding to target sequences (targets) of interest are synthesized and reassembled in PCR or ligation reactions involving oligonucleotides corresponding to more than one parent nucleic acid, thereby generating new recombinant nucleic acids. Oligonucleotides can be made by standard nucleotide addition methods or can be made, for example, by synthetic tri-nucleotide approaches. Details relating to such approaches can be found in the references cited above, including, for example, WO 00/42561, Crameriet al,"Oligonucleotide Mediated Nucleic Acid Recombination;" WO 01/23401, Weltchet al,"Use of Codon-Varied Oligonucleotide Synthesis for Synthetic Shuffling;" WO 00/42560, Selifonovet al,"Methods for Making Character Strings, Polynucleotides & Polypeptides Having Desired Characteristics;" and in WO 00/42559 by Selifonov and Stemmer "Methods for Populating Data Structures for Use in Evolutionary Simulations;" In silico methods of recombination can be influenced, using genetic algorithms in a computer to recombine strings of sequences that correspond to homologous (or even non-homologous) nucleic sequences. The resulting recombined arrays of sequences are optionally converted to nucleic acids by synthesizing nucleic acids corresponding to the recombined sequences, for example, according to oligonucleotide-synthesized gene rearrangement techniques. This approach can generate random, partially random, or designed variants. Many details related to in silico recombination, including the use of genetic algorithms, genetic operators and the like in computer systems, in combination with obtaining suitable nucleic acids (and/or proteins), as well as combinations of designed nucleic acids and/or proteins (for example, based on selection of "cross over" sites) as well as methods for designed, pseudo-random or random recombination are described in WO 00/42560, Selifonovet al,"Methods for Making Character Strings, Polynucleotides & Polypeptides Having Desired Characteristics;" and in WO 00/42559 by Selifonov and Stemmer "Methods for Populating Data Structures for Use in Evolutionary Simulations". Additional details regarding the in silico method of recombination can be found in these applications. The methodology is generally applicable to this invention in order to provide recombination of nucleic acid sequences and/or gene fusion constructs that encode proteins participating in various metabolic pathways (such as, for example, carotenoid biosynthetic pathways, ectoine biosynthetic pathways, polyhydroxyalkanoate biosynthetic pathways, aromatic polyketide biosynthetic pathways, and the like in silico/or in the generation of appropriate nucleic acids or proteins. Many methods can be used to assess natural diversity, for example hybridization of diverse nucleic acids or nucleic acid fragments to single-stranded templates, followed by polymerization and/or ligation to regenerate full-length sequences, optionally followed by degradation of the templates and recovery of the resulting modified nucleic acids. In one method using a single-stranded template, a population of fragments obtained from a genomic library(s) is annealed to partial or more often - almost complete ssDNA (single-stranded DNA) or RNA corresponding to the opposite strand. Assembly of complex chimeric genes from the population is then performed by removing the ends of non-hybridized fragments, using a nuclease-based polymerization process to fill the gaps between such fragments, followed by single-stranded ligation. The parent polynucleotide strand can be removed by cleavage digestion (for example, if it is RNA or if it contains uracil), magnetic separation under denaturing conditions (if it is labeled in a way that allows such separation to be performed), and other separation and/or purification methods. Alternatively, the parental strand is optionally co-purified with chimeric strands and removed during further screening and processing steps. Additional details regarding this approach can be found, for example, in "Single-Strained Nucleic Acid Template-Mediated Recombination and Nucleic Acid Fragment Isolation" by Affholter, WO 01/64864. ;In the second approach, single-stranded molecules are converted to double-stranded DNA (dsDNA) and then the dsDNA molecules are bound to a solid support via Uganda-mediated binding. After separation of unbound DNA, selected DNA molecules are released from the carrier and introduced into a suitable host cell to generate a library of enriched sequences that hybridize to the probe. The library thus obtained provides the desired substrate for further diversification using any of the procedures described herein. Any of the foregoing general recombination formats can be practiced in a repetitive fashion (eg, one or more rounds of mutation/recombination or other methods to generate diversity, optionally followed by one or more selection methods) to obtain an even more diverse set (pool) of recombinant nucleic acids. Mutagenesis using polynucleotide chain termination methods has also been proposed (see, for example, U.S. Patent No. 5,965,408, "Method of DNA reassembly by interrupting synthesis", Short, and references cited above), and can be applied to this invention. In this approach, double-stranded DNAs corresponding to one or more genes that share regions of sequence similarity are combined and denatured, in the presence or absence of gene-specific primers. The single-stranded polynucleotides are then ligated and incubated in the presence of a polymerase and a chain termination reagent (eg, ultraviolet, gamma, or X-ray illumination; ethidium bromide or other compounds that incorporate into DNA, such as single-stranded DNA-binding proteins, or histones; trivalent chromium or trivalent chromium salt, resulting in the production of partial duplex molecules, for example, which are denatured and rejoin in new rounds of replication or partial replication, resulting in polynucleotides that share different levels of sequence similarity and that are diversified relative to the initial population of DNA molecules. Optionally, products or partial groups (pools) of products can be multiplied by one or more levels in the process. Polynucleotides produced by the chain termination method as described above are suitable substrates for any desired recombination format. Diversity can also be generated in nucleic acids or populations of nucleic acids using a recombination method called "increase truncation to create hybrid enzymes" (ITCHY,) described in Ostermeieret al. (1999) "A combinatorial approach to hybrid enzymes independent of DNA homologs" Nature Biotech 17:1205. This approach can be used to generate an initial variant library that optionally serves as a substrate for one or more in vitro or in vivo recombination methods. See also, Ostermeireret al.( 1999) "Combinatorial Protein Engineering by Incremental Truncation;" Proc Natl. Acad. Sci. USA, 96/3562-67; and Ostermeireret al. (1999), "Incremental Truncation as a Strategy in the Engineering of Novel Biocatalysts," Biological and Medicina! Chemistry, 7:2139-44. Mutational methods that result in the alteration of individual nucleotides or groups of contiguous or non-contiguous nucleotides can be leveraged to introduce nucleotide diversity into nucleic acid sequences and/or gene fusion constructs of the present invention. Many methods of mutagenesis can be found in the references cited above; additional details relating to mutagenesis methods can be found in the text that follows and may also apply to the present invention. For example error-prone PCR can be used to obtain nucleic acid variants. Using this technique, PCR is performed under conditions under which the accuracy of DNA polymerase copying is low, so it is obtained high rate of point mutations throughout the length of the PCR product. Examples of such techniques can be found in the foregoing references and for example in Leunget al. (1989) Technique 1:11-15 and Caldvvellet al. (1992) PCR Methods Applicat. 2:28-33. Similarly, assembly PCR can be used in a process that involves assembling a PCR product from a mixture of small DNA fragments. A large number of different PCR reactions can be performed simultaneously in the same reaction mixture, where the products of one reaction represent primers for another reaction. Oligonucleotide-directed mutagenesis can be used to introduce site-specific mutations into a nucleic acid of interest. Examples of such specific mutations are found in the references above, and in Reidhaar-Olson et al. (1988) Science 241:53-57. Similarly, cassette mutagenesis can be used in a process that replaces a small region of a double-stranded DNA molecule with a synthetic one with an oligonucleotide cassette that differs from the native sequence. An oligonucleotide may contain, for example, complete and/or partially random native sequence(s). ;Set recursive mutagenesis is a process in which a protein mutagenesis algorithm is used to produce different populations of phenotypically related mutants, members that differ in amino acid sequence. The method uses a feedback mechanism to monitor successive rounds of mutagenesis with combinatorial cassettes. Examples of this approach can be found in Arkin & Youvan (1992) Proc. Nat' l. Acad. Sci. USA89:7811-7815. ;Exponential set - mutagenesis can be used to obtain combinatorial libraries with a high percentage of unique and functional mutants. Small groups of sequence residues of interest were compared randomly to identify, at each changed amino acid position, leading to functional proteins. Examples of such procedures are found in Delegrave & Youvan (1993)Biotech. Res. 11-1548-1552. In vivo mutagenesis can be used to produce random mutations in any cloned DNA of interest by DNA propagation, for example in the strain E. coli carrying mutations in one or more DNA repair pathways. These "mutator" strains have a higher random mutation rate than the parental "wild" type. Propagation of DNA in one of these strains will eventually generate random mutations in the DNA. Such procedures are described in the references mentioned earlier in the text. Other procedures for introducing diversity into a genome, for example a bacterial, fungal or plant genome, may be used in conjunction with the methods described above and/or referenced. For example, in addition to the aforementioned methods, techniques have been proposed that produce multimeric nucleic acids that are suitable for transformation into various species (see, for example, Schellenberger U.S. Patent No. 5,756,316 and references therein above). Transformation of a suitable host with such multimers, consisting of genes that are divergent from each other (for example, derived from natural diversity or through the application of site-directed mutagenesis, error-prone PCR, passaging through mutagenic bacterial strains, and the like), provides a source of nucleic acid diversity for DNA diversification, for example, in vivo recombination processes as shown above. Alternatively, a plurality of monomeric polynucleotides sharing regions of partial sequence similarity can be transformed into the host species and recombined in vivo in the host cell. Further rounds of cell division can be used to obtain libraries whose members comprise a single homogeneous population or pool of monomeric polynucleotides. Alternatively, monomeric nucleic acids can be recovered and obtained by standard techniques, for example PCR and/or cloning, and recombined in any recombination format, including the recursive recombination formats previously described. ;Methods are described for obtaining expression libraries for more species, see for example, Peterson et al. (1998) U.S. Pat. No. 5,783,431 "METHODS FOR GENERATING AND SCREENING NOVEL METABOLIC PATHWAYS:" and Thompson, et al. (1998) U.S. Pat. No. 5,824,485 METHODS FOR GENERATING AND SCREENING NOVEL METABOLIC PATHWAYS) and their use in the identification of protein activities of interest is proposed (as an addition to the mentioned references see Short (1999) U.S. Pat. No. 5,958,672 ;"PROTEIN ACTIVITY SCREENING OF CLONES HAVING DNA FROM ;UNCULTIVATED MICROORGANISMS"). Multispecies expression libraries include, in general, libraries comprising cDNA or genomic sequences from a plurality of species or strains operably linked to appropriate regulatory sequences in an expression cassette. cDNA and/or genomic sequences are optionally randomly ligated to further increase diversity. The vector may be a "shuttle" vector suitable for transformation and expression in more than one type of host organism, for example bacterial species or eukaryotic cells. In some cases, the library is directed by preselection of sequences that encode the protein of interest or that hybridize to the nucleic acid of interest. Any such library may be provided as a substrate for any of the methods described herein. The procedures described above were mainly aimed at increasing the diversity of nucleic acid and/or encoded protein. However, in many cases, not all diversity is useful, for example functional, and mostly contributes to increasing the background of variants that must be screened or selected to identify a few favoring variants. In some applications, it is desirable to pre-select or pre-screen the libraries (eg, amplified library, genomic library, cDNA library, normalized library, etc.) or nucleic acid substrate prior to diversification, for example via recombination-based mutagenesis procedures or otherwise to direct the substrates to antibodies with functional antigen binding sites exploiting in vivo recombination events prior to manipulation by any described method. For example, recombined CDRs derived from B cell cDNA libraries can be amplified and assembled into framework regions (eg, Jirholtet al. (1998) "Exploiting sequence space: shufflingin vivoformed complementarity determining regions into a master framework" Gene 215: 471), prior to diversification by any of the methods described herein. ;Libraries can be directed toward nucleic acids that encode proteins with desired enzymatic activities. For example, after identifying a clone from a library that exhibits a specified activity, the clone can be mutated using methods to introduce DNA changes. The library containing the mutated homologues is then screened for the desired activity, which may be the same or different from the initially specified activity. An example of such a procedure is proposed in Short (1999) U.S. Pat. No. 5,939,250 for "PRODUCTION OF ENZYMES HAVING DESIRED ACTIVITIES BY MUTAGENESIS." Desired activities can be identified by any method known in the art. For example, WO 99/10539 proposes that gene libraries can be screened by combining extracts from the gene library with components obtained from metabolically rich cells and identifying combinations that exhibit the desired activity. It has also been proposed (for example WO 98/58085) that clones with desired activities can be identified by injecting the fluorescence corresponding to the product of the desired activity using a fluorescence analyzer, for example, a flow cytometer, CCD, fluorometer or spectrophotometer. ;Libraries can also be directed to nucleic acids that have specific characteristics, for example to hybridize to a selected nucleic acid probe. For example, WO 99/10539 proposes that polynucleotides encoding a desired activity (eg, an enzymatic activity, eg: lipase, esterase, proteinase, glycosidase, glycosyl transferase, phosphatase, kinase, oxygenase, peroxidase, hydrolase, hydratase, nitrilase, transaminase, amidase, or acylase) can be identified within genomic sequences. In particular, single-stranded DNA molecules from a population of genomic DNA are hybridized with a ligand-conjugated probe. Genomic DNA can be obtained either from a cultured or uncultured microorganism or from environmental samples. Alternatively, genomic DNA may be obtained from a multicellular organism or its tissue. Second strand synthesis can be carried out directly from the hybridization probe used in the capture process, with or without prior release of the capture medium, or by other various strategies known in the art. Alternatively, an isolated single-stranded genomic DNA population can be fragmented without further cloning, using a single-stranded template, as described above. "Non-stochastic" methods for generating nucleic acids and polypeptides are described in Short, "Non-Stochastic Generation of Genetic Vaccines and Enzymes" WO 00/46344. These methods, including the proposed non-stochastic polynucleotide assembly and site-saturation mutagenesis methods, can be applied to the present invention. Random or semi-random mutagenesis using native oligonucleotides is also described, for example, in Arkin and Youvan (1992) "Optimizing nucleotide mixtures to encode subsets of amino acids for semi-random mutagenesis"Biotechnology10:237-300; Eridhaar-Olsonet al. (1991) "Random mutagenesis of protein sequences using oligonucleotide cassettes" Methods Enzymol. 208:564-86; Lim and Sauer (1991) "The role of internal packing interactions in determining the structure and stability of a protein". Mol. Biol. 219:359-76; Brewer and Sauer (1989) "Mutational analysis of the fine specificity of binding of monoclonal antibody 51F to lambda repressor"J. Biol. Chem. 264:13355-60); "Walk-Through Mutagenesis" (Crea, R; U.S. Pat. Nos. 5,830,650 and 5,798,208 and EP Patent 0527809 BI. ;It will also be understood that any of the techniques described above suitable for library enrichment prior to diversification can be used to screen products or libraries of products produced by diversity generation methods. Any of the methods described above can be practiced recursively or in combination, to alter nucleic acids, for example GAT encoding polynucleotide. Kits for mutagenesis, library construction, and other methods for generating diversity are also commercially available. For example, kits available from Stratagene (for example OuickChange™ site-directed mutagenesis kit); and Chameleon™ double-stranded, site-directed mutagenesis kit; Bio/Can Scientific, Bio-Rad (for example, using the Kunkel method described above); Boehringer Mannheim Corp.; Clonetech Laboratories; DNA Technologies" Epicentre Technologies (e.g. 5 prim 3 prim kit); Genpak Inc.; Lemargo Inc.; Life Technologies (Ginco BRL); New England Biolabs, Pharmacia Biotech; Promega Corp.; Quantum Biotechnologies; Amersham International plc (e.g. using the Eckstein method mentioned above); and Anglian Biotechnology Ltd (e.g. using the CarterAVinter method described above). ;The above references provide many mutational formats including recombination, recursive recombination and combinations recombination with other forms of mutagenesis, as well as many modifications of these formats Regardless of the format for creating diversity, the nucleic acids of the present invention can be recombined (with each other or with related (or even unrelated) sequences) to produce a group of recombinant nucleic acids for use in gene fusion constructs and modified gene fusion constructs of the present invention, including, for example, groups of homologous nucleic acids acid, as well as the corresponding polypeptides. Many of the aforementioned methodologies for generating modified polynucleotides generate a large number of different variants of the parent sequence or sequences. In some preferred embodiments of the invention, modification techniques (eg, some form of switching) are used to generate a library of variants which are then screened for a modified polynucleotide or group of modified polynucleotides that encode some desired functional attribute, eg, improved GAT activity. Examples of enzyme activities that can be examined include catalytic rates (conventionally characterized in terms of kinetic constants as kcati KM), substrate specificity, and susceptibility to activation or inhibition by a substrate, product, or other molecule (eg, inhibitor or activator). One example of selection for a desired activity involves growing host cells under conditions that inhibit the growth and/or survival of cells that do not sufficiently express the enzyme activity of interest, for example GAT activity. Using such a selection process can eliminate from consideration those modified polynucleotides that they do not encode the desired enzymatic activity. For example, in some embodiments of the invention, host cells are maintained under conditions that inhibit cell growth or survival in the absence of sufficient levels of GAT, for example at a concentration of glyphosate that is lethal or inhibits the growth of a wild plant species of the same variety that either lacks or does not express the GAT polynucleotide. Under these conditions, only a host carrying a modified nucleic acid encoding an enzymatic activity or activities capable of catalyzing the production of sufficient levels of product can survive and grow. Some embodiments of the invention employ multiple rounds of screening at increasing concentrations of glyphosate or glyphosate analogs. ;In some embodiments, mass spectrometry is used to detect acetylation of glyphosate, glyphosate analogs, or metabolites. The use of mass spectrometry is described in more detail in the examples that follow. For convenience and throughput, it is often desirable to screen/select the desired modified nucleic acids in a microorganism, for example a bacterium such as E. coli. On the other hand, browsing in plant cells or plants may in some cases be preferred where the ultimate goal is to generate a modified nucleic acid for expression in a plant system. In some preferred embodiments of the invention, throughput is increased by screening pools of host cells expressing various modified nucleic acids, either alone or as part of a gene fusion construct. That pool showing significant activity can be analyzed backwards to detect individual clones expressing the desired activity. ;Trained scientists will appreciate that the relevant assay, screening or selection method will depend on the desired host organism and other parameters known in the art. It is normal to rather use a practiceable essay in a high-throughput format. ;In high-throughput essays, it is possible to review several thousand different variants in a single day. For example, each well of a microtiter plate can be used to perform a separate assay, or if the effects of incubation time are to be observed every 5-10 wells can test one variant. ;In addition to fluidic approaches, it is possible, as mentioned above, to simply grow cells on cups with a medium that selects for the desired enzymatic or metabolic function. This approach provides the simple and high-throughput power of this method. A number of well-known robotic systems have also been developed for solution phase chemistries useful in assay systems. These systems include automated workstations such as the automated synthesis apparatus developed by Takeda Chemical Industries, LTD. (Osaka, Japan) and many robotic systems possessing robotic arms (Zvmate II, Zvmark Corporation, Hopkinton, MA; and Orca, Hewlett-Packard, Paolo Alto, CA) that synthetically mimic manual operations performed by scientists. Any of the devices mentioned above are suitable for application to the present invention. The nature and implementation of modifications to these devices (if any) so that they can operate as discussed herein with reference to the integrated system will be apparent. to those who deal with this part of science. High throughput screening systems are commercially available (see Zvmark Corporation, Hopkinton, MA; Air Technical Industries, Mentor, OH; Beckman Instruments, Inc. Fullerton, CA; Precision Systems, Inc., Natick, MA etc.). These systems typically automate the entire procedure including pipetting of all samples and reagents, liquid ejection, time-limited incubation, and final microplate readings in the detector(s) appropriate for the respective assay. These configurable systems provide high bandwidth and fast startup as well as a high degree of flexibility and adaptability. ;Manufacturers of such systems provide detailed protocols for various high-bandwidth devices. So, for example, Zvmark Corp. provides technical guidance describing screening systems, gene transcription modulation detection systems, ligand binding, and the like. Microfluidic approaches to reagent manipulation have also been developed, for example by Caliper Technologies (Mountain View, CA). ;Images that can be seen (i optionally recorded) by a camera or other recording means (eg photo iodide) and data storage devices are optionally further processed for any of the embodiments described herein, eg by digitizing the image and/or storing and analyzing the image in a computer. A range of commercially available peripherals and software support is available for digitizing, hosting and analyzing digitized video material or digitized optical images, for example using PC (Intel x86 or Pentium chip compatible DOS™, OS2™, WTNDOWS™, WINDOWS NT™ or WINDOWS 95™ based machines), MACINTOSH or UNLX based (e.g., SUN workstations) computers. ;One conventional system transmits light from an assay device to a cooled CCD (Charged-Coupled-Device) camera, as is often used in science. A CCD camera contains an organized matrix of image elements (pixels). Light from the sample is transferred to the CCD image. Certain pixels corresponding to sample regions (for example individual hybridization sites on arrays of biological polymers) are sampled to obtain the light reading intensity for each position. Multiple pixels are processed in parallel (simultaneously) to increase speed. The apparatus and methods of the invention are readily used to visualize any sample, for example by fluorescence microscopy or dark field microscopy techniques. ;OTHER POLYNUCLEOTIDE COMPOSITIONS ;This invention also includes compositions containing 2 or more nucleotides of the invention (eg recombination substrates). The compositions may contain a library of recombinant nucleic acids where the library contains at least 2, 3, 5, 10, 20 or 50 or more polynucleotides. Polynucleotides are optionally cloned into expression vectors and provide expression libraries. The invention also includes compositions obtained by digesting one or more polynucleotides of the invention with a restriction endonuclease, RNAse or DNAse (for example performed in certain mentioned recombination formats); and compositions produced by fragmenting or cutting one or more polynucleotides of the invention by mechanical means (eg, sonication, vortexing, and the like), which may also be used to provide recombination substrates in the aforementioned methods. Similarly, compositions containing groups of oligonucleotides corresponding to more than one nucleic acid of the invention are useful as recombination substrates and are a feature of the present invention. For convenience, these fragmented, sheared, or synthesized oligonucleotide mixtures are referred to as fragmented nucleic acid sets. Also included in the invention are compositions produced by incubating one or more sets of fragmented nucleic acids in the presence of ribonucleotide or deoxyribonucleotide triphosphate and nucleic acid polymerase. The resulting compositions form a recombination mixture for many of the recombination formats mentioned above. The nucleic acid polymerase can be RNA polymerase, DNA polymerase, or RNA-directed DNA polymerase (for example "reverse transcriptase"); the polymerase may be, for example, a thermostable DNA polymerase (such as VENT, TAQ or the like). ;INTEGRATED SYSTEMS ;The present invention provides computers, computer-readable media, and integrated systems containing sequences of characters corresponding to the sequence information described herein for the polypeptides and nucleic acids described herein, including for example those sequences listed herein in the sequence listing and their various silent substitutions and conservative substitutions. For example, various methods and genetic algorithms (GA) known in the art can be used to detect homology or similarity between different sequences of characters, or can be used to perform certain functions such as controlling output files, providing a basis for making presentations of information, including sequences, and the like. Examples include BLAST described above. Consequently, different types of homology and similarity of different stringency and length can be detected and recognized in the integrated systems described herein. For example, many methods for determining homology are designed for comparative analyzes of biopolymer sequences for spell checking in word processing and for extracting information from different databases. In order to understand the complementary interactions within the double helix pairs between the four basic nucleotide bases in natural polynucleotides, models simulating the binding of complementary homologous polynucleotide string characters can also be used as a basis for sequence comparison or other operations applied to character sequences corresponding to the sequences described here (for example manipulations in word processing, construction of images containing sequences or subsequences of character sequences, output tables, etc.). An example software package with a GA for calculating sequence similarity is BLAST which can be adapted to the present invention by introducing sequences of characters corresponding to the sequences described herein. ;Similarly, standard computer programs such as word processing programs (for example, MicrosoftWord™ or Corel WordPerfect™) and database programs (spreadsheet programs such as MicrosoftExcel™, Corel Quattro Pro™ or database programs such as Microsoft Acce) of characters corresponding to GAT homologues of the present invention (either nucleic acids or proteins, or both). For example, integrated systems may include programs described above that have the corresponding character sequence information, for example used in conjunction with a user by an "interface" (for example, a GUI in a standard operating system such as a Windows, Macintosh, or LINUX system) to manipulate character sequences. As noted, specialized comparison programs such as BLAST can also be applied to systems of the invention for comparing nucleic acids or proteins (or to corresponding character sequences). include any of the sequences described herein. The computer may be, for example, a PC (Intel x86 or Pentium chip compatible DOS™, OS2™, WINDOWS™, WINDOWS NT™, WTNDOWS 95™, WINDOWS 98™, LINUX based machine), MACINTOSH™, Povver PC or UNIX based (e.g., SUN™ workstation) machine) or other commercial common computers known to those skilled in the art. ;A program for comparison or other sequence manipulation is available or can be easily constructed by one skilled in the art using a standard programming language such as Viasualbasic, Fortran, Basic, Java, or si. Each controller or computer optionally includes a display, often based on a cathode ray tube ("CRT"), or a flat (eg, active matrix liquid crystal display, liquid crystal display) or other. Computer circuits are often housed in a box that includes numerous integrated circuit chips, such as a microprocessor, memory, interface circuits, and others. The box optionally includes a hard disk, a floppy drive, a removable high-capacity drive such as a CD-ROM (on which the contents can be erased and rewritten), and other common peripherals. ;Input devices such as keyboard and mouse optionally provide input by the user as well as selection of sections to be compared or otherwise manipulated in the relevant computer system. A computer typically includes appropriate software support for receiving instructions from the user, either in the form of input into parameter fields, for example in a GUI, or in the form of preprogrammed instructions, for example, preprogrammed for a variety of specific operations. The program then converts these instructions into the appropriate language that defines the operation in the fluid direction and transport of the controller in order to perform the desired operation. ;The program may also include output elements for controlling nucleic acid synthesis (for example, based on the sequence or on a comparison of the sequences described herein) or other operations that take place downstream of the comparison operation or other operations that are performed using character sequences corresponding to the sequence described herein. Nucleic acid synthesis equipment may, accordingly, be a component in one or more of the integrated systems described herein. Additionally, the present invention provides kits that implement the methods, compositions, systems and apparatus described herein. Kits of the invention optionally include one or more of the following: (1) an apparatus, system, system component, or apparatus component as described herein; (2) instructions for practicing the methods described herein and/or for the use of the apparatus or components of the apparatus described herein and/or for the use of the compositions described herein; (3) one or more GAT compositions or components; (4) a container for holding the components or compositions and (5) packaging materials. In a further aspect, this invention provides the use of any apparatus, apparatus component, composition or kit described herein, the performance of any method or assay described herein, and/or the use of any apparatus or kit for the performance of any assay or method described herein. ;HOST CELLS AND ORGANISMS ;The host cell may be eukaryotic, for example, a eukaryotic cell, plant cell, animal cell, protoplast, or tissue culture cell. The host cell optionally contains a plurality of cells, for example an organism. Alternatively, the host cell may be prokaryotic including, but not limited to, bacteria (ie, gram positive bacteria, purple bacteria, green sulfur bacteria, green non-sulfur bacteria, cyanobacteria, spirochetes, termatogales, flavo bacteria, and bacteroids) and archaebacteria (ie, Korarchaeota, Thermoproteus, Pvrodictium, Thermococcales, Methanogens, Archaeoglobus, and extreme halophiles). ;Transgenic plants or plant cells that have incorporated GAT nucleic acids and/or express GAT polypeptides of the invention are a feature of this invention. Transformation of plant cells and protoplasts can be performed in essentially any of a number of ways known to those skilled in the art related to plant molecular biology, including but not limited to the methods described herein. See generally Methods in Enzymology, Vol. 153 (Recombinant DNA Part D) Wu and Grossman (eds.) 1987, Academic Press; and Weising et al., Ann. Rev. Genet. 22:421-477 (1988), incorporated herein by reference. For example, a DNA construct can be introduced directly into the genomic DNA of a plant cell using techniques such as electroporation, PEG-mediated transfection, particle bombardment, silicon fiber delivery, or microinjection of plant cell protoplasts or embryogenic callus. See, for example, Tomes, et al. (1995) "Direct DNA Transfer into Intact Plant Cell Via Microprojectile Bombardment," in Plant Cell, Tissue and Organ Culture, Fundamental Methods, eds. Gamborg and Phillips (Springer-Verlag, Berlin), pp. 197-213. Further methods for transformation of various host cells are described in Kleinet al. (1992) "Transformation of microbes, plants and animals by particle bombardment," Bio/ Technol. 10 (3): 286-291. Introduction of DNA constructs using polyethylene glycol precipitation is described in Paszkowski et al. (1984) EMBO J. 3:2717-2822. Electroporation techniques are described in Frommet al, (1985) Proc Natl. Acad. Sci.82:5824. Ballistic transformation techniques are described in Klein et al. (1987) Nature 327:70-73. Alternatively, the DNA constructs can be combined with suitable T-DNA flanking regions and introduced into the conventional host vector Agrobacterium tumefaciens. The virulence functions of the Agrobacterium tumefaciens host will direct the insertion of the construct and the adjacent marker into the DNA of the plant cell when the cell is infected with the bacterium. See U.S. Patent No. 5,591,616. Agrobacterium tumefaciens-induced transformation techniques are described in detail in the scientific literature. See, for example, Horschet al. (1984) Science 233: 496-498, and Fraley et al.; (1983) Proc Natl. Acad. Sci80:4803. For example, the transformation of maize with Agrobacterium is described in the U.S. Patent Nos. 5,550,318 and 5,981,840. Other methods of transformation include: (1) transformation mediated by Agrobacterium rhizogenes (see, for example, Lichtenstein and Fuller in: Genetic Engineering, Vol. 6, PWJ Rigby, ed. London, Academic Press, 1987; Lichtenstein, C.P. and Draper, J. in: DNA Cloning, Vol. II D. M. Glover, Ed., Oxford, IRI Press, 1985; WO 88/02405 describes the use of A. rhizogenesoi A4 and its Ri plasmid together with A. tumefaciens vectors pARC8 or pARC16); (2) liposome-mediated delivery of DNA (see, e.g., Freeman et al.; (1984) Plant Cell Physiol. 25:1353; (3) vortex methods (see, e.g., Kindle (1990) Proc. Nat'l. Acad. SciUSA 87:1228. ; DNA can also be introduced into plants by direct DNA transfer to pollen as described by Zhou et al. ( 1983)Methods in Enzymology 101:433;D. DNA can also be injected into immature cells embryos and into a rehydration solution for dried embryos as described in Neuhauset al. (1987) Theor. Appl. Genet. 75:30; and in Benbrook et al. (1986) in Proceedings Bio Expo 1986, Buttenworth, Stoneham, Mass., pp. 27-54. ;Animal host cells and lower eukaryotic host cells (eg yeast) are competent or have been prepared to be competent for transfection in various ways. There are several well-known methods for introducing DNA into animal cells. These methods include: calcium phosphate precipitation; fusion of recipient cells with bacterial protoplasts containing DNA; treating recipient cells with liposomes containing DNA; DEAE dextra; electroporation; "biolistics" (a method of inserting DNA into an organelle using a gene gun) and microinjection of DNA directly into the cell. Transfected cells are cultured by methods well known in the art. see, Kuchler, RJ. (1977) Biochemical Methods in Cell Culture and Virology (Dowden, Hutchinson and Ross, Inc.). As used herein, the term "transformation" refers to altering the genotype of a host plant by introducing a nucleic acid sequence, for example a "heterologous," or "foreign" nucleic acid sequence. A heterologous nucleic acid sequence does not have to originate from a different source, but will at some point be external to the cell into which it is inserted. ;In addition, Berger, Ausubel, and Sambrook useful references for plant cell cloning, cultivation, and regeneration include Jones, ed. (1995) Plant Gene Transfer and Expression Protocols—Methods in Molecular Biology, volume 49 (Humana Press, Towata, NJ); Payneet al. (1992) Plant Cell and Tissue Culture in Liquid Systems (John Wiley & Sons, Inc. New York, NY) ("Payne"); and Gamborg and Phillips, eds. (1995) Plant Cell, Tissue and Organ culture; Fundamental Methods/ Springer Lab Manual, (Springer-Verlag, Berlin) ;("Gamborg"). Various cell culture media are described in Atlas and Parks, eds. The Handbook of Microbiological Media (CRC Press, Boca Raton, FL) ("Atlas"). Additional information regarding plant cell culture can be found in available commercial literature such as the Life Science Research Cell Culture Catalog (1988) from Sigma-Aldrich, Inc. (St Louis, MO) (Sigma-LSRCCC) and, for example, Plant Culture Catalog and Supplement (1977) also from Sigma-Aldrich, Inc. (St Louis, MO) (Sigma-PCCS). Additional details related to plant cell culture are described in Croy, ed. (1993) Plant Molecular Biology (Bios Scientific Publishers, Oxford, UK). In one embodiment of the present invention, recombinant vectors including one or more GAT polynucleotides, suitable for plant cell transformation, are prepared. A DNA sequence encoding the desired GAT polypeptide, for example, selected from SEQ ID NO: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 534, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 620, 622, 624, 626, 628, 630, 632, 634, 636, 638, 640, 642, 644, 646, 648, 650, 652, 654, 656, 658, 660, 662, 664, 666, 668, 670, 672, 674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726, 728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788, 790, 792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814, 816, 818, 820, 822, 824, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916, 918, 920, 922, 924, 926, 928, 930, 932, 933, 934, 935, 936, 937, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952, has been conventionally used in order to construct a recombinant expression cassette that can be inserted into the desired plant. In the context of the present invention, an expression cassette will typically comprise a selected GAT polynucleotide operably linked to a promoter sequence and other transcriptional and translational initiation regulatory sequences sufficient to direct transcription of the GAT sequence to the desired tissues (eg, whole plant, leaves, roots, etc.) of the transformed plant. Constitutive promoters include, for example, "core" promoters from the Rsyn7 promoter and other constitutive promoters disclosed in WO 99/43838 and U.S. Pat. Pat. No. 6,072.50; core CaMV 35S promoter (Odellet al. (1985) Nature 313:810-812); rice actin (McElroyet al.; (1990) Plant Cell 2:163-171; ubiquitin (Christensenet al. (1989) Plant Mol. Biol. 12:619-632 and Christensenet al. (1992) Plant Mol Biol. 18:675:689); pEMU (Lastet al. (1991) Theor. Appl. Genet. 81:581-588); MAS (Veltenet al. (1984) EMBO J.3:2726-2730); ALS promoter (U.S. Pat. No. 5,659,026) and the like. Other constitutive promoters include, for example, those disclosed in U.S. Pat. Patent Nos. 5,608,149; 5,608,144; 5,604,121; 5.569597; 5,546,785; 5,399,680; 5,268,463; 5,608,142; and 6,177,611. Chemically regulated promoters can be used to modulate gene expression in a plant through the application of an exogenous chemical regulator. Depending on the target, the promoter can be a chemically-inducible promoter, where the application of a chemical induces gene expression, or a chemically-repressed promoter, where the application of chemicals represses gene expression. Chemically inducible promoters are known in the art and include, but are not limited to, the In2-2 maize promoter which is activated by benzene sulfonamide herbicide safeners (chemicals added to herbicides to protect plants from its effects); GST promoter of corn, which is activated by hydrophobic electrophilic compounds used as "pre-emergent" herbicides - herbicides that are applied before the seed germination process; and PR-la of tobacco, which is activated by salicylic acid. Other chemically-regulated promoters of interest include steroid-responsive promoters. See for example the glucocorticoid-inducible promoter in Schenaet. al.; (1991) Proc. Nat' l. Acad. Sci. USA88:10421-10425 and McNelliset al.(1998)Plant J.14(2):247-257 and tertacycline-inducible and tetracycline-repressible promoters, for example Gatzet al. (1991) Mol. Gen. Genet. 227:229-237, and U.S. Patent Nos. 5,514,618 and 5,789,156 incorporated herein by reference. Tissue-preferred promoters can also be used to target GAT expression within a specific plant tissue. Tissue-preferred promoters include those disclosed in Yamamoto et al. (1997) Plant J. 12(2):255-265; Kavvamata et al. (1997) Plant Cell Physiol. 38(7):792-803; Hansenet al. (1997) Mol. Gen Genet.254(3):337-343; Russell et al. (1977) Transgenic Res. 6(2):157-168; Rinehartet al. (1996) Plant Physiol. 112(3): 1331 -1341; Van Campet al.; (1996) Plant Physiol. 112(2):525-535; Canevasciniet al. (1996) Plant Physiol. 112(2):513-524; Yamamoto et al. (1994) Plant Cell Physiol. 35(5):773-778; Lam (1994Results Probi. CellDiffer.20:181-196; Orozcoet al.(1993)Plant Mol Biol.23(6):1129-1138; Matsuoka et al.(1993)Proc Natl. Acad. Sci.USA 90(20):9586-9590; and Guevara-Garcia et al.(1993)Plant. J.4(3):495-505. If necessary, leaf-specific promoters are known in the art. (1997) Plant J. (1994) Plant Physiol. (1994). Cell Physiol.35(5):773-778; Gotoret al.(1993; Plant J.3:509-18; Orozcoet al.(1993)Plant Mol. Biol.23(6):1129-1138; and Matsuokaat al.(1993)Proc Natl. Acad. Sci. USA90(20):9586-9590.; Root-preferring promoters are known in the art and can be selected from the literature or isolated from different species. See, for example, Plant Mol. 207-218 (1991) Proc. Natl. Sci 3(10):1051-1061 (root-specific control element in GRP 1.8 gene of French bean); Sangeret al.; (1990) Plant Mol. Biol.14(3):433-443 (root-specific promoter of mannopin synthetase (MAS) gene from Agerobacterium Tumefaciens); iMiao et al. (1991) Plant Cell 3(1): 11-22 (complete cDNA clone encoding cytosolic glutamine synthetase (GS), which is expressed in soybean roots and root nodules). See also Bogusz et al. (1990)Plant Cell2(7):633-641, which discloses two root-specific promoters isolated from hemoglobin genes and from the nitrogen-fixing non-leguminous Parasponia andersoniii related non-nitrogen-fixing non-leguminous Trema tomentosa. The promoters of these genes are associated with the P-glucuronidase reporter gene and inserted into the non-leguminous Nicotinia tabacumi leguminous Lotus corniculatusi in both cases the root-specific promoter activity was preserved. Leachet et al. (1991) describe their promoter analyzes of the highly expressed rolCirolDroot-inducible genes of Agrobacterium rhizogenes (see Plant Science (Limerick) 79(1):69-76). They concluded that the enhancer and tissue-preferred determinants are separate in these promoters. Terriet al. (1989) EMBO J.8(2):343-350 used gene fusions in lettuce to show that the T-DNA gene of Agrobacterium- akoji encoding octopine synthase is particularly active in the root tip epidermis and provides a root-specific TR2' gene in the intact plant and stimulated by wounding leaf tissue, which represents a particularly desirable combination of characteristics for use with an insecticidal or larvacidal gene. THREE' the sanptll (neomocine phosphotransferase II) fusion gene showed similar characteristics. Additional root-preferred promoters include the VfENOD-GRP3 gene promoter (Kusteret al. (1995) Plant Mol Biol. 29(4):759-772); the ZRP2 promoter (U.S. Patent No. 5,633,636); the IFSI promoter (U.S. Patent Application Serial No. 10/104,706) and the rolB promoter (Capanaet al. (1994) Plant Mol. Biol. 24(4):681-691). See also U.S. Patent Nos. 5,837,876; 5,750,386; 5,459,252; 5,401,836; 5,110,732 and 5,023,179. ;"Seed-preferred" promoters include both "seed-specific" promoters (promoters active during seed development, such as seed reserve protein promoters) and "seed-germinating" promoters (those promoters active during seed germination). See Thompson et al. (1989) BioEssavs 10:108, herein incorporated by reference. Such seed-preferred promoters include, but are not limited to, Cimi (cytokinin-induced message); cZ19Bl (maize 19kDa zein); milps (myo-inositol-l-phosphate synthase); icei A(cellulose synthase) ; (see U.S. Patent No. 6,225,529, herein incorporated by reference). Gamma-zein is an endosperm-specific promoter. Glob-1 is an embryo-specific promoter. For dicotyledons, seed-specific promoters include, but are not limited to, P-phaseolin, napin, P-conglycinin, soy lecithin, cruciferin and so on. For monocots, seed-specific promoters include, but are not limited to, 15 kDa maize zein, 22 kDa zein, 27 kDa zein, g-zein, waxy, shrunken 1, shrunken 2, globulin 1, etc. See also WO 00/12733, which discloses seed-preferred promoters of the izandliand2gene; incorporated herein by reference. Particularly strong or weak constitutive plant promoters that direct the expression of GAT nucleic acid in all tissues of the plant may preferably be used. Such promoters are active in most environmental conditions and phases of development or cell differentiation. In addition to the promoters mentioned above, examples of constitutive promoters include the 1' - or 2' promoter of Agrobacterium tumefaciens and other transcription initiation regions from various plant genes known to those skilled in the art. While overexpression of the GAT polypeptide of the invention is detrimental to plant, the skilled person will appreciate that weak constitutive promoters can be used for low expression levels. In general, the term "weak promoter" refers to a promoter that directs the expression of a coding sequence at a low level. By "low level" is meant levels from 1/1000 transcripts to about 1/100,000 transcripts, to as low as 1/500,000 transcripts per cell. Alternatively, it will be recognized that weak promoters also include promoters that are expressed only in a few cells and not in other cells, to achieve an overall low level of expression. Where a promoter is expressed at unacceptably high levels, portions of the promoter sequence may be deleted or modified to reduce expression levels. In those cases where high levels of expression are not harmful to the plant, a strong promoter, for example a t-RNA, or another polIII promoter or a strong polll promoter, (for example the promoter of Cauliflower mosaic virus, CaMV, 35S promoter). ;Alternatively, the plant promoter may be under environmental control. Such promoters are referred to as "inducible" promoters. Examples of environmental conditions that can alter transcription through inducible promoters include pathogen attack, anaerobic conditions, or the presence of light. In some cases, it is desirable to use promoters that are "tissue-specific" and/or developmentally controlled, so that the GAT polynucleotide is expressed only in certain tissues or stages of development, for example leaves, roots, shoots, etc. Endogenous gene promoters associated with herbicide tolerance and related phenotypes are particularly useful for directing expression of GAT nucleic acids, for example P450 monooxygenases, glutathione-S-transferase, homoglutathione-S-transferase, glyphosate oxidase, and 5-enolpyruvylshikimate-2-phosphate synthase. Tissue-specific promoters can also be used to direct the expression of heterologous structural genes, including the GAT polynucleotides described herein. Therefore, promoters can be used in recombinant expression cassettes to direct the expression of any gene whose expression is desired in the transgenic plants of the invention, for example GAT and/or other genes that provide herbicide resistance or tolerance, genes that affect other beneficial characteristics, such as heterosis. Similarly, enhancer elements, for example an enhancer element derived from 5' regulatory sequences or introns of a heterologous gene, can also be used to enhance expression of a heterologous structural gene such as a GAT polynucleotide. In general, the particular promoter used in an expression cassette in plants depends on the desired application. Any of the many promoters that direct transcription in plant cells may be suitable. A promoter can be constitutive or inducible. In addition to the promoters mentioned above, promoters of bacterial origin that function in plants include the octopine synthase promoter, the nopaline synthase promoter, and other Ti plasmid-derived promoters. See Herrera-Estrellaet al. (1983) Nature 303:209. Viral include the 35S and 19S RNA promoters of CaMV. See, Odellet et al. (1985) Nature 313:810. Other plant promoters include the ribulose-1,3-bisphosphate carboxylase small subunit promoter and the phaseolin promoter. Promoter sequences from the E8 gene (see Deikman and Fischer (1998) EMBO J.7:3315) and other genes are also preferably used. Monocot species-specific promoters have also been considered (McElrow and Brettell 1994) "Foreign gene expression in transgenic cereals"Trends Biotech.12:62-68). Alternatively, novel promoters with useful characteristics can be identified from any viral, bacterial, or plant source using methods, including sequencing, enhancer or promoter trapping, and the like, known in the art. In the preparation of expression vectors of the invention other sequences than the promoter and GAT coding genes may also preferably be used herein. If appropriate expression of the polypeptide is required, the polyadenylation region can be obtained from a native gene, from various other plant genes, or from T-DNA. Signal/localization peptides that, for example, facilitate translocation of the expressed polypeptide to internal organelles (eg, chloroplasts) or facilitate extracellular secretion may also be used. A vector containing a GAT polynucleotide may also contain a marker gene that confers a selectable phenotype to plant cells. For example, the marker may encode biocide tolerance, particularly antibiotic tolerance, such as tolerance to kanamycin G418 bleomycin, hygromycin, or herbicide tolerance, such as tolerance to chlorsulfuron or fofinothricin. Reporter genes used to monitor gene expression and protein localization via visible reaction products (for example beta-glucuronidase, beza-galactosidase and chloramphenicol acetyltransferase) or through direct visualization of the gene product itself (for example green fluorescent protein, GFP; Sheenet al. (1995) The Plant Journal8:777) can be used to, for example, monitor transient gene expression in plant cells. Transient expression systems can be used in plant cells, for example in screening plant cell cultures for activities that confer tolerance to herbicides. ;PLANT TRANSFORMATION ;Protoplasts ;Numerous protocols for establishing transformable protoplasts from various plant types and then transforming the cultured protoplasts are available in the art and are incorporated herein by reference. For example, see Hashimoto et al. (1990) Plant Physiol. 93:857; Fowke and Constable, eds. (1994) Plant Protoplasts; Saunderset al. (1993) Applications of Plant In vitro Technologv Svmposium, UPM 16-18; and Lyzniket al. (1991) BioTechniques 10:295, each of which is incorporated herein by reference. ;Chloroplasts ;Chloroplasts are sites of action of herbicide tolerance activities and in some cases the GAT polynucleotide is fused to a chloroplast peptide transit sequence to facilitate translocation of gene products into chloroplasts. In these cases it may be desirable to transform the GAT polynucleotide into the chloroplasts of plant and host cells. A number of methods are available in the art that allow chloroplast transformation and expression (eg Daniellet et al. (1989) Nature Biotech. 16:346; 0 <*>Neillet al. (1993) The Plant Journal 3:729; and Malliga (1993)T1BTECH11:1). The expression construct contains a transcriptional regulatory sequence that is functional in plants and that is operably linked to a polynucleotide encoding a GAT polypeptide. Expression cassettes designed to function in chloroplasts (such as an expression cassette comprising a GAT polynucleotide) include the sequences necessary to ensure expression in the chloroplast. Typically, the coding sequence is flanked by two regions of homology to the chloroplast genome to affect homologous recombination within the chloroplast genome; often a selectable marker gene is present within the surrounding plastid DNA sequences, to facilitate the selection of genetically stable transformed chloroplasts in the resulting transplastonic plant cells (see, for example, Maliga (1993) and Daniell (998) already mentioned, with all references cited therein.

General transformation methods

The DNA constructs of the invention can be inserted into the genome of the desired plant host by various conventional techniques. Techniques for the transformation of a wide range of higher plant species are well known and described in the technical and scientific literature. See, for example, Payne, Gamborg, Croy, Jones, etc., all cited above, as well as, for example, Weisinet al. (1988) Ann. Rev. Genet. 22:421 and U.S. Patent Nos. 5,889,190; 5,866,785, 5,589,367 and 5,316,931, incorporated herein by reference.

A large number of transformation protocols are analyzed in this invention. Transformation protocols as well as protocols for introducing nucleotide sequences into plants may vary depending on the type of plant or plant cell, i.e., monocots or dicots, that is the target of transformation. Suitable methods for introducing nucleotide sequences into plant cells, and subsequently inserting them into the plant genome, include microinjection (Crossway et al.(1986)Biotechniques 4:320-334), electroporation (Riggset al.(1986)Proc. Nat'l. Acad. Sci.USA 83:5602-5606), Agrobacterium-mediated transformation (U.S. Patent Nos. 5,563,055 and 5,981-840), direct gene transfer (Paszkovvskiet al.((1984)EMBO J.3:2717-2722), and ballistic particle acceleration (see, for example, U.S. Patent Nos. 4,945,050; U.S. Patent Nos. 5,879,918; 5,886,244; 5,932,782; Tomeset al. (1995) "Direct DNA Transfer into Intact Plant Cells via Microprojectile Bombardment," in Plant Cell Tissue, and Organ Culture: Fundamental Methods, Eds. Gambord and Phillips (Spinger-Verlag, Berlin); McCabeet al.

(1988)Biotechnology6:923-926) and Lecitransformation (WO 00/28058). See also, Weissingeret al. (1988) Ann. Rev. Genet. 22:421-477; Sanford et al. (1987) ParticularScience and Technology5:27-37 (onion); Christouet al. (1988) Plant Psysiol. 87:671-674 (soybean); McCabeet al. (1988) Bio/Technology 6:923-926 (soybean); Finer and McMullen (1991) In Vitro CellDev. Biol.27P: 175-182 (soy); Singhet al. (1998) Theor. Appl. Genet.96:319-324 (soy); Datta et al. (1990) Biotechnology 8:736-740 (rice); Kleinet al. (1988) Proc. Nat' l. Acad. Sci.USA 85:4305-4309 (maize); Kleinet al. (1988) Biotechnology 6:559-563 (maize); U.S. Patent Nos. 5,240,855; 5,322,783 and 5,324,646; Kleinet al. (1988) Plant Physiol. 91:440-444 (maize); Frommet al. (1990) Biotechnology 8:833-839 (maize); Hooykaas-Van Slogterenet al. (1984) Nature (London) 311:763-764; U.S. Patent No. 5,736,369 (cereals); Bvtebieret al. (1987) Proc. Nat' l. Acad. Sci. USA84:5345-5349 (Liliaceae); De Wetet al. (1985) in The Experimental Manipulation of Ovule Tissues, Eds., Chapman et al. (Longman, New York), pp. 197-209 (pollen); Kaeppleret al. (1990) Plant Cell Reports 9:415-418 and Kaeppleret al. (1992) Theor. Appl. genet.84:560-566 (whisker-mediated transformation); D'Halluinet al. (1992) Plant Cell 4:1495-1505 (electroporation); Liet al. (1993) Plant Cell Reports 12:250-255 and Christou and Ford (1995) Annals of Botany 75:407-413 (rice); Osjodaet al. (1996) Nature Biotechnology 14:745-750 (maize via Agrobacterium tumafaciens); all are incorporated herein by reference.

For example, DNAs can be inserted directly into the genomic DNA of plant cells using techniques such as electroporation or microinjection of plant cell protoplasts, or DNA constructs can be inserted directly into plant tissue using ballistic methods such as DNA particle bombardment. Alternatively, the DNA constructs can be combined with suitable T-DNA flanking regions and inserted into the conventional host vector Agrobacterium tumefaciens. The virulence functions of the Agrobacterium host will direct the insertion of the construct and the adjacent marker into the DNA of the plant cell when the plant cell is infected with the bacterium.

Microinjection techniques are known in the art and described in the scientific and patent literature. Insertion of DNA constructs by polyethylene glycol precipitation is described in Paszkowski et al. (1984) EMBO J 3:2717. Electroporation techniques are described in Frommet al. (1985) Proc. Nat' l. Acad. Sci. USA 82:5824. Ballistic transformation techniques are described in et al. (1987) Nature 327:70; and Weekset al. Plant. Phvsiol. 102:1077.

In some embodiments, Agrobacterium-mediated transformation techniques are used to transfer the GAT sequences of the invention into transgenic plants. Agrobacterium-mediated transformation is often used to transform dicots, however certain monocots can also be transformed by Agrobacterium. For example, transformation of rice with Agrobacterium is described in Heiet al. (1994) Plant J. 6:271; U.S. Patent No. 5,187,073; U.S. Patent No. 5,591,616; Liet al.(1991JScience in China35:54; and Raineriet al.(1990)Bio/Technology8:33. Also described are transformed maize, barley, triticale and asparagus through Agrobacterium-mediated transformation. Described in (Xuet al.(1990)Chinese J

Bot 2:81).

Agrobacterium-mediated transformation techniques exploit the tumor-inducing ability of the Ti plasmidA. tumefaciens when integrated into the genome of a plant cell, to co-transfer the nucleic acid of interest into the plant cell. Typically, an expression vector is produced wherein a nucleic acid of interest, such as a GAT polynucleotide of the invention is ligated into an autonomously replicating plasmid that also contains T-DNA sequences. T-DNA sequences typically flank the nucleic acid of interest in the expression cassette and include sequences for plasmid integration. In addition to the expression cassette, the T-DNA typically contains a marker sequence, for example antibiotic resistance genes. The T-DNA plasmid and expression cassette are then transfected into Agrobacterium cells. Typically, for effective transformation of plant cells, bacteriaA. tumefaciens also possesses the necessary virregions on the plasmid or integrated into its chromosome. For a discussion of Agrobacterium-mediated transformation, see Firoozabad and Kuehnle, (1995) in Plant Cell Tissue and Organ Culture Fundamental Methods, eds. Gamborg and Phillips.

In certain embodiments, the polynucleotides of the present invention can be combined with any combination of polynucleotide sequences of interest to create plants with a desired phenotype. For example, the polynucleotides of the invention can be combined with any other polynucleotides that encode polypeptides having pesticidal and/or insecticidal activity, such as the toxic proteins of Bacillus thuringiensis (described in U.S. Patent Nos. 5,366,892; 5,747,450; 5,737,514; 5,723,756; 5,593,881; and Geiseret al.(1986)Gene48:109), lectins (Van Damme et al. (1994)Plant. Mol Biol.24:825, peptin (described in U.S. Patent No. 5,981,722) and the like. The resulting combinations may also include multiple copies of any polynucleotide of interest. The polynucleotides of the present invention may also be combined with any other gene or combination of genes to produce plants with different combinations of desired features including, but not limited to, forage desirable traits such as highly expressed high oil genes (eg, U.S. Patent No. 6,232,529); balanced amino acids (eg, hordothiobins (U.S. Patent Nos. 5,990,389; 5,885,801; 5,885,802; and 5,703,409)); high level of lysine in barley (Williamson et al.

(1987) Eur. J. Biochem. 165:99-106; and WO 98/20122) and high methionine proteins (Pedersenet al.(1986)J. Biol. Chem.261:6279; Kriharaet al.(1988) Gene 71:359; and Musumuraet al.(1989)Plant Mol. Biol.12:123)); increased digestibility (eg modified reserve proteins (U.S. Application Serial No. 10/053,410 filed Nov. 7, 2001); and thioredoxins (U.S. Application Serial No. 10/005,429 filed Dec. 3, 2001)); the disclosures of which are incorporated herein by reference.

Polynucleotides of the present invention may also be combined with traits required for disease or herbicide resistance (eg, fumonisin detoxification genes (U.S. Patent No. 5,792,931); disease resistance and avirulence genes (Joneset. al.(1994)Science266:789; Martinet al.(1993)Science262:1432; Mindrinoset et al. al.(1994)Cell78:1089); mutants for acetolactate synthase (ALS) leading to herbicide resistance such as S4 and/or Hra mutations; glutamine synthase inhibitors such as phosphinothricin or basta (eg, bar gene)); and properties desirable for processing or processing products such as high oil content (U.S. Patent No. 6,232,529); modified oils (U.S. Patent No. 5,952,544; WO 94/11516)); modified starches (eg, ADPG pyrophosphorylases (AGPases), starch synthases (SS), starch bifurcation enzymes (SBEs), and starch cleavage enzymes (SDBEs); and polymers or bioplastics (eg, U.S. Patent No. 5,602,321; beta-ketothiolase polyhydroxybutyrate synthase and acetoacetyl-CoA reductase (Schubertet al. (1988) Bacteriol. 170:5837-5874) facilitate the expression of polyhydroxyalkanoates (PHA), the disclosures of which are incorporated herein by reference. Polynucleotides of the present invention can also be combined with polynucleotides that provide agronomic traits such as male sterility (e.g., U.S. Patent No. 5,583,210), stem vigor, flowering time, or traits related to transformation technology such as regulation cell cycle or gene targeting (eg, WO 99/61619, WO 00/17364 and WO 99/25821); disclosures are incorporated herein by reference.

These related combinations can be created by any method, including, but not limited to, cross-breeding plants by any conventional or

TopCross methodology or genetic transformation. If traits are linked by genetically transforming plants, the polynucleotide sequences of interest can be combined at any time or in any order. For example, a transgenic plant containing one or more desired traits can be used as a target for further introduction of traits through subsequent transformation. Traits can be introduced simultaneously using co-transformation protocols with polynucleotides of interest provided by any combination of transformation cassettes. For example, if two sequences need to be inserted, the two sequences may be in separate transformation cassettes (trans) or they may be within the same transformation cassette (cis). Expression of the sequences can be directed from the same promoter or from different promoters. In certain cases it may be desirable to insert a transformation cassette that will suppress expression of the polynucleotide of interest. It can be combined with any combination of other suppressor cassettes or overexpressed cassettes to produce the desired combination of traits in a plant. It is further recognized that polynucleotide sequences can be linked at a desired genomic location by a site-specific recombination system. See, for example, WO99/25821, W099/25854, WO99/25840, W099/25855, W099/25853, all incorporated herein by reference.

Regeneration of transgenic plants

Transformed plant cells obtained by seed transformation techniques, including those described herein, can be cultured to regenerate an entire plant that possesses the transformed genotype (ie, GAT polynucleotide) and thus a desired phenotype, such as acquired resistance (ie, tolerance) to glyphosate or a glyphosate analog. Such regeneration techniques rely on the manipulation of certain phytohormones in the tissue culture growth medium, typically relying on a biocidal and/or herbicidal marker inserted along with the desired nucleotide sequences. For transformation and regeneration of maize, see Gordon-Kammet al, The Plant Cell, 2:603-618 (1990). Alternatively, selection for glyphosate resistance obtained via the GAT polynucleotides of the invention can be performed. Plant regeneration from protoplast culture is described in Evans et al. (1983) Protoplast Isolation and Culture, Handbook of Plant Cell Culture, pp 124-176, Macmillan Publishing Company, New York; and Binding (1985) Re<g>eneration of Plants, Plant Protoplasts pp 21-73, CRC Press, Boca Raton. Regeneration can also be achieved from plant callus, explants, organs or parts thereof. Such regeneration techniques are generally described in Klee et al. (1987) Ann Rev of Plant Phys 38:467. See also Payne and Gamborg.

Transformed plant cells, calli or explants can be grown in regeneration medium in the dark for several weeks, generally about 1 to 3 weeks to allow somatic embryos to mature. Preferred regeneration media include media containing MS salts. Plant cells, calli, or explants are then typically grown on a rooting medium, under alternating light/dark cycles, until shoots and roots develop. Methods for regenerating a plant are known in the art and preferred methods are provided by Kamoet al, (Bot Gaz. 146(3):324-334; Westet al, (The Plant Cell 5:1361-1369, 1993); and Duncan et al. (Planta 165:322-332, 1985).

Small young plants can be transferred to tubes containing rooting medium and then allowed to grow and develop more roots for about another week. The plants can then be transplanted to potted soil mix in the greenhouse.

Regeneration of plants containing a foreign gene inserted by Agrobacterium can be achieved as described in Horschet al, Science, 227:1229-1231 (1985) and Fralevet al., Proc. Nat' l. Acad. Sci. U.S.A., 80:4803 (1983). This procedure typically produces shoots within two to four weeks and these shoot-transformants are then transferred to an appropriate root induction medium containing a selective agent and an antibiotic to prevent bacterial growth. Transgenic plants of the present invention may be fertile or sterile.

Regeneration can also be achieved from callus, explants, organs or parts thereof. Such regeneration techniques are described generally in Kleeet al, Ann. Rev. of Plant Phys. 38:467-486

(1987). Regeneration of plants whether from protoplasts of a single plant or different explants is well known in science. See, for example, Methods for Plant Molecular Biology, A. Weissbach and H. Weissbach, eds., Academic Press, Inc., San Diego, Calif. (1988). For corn cell cultivation and regeneration, see generally, The Maize Handbook, Freeling and Walbot, eds., Springer, New York (1994); Corn and Corn Improvement3<rd>Ed., Sprague and Dudlev eds., American Society of Agronomy, Amdison, Wisconsin (1988).

After transformation with Agrobacterium, explants are typically transferred to a selective medium. One skilled in the art will appreciate that the selection of the medium depends on the selectable marker that is co-transfected into the explants. After a suitable period of time the transformants will begin to develop shoots. After the shoots reach 1-2 cm in length, the shoots should be transferred to a suitable root and shoot medium. Selective pressure should be maintained in both root and shoot media.

Typically, transformants will develop shoots in about 1-2 weeks and form young plants. When the young plants reach a height of three to five centimeters, they are then placed in sterile soil in plastic pots. Those skilled in the art will appreciate that different acclimation procedures have been used to obtain transformed plants from different species. For example, after the development of roots and shoots, cuttings as well as somatic embryos of transformed plants are transferred to the medium for the emergence of young plants. For a description of the selection and regeneration of transformed plants, see for example Dodds and Roberts (1995) Experiments in Plant Tissue Culture, 3<rd>Ed., Cambridge University Press.

Also, there are methods for Agrobacterium - Arabidopsis transformation using vacuum infiltration (Bechtolds N., Ellis J. and Pelletier G., 1993, In Planta Agrobacterium moderated

gene transfer by infiltration of adult Arabidopsis thaliana plant. CR Acad Sci Parish Life Sci

316:1194-1199) and by simple dipping of flowering plants (Desfeux, C, Clough S.J., and Bent A.F., 2000, Female reproductive tissues are the primary target of Agrobacterium-mediated transformation by the Arabidopsis floral-dip method, Plant Physiol. 123:895-904). Using these methods, transgenic seeds are produced without the need for tissue culture.

There are various species for which effective Agrobacterium-mediated transformation protocols have yet to be developed. For example, successful tissue transformation coupled with regeneration of the transformed tissue to produce a transgenic plant has not yet been reported for some of the most relevant commercial cotton cultivars. However, an approach that can be used for these plants involves stably introducing the polynucleotide into a related plant variety via Agrobacterium-mediated transformation, confirming operability, and then transferring the transgene into the desired commercial strain using standard sexual crossing or backcrossing techniques. For example, in the case of cotton, Agrobacterium can be used to transform a Coker line of Gossypium hirustum (eg Coker lines 310, 312, 5110 Deltapine 61 or Stoneville 213), and then transgenes can be inserted into other more commercially relevant G. hirustumcultivar through back-crossing.

Transgenic plants of the present invention can be characterized either genotypically or phenotypically to determine the presence of the GAT polynucleotide of the invention. Genotypic analyzes can be performed by any of the well-known techniques, including PCR amplification of genomic DNA and hybridization of genomic DNA with specifically labeled probes. Phenotypic analyzes include, for example, the survival of plants or plant tissues exposed to a selected herbicide such as glyphosate.

One skilled in the art will recognize that once an expression cassette containing the GAT gene has been stably incorporated into transgenic plants and confirmed to be operative, it can be introduced into other plants by sexual crossing. Any of a number of standard crossing techniques can be applied depending on the species to be crossed.

In vegetatively propagated crops, mature transgenic plants can be propagated by cuttings or tissue culture techniques to produce large numbers of identical plants. A selection of desired transgenic plants is made and new varieties are obtained and then propagated vegetatively for commercial use. In crops propagated from seed, mature transgenic plants can be crossed with themselves to produce a homozygous "inbred" plant (obtained by inbreeding). An inbred plant produces seeds that contain the newly introduced heterologous nucleic acid. These seeds can be cultivated to produce plants that will eventually produce the selected phenotype.

Parts obtained from a regenerated plant, such as flowers, seeds, leaves, branches, fruit, and the like, are included in the invention, wherein these parts contain cells that comprise the isolated GAT nucleic acid. Progeny and variants and mutants of the regenerated plants are also included within the scope of this invention, provided that these parts contain inserted nucleic acid sequences.

Transgenic plants expressing a selectable marker can be screened for GAT nucleic acid transfer, for example by standard "immunoblot" and DNA detection techniques. Transgenic lines are also typically evaluated for expression levels of heterologous nucleic acids. Expression at the RNA level can be determined initially in order to identify and quantify expression-positive plants. Standard techniques for RNA analysis can be used and include PCR amplification assays using oligonucleotide primers designed to amplify only heterologous RNA templates and a solution hybridization assay using specific probes for heterologous nucleic acids. RNA-positive plants can then be analyzed for protein expression by Western immunoblot analysis using specific reactive antibodies of the present invention. In addition, in situ hybridization and immunocytochemistry can be performed based on standard protocols using oligonucleotide probes and heterologous nucleic acid-specific antibodies to localize expression sites within transgenic tissue. Generally, a large number of transgenic lines are usually screened for incorporated nucleic acid to identify and select plants with the best and most desirable expression profiles.

A preferred embodiment is a transgenic plant that is homozygous for the added heterologous nucleic acid; that is, a transgenic plant containing two additional nucleic acid sequences, one gene at the same locus on each chromosome of a chromosome pair. A homozygous transgenic plant can be obtained by sexual mating (self-fertilization, autogamy) of a heterozygous transgenic plant containing one added heterologous nucleic acid, growing a portion of the produced seed and analyzing the resulting plants for altered cell division relative to a control plant (that is, the native non-transgenic). Backcrossing with the parent plant as well as out-crossing with the non-transgenic plant is also contemplated.

Essentially, any plant can be transformed with the GAT polynucleotides of the invention. Suitable plants for transformation and expression of the novel GAT polynucleotides of the present invention include species important for both agronomy and horticulture. Such species include members of the families, but are not limited to: Graminae (including maize, rye, triticale, barley, millet, ryegrass, wheat, oats, etc.); Leguminosae (including peas, beans, lentils, peanuts, yam beans, cowpeas, velvet beans, soybeans, clover, alfalfa, lupins, vetches, lotus, sweet clover, Wisteria, and sweet peas); Compositae (the largest family of vascular plants, including at least 1,000 genera including important commercial crops such as sunflower); and Rosaciae (including raspberry, apricot, almond, peach, rose, etc.); as well as stone plants (including walnut, hickory nut, hazelnut, etc.); and forest trees (including Pinus, Quercus, Pseutotsuga, Sequoia, Populus etc.).

Additional targets for modification of the GAT polynucleotides of the invention, as well as those specified above, include plants from the genera: Agrostis, Allium, Antirrhinum, Apium, Arachis, Asparagus, Atropa, Avena (for example oats), Bambusa, Brassica, Bromus, Browaalia,

Camellia, Cannabis, Capsicum, Cicer, Chenopodium, Chichorium, Citrus, Coffea, Coix,

Cucumis, Curcubita, Cyodon, Dactylis, Datura, Daucus, Digitalis, Dioscorea, Elaeis,

Eleusine, Festuca, Fragaria, Geranium, Gossipum, Glycine, Helianthus, Heterocallis, Hevea,

Hordeum (eg barley), Hyoscyamus, Ipomea, Lactuca, Lens, Lilium, Linum, Lolium,

Lotus, Lycopersicon, Majorana, Malus, Mangifera, Manihot, Medicago, Nemesia, Nicotiana,

Onobrychis, Oryza (eg rice), Panicum, Pelargonium, Pennisetum (eg millet), Petunia, Pisum, Phaseolus, Phleum, Poa, Prunus, Ranunculus, Raphanus, Ribes, Ricinus, Rubus, Saccharum, Salpoglossis, Secale (eg rye), Senecio, Setaria, Synapsis, Solanum, Sorghum, Stenotaphrum, Theobroma, Trifolium, Trigonella, Triticum (eg wheat), Vida, Vigna, Vitis, Zea (eg maize) and Olyreae, Pharoidea and many others. As mentioned, plants of the family Graminae are particularly preferred target plants for the methods of the present invention.

Common crop plants that are target plants of the present invention include corn, rice, triticale, rye, cotton, soybeans, Chinese sugar cane, wheat, oats, barley, millet, sunflower, canola, peas, lentils, peanuts, yam beans, cowpeas, velvet beans, clover, alfalfa, lupins, vetch, lotus, sweet clover, safflower. generaJWisteria, sweet pea and stone plants (for example walnut, hickory nut, etc.).

In one aspect, the invention provides a method for producing a crop by growing a crop plant that is tolerant to glyphosate as a result of being transformed with a gene encoding glyphosate N-acetyltransferase, under such conditions that the crop plant produces a crop, and a method for harvesting the crop. Preferably, the glyphosate is applied to the plant or near the plant at a concentration effective to control weeds without preventing the transgenic crop plant from growing and producing a crop. Glyphosate can be applied before planting or at any point after planting up to and including harvest time. Glyphosate can be applied once or multiple times. The time of application of glyphosate, the amount that is applied, the method of application and other parameters will vary depending on the specific nature of the crop plant and the environment in which it grows and can be easily determined by experts in this field of science. The invention further provides a crop produced by this method.

The invention provides for the propagation of a plant containing a GAT polynucleotide transgene. A plant can be, for example, a monocot or a dicot. In one embodiment, the propagation results in crossing a plant containing the GAT polynucleotide transgene with another plant, such that at least a portion of the progeny of this cross exhibits glyphosate tolerance.

In one aspect, the invention provides a method for selectively controlling weeds in a field where a crop is grown. The method includes planting seeds of crops or plants that are glyphosate tolerant as a result of being transformed with a gene encoding a GAT, for example a GAT polynucleotide, and applying glyphosate to the crop and weeds, if any, in sufficient quantity to control the weeds without significantly adversely affecting the crop. It is important to note that it is not necessary for a crop to be completely insensitive to the herbicide, as long as the benefit obtained from weed inhibition outweighs any adverse effect of glyphosate or glyphosate analogs on the crop or crop plant.

In another aspect, the invention provides the use of a GAT polynucleotide as a selectable marker gene. In this embodiment of the invention, the presence of a GAT polynucleotide in a cell or organism provides the cell or organism with a detectable phenotypic trait of glyphosate resistance and thus enables the selection of cells or organisms that have been transformed with a gene of interest linked to the GAT polynucleotide. Therefore, for example, a GAT polynucleotide can be inserted into a nucleic acid construct, e.g., a vector, thereby allowing identification of a host (eg, a cell or transgenic plant) containing the nucleic acid construct by growing the host in the presence of glyphosate and selecting for its ability to survive and/or grow at a rate that is demonstrably greater than would survive and/or grow in a host lacking the nucleic acid construct. The GAT polynucleotide can be used as a selectable marker in a variety of glyphosate-susceptible hosts, including plants, most bacteria (including E. coli), actinomycetes, yeasts, algae and fungi. One benefit of using herbicide resistance as a marker in plants, as opposed to conventional antibiotic resistance, is that it removes the concern of some of the public that antibiotic resistance can "escape" into the environment. Some experimental data from experiments demonstrating the use of GAT polynucleotides as a selectable marker in various host systems are described in the Examples section of this specification.

Selection of GAT polynucleotides that provide increased

glyphosate resistance in transgenic plants

Libraries of GAT-encoding nucleic acids diversified based on the methods described herein can be selected for the ability to confer glyphosate resistance in transgenic plants. After one or more cycles of diversification and selection, the modified GAT genes can be used as a selection marker to facilitate the production and evaluation of transgenic plants and as a means of providing herbicide resistance in experimental or agricultural plants. For example, after diversifying any one or more of, for example, SEQ ID NOs: 1-5 to obtain a library of altered GAT polynucleotides, the initial functional change can be performed by expressing the library of GAT coding sequences in E. coli. Expressed GAT polynucleotides can be purified or partially purified as described herein and screened for improved kinetics by mass spectrometry. After one or more preliminary rounds of diversification and selections, the polynucleotides encoding the improved GAT polypeptides are cloned into a plant expression vector operably linked to, for example, a strong constitutive promoter such as the CaMV 35S promoter. Expression vectors containing modified GAT nucleic acids are transformed, typically by Agrobacterium-mediated transformation into Arabidopsis Thaliana host plants. For example, Arabidopsis hosts are easily transformed by submerging inflorescences in Agrobacterium solutions and allowing them to grow and produce seeds. About a thousand seeds are obtained in about six weeks. These seeds are then collected in a pile from the submerged plants and sown in the soil. In this way, it is possible to generate several thousand independently transformed plants for evaluation that make up a high-throughput plant transformation format. The seedlings growing in the pile are then sprayed with glyphosate and the surviving seedlings that show resistance to glyphosate survive the selection process, while the non-transgenic plants and plants in which the less desirable modified GAT nucleic acids are incorporated are damaged or killed by the herbicide treatment. Optionally GAT-encoding nucleic acids that provide improved glyphosate resistance are recovered, for example by PCR amplification using tDNA primers flanking inserts from the library and then further used for diversification procedures or to produce additional transgenic plants of the same or different species. If necessary, additional rounds of diversification and selection can be performed using increased concentrations of glyphosate in each subsequent selection. In this way, GAT polynucleotides and polypeptides can be obtained that provide resistance to glyphosate concentrations that are useful in field conditions where they are grown.

Herbicide resistance

The present invention provides a composition comprising two or more polynucleotides of the invention. Preferably, the GAT polynucleotides encode GAT polypeptides having different kinetic parameters, ie. A GAT variant that has a lower Km can be combined with one that has a higher kcat- In a further embodiment, different GAT polynucleotides can be linked to a chloroplast transit sequence or another signal sequence and thus ensure the expression of GAT polypeptides in different cell compartments, organelles or the secretion of one or more GAT polypeptides.

The glyphosate resistance mechanism of the present invention can be combined with other glyphosate resistance modes known in the art to produce plants or plant explants with superior glyphosate resistance. For example, glyphosate-tolerant plants can be produced by inserting into the plant's genome the capacity to produce higher levels of 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) as fully described in U.S. Pat. Patent Nos. 6,248,876 BI; 5,627,061; 5,804,425; 5,633,435; 5,145,783; 4,971,908; 5,312,910; 5,188,642; 4,940,835; 5,866,776; 6,225,114 BI; 6,130,366; 5,310,667; 4,535,060; 4,769,061; 5,633,448; 5,510,471; Re36,449; RE 37,287 E and 5,491,288; and international publications WO 97/04103; WO 00/66746; WO 01/66704 and WO 00/66747, which are hereby incorporated by reference in their entirety for all purposes. Glyphosate resistance also exists in plants expressing the gene encoding the enzyme glyphosate oxidoreductase, as described in more detail in U.S. Pat. Patent Nos. 5,776,760 and 5,463,175, which are hereby incorporated by reference in their entirety for all purposes.

Furthermore, the glyphosate resistance mechanism of the present invention can be combined with other herbicide resistance modes to provide plants or plant explants that are resistant to glyphosate and one or more herbicides. For example, hydroxyphenylpyruvate dioxygenases are enzymes that catalyze the reaction in which para-hydroxyphenylpyruvate (HPP) is transformed into a homogenate. Enzyme-inhibiting molecules that bind to the enzyme to inhibit the transformation of HPP into the homogenate are useful as herbicides. Plants that are more resistant to certain herbicides are described in U.S. Pat. Patent Nos. 6,245,968 BI; 6,268,549 and 6,069,115; and International Publication WO 99/23886, which are fully incorporated herein by reference for all purposes.

Sulfonylurea and imidazolinone herbicides also inhibit the growth of higher plants by blocking acetolactate synthase (ALS) or acetohydroxy acid synthase (AHAS). The production of sulfonylurea and imidazolinone tolerant plants is described in more detail in U.S. Pat. Patent Nos. 5,605,011; 5,013,659; 5,141,870; 5,767,361; 5,731,180; 5,304,732; 4,761,373; 5,331,107; 5,928,937 and 5,378,824; and International Publication WO 96/33270, which are fully incorporated herein by reference for all purposes.

Glutamine synthetase (GS) appears to be an essential enzyme required for the development and life of most plant cells. GS inhibitors are toxic to plant cells. Glufosinate herbicides were developed based on the toxic effect due to GS inhibition in plants. These herbicides are non-selective. They inhibit the growth of all the different plant species that are present, causing their total destruction. The development of plants having internal phosphinothricin acetyltransferase is described in U.S. Pat. Patent Nos. 5,969,213; 5,489,520; 5,550,318; 5,974,265; 5,919,675; 5,561,236; 5,648,477; 5,646,024; 6,177,616 BI and 5,879,903, which are incorporated herein by reference in their entirety for all purposes.

Protopophyrinogen oxidase (protox) is essential for the production of chlorophyll, which is essential for plant survival. The protox enzyme serves as a target point for various herbicidal compounds. These herbicides also inhibit the growth of all the different species that are present, causing their total destruction. The development of plants containing altered protox activity that are resistant to these herbicides is described in U.S. Pat. Patent Nos. 6,288,306 BI; 6,282,837 BI and 5,767,373; and International Publication WO 01/12825, which are fully incorporated herein by reference for all purposes.

Accordingly, the invention provides methods for selective weed control in a field, which include planting a field with crop seed or plants that are glyphosate-tolerant as a result of transformation with a gene encoding glyphosate N-acetyltransferase and applying to the crop and weeds in the field sufficient amounts of glyphosate to control the weeds without significantly affecting the crop.

The invention further provides methods for controlling weeds in a field and preventing the emergence of weeds resistant to glyphosate in a field containing a crop which include planting the field with crop seed or plants that are glyphosate-tolerant as a result of transformation with a gene encoding glyphosate N-acetyltransferase and a gene encoding a polypeptide that provides glyphosate tolerance by another mechanism, such as glyphosate-tolerant 5-enolpyruvylshikimate-3-phosphate synthase and/or glyphosate-tolerant glyphosate oxido-reductase and applying to the crop and weeds in the field sufficient amounts of glyphosate to control weeds without significantly affecting the crop.

In a further embodiment, the invention provides methods for controlling weeds in a field and preventing the emergence of herbicide-resistant weeds in a field in which a crop is located, comprising planting seeds of crops or plants that are tolerant to glyphosate as a result of transformation with a gene encoding glyphosate N-acetyltransferase, a gene encoding a polypeptide that provides tolerance to glyphosate by another mechanism, such as, for example, glyphosate-tolerant 5-enolpyruvylshikimate-3-phosphate synthase and/or glyphosate-tolerant oxido-reductase and a gene encoding a polypeptide that confers tolerance to an additional herbicide, such as mutated hydroxyphenylpyruvate dioxygenase, sulfonamide-tolerant acetolactate synthase, sulfonamide-tolerant acetohydroxy acid synthase, imidazolinone-tolerant acetohydroxy acid synthase, imidazolinone-tolerant acetohydroxy acid synthase, phosphinothricin acetyltransferase, and mutated protoporphyrinogen oxidase and application to a crop and sufficient amount of weeds in the field glyphosate and an additional herbicide, such as hydroxyphenylpyruvate dioxygenase inhibitor, sulfonamide, imidazolinone, bialaphos, phosphinothricin, azafenidin, butafenacil, sulfosate, glufosinate, and protox inhibitor to control weeds without significant impact on the crop.

The invention further provides methods for controlling weeds in a field and preventing the emergence of herbicide-resistant weeds in a field where a crop is located, comprising planting seeds of crops or plants that are tolerant to glyphosate as a result of transformation with a gene encoding glyphosate N-acetyltransferase, a gene encoding a polypeptide that provides tolerance to glyphosate by another mechanism, such as, for example, mutated hydroxyphenylpyruvate dioxygenase, sulfonamide-tolerant acetolactate synthase, sulfonamide-tolerant acetohydroxy acid synthase, imidazolinone-tolerant acetolactate synthase, imidazolinone-tolerant acetohydroxy acid synthase, phosphinothricin acetyltransferase and mutated protoporphyrinogen oxidase applying to the crop and weeds in the field a sufficient amount of glyphosate and an additional herbicide, as an inhibitor of hydroxyphenylpyruvate dioxygenase, sulfonamide, imidazolinone, bialaphos, phosphinothricin, azafenidin, butafenacil, sulfosate, glufosinate, i protox inhibitor, to control weeds without significant impact on the crop.

EXAMPLES

The following examples are provided by way of illustration and are not intended to be limiting. One skilled in the art will appreciate that non-critical parameters can be varied to obtain essentially similar results.

EXAMPLE 1: ISOLATION OF NEW GAT POLYNUCLEOTIDES

Five native GAT polynucleotides (that is, GAT polynucleotides found naturally in a non-genetically modified organism) were discovered by expression of cloned sequences from Bacillus strains exhibiting GAT activity. Their nucleotide sequences have been determined and are provided herein as SEQ ID NO.T-5. Briefly, a collection of approximately 500 strains of BacillusPseudomonas were screened for their native ability to N-acetylate glyphosate. Strains were grown overnight in LB, bacteria were collected by centrifugation, permeabilized in dilute toluene, and washed and resuspended in a reaction mixture containing buffer, 5 mM glyphosate, and 200 µM acetyl-CoA. Cells were incubated in the reaction mixture for between 1 and 48 hours, when an equal volume of methanol was added to the reaction. Cells were then harvested by centrifugation and supernatants were filtered before analysis by "parent ion mode" mass spectrometry. The product of the reaction was positively identified as N-acetylglyphosate by comparing the reaction mixture profile obtained on the mass spectrometer against the N-acetylglyphosate standard, as shown in Figure 2. Product detection was dependent on the inclusion of both substrates (acetyl-CoA and glyphosate) and was terminated by heat denaturation of the bacterial cells.

Individual GAT polynucleotides were cloned from identified strains by functional screening. Genomic DNA was prepared and partially digested with Sau3 Al enzyme. Fragments of about 4 kb were cloned into E. coli expression vector and transformed into electrocompetent E. coli. Individual clones that exhibited GAT activity were identified by mass spectrometry following the reactions described previously, except that the toluene wash was replaced by PMBS permeabilization. Genomic fragments were sequenced and the putative GAT polypeptide-encoding open reading frame was identified. The identity of the GAT gene was confirmed by expression of the uE open reading frame. colii by detecting high levels of N-acetylglyphosate produced in the reaction mixtures.

EXAMPLE 2: CHARACTERIZATION OF GAT POLYPEPTIDE

ISOLATED IZB. LICHENIFORMISSOYA B6

Genomic DNA from B. licheniformes strain B6 was purified, partially excised with Sau3Ai and fragments of about 1-10 kb were cloned into an E. coli expression vector. The clone with the 2.5kb insert provided glyphosate-N-acetyltransferase (GAT) activity to the E. coli host as determined by mass spectrometry analysis. Sequencing of the insert revealed one complete open reading frame of 441 base pairs. Further cloning of this open reading frame confirmed that it encodes a GAT enzyme. The plasmid, pMAXY2120 is shown in Figure 4. The gene encoding the GAT enzyme B6 was transformed into E. size XL1 Blue. A 10% inoculum of the saturated culture was added to Lauria Broth and the culture was incubated at 37°C for 1 hour. GAT expression was induced by adding IPTG at a concentration of 1 mM. The culture was incubated for another 4 hours, after which the cells were collected by centrifugation and the cell pellets were stored at -80°C.

Cell lysis was performed by adding 1 ml of the following buffer to 2 g of cells: 25 mM HEPE, pH 7.3, 100 mM KCl, and 10% methanol (HKM) plus 0.1 mM EDTA, 1 mM DTT, 1 mg/ml chicken egg lysozyme, and a protease inhibitor cocktail obtained from Sigma and used according to the manufacturer's recommendations. After 20 min of incubation at room temperature (eg, 22-25°C), lysis was terminated by brief sonication. The lysate was centrifuged and the supernatant was desalted by passing it through a Sephadex G 25 column equilibrated with HKM. Partial purification was achieved by affinity chromatography on CoA agarose (Sigma). The column was equilibrated with KHM and then the purified extract was passed through the column under hydrostatic pressure. Non-binding proteins were removed by washing the column with KHM containing 1 mM coenzyme A. The procedure provided a fourfold purification. At this level, approximately 65% of the stained protein on an SDS polyacrylamide gel blotted with crude lysate was GAT, while the other 20% was vector-encoded chloramphenicol acetyltransferase.

Purification to homogeneity was achieved by gel filtration of the partially purified protein through Superdex 75 (Pharmacia). The mobile phase was HKM, in which GAT activity eluted in a volume corresponding to a molecular diameter of 17 kD. This material was homogenous based on Coomassie staining of a 3 µg sample of GAT subjected to SDS polyacrylamide electrophoresis on a 12% acrylamide gel, which is 1 mm thick. Purification was achieved with a 6-fold increase in specific activity.

The exact Kmza of glyphosate was determined with a reaction mixture containing saturated (200 uM) Acetyl CoA of various concentrations of glyphosate and 1 pM purified GAT in a buffer containing 5 mM morpholine adjusted to pH 7.7 with acetic acid and 20% ethylene glycol. The initial reaction rates were determined by constantly monitoring the hydrolysis of the thioester bond in Acetyl CoAna 235 nM (E=3.4 OD/mM/cm). Hyperbolic saturation kinetics were observed (Figure 5), based on which an apparent KMod of 2.9 ± 0.1 (SD) mM was obtained.

Apparent KM for acetyl CoA was determined based on reaction mixtures containing 5 mM glyphosate, various concentrations of Acetyl CoA and 0.19 pM GAT in a buffer containing 5 mM morpholine adjusted to pH 7.7 with acetic acid and 50% methanol. Initial reaction rates were determined using mass spectrometric detection of N-acetyl glyphosate. Five oils were repeatedly injected into the instrument and reaction rates were obtained by comparing the reaction time against the integrated peak (Figure 6). Hyperbolic saturation kinetics were observed (Figure 7), on the basis of which a clear (apparent) KMod 2 pM was obtained. From the values for Vmax obtained for the known enzyme concentration, kcatod 6/min was calculated.

EXAMPLE 3: REVIEW PROCESS USING MASANA

SPECTROMETRY (SM)

A sample (5pl) was taken from a 96-well microtiter plate and injected at a rate of one sample per 26 seconds into a mass spectrometer (Micromass Quattro LC, triple quadrupole - quadrupole mass spectrometer) without separation. The sample was introduced into the mass spectrometer with a mobile phase of water/methanol (50:50) at a flow rate of 500 U/min. Each injected sample was ionized using a negative electrospray ionization process (needle voltage, -3.5 kV; cup voltage, 20 V; source temperature, 120°C; desolvation temperature, 250°C; cup gas flow, 90 L/hour; and desolving gas flow, 600 L/hour). The molecular ions (m/z 210) formed during these processes were selected by the first quadrupole to perform collision induced dissociation (CID) in the second quadrupole, where the pressure was set to 5 x 10"4 mBar and the collision energy was set to 20 Ev. The third quadrupole was set to allow only one of the "daughter" ions (m/z 124) produced from the parent ion (m/z 210) to enter the signal recording detector. The first and third quadrupoles were set to unity resolution while the photomultiplier was operated at 650 V. Pure N-acetylglyphosate standards were used for comparison and "peak" integration was used with this method.

EXAMPLE 4: DETECTION OF NATIVE GAT ENZYMES OR GAT

ENZYMES WITH LOW ACTIVITY

Native GAT enzymes or non-GAT enzymes with low activity typically have a kcatod of approximately lmin '' and a KM for glyphosate of 1.5 - 10 Mm. KM for acetyl CoA was typically less than 25 µM.

Bacterial cultures were grown in rich medium in deep 96-well plates and 0.5 ml cells from the stationary phase were collected by centrifugation, washed with 5 mM morpholine acetate pH 8 and resuspended in 0.1 ml reaction mixture containing 200 pM ammonium acetyl CoA, 5 mM ammonium glyphosate and 5 pg/ml PMBS (Sigma) in 5 mM morpholine acetate pH 8. PMBS permeabilizes the cell membrane and allows substrates and products to move from the cell into the buffer without releasing all cell contents. Reactions were performed at 25-37°C for 1-48 hours. Reactions were stopped by adding an equal volume of 100% ethanol and the entire mixture was filtered on a 0.45 µm MAHV Multiscreen filter plate (Millipore). Samples were analyzed on a mass spectrometer as described above and compared externally with synthetic N-acetylglyphosate standards.

EXAMPLE 5: DETECTION OF GAT ENZYME WITH HIGH ACTIVITY

GAT enzymes with high activity typically have kcatdo 400 lmin<_1>and Kmisunder 0.1 mM glyphosate.

Genes encoding GAT enzymes were cloned in E. coli expression vector pQE80 (Qiagen) and inserted E. coli XL1 Blue (Stratagene). Cultures were grown in 150 µl of rich medium (LB with 50 µg/ml carbelicillin) in shallow U-bottom 96-well polystyrene plates to late log phase and diluted 1:9 with fresh medium containing 1 mM IPTG (USB). After 4-8 hours of induction the cells were harvested, washed with 5 mM morpholine acetate pH 6.8 and resuspended in the same volume of the same morpholine buffer. Reactions were performed with up to 10 µl of washed cells. At higher activity levels, cells were first diluted up to 1:200 and 5 µl was added to 100 µl of the reaction mixture. To measure GAT activity, the same reaction mixture as described for low activity was used. However, for the detection of highly active GAT enzymes, the concentration of glyphosate was reduced to 0.15-0.5 mM, the pH was reduced to 6.8 and the reactions were performed for 1 hour at 37°C. Complete workup as well as MS detection were performed as described here.

EXAMPLE 6: PURIFICATION OF GAT ENZYME

Enzyme purification was achieved by affinity chromatography of cell lysates on CoA-agarose and gel filtration on Superdex-75. Quantities of purified GAT enzyme up to 10 mg were obtained as follows: 100 ml culture of E. coli carrying the GAT polynucleotide on the pQE80 vector and grown overnight in LB containing 5 µg/ml carbenicillin was used to inoculate 1 L of LB plus 50 µg/ml carbenicillin. After 1 hour, IPTG was added at a concentration of 1 mM and the culture was grown for another 6 hours. Cells were harvested by centrifugation. Lysis was performed by dissolving cells in 25 mM HEPES (pH 7.2), 100 mM KCl, 10% methanol (HKM), 0.1 mM EDTA, 1 mM DTT, protease inhibitor cocktail provided by Sigma-Aldrich, and 1 mg/ml chicken egg lysozyme. After 30 minutes at room temperature, the cells were briefly sonicated. The coarse material was removed by centrifugation and the lysate was passed through a bed of coenzyme A-agarose. The column was washed with several bed volumes of HKM and GAT was eluted in 1.5 bed volumes of HKM containing 1 mM acetyl CoA. The GAT in the eluate was concentrated by trapping it on a Centricon YM 50 ultrafiltration membrane. Further purification was done by passing the protein through a Superdex-75 column through a series of 0.6 ml injections. The peak of GAT activity was eluted in a volume corresponding to a molecular weight of 17 kD. The method resulted in the purification of the GAT enzyme to homogeneity with >85% recovery. A similar procedure was used to obtain 0.1 to 0.4 mg quantities and up to 96 mixed varieties in the same verme. The volume of the induced culture was reduced to 1 to 10 ml, coenzyme A-agarose affinity chromatography was performed in 0.15 ml columns packed on MAHV filter plates (Millipore) and chromatography with Superdex-75 was skipped.

EXAMPLE 7: STANDARD PROTOCOL FOR DETERMINING Kcat AND KM

^ and KM for glyphosate purified protein were determined using a continuous spectrophotometric assay in which hydrolysis of the sulfoester bond of Acetyl CoA was observed at 235 nm. Reactions were performed at ambient temperature (about 23°C) in wells of a 96-well assay plate, with the following components present in a final volume of 0.3 ml: 20 mM HEPES, pH 6.8, 10% ethylene glycol, 0.2 mM acetyl CoA, and varying concentrations of ammonium glyphosate. To compare the kinetics of two GAT enzymes, assays were performed for both enzymes under the same conditions, for example, both at 23°C. k^t was calculated from the Vmaxi concentration of the enzyme determined by the Bradford assay. KM was calculated from the initial reaction rates obtained from glyphosate concentrations in the range of 0.125 to 10 mM, using the Lineweaver-Burke transformation of the Michaelis-Menten equation. kcat/Km is determined by dividing the value determined for kcatsa by the value determined for Km.

Using this methodology, the affinity parameters for a number of GAT polypeptides are shown as examples herein. For example, kcat, Kmati, kcat/Kmat for the GAT polypeptide corresponding to SEQ ID NO:445 were determined to be 332 min '', 0.5 mM and 660 mM"<1>min "' using the assay conditions described above. kcat, Kmat and kcat/Kmat for the GAT polypeptide corresponding to SEQ ID NO:457 were determined to be 118 min "', 0.1 mM and 1184 mM" min_<1> using the assay conditions described above. kcat, Kmat and kcat/Kraatza GAT polypeptide corresponding to SEQ ID NO:300 determination gives 296 min "', 0.65 mM and 456 mM"<1>min " using the assay conditions described above. One skilled in the art can use these numbers (values) to confirm that the GAT activity assay generates GAT parameters suitable for comparison with the values given herein. For example, the conditions used to compare GAT activity should lead to the same kinetic constants for SEQ ID NO: 200, 445 and 457 (within normal experimental variance) as those reported herein, when the conditions used to compare the test GAT with the GAT polypeptide exemplified herein.

Kmza acetyl CoA was measured using a mass spectrometry method with repeated sampling during the reaction. Acetyl CoA and glyphosate (ammonium salt) were placed in 50-fold-concentrated stock solutions in a well of a mass spectrometry sample plate. Reactions were initiated by adding enzyme appropriately diluted in a volatile buffer such as morpholine acetate or ammonium carbonate, pH 6.8 or 7.7. The sample is injected repeatedly into the instrument and the initial rate is calculated from the comparison of the retention time and the peak area. Kmje calculated for glyphosate.

EXAMPLE 8: SELECTION OF TRANSFORMED . COLI

The evolved GAT gene (a chimera with a native B. licheniformes ribosome binding site (AACTGAAGGAGGAATCTC; SEQ ID NO:515 which is linked directly to the 5' end of the GAT coding sequence) was cloned into the expression vector pQE80 (Qiagen) between the EcoRI and HindIII sites, resulting in plasmid pMAXY2190 (Figure 11). This eliminated the His "tag" domain (tail of several histidines) from a plasmid carrying ampicillin and carbenicillin resistance. pMAXY2190 was electroporated (BioRAd Gene Pulser) into E. coli cells. The cells were then gently pelleted and washed once with M9 minimal medium. lacking aromatic amino acids (12.8 g/L Na2HP04.7 H20, 3 g/L KH2PO4, 0.5 g/L NaCl, 1.0 g/L NH4C1, 0.4% glucose, 2 mM MgSO4, 0.1 mM CaCl2, 10 mg/L thiamine, 10 mg/L proline, 30 mg/L carbenicillin), and resuspended in 20 ml of the same M9 medium. After overnight growth at 37°C at 250 rpm, equal volumes of cells were seeded onto M9 medium or M9 medium plus 1 mM glyphosate. The pQE80 vector without the GAT gene was similarly introduced into E. coli and seeded to single colonies for comparison. Table 3 summarizes the results and demonstrates that GAT activity enables the selection and growth of transformed E. colicells with less than 1%> background signal. Pay attention to IPTG induction was necessary for sufficient GAT activity to allow growth of the transformed cells. Transformation was confirmed by isolation of pMAXY2190 from E. coli cells that grew in the presence of glyphosate.

EXAMPLE 9: SELECTION OF TRANSFORMED PLANT CELLS

Agrobacterium-mediated transformation of plant cells occurs with low efficiency. To allow the propagation of transformed cells while inhibiting the proliferation of non-transformable cells requires a selectable marker. Antibiotic markers for kanamycin and hygromycin ibargen that modify the herbicide that detoxifies the herbicide compound phosphinothricin are examples of selectable markers used in plants (Methods in Molecular Biology, 1995, 49:9-18). Here we demonstrate that GAT activity serves as an efficient selectable marker for plant transformation. The evolved GAT gene (0 5B8) SEQ ID NO: 190 was cloned between a plant promoter (Strawberry vein curl virus amplified) and a ubiquinone terminator and inserted into the T-DNA region of the binary vector pMAXY3793 suitable for plant cell transformation by Agrobacterium tumefaciensEHA 105, as shown in Figure 12. A screenable GAT marker was present in T-DNA to enable confirmation of transformation. Transgenic tobacco shoots were obtained using glyphosate as the sole selective agent.

Axillary (underarm) buds of Nicotiana tabacumL. Xanthi were subcultured in half-strength MS medium with sucrose (1.5%) and Gelrite (0.3%) under light conditions - 16 hours (35-42 pEinstein m"<1>s~', white cool fluorescent lamps) at 24°C every 2-3 weeks. Young leaves were cut from the plants after 2-3 weeks of sub-cultivation and were chopped into segments of size 3 x 3 mm.A. tumefaciensisEHA105 was inoculated into LB medium and grown overnight to an optical density of A600=l.Cells were harvested at 4000 rpm for 5 min and resuspended in 3 volumes of liquid co-cultivation medium consisting of Musrashige and Skoog (MS) medium (pH 5.2) with 2 g/L N6-benzyladenine (BA), 1% glucose and 400 µM The pieces of leaves are then completely immersed in 20 mlA. tumefaciensis in 100 x 25 mm Petri dishes for 30 minutes, and blotted with autoclavable filter paper and then placed on solid co-cultivation medium (0.3% Gerlite) and incubated as described above. After 3 days of co-cultivation, 20-30 segments were transferred to basal shoot induction (BSI) medium consisting of MS solid medium (pH 5.7) with 2 mg/L BA, 3% sucrose, 0.3% Gerlite, 0-200 uM glyphosate and 400 ug/ml Timentin.

After three weeks, shoots were evident on explants placed on medium without glyphosate, regardless of the presence or absence of the GAT gene. T-DNA transfer from both constructs was confirmed with GUS histochemical staining of leaves from regenerated shoots. A concentration of glyphosate greater than 20 µM completely inhibited any shoot formation from explants lacking the GAT gene. Explants infected with A. tumefaciensissa with the GAT construct regenerated buds at glyphosate concentrations up to 200 µM (the highest tested concentration). Transformation was confirmed by GUS histochemical staining and by PCR amplification of the GAT gene fragment using primers that bind to the promoter and 3' region. The results are summarized in Table 4.

EXAMPLE 10: SELECTION OF TRANSFORMED YEAST CELLS WITH GLYPHOSATE

Selective markers for yeast transformation are usually auxotrophic genes that enable the growth of transformed cells in a medium lacking a specific amino acid or nucleotide. Since Saccharomyces cervisia is sensitive to glyphosate, GAT can also be used as a selective marker. To demonstrate this, the evolved GAT gene (0_6D10), SEQ ID NO: 196, was cloned from the T-DNA vector pMAXY3793 (as shown in Example 9) as a Pstl-Clal fragment containing the entire coding region and ligated with Pstl-Clal cut p424TEF (Gene, 1995, 156:119-122) as shown in figure 12. This plasmid contains "origin" - the beginning of replication from E. coli gene conferring resistance to cerebenicillin as well as TRPI, a selective tryptophan auxotrophy marker for yeast transformation.

The GAT-containing construct was transformed into E. coliXL1 Blue (Stratagene) and plated on solid medium-LB-agar with carbenicillin (50 µg/ml). Plasmid DNA was prepared and used to transform yeast strain YPH499 (Stratagene) using a transformation kit (BiolOl). Equal amounts of transformed cells were seeded on dishes with CSM-YNB-glucose medium (BiolOl) without aromatic amino acids (tryptophan, tyrosine, and phenylalanine) with added glyphosate. For comparison, p424TEF lacking the GAT gene was also introduced into YPH499 and plated as described. The results demonstrated that GAT activity will function as a selectable marker. The presence of the GAT-containing vector in glyphosate-selected colonies can be confirmed by plasmid re-isolation and restriction digestion analysis.

EXAMPLE 11: SPRAY TESTS OF TOBACCO PLANTS EXPRESSING GAT

WITH HERBICIDE

The tobacco shoots obtained in the manner described in EXAMPLE 9 were cut from the explants and transferred to basal root induction medium (BRI) consisting of half-strength Murashige and Skoog (MS) medium, pH 5.7, with 1.5% sucrose, 0.3% Gelrite, 0-200 uM glyphosate and 400 ug/ml Timentin. Plants with roots and axillary shoots were clonally propagated by cutting the petiole and transferring it to fresh medium until the desired number of clones was obtained. Before placing the plants in small pots with soil, the roots were washed to remove Gerlite residues. A protective plastic cover was placed over the plants for at least one week until the plants were well received.

To determine whether GAT-expressing tobacco plants could tolerate simulated field spray rates with glyphosate, clonal lines of several events per GAT variant were tested. A typical test is set up as follows. One clone of each variant was sprayed with 1 ml of a solution containing the isopropylamine salt of glyphosate (Sigma P5671) and 0.125% Triton X-100, pH 6.8 so that the sprayed amount of active substance was equal to that present in commercial products with glyphosate. For example, to achieve 32 oz/acre (IX) of herbicide containing 40% active ingredient ("as"), 2.4 ul of the 40% as formulation was diluted in 1 ml of water and sprayed onto plants in 4-inch (16 in<2>) square pots. A control application (mock) (0X) with only surfactant (surfactant) is also included. In some cases, after 1-4 weeks another, second spraying was applied. Plants were kept in controlled growth rooms at 25°C and 70% humidity with a 16-hour light period.

In this example, 10 events were confirmed positive for GAT0_610 (SEQ ID NO: 196). ten for GAT0 5D3 (SEQ ID NO: 193), 8 events for GAT0 5B8 (SEQ ID NO: 190) and plants transformed with vector alone (without GAT) were clonally propagated, transferred to soil and sprayed - when the plants had an average of 5 leaves.

Wild plants grown from seed are also sprayed. After two weeks vector-only plants and plants grown from seed that were sprayed with 0.5, 2 or 4 x glyphosate stopped growing, wilted and turned brown. Each transgenic GAT plant survived the spray procedure without signs of glyphosate damage, such as chlorosis, leaf elongation, stunting, or browning. All 0X plants were healthy, including non-GAT control plants. Three weeks later, all surviving plants were sprayed with an 8X dose. 0X control plants died within two weeks. Again, all GAT plants survived.

Tobacco plants transformed with GAT and selected on glyphosate were fertile. Flowering pattern and seed set were not detectably different from the wild plant strain.

EXAMPLE 12: MENDELJIAN INHERITANCE OF GAT GENE I

GLYPHSATE-TOLERANT GENOTYPE

Mendelian inheritance of the GAT gene and the glyphosate-tolerant genotype was demonstrated with transformed Arabidopsis. Columbia-type Arabidopsis plants were grown and transformed using the submersion method (Clough, SJ and Bent, AF, (1998) Plant J. 16(6):735-43) with a construct containing a GAT variant called (SEQ ID NO: 16). Bunch seeds were collected and GAT plants were confirmed by PCR with primers specific for the insert within the T-DNA. TI seeds from individual events were sown on the ground at 10-30 seeds per 2-square-inch pot. When the first set of true leaves emerged, the pots were sprayed with glyphosate equal to 0.5 and IX of the commercial product (as calculated in Example 11). After two weeks the segregation of the transgene and the tolerant phenotype was evident as shown in Table 5.

Ratios of approximately 3:1 indicate a dominant segregation event. Ratios greater than 3:1 indicate several segregating inserts. Ratios less than 3:1 may be due to small sample size effects, incomplete dominance, or positional effects that alter expression that is then too low to confer herbicide tolerance. When compared to controls, it is clear that the GAT gene is transmitted to the TI generation and confers confirmed glyphosate tolerance.

EXAMPLE 13: PRODUCTION OF GLYPHOSATE RESISTANT CORN

EXPRESSING GAT TRANSGENES

Maize plants expressing GAT variant transgenes were produced using methods described in U.S. Pat. Patent No. 5,981,849, which is incorporated herein by reference. Specifically, Agrobacterium tumefaciens vectors were constructed based on methods known in the art. Each vector contained an insert that has an ubiquitin promoter and an intron, a GAT variant, and a Pinll terminator. Immature maize embryos were excised and infected with an Agrobacterium tumefaciens vector containing the GAT variant of interest. After infection, embryos were transferred and grown in co-cultivation medium. After co-cultivation, infected immature embryos were transferred to medium containing 1.0 mM glyphosate (Roundup ULTRA MAX™). This selection continued until actively growing putative transgenic calli were identified. Tissues of putative transgenic calli were sampled for PCR Western assay (data not shown) to confirm the presence of the GAT gene. Tissues of presumptive transgenic calli were maintained on selection in medium with 1.0 mM glyphosate and were selected before plant regeneration. During the regeneration of the callus tissue, which was confirmed to be transgenic, it was transferred to the maturation medium with 0.1 mM glyphosate and grown until the maturation of the somatic embryo. Mature embryos were then transferred to a regeneration medium with 0.1 mM glyphosate for the formation of shoots and roots. After emergence of shoots and roots, individual young plants were transferred to tubes with root development medium containing 0.1 mM glyphosate. Young plants with developed shoots and roots were transplanted into pots in the greenhouse for further growth to generate TO spray data and produce TI seeds.

In order to assess the level of glyphosate resistance of transgenic maize plants expressing the GAT variant of the transgene, TO plants were sprayed with glyphosate (Roundup ULTRA MAX™) in the greenhouse. Plant resistance levels were estimated based on the results of plant decolorization and plant height measurements. Plant discoloration and plant height were evaluated based on the following scales:

Decoloration value after 1, 2, 3 and 4 weeks after spraying with glyphosate

9 = no leaves/discolored petiole

7 = few leaves/discolored petiole

5 = diseased leaves/discolored petiole

3 = severely discolored plant or dying plant

1 = dead plant

Plant height measurements

before spraying with glyphosate

after spraying with glyphosate at 1, 2, 3 and 4 weeks

mature plants (per bunch)

Two plants from each event listed in Table 6 were transferred to the greenhouse (independent transgenic callus). Plant 1 was kept for seed production and was not sprayed with glyphosate. Plant 2 was sprayed with 4X glyphosate (1Xglyphosate=26 ounces/acre) 14 days after transplanting. Decoloration values of TO plants with 4X spraying 7 and 14 days after spraying are shown in Tables 6 and 7. Values related to height at tasseling are shown in Figure 14. An additional experiment was performed in which TO plants were sprayed with 6X glyphosate. The decolorization values of TO plant with 6X spraying 10 days after spraying are shown in Table 8.

EXAMPLE 14: GAT IS ALSO AN ACETYLTRANSFERASE

The ability of GAT variants (B6 (SEQ ID NO:7), 0 6D10 (SEQ ID NO:448), 17-15H3 (SEQ ID NO:601), and 20-8H12c (SEQ ID NO:817)) to transfer a propionyl group from propionyl CoA to glyphosate was tested in a reaction mixture containing 5 mM glyphosate or without glyphosate. PropionylCoA was present at 1 mM. After 30 minutes the reactions were stopped and the presence of free propionyl CoA was determined by adding DNTB. All variants showed the ability of glyphosate-dependent hydrolysis of propionyl CoA. The results indicate that GAT also functions as an acetyltransferase.

EXAMPLE 15: TI STUDIES OF GLYPHOSATE-RESISTANT

MAIZE EXPRESSING GAT TRANSGENES

Maize plants expressing the GAT variant of transgenes 18-28D9b (SEQ ID NO:814) and 17-15H3 (SEQ ID NO:549) were produced using the methods described in Example 13.

TI plants were used to obtain glyphosate tolerance data in the field. TI plants were treated in the field with four different glyphosate spray treatments (0X, 4X, 8X, and 4X + 4X) for each event. The plants were sprayed at V3 V8. Results for leaf discoloration and plant height comparisons were taken 10 days after treatment as described in Example 13. The TI field spray data correlated well with previously obtained greenhouse results as reported in Example 13. T2 seeds were collected for further studies.

EXAMPLE 16: THERMOSTABILITY OF GAT POLYPEPTIDE

A. EFFECT OF TEMPERATURE VARIATION ON GLYPHOSATE TOLERANCE

GLYPHOSATE RESISTANT MAIZE EXPRESSING GAT TRANSGENES

Maize plants expressing the GAT variants of transgenes 10_4F2 (SEQ ID NO:203), 17-15H3 (SEQ ID NO:549), and 18-28D9b (SEQ ID NO:814) were produced using the methods described in Example 13.

The effect of temperature on glyphosate tolerance was evaluated in TI plants. TI plants were grown in cool/cold conditions (day 14° C, night 8° C), warm (day 28° C, night 20° C), and hot (day 37° C, night 20° C). TI plants were sprayed at V2 with four different glyphosate spray treatments (0X, 4X, 6X, and 8X). Results for leaf discoloration and plant height comparisons were taken on days 5 and 14 after treatment, as described in Example 13. Visual observations indicated that the range of temperatures tested had no detrimental effect on glyphosate tolerance.

B. EFFECTS OF TEMPERATURE VARIATION ON GAT ACTIVITY IN VITRO

In vitro thermostability of several GAT polypeptides (DS3 (native GAT polypeptide corresponding to SEQ ID NO: 8), 6 6D5 (SEQ ID NO: 410), 17-15H3 (SEQ ID NO: 601), 20-8H12 (SEQ ID NO: 739), 22-13B12 (SEQ ID NO: 781) and 401 (native GAT polypeptide corresponding to corresponding to SEQ ID NO: 6)) was evaluated according to the following method. Enzymes were dispensed into 200 µl PCR tubes (VWR, San Francisco, CA) and incubated in a gradient thermocycler (ML Research, Watertown, MA) for 15 minutes at various temperatures between 30°C and 60°C as marked in Figure 17. Precipitated proteins were removed by centrifugation and the remaining enzyme activity of the remaining soluble proteins was measured at 22°C via continuous spectrometric assay, as described in Example 7. Saturation concentrations of glyphosate were used (10 mM for DS3 (SEQ ID NO: 8), 401 (SEQ ID NO: 6), and 6 6D5 (SEQ ID NO: 410); 5 mM for 17-15H3 (SEQ ID NO: 601), 20-8H12 (SEQ ID NO: 739), and 22-13B12 (SEQ ID NO: 781) and AcCoA (167 pM).

The data are shown in Figure 17. Native (ie, wild type) GAT polypeptides DS3 (SEQ ID NO: 8) and 401 (SEQ ID NO: 6) appeared to be stable in activity at temperatures up to about 42 to about 44°C. GAT polypeptides that are not native to any organism (ie, wild type) functioned stably at temperatures ranging from about 47°C to about 54°C.

The half-lives of several GAT polypeptides were also measured at 37.5°C based on the following procedure. GAT polypeptides 401 (SEQ ID NO: 6), 17-15H3 (SEQ ID NO: 601), 20-8H12 (SEQ ID NO: 739), 22-13B12 (SEQ ID NO: 781), 22-15B4 (SEQ ID NO: 946) and 22-18C5 (SEQ ID NO: 795) were incubated in a matrix of 25 mM Hepes, pH 7.2, 10 mM KCl and 10% methanol ("HKM"). Aliquots were taken at various time points and assays were performed in triplicate at 22°C using the continuous spectrometric assay described in Example 7 using saturating concentrations of glyphosate (20 mM for 401, 5 mM for others) and AcCoA (167 µM). The standard error at each time point averaged about 2.9%. GAT activity was plotted as a function of incubation time and the data were fitted to an exponential decay curve (y=e_<x>), where y is the enzyme activity and x is the time in hours, from which the half-life was calculated. The data is shown below in Table 9.

EXAMPLE 17: PRODUCTION OF GLYPHOSATE-RESISTANT SOYBEAN

EXPRESSES GAT TRANSGENE

Soybean plants expressing GAT variants of the transgene were produced using particle gun bombardment (see Kleinet al. (1987) Nature 327:10-13) using a DuPont Biolistic PDS1000/He instrument. The agent of choice used during the transformation process was hygromycin. Either the hygromycin selectable gene marker remained in the transgenic events, or the hygromycin gene was excised by methods known in the art. DNA fragments were prepared with a synthetic constitutive promoter, a GAT variant and a Pinll terminator. A selectable marker gene containing the 35S CaMV promoter, HPT genes and NOS terminator was co-bombarded with the GAT gene variant as described above. Bombarded embryogenic soybean tissue suspension was grown for one week in the absence of selection agent. Embryogenic tissue suspension was plated on selective liquid medium for 6 weeks. A putative transgenic tissue suspension was sampled for PCR analyzes to determine the presence of the GAT gene. The putative transgenic tissue culture suspension was maintained in selective medium for 3 weeks to obtain sufficient tissue for plant regeneration. Suspension tissue was matured for 4 weeks using standard procedures; matured somatic embryos were dried in a desiccator for 4-7 days and then placed on germination induction medium for 2-4 weeks. Young germinal plants were transferred to the soil in a cell tray pack for 3 weeks for acclimatization, to assess resistance to glyphosate, young plants were placed in a greenhouse in pots of 10.

To determine the glyphosate resistance of transgenic soybeans expressing the GAT variant of the transgene, TO plants were sprayed with glyphosate (Roundup ULTRA MAX™) in the greenhouse. Plant resistance levels were assessed using plant decolorization values and plant height measurements.

Decolorization value 2 weeks after spraying with glyphosate

9 = no leaves/discolored petiole

7 = few leaves/discolored petiole

5 = diseased leaves/discolored petiole

3 = severely discolored plant or dying plant

1 = dead plant

One to four plants were sent to the greenhouse for each independent transgenic event. An additional 1-2 plants per event were grown in controlled environment growth rooms for seed production and were not sprayed with glyphosate. Greenhouse plants were sprayed with IX, 2X or 4X glvphosate (IX glyphosate = 26 ounces/acre RoundUp ULTRA MAX™) 3-4 weeks after transfer to soil. Plant decolorization values for TO plants at 2X and 4X spray rates are shown in Table 10 and Table 11.

These results show that soybeans are efficiently transformed with GAT gene variants as confirmed by PCR analysis. Transgenic soybeans expressing GAT gene variants are resistant to glyphosate at 2X and 4X spray rates. Events surviving the 4X glyphosate spray rate showed some minor discoloration, however during the 2 week spray test, plants recovered and displayed normal leaf morphology.

EXAMPLE 18: THE EFFECT OF SALT ON THE KINETICS OF GAT

In order to better determine the physiological conditions under which the GAT enzymes of the invention are intended to be used (eg plant cells) the activities of some of the GAT enzymes of the invention were re-evaluated in the presence of added salts. Figures 15A and 15B provide a comparison of the kinetic parameters Kmand kcat/Km, for the native GAT enzymes GAT401 (SEQ ID NO:6), B6 (SEQ ID NO:7), and DS3 (SEQ ID NO:8), and the engineered GAT enzymes 0 6D10 (SEQ ID NO:448), 10 4F2 (SEQ ID NO:454), 18-28D9 (SEQ ID NO:448). NO:618), 17-15H3 (SEQ ID NO:601), 17-10B3 (SEQ ID NO:592), 20-8H12 (SEQ ID NO:739), 20-16A3 (SEQ ID NO:639), and 20-30C6 (SEQ ID NO:683), which were assayed either in the absence or presence of added KC1 (unshaded columns). 20 mM KC1 (shaded columns). Protein concentrations were determined using the Bradford assay as described in Example 7. Due to their extremely low Kms for glyphosate in the absence of KC1, the kinetic parameters for the developed GAT enzymes 0_6D10, 18-28D9 and 20-8H12 were determined in the absence of KC1 using a mass spectrometer assay as described in Example 3, while the other kinetic parameters (either in the absence or in the presence of KCl) determined by a continuous spectrophotometric assay, as described in Example 7.

"Error bars" represent the standard deviation of multiple essays, where shown. Figure 15 shows that addition of salt (20 mM KCl) to the assay buffer significantly increases the K value for glyphosate. The kcat value remains relatively unchanged or slightly increased, the overall result being observed as a lower kcat/Km value for GAT enzymes assayed in the presence of 20 mM KCl than in the absence of added KCl (Figure 15B).

EXAMPLE 19: ENZYMES WITH EXTREMELY HIGH ACTIVITY

Additional iterations of directed molecular evolution have led to the creation of further developed gatgenes that encode GAT enzymes that exhibit extremely high GAT activity, for example, exhibit one or more improved traits such as reduced Kmza glyphosate, increased kcat, or increased kcat/Kmako compared to previously described GAT enzymes.

Further developed genes were first selected for growth in E. coli in minimal M9 medium as described in Example 8, except that 5 mM rather than 1 mM glyphosate was used for selection. Proteins were purified as described in Example 6 above.

Protein concentrations were determined by UV absorbance at 205 nm. The extinction coefficient was determined by the method described by Scopes (1994; Protein Purification, Principles and Practice, Springer, New York) based on the formula E (mg ml"<1>cm"<1>) = 27 + 120(A280/A205) = 30.5. Prior to quantification by UV absorption, the protein solution was buffer exchanged to 50 mM Na2SO4 using a NAP-5 column (Amersham-Pharmacia Biotech).

Examples of further altered Gat coding sequences include the nucleic acid sequences identified herein as SEQ ID NO: 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916, 918, 920, 922, 924, 926, 928, and 930, which encode further altered GAT enzymes comprising the amino acid sequences identified herein as SEQ ID NO: 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 929, and 931. Some further modified GAT enzymes exhibit extremely high GAT activity, thus exhibiting one or more improved traits such as reduced Kmza glyphosate, increased kcat, or increased kcat/Kmako are compared with previously described GAT enzymes for which assays were performed under the same conditions.

Figures 16A, 16B and 16C provide a comparison of the kinetic parameters, Km, kcat, and kcat/Km, of several previously described GAT enzymes (unshaded columns) with the kinetic parameters of some further modified GAT enzymes of the invention (shaded columns), which were assayed using a continuous spectrophotometric assay in the presence of 20 mM KCl by determining the amount of protein via UV absorbance, as described in the text above. "Error bars" represent the standard deviation of multiple essays. Under these assay conditions, the native GAT enzyme GAT401 (SEQ ID NO:6) showed a Km for glyphosate of about 4 mM, and a k^t of about 5.4 min"1, and a kcat/Kmod of about 1.35 mM"<1>min"<1.>When the assays were performed under these conditions, some further developed GAT enzymes of the invention (shaded columns) showed a range of Km values for glyphosate of less than about 0.4 mM (such as between about 0.4 mM and 0.1 mM), kcat values of less than about 1000 min"<1> (such as between about 1000 min"<1> and about 2500 min"<1>), and kcat/Km values of at least about 4800 mM" min" (such as between about 4800 mM" min" and about 8000 mM" min"). for example, some further modified GAT enzymes of the invention show at least about a 7000-fold increase in kcat/Km over the native GAT enzyme GAT401 under these assay conditions.

Some further developed GAT enzymes of the invention contain one or more amino acid residue positions not observed in previously described GAT polypeptides and GAT enzymes, such as an amino acid residue at position 27, BI, Zl or A; an amino acid residue at position 33, N or G; an amino acid residue at position 46, and B2, Z4, or H; and an amino acid residue at position 93, R; wherein BI is an amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S, and T; Z1 is an amino acid selected from the group consisting of A, I, L, M and V; and Z4 is an amino acid selected from the group consisting of R, H, and K. For example, some further modified GAT enzymes of the invention contain one or more of: Ala at position 27 (ie, Ala27); Asn or Gly at position 33 (ie, Asn33 or Gly33); and His at position 46 (ie, His46); and an Arg at position 93 (that is, Arg93), with the assignment of sequence numbers corresponding to, for example, SEQ ID NO: 907.

Sequence/activity analyzes were performed to identify amino acid residues that positively correlate with high kcat/Km (as manifested by high kcat, low Km, or both). Amino acid residues that appear to correlate positively with high kcat/Kmu include Glul4, Asp32, Asn33, Gly38, and Thr62 (sequence number designations corresponding to that of SEQ ID NO:907). Additional GAT enzymes can be constructed by codon substitution for one or more of these residues at the appropriate position(s) of the coding sequence of the template GAT polypeptide. For example, additional GAT enzymes are obtained by substituting one or more codons encoding Glu at codon position 14, Asp at position 32, Asn at position 33, Gly at position 38, and Thr at position 62, in the nucleic acid sequence encoding the matrix polypeptide, such as GAT 24-5H5 (SEQ ID NO:845) or GAT 25-8H7 (SEQ ID NO:907), two further altered GAT enzymes exhibiting extremely high activity as described above. Examples of further altered GAT enzymes obtained in this manner, identified herein as R12G1 (SEQ ID NOs917), R12G2 (SEQ ID NO:919), R12G3 (SEQ ID NO:921), R12G4 (SEQ DD NO:923), R12G5 (SEQ ID NO:925), R12G6 (SEQ ID NO:927), R12G7 (SEQ ID NO:929), and R12G8 (SEQ ID NO:931)~ encoding nucleic acids identified as SEQ ID NO: 916, 918, 920, 922, 924, 926, 928, and 930, exhibited extremely high GAT activities comparable to that of matrix polypeptides.

EXAMPLE 20: AMINO ACIDS CORRELATING WITH HEIGHT

GAT ACTIVITY

The amino acids: aspartic acid (Asp, D), histidine (His, H) and cysteine (Cys, C) are known to be associated with the active sites of various acetyltransferase enzymes. To determine whether any such residue plays a role in GAT activity, all D, C, and H residues of GAT20-30C6 (SEQ ID NO:683) were individually mutated to alanine (Ala, A) and the mutated enzymes were assayed for N-acetylgluphosate activity. Variants containing the D34A and H41A substitutions retained only about 2%-3% activity relative to the unmodified enzyme, while variants containing the H138A substitution showed essentially no measurable GAT activity. On the other hand, variants containing the H138R and H138S substitutions retained low but measurable GAT activity (especially at pH greater than 6.8), indicating that His (and nominally Arg and Ser) at position 138 may serve as an active site base.

EXAMPLE 21: ENHANCEMENT OF GAT ACTIVITY IN PLANTS

Plants, animals, and microbes are known to have preferences for specific codons that influence the efficiency of amino acid incorporation during translation of gene transcripts. Rare codons can cause a problem with the recruitment of tRNA during translation, which could then lead to accumulation of the encoded protein. The original parental genes are of bacterial origin, such as Baccillus licheniformes, and thus may not have an optimal codon distribution for expression in plants. The modified genes of the invention have been successfully expressed in plants (see, for example, Examples 9, 11, 13 and 17 above), but there is a chance to improve protein production by increasing translation efficiency in plants. One way to achieve this is by substituting one or more codons in the coding sequence that are rarely used in plants for codons for the same amino acid(s) that are more commonly used in plants, thus producing "silent" mutations in the coding sequence with an unchanged protein-encoding sequence.

Tables showing the frequency of codon usage in cotton, maize and soybeans (available, for example, from the website maintained by the Kazus DNA Research Institute, Chiba, Japan) were compared to obtain the following table (Table 13) which shows the codons that are generally more frequently or less frequently used in both monocots and dicots.

Another way to increase plant expression of microbial genes is to increase the G+C content near the site of the initial methionine residue. Coding sequences found naturally in plants tend to contain three G and/or C residues downstream of the ATG initiation codon (Joshiet et al. (1997) Plant Mol. Biol. 35:993-1001). Insertion of the coding sequence of one or more codons immediately downstream of the ATG initiation codon can create a more plant-like coding sequence and this can enhance their expression in plants. Substitution of the second codon (isoleucine, ATA) for an alanine codon (GCG) resulted in an Ile2Ala variant with reduced kcat, when compared to the unmodified enzyme. On the other hand, the insertion of an alanine codon (either GCG or GCT) between the codon for Met codon position 1 and Ile in codon position 2 resulted in a non-coding sequence encoding a GAT enzyme possessing an Ala residue inserted between Met in position 1 and Ile in position 2. Examples of the GAT enzyme variant containing two alanines inserted between Met and Ile2 that have been mentioned are identified as 22-15B4 M1MAA (to highlighted the insertion of two alanine residues immediately after Met at position 1) and having the protein sequence SEQ ID NO:948, showed reduced kcat when compared to the unmodified enzyme 22-15B4 (SEQ ID NO:789). An example of a GAT enzyme containing a single alanine inserted between Met and Ile2, designated 22-15B4 Ml MA (to emphasize the insertion of an Ala residue immediately after Met at position 1), having the protein sequence of SEQ ID NO:946, showed essentially unchanged kinetics when compared to the unmodified 22-15B4 enzyme.

A general strategy for improving GAT expression in plants has been developed. Altered non-coding sequences can be changed by substituting codons used in plants for codons more commonly used in plants, for example based on the table below. Codons that are used in plants (for example, based on the table below) should generally be avoided. In this way, at least one codon (such as at least three codons, at least five codons, or at least ten codons) can be changed in the coding sequence from codons used less frequently in plants to codon(s) more commonly used in plants. The codons to be replaced may be located at the 5' end of the coding sequence (eg, within the first 10 codons, within the first 20 codons, within the first 50 codons, or within the first 100 codons) of the coding sequence. Alternatively, the codons that are substituted can be located throughout the coding sequence. More commonly used codons can further be selected to avoid more than 5-10 (such as more than about 5, more than about 6, more than about 7, more than about 8, even more than about 9 or more than about 10) consecutive occurrences of G+C or A+T within the coding sequence. The coding sequence may also be altered to contain one or two CG-rich codons immediately downstream of the ATG initiation codon, such as by inserting an Ala codon (eg, the commonly used Ala codon) immediately downstream of, and adjacent to, a Met codon in the coding sequence.

Table 14 presents examples of gene coding sequences that have been altered as described above.

A binary vector with a dMMV-gaMJBQ3 cassette in T-DNA was transformed into competent Agrobacterium Ttumefaciens C58 cells by electroporation (McCormacet al., Mol Biotechnol. 9:155-159, 1998). After growth on LB + 40 ug/ml kanamycin cups for 2 days at 28°C, colonies were inoculated into LB + 40 ug/ml kanamycin liquid medium and shaken overnight at 28°C. Agrobacterium cells were harvested by centrifugation at 4000g, 10 minutes and then resuspended in a volume of 10mM MgSO4 equivalent to the initial culture volume. The bacterial suspension was forced or "infiltrated" into the intracellular spaces of Nicotiana benthamiana leaves using a 1 ml plastic syringe (no needle). By infiltrating 200-300 µl of the bacterial suspension to each site (typically 3-4cm<2>in the infiltrated area), 4 or more sites could be accommodated on a single leaf still attached to the plant. In some cases, an Agrobacterium strain containing gat is diluted 5:1 or 10:1 with another Agrobacterium strain that lacks gat, before infiltration.

The dilution step has the effect of reducing overall gat gene expression in plant cells, thus preventing saturation and allowing visualization of expression differences between variants and constructs. After 3 days, the leaf material was crushed, extracted in an aqueous buffer and centrifuged. The supernatant, which contains soluble proteins, was put on SDS-PAGE and the gel was blotted, and a test was performed with an antiGAT polyclonal antibody.

The level of GAT protein accumulated in tobacco leaves infiltrated with the GAT4620 gene was comparable to the level of protein accumulated in leaves transformed with the non-modified GAT25-8H7/4618 gene. Tobacco leaves carrying the GAT4621 gene, on the other hand, showed about twice the accumulation of GAT protein, as a percentage of total protein, when compared to leaves expressing the unmodified GAT25-8H7/4618 gene.

EXAMPLE 22: TI STUDIES OF GLYPHOSATE-RESISTANT SOYBEAN

EXPRESSING THE GAT TRANSGENE

Soybean plants expressing the GAT transgene 18-28D9c (SEQ ID NO:824) were produced using the methods described in Example 17. TI seeds were collected from TO plants sprayed with glyphosate. TI seeds were germinated under greenhouse conditions in RediEarth<R>360 medium, available from Scotts, Marvesville, OH, and sprayed at the V2-V3 level with either 2X or 4X Glvphosate (RoundUp ULTRA MAX™, available from Monsanto, St.Louis, MO) as in the methods described in Example 17. Plants were counted after 10 days and leaf decolorization scores were taken as described in Example 17. TI greenhouse spray data correlated well with previous results at the TO plant level. T2 seeds were collected for further studies.

EXAMPLE 23: PRODUCTION OF GLYPHOSATE-RESISTANT SOYBEAN I

SULFONAMIDE EXPRESSING GAT AND HRA TRANSGENES

Soybean plants expressing GAT & HRA, a highly resistant allele of acetolactate synthase (U.S.

Patent Nos. 5,605,011, 5,378,824, 5,141,870, and 5013,659), genes were produced using the methods described in Example 17. This selective agent was used as a selectable marker gene for transformation. The selective agent is chlorsulfuron at a concentration of 100 ng/ml.

A selectable marker is included with the S-adenosyl-L-methionine synthetase (SAMS) promoter from Glycine max (U.S. 2003/226166), the HRA coding sequence from Glycine maxi acetolactate synthetase terminator from Glycine max. The selectable marker gene is either co-bombarded with a GAT construct consisting of a synthetic constitutive promoter (U.S. Patent Nos. 6,072,050 and 6,555,673) or the maize Histone 2B promoter (U.S. Patent No. 6,177,611), the GAT variant (18-28D9c (SEQ ID NO:824)) and the Pin II terminator (Gwheung et al, Plant Cell 1:115:122(1989)). Transgenic plants were obtained as described in Example 17. Levels of glyphosate resistance were determined as described in Example 17 using decolorization score values after 2X or 4X application rates of glyphosate. The results shown in Table 15 show that different constitutive promoters driving GAT variants (18-28D9c (SEQ ID NO:824)) confer glyphosate resistance in TO plants.

EXAMPLE 24: TI "PRE-EMERGENCY" (SPRAYING BEFORE SEED GERMINATION) STUDIES

SOYBEAN EXPRESSING GAT AND HRA TRANSGENES

TI seeds generated from the experiments, as described in Example 17, were sown in pots with Tama Slit loam in the greenhouse. The pots were immediately sprayed with a "pre-emergent" (herbicide spray before seed germination) application of chlorimuron, rimsulfuron or tribeneuron at a rate of 70 grams a.i./hectare. Germinating plants were analyzed 10 days post-spray based on plant decolorization results as described in Example 17. All HRA and GAT events survived all pre-emergency spray applications with a score of 9 (uninjured). These results demonstrate "pre-emergence" resistance to sulfonamide hernia in soybean.

EXAMPLE 25: TI "POST-EMERGENCY" (SPRAYING AFTER SEED GERMINATION)

STUDIES OF SOYBEAN EXPRESSING GAT AND HRA TRANSGENES

TI seeds obtained from experiments, as described in Example 17, were germinated in RediEarth<R>360 medium in a greenhouse. Plants were sprayed at V2-V3 stage (14 days after planting) with thifensulfuron, rimsulfuron or tribenuron (70, 70, 35, 35 gm a.i./hectare). Plants were analyzed 10 days after application based on the decolorization results of the plant described in Example 17. The results are shown in Table 16.

Events in which plant decoloration occurred at rank 7 or 8 after tifensulfuron spraying were sprayed with - either a 2X or 4X application of glyphosate after 10 days, as per the methods described in Example 17. Events were evaluated based on the decolorization results described in Example 17. All thifensulfuron tolerant events survived the 7 or 8 glyphosate sprays (results not shown). These results show a 100% correlation of thifensulfuron tolerance under greenhouse conditions provided by the HRA and GAT genes, at 70 gm a.i./ha of thifensulfuron and 2X glyphosate.

EXAMPLE 26: T3 GLYPHOST STUDIES OF RESISTANT PLANTS

MAIZE EXPRESSING GAT TRANSGENES

Maize plants expressing the GAT transgenes 20-H812 (SEQ ID NO:738) and 20-16A3 (SEQ ID NO:638) were produced using the methods described in Example 13. Specifically, the plants were sprayed at the V4 leaf level. Plants are thinned to equal distances and "stand counts"

(determining the number of plants in a row for example) after applying the spray treatment. Commercially available NK603 (Monsanto, St. Louis, MO) was used as a control. Resistance values are shown in Table 18. Plant height measurements were also taken 10 days after treatment and are shown in Table 18.

EXAMPLE 27: T3 YIELD STUDIES OF GLYPHOSATE RESISTANT

MAIZE EXPRESSING THE GAT TRANSGENE

The T3 seed of Example 15 was used to obtain T3 plants to generate field data on hybrid tolerance to glyphosate. The experiment was conducted in Viluco, Chile, with four (4) replications using a "split-plot" design. Specifically, 3 entries are included. Two entries contained maize plants expressing the GAT variant of the 17-15H3 transgene (SEQ ID NO:549). The glyphosate-resistant control NK603, which is commercially available from Monsanto, was the third entry. All entries were treated in the field with four different glyphosate spray treatments (0X, 4X at V4, 8X at V4, and 4X at V4 and 4X at V8) for each event. Plants were scored 10 days after plant treatment to compare plant heights as described in Example 13. Field data, for the T3 spray, correlated well with results previously obtained in the field as reported in Example 15. Specifically, all entries sprayed with IX and 4X glyphosate were similar in height to unsprayed controls. Increasing 4X at V4 and 4X at V8 rates, GAT entries were temporarily set back between 12 and 17% in height and NK603's entry was set back 6%, however later in the season (during reproductive maturation) the height of glyphosate-treated entries was the same as in unsprayed entries. However, yields among glyphosate-treated entries were neither numerically nor statistically reduced relative to unsprayed entries ((LSD005=11.8 bu./acre, mean yield per entry = 243 bu./acre). Similar results obtained in preliminary agronomic trials with T2 plants in the same event were reported in Si Johnston, IA and York, NE (data not shown).

EXAMPLE 28: T2 STUDIES OF GLYPHOST-TOLERANT MAIZE

EXPRESSES GAT TRANSGENE

Experiments were performed on GAT-positive and GAT-negative iso-lines. Maize plants expressing transgenes 18-28D9b (SEQ ID NO:814), 17-15H3 (SEQ ID NO:549), 20-8H12 (SEQ ID NO:738), 20-16A3 (SEQ ID NO:638) were produced using the methods described in Example 17. T2 plants were examined. GAT positive T2 plants were sprayed at V4 with 1X1X (26 oz/A ULTRA MAX™). GAT negative plants were sampled for PCR at V4. GAT positive plants were removed from the row. No glyphosate was applied to the GAT negative plants. Plants were thinned to obtain equal distances between plants within each row. Four (4) replications were performed. Beans from five (5) cobs collected from the center of each row were dried and weighed. As shown in Table 20, no reduction in yield was detected for any construct.

EXAMPLE 29: AMINO ACID SUBSTRATES OF GAT POLYPEPTIDES

The GAT activity of several GAT polypeptides of the present invention was evaluated against a number of amino acid substrates. GAT polypeptides, AcCoA and amino substrate were incubated in 25 mM Hepes, pH 6.8, 10% ethylene glycol in wells of a 96-well polystyrene plate. After 30 min, the reaction was stopped by adding 30 µl of 10 mM 5,5'-dithiobis-2-nitrobenzoate (DTNB) in 500 mM Tris, pH 7.5. After 2 minutes, the absorbance was read at 412 nm in a Spectramax Plus plate reader (Molecular Devices, Sunnvale, CA).

In addition to glyphosate, the native GAT polypeptide 401 (SEQ ID NO: 6) (or B6 (SEQ ID NO: 7), in the case of phosphoserine) showed activity with 12 amino acids. The native GAT polypeptide was as active with L-aspartate, about 4.7 times more active with L-serine and about 2 times more active with phospho L-serine as with, ie. compared to glyphosate. When compared to the native GAT polypeptide, the non-native GAT polypeptides 17-15H3 (SEQ ID NO: 601) and 25-8H7 (SEQ ID NO: 907) showed a 40-fold increase in activity with aspartate, but a loss of activity with respect to serine and phosphoserine.

In addition to aspartate and serine, activity of the native GAT polypeptide at 3% or more relative to that with glyphosate when present at 1 mM was observed with the following amino acids: histidine (10%), tyrosine (18%), threonine (250%), valine (12%), glutamate (51%), asparagine (27%), glutamine (32%), alanine (33%), glycine (21%) and cysteine (50%). Activity with other protein amino acids was either undetectable or less than 3% relative to that with glyphosate as substrate. No activity was noted against the native GAT polypeptide with the N-derivatives of L-aspartate (2 mM), L-alanine (10 mM), and glycine (ie, sarcosine, 10 mM). The percentages refer to the percentage of activity in relation to the activity of the GAT polypeptide towards the substrate, glyphosate. Some data are shown below in Table 21.

EXAMPLE 30: EFFECTS OF H ON GAT ACTIVITY

The optimal pH for kcati Km for wild-type enzyme B6 (SEQ ID NO: 7) and GAT polypeptide 17-15H3 (SEQ ID NO: 601) was determined using the spectrophotometric assay described in Example 7, except that the assay buffer was 50 mM Hepes and 10% ethylene glycol, titrated over the pH range. Protein concentrations were determined using a UV absorbance assay as described in Example 19. The effect of pH on pH on Kmi is shown in Figure 18 for clones B6 (SEQ ID NO: 7) and 17-15H3 (SEQ ID NO: 601).

While the foregoing invention has been described in some detail for clarity and understanding, it will be apparent to those skilled in the art from reading this disclosure that various changes in form and detail may be made without departing from the true scope of the invention. For example, all of the techniques, methods, compositions, apparatus and systems described above may be used in various combinations. The invention is intended to include all methods and reagents described herein as well as all polynucleotides, polypeptides, cells, organisms, plants, crops, etc., which are products of these new methods and reagents.

All publications, patents, patent applications or other documents cited in this application are incorporated by reference for all purposes to the same extent as each individual publication, patent, patent application or other document, individually designated as incorporated by reference for all purposes.

Claims (125)

1. An isolated or recombinant polynucleotide comprising: (a) A nucleotide sequence encoding an amino acid sequence that can be optimally aligned with a sequence selected from the group consisting of SEQ ID NO:300, SEQ ID NO:445 and SEQ ID NO:457 to obtain a similarity score of at least 460 using the BLOSUM62 matrix, a "penalty" of having breaks of 11 and "penalty" span breaks of 1, indicated that the amino acid sequence contains one or more amino acid residues satisfying at least one restriction selected from the group consisting of: (i) at positions 18 and 38, a Z5 amino acid residue; (ii) at position 62, a Z1 amino acid residue; (iii) at position 124, a Z6 amino acid residue; and (vi) at position 144, a Z2 amino acid residue wherein: Z1 is an amino acid residue selected from the group consisting of A, I, L, MiV; Z 2 is an amino acid residue selected from the group consisting of F, W and Y; Z5 is an amino acid residue selected from the group consisting of D and E; Z6 is an amino acid residue selected from the group consisting of C, G and P; or (b) their complementary nucleotide sequence. 2. The isolated or recombinant polynucleotide of claim 1, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions, at least 90% fit the following restrictions: (a) at positions 2, 4, 15, 19, 26, 28, 31, 45, 51, 54, 86, 90, 91, 97, 103, 105, 106, 114, 123, 129, 139, and/or 145 amino acid residues of BI; and (b) at positions 3, 5, 8, 10, 11, 14, 17, 24, 27, 32, 37, 47, 48, 49, 52, 57, 58, 61, 63, 68, 69, 79, 80, 82, 83, 89, 92, 100, 101, 104, 119, 120, 125, 126, 128, 131 and/or 143 are amino acid residues B2; characterized in that: a BI amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S and T. 3. The isolated or recombinant polypeptide of claim 1, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions are at least 80% compatible with the following restrictions: (a) at positions 2, 4, 15, 19, 26, 28, 51, 54, 86, 90, 91, 97, 103, 105, 106, 114, 129, 139, and/or 145 amino acid residues Z1; (b) at positions 31 and/or 45 amino acid residues Z2; (c) at position 8 amino acid residues Z3; (d) at position 89 amino acid residues Z3 or Z6; (e) at positions 82, 92, 101 and/or 120 amino acid residues Z4; (f) at positions 3, 11, 27 and/or 79 amino acid residues Z5; (g) at position 18 amino acid residues Z4 or Z5; (h) at position 123 amino acid residues Z1 or Z2; (i) at positions 12, 33, 35, 39, 53, 59, 112, 132, 135, 140 and/or 146 are amino acid residues Z1 or Z3; (j) at position 30 amino acid residues Zl; (k) at position 6 amino acid residues Z6; (1) at position 81 amino acid residues Z2 or Z4; (m) at position 113 amino acid residues Z3; (n) at position 138 amino acid residues Z4; (o) at position 142 amino acid residues Z2; (p) at positions 57 and/or 126 amino acid residues Z3 or Z4; (q) at positions 5, 17 and/or 61 amino acid residues Z4; (r) at position 24 amino acid residues Z3; (s) at position 104 amino acid residues Z5; (t) at positions 52 and/or 69 amino acid residues Z3; (u) at positions 14 and/or 119 amino acid residues Z5; (v) at positions 10, 32, 63 and/or 83 amino acid residues Z5; (w) at positions 48 and/or 80 amino acid residues Z6; (x) at position 40 amino acid residues Z1 or Z2; (y) at position 96 amino acid residues Z3 or Z5; (z) at position 65 amino acid residues Z3, Z4 or Z6; (aa) at positions 84 and/or 115 amino acid residues Z3; (ab) at position 93 the amino acid residue is Z4; (ac) at position 130 the amino acid residue is Z2; (ad) at position 58 amino acid residues Z3, Z4 or Z6; (ae) at position 47 amino acid residues Z4 or Z6; (af) at positions 49 and/or 100 amino acid residues Z3 or Z4; (ag) at position 68 amino acid residues Z4 or Z5; (ah) at position 143 amino acid residues Z4; (ai) at position 131 amino acid residues Z5; (aj) at positions 125 and/or 128 amino acid residues Z5; (ak) at position 67 amino acid residues Z3 or Z4; (al) at position 60 amino acid residues Z5; and (am) at position 37 amino acid residues Z4 or Z6; characterized in that: Zl amino acid selected from the group consisting of A, I, L, M, and V; Z 2 is an amino acid selected from the group consisting of F, W and Y; Z3 is an amino acid selected from the group consisting of N, Q, S and T; Z4 is an amino acid selected from the group consisting of R, H and K; Z5 is an amino acid selected from the group consisting of D and E; Z6 is an amino acid selected from the group consisting of C, G and P. 4. The isolated or recombinant polynucleotide of patent claim 3, characterized in that the amino acid residues in the amino acid sequence corresponding to the positions specified in (a-an), at least 90% fit into the restrictions of the amino acid residues specified in (a) - (an). 5. An isolated or recombinant polynucleotide from any of claims 1-4, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions fit at least 90% in the following restrictions: (a) at positions 1, 7, 9, 13, 20, 36, 42, 46, 50, 56, 64, 70, 72, 75, 76, 78, 94, 98, 107, 110, 117, 118, 121 and/or 141 amino acid residues BI; and (b) at positions 16, 21, 22, 23, 25, 29, 34, 41, 43, 44, 55, 66, 71, 73, 74, 77, 85, 87, 88, 95, 99, 102, 108, 109, 111, 116, 122, 127, 133, 134, 136 and/or 137 are amino acid residues B2; characterized in that: a BI amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S and T. 6. An isolated or recombinant polynucleotide from any of claims 1-4, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions, at least 90% fit the following restrictions: (a) at positions 1, 7, 9, 13, 20, 42, 46, 50, 56, 64, 70, 72, 75, 76, 78, 94, 98, 107, 110, 117, 118, 121 and/or 141 amino acid residues BI; and (b) at positions 16, 21, 22, 23, 25, 29, 34, 36,41, 43,44, 55, 66, 71, 73, 74, 77, 85, 87, 88, 95, 99, 102, 108, 109, 111, 116, 122, 127, 133, 134, 136 and/or 137 amino acid residues B2; characterized in that: a BI amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S, and T. 7. An isolated or recombinant polynucleotide from any of claims 1-4, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions fit at least 90% in the following restrictions: (a) at positions 1, 7, 9, 20, 42, 50, 72, 75, 76, 78, 94, 98, 110, 121 and/or 141 amino acid residues Z1; (b) at positions 13, 46, 56, 70, 107, 117 and/or 118 amino acid residues Z2; (c) at positions 23, 55, 71, 77, 88 and/or 109 amino acid residues Z3; (d) at positions 16, 21, 41, 73, 85, 99 and/or 111 amino acid residues Z4; (e) at positions 34 and/or 95 amino acid residues Z5; (f) at positions 22, 25, 29, 43, 44, 66, 74, 87, 102, 108, 116, 122, 127, 133, 134, 136 and/or 137 amino acid residues Z6; characterized in that: Zl amino acid selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid selected from the group consisting of F, W and Y; Z3 is an amino acid selected from the group consisting of N, Q, S and T; Z4 is an amino acid selected from the group consisting of R, H and K; Z5 is an amino acid selected from the group consisting of D and E; Z6 is an amino acid selected from the group consisting of C, G and P. 8. The isolated or recombinant polynucleotide of claim 7, characterized in that the amino acid sequence contains at position 36 an amino acid residue selected from the group consisting of Z1 and Z3. 9. Isolated or recombinant polynucleotide from patent claim 7 or patent claim 8, characterized in that the amino acid sequence contains at position 64 an amino acid residue selected from the group consisting of Z1 and Z2. 10. Isolated or recombinant polynucleotide from any of claims 1-9, characterized in that the amino acid residues from the amino acid sequence corresponding to the following positions, at least 80% fit the following restrictions: (a) at position 2 amino acid residues I or L; (b) at position 3 amino acid residues E; (c) at position 4 the amino acid residue is V or I; (d) at position 5 amino acid residues K; (e) at position 6 amino acid residues P; (f) at position 8 amino acid residues N; (g) at position 10 the amino acid residue is E; (h) at position 11 amino acid residues D or E; (i) at position 12 amino acid residues T; (j) at position 14 amino acid residues E or D; (k) at position 15 the amino acid residue is L; (1) at position 17 amino acid residues H; (m) at position 18 amino acid residues R, E or K; (n) at position 19 amino acid residues I or V; (o) at position 24 amino acid residues Q; (p) at position 26 amino acid residues M, L, V, or I; (q) at position 27 amino acid residues E; (r) at position 28 amino acid residues A or V; (s) at position 30 the amino acid residue is M; (t) at position 31 amino acid residues Y or F; (u) at position 32 amino acid residues E or D; (v) at position 33 amino acid residues T or S; (w) at position 35 amino acid residues L; (x) at position 37 amino acid residues R, G, E or Q; (y) at position 39 amino acid residues A or S; (z) at position 40 amino acid residues F or L; (aa) at position 45 amino acid residues Y or F; (ab) at position 47 the amino acid residue is R or G; (ac) at position 48 the amino acid residue is G; (ad) at position 49 the amino acid residue is K, R or Q; (ae) at position 51 amino acid residues I or V; (af) at position 52 amino acid residues S; (ag) at position 53 amino acid residues I or V; (ah) at position 54 amino acid residues A; (ai) at position 57 the amino acid residue is H or N; (aj) at position 58 are amino acid residues Q, K, R or P; (ak) at position 59 amino acid residues A; (al) at position 60 amino acid residues E; (am) at position 61 amino acid residues H or R; (an) at position 63 amino acid residues E or D; (ao) at position 65 amino acid residues E, P or Q; (ap) at position 67 amino acid residues Q or R; (aq) at position 68 amino acid residues K or E; (ar) at position 69 amino acid residues Q; (as) at position 79 amino acid residues E; (at) at position 80 amino acid residues G; (au) at position 81 amino acid residues Y, H or F; (av) at position 82 amino acid residues R; (aw) at position 83 the amino acid residue is E or D; (ax) at position 84 amino acid residues Q; (ay) at position 86 amino acid residues A; (az) at position 89 amino acid residues G, T or S; (ba) at position 90 amino acid residues L; (bb) at position 91 amino acid residues L, I or V; (bc) at position 92 amino acid residues R or K; (bd) at position 93 amino acid residues H; (be) at position 96 amino acid residues E or Q; (bf) at position 97 amino acid residues I; (bg) at position 100 amino acid residues K or N; (bh) at position 101 amino acid residues K or R; (bi) at position 103 amino acid residues A or V; (bj) at position 104 amino acid residues D; (bk) at position 105 amino acid residues M, L or I; (bi) at position 106 amino acid residues L; (bm) at position 112 amino acid residues T or A; (bn) at position 113 amino acid residues S or T; (bo) at position 114 amino acid residues A; (bp) at position 115 amino acid residues S; (bq) at position 119 amino acid residues K or R; (br) at position 120 the amino acid residue is K or R; (bs) at position 123 amino acid residues F or L; (bt) at position 125 amino acid residues E; (bu) at position 126 amino acid residues Q or H; (bv) at position 128 amino acid residues E or D; (bw) at position 129 amino acid residues V or I; (bx) at position 130 amino acid residues F; (by) at position 131 amino acid residues D or E; (bz) at position 132 amino acid residues T; (ca) at position 135 amino acid residues V; (cb) at position 138 amino acid residues H; (cc) at position 139 amino acid residues I; (cd) at position 140 amino acid residues L or M; (ce) at position 142 amino acid residues Y; (cf) at position 143 amino acid residues K or R; (cg) at position 145 amino acid residues L or I; and (ch) at position 146 amino acid residues T. 11. The isolated or recombinant polynucleotide of claim 10, characterized in that the amino acid residues in the amino acid sequence corresponding to the positions specified in (a) - (ch), at least 90% fit within the restrictions of the amino acid residues specified in (a) - (ch). 12. The isolated or recombinant polynucleoid of claim 1, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions, at least 80% fit the following restrictions: (a) at positions 9, 76, 94 and 110 amino acid residues A; (b) at positions 29 and 108 amino acid residues C; (c) at position 34 amino acid residues D; (d) at position 95 amino acid residues E; (e) at position 56 amino acid residues F; (f) at positions 43, 44, 66, 74, 87, 102, 116, 122, 127 and 136 amino acid residues G; (g) at position 41 amino acid residues H; (h) at position 7 amino acid residues I; (i) at position 85 amino acid residues K; (j) at position 20, 42, 50, 78 and 121 amino acid residues L; (k) at position 1 and 141 amino acid residues M; (1) at position 23 and 109 amino acid residues N; (m) at positions 22, 25, 133, 134 and 137 amino acid residues P; (n) at position 71 amino acid residues Q; (0) at positions 16, 21, 73, 99 and 111 amino acid residues R; (p) at position 55 amino acid residues S; (q) at position 77 amino acid residues T; (r) at position 107 amino acid residues W; (s) at positions 13, 46, 70 and 118 amino acid residues Y. 13. The isolated or recombinant polynucleotide of any patent claim 1-12, characterized in that the amino acid sequence contains an amino acid residue from the group consisting of: (a) at position 36 amino acid residues M, L or T; (b) at position 72 amino acid residues L or I; (c) at position 75 amino acid residues M or V; (d) at position 64 amino acid residues L, I or F; (e) at position 88 amino acid residues T or S; (f) at position 117 amino acid residues Y or F. 14. Isolated or recombinant polynucleotide from any patent claim 1-13, characterized in that the amino acid sequence contains one or more amino acid residues from the group consisting of: (a) at position 14 amino acid residues D; (b) at position 18 amino acid residues E; (c) at position 26 amino acid residues M or V; (e) at position 30 amino acid residues I; (f) at position 32 amino acid residues D; (g) at position 36 amino acid residues M or T; (h) at position 37 amino acid residues C; (1) at position 38 amino acid residues D; (j) at position 53 amino acid residues V; (k) at position 58 amino acid residues R; (1) at position 61 amino acid residues R; (m) at position 62 amino acid residues L; (n) at position 64 amino acid residues I or F; (o) at position 65 amino acid residues P; (p) at position 72 amino acid residues I; (q) at position 75 amino acid residues V; (r) at position 88 amino acid residues T; (s) at position 89 amino acid residues G; (t) at position 91 amino acid residues L; (u) at position 98 amino acid residues I; (v) at position 105 amino acid residues I; (w) at position 112 amino acid residues A; (x) at position 124 amino acid residues G or C; (y) at position 128 amino acid residues D; (z) at position 140 amino acid residues M; (aa) at position 143 amino acid residues R; and (ab) at position 144 amino acid residues W. 15. The isolated or recombinant polynucleotide of claim 14, characterized in that the amino acid residues from the amino acid sequence corresponding to the positions specified in (a) - (ab), at least 80% fit into the restrictions of the amino acid residues specified in (a) - (ab). 16. The isolated or recombinant polynucleotide of any patent claim 1-15, characterized in that the amino acid sequence contains one or more amino acid residues from the group consisting of: (a) at position 41 amino acid residues H; (b) at position 138 amino acid residues H; (c) at position 34 amino acid residues N; and (d) at position 55 amino acid residues S. 17. An isolated or recombinant polynucleotide comprising a nucleotide sequence selected from the group consisting of: (a) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:577; (b) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO:578; (c) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO:621; (d) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:579; (e) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:602; (f) a nucleotide sequence encoding an amino acid sequence that is at least 95% identical to SEQ ID NO:697; (g) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO:721; (h) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ IDNO:613; (i) a nucleotide sequence encoding an amino acid sequence that is at least 89% identical to SEQ ID NO:677; (j) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO:584; (k) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:707; (1) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:616; (m) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO:612; (n) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:590; (0) a nucleotide sequence which is complementary to any sequence from (a) to (n). 18. The isolated or recombinant polynucleotide of claim 17, characterized in that the amino acid sequence contains one or more amino acid residues selected from the group consisting of: (1) at positions 18 and 38, a Z5 amino acid residue; (ii) at position 62, a Z1 amino acid residue; (iii) at position 124, a Z6 amino acid residue; and (Iv) at position 144, a Z2 amino acid residue characterized in that: Z1 is an amino acid residue selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid residue selected from the group consisting of F, W and Y; Z5 is an amino acid residue selected from the group consisting of D and E; Z6 is an amino acid residue selected from the group consisting of C, G and P. 19. The isolated or recombinant polynucleotide of claim 17, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions at least 90%> fit the following restrictions: (a) at positions 2, 4, 15, 19, 26, 28, 31, 45, 51, 54, 86, 90, 91, 97, 103, 105, 106, 114, 129, 139, and/or 145 amino acid residues of BI; and (b) at positions 3, 5, 8, 10, 11, 14, 17, 24, 27, 32, 37, 47, 48, 49, 52, 57, 58, 61, 63, 68, 69, 79, 80, 82, 83, 89, 92, 100, 101, 104, 119, 120, 125, 126, 128, 131 and/or 143 amino acid residues B2; characterized in that: a BI amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S and T. 20. The isolated or recombinant polynucleotide of claim 17, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions fit at least 80% in the following restrictions: (a) at positions 2, 4, 15, 19, 26, 28, 51, 54, 86, 90, 91, 97, 103, 105, 106, 114, 129, 139, and/or 145 amino acid residues Z1; (b) at positions 31 and/or 45 amino acid residues Z2; (c) at position 8 amino acid residues Z3; (d) at position 89 amino acid residues Z3 or Z6; (e) at positions 82, 92, 101 and/or 120 amino acid residues Z4; (f) at positions 3, 11, 27 and/or 79 amino acid residues Z5; (g) at position 18 amino acid residues Z4 or Z5; (h) at position 123 amino acid residues Z1 or Z2; (i) at positions 12, 33, 35, 39, 53, 59, 112, 132, 135, 140 and/or 146 are amino acid residues Z1 or Z3; (j) at position 30 amino acid residues Zl; (k) at position 6 amino acid residues Z6; (1) at position 81 amino acid residues Z2 or Z4; (m) at position 113 amino acid residues Z3; (n) at position 138 amino acid residues Z4; (o) at position 142 amino acid residues Z2; (p) at positions 57 and/or 126 amino acid residues Z3 or Z4; (q) at positions 5, 17 and/or 61 amino acid residues Z4; (r) at position 24 amino acid residues Z3; (s) at position 104 amino acid residues Z5; (t) at positions 52 and/or 69 amino acid residues Z3; (u) at positions 14 and/or 119 amino acid residues Z5; (v) at positions 10, 32, 63 and/or 83 amino acid residues Z5; (w) at positions 48 and/or 80 amino acid residues Z6; (x) at position 40 amino acid residues Z1 or Z2; (y) at position 96 amino acid residues Z3 or Z5; (z) at position 65 amino acid residues Z3, Z4 or Z6; (aa) at positions 84 and/or 115 amino acid residues Z3; (ab) at position 93 amino acid residues Z4; (ac) at position 130 amino acid residues Z2; (ad) at position 58 amino acid residues Z3, Z4 or Z6; (ae) at position 47 amino acid residues Z4 or Z6; (af) at positions 49 and/or 100 amino acid residues Z3 or Z4; (ag) at position 68 amino acid residues Z4 or Z5; (ah) at position 143 amino acid residues Z4; (ai) at position 131 amino acid residues Z5; (aj) at positions 125 and/or 128 amino acid residues Z5; (ak) at position 67 amino acid residues Z3 or Z4; (al) at position 60 amino acid residues Z5; and (am) at position 37 amino acid residues Z4 or Z6; characterized in that: Zl amino acid selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid selected from the group consisting of F, W and Y; Z3 is an amino acid selected from the group consisting of N, Q, S and T; Z4 is an amino acid selected from the group consisting of R, H and K; Z5 is an amino acid selected from the group consisting of D and E; Z6 is an amino acid selected from the group consisting of C, G and P. 21. The isolated or recombinant polynucleotide of claim 20, characterized in that the amino acid residues from the amino acid sequence corresponding to the positions specified in (a) - (am), at least 90% fit into the restrictions of the amino acid residues specified in (a) - (am). 22. The isolated or recombinant polynucleotide of any of claims 17-21, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions, at least 90% fit the following restrictions: (a) at positions 1, 7, 9, 13, 20, 36, 42, 46, 50, 56, 64, 70, 72, 75, 76, 78, 94, 98, 107, 110, 117, 118, 121 and/or 141 amino acid residues BI; and (b) at positions 16, 21, 22, 23, 25, 29, 34, 41, 43, 44, 55, 66, 71, 73, 74, 77, 85, 87, 88, 95, 99, 102, 108, 109, 111, 116, 122, 127, 133, 134, 136 and/or 137 are amino acid residues B2; characterized in that: a BI amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S, and T. 23. The isolated or recombinant polynucleotide of any of claims 17-22, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions, at least 90% fit the following restrictions: (a) at positions 1, 7, 9, 13, 20, 42, 46, 50, 56, 64, 70, 72, 75, 76, 78, 94, 98, 107, 110, 117, 118, 121 and/or 141 amino acid residues BI; and (b) at positions 16, 21, 22, 23, 25, 29, 34, 36, 41, 43, 44, 55, 66, 71, 73, 74, 77, 85, 87, 88, 95, 99, 102, 108, 109, 111, 116, 122, 127, 133, 134, 136 and/or 137 amino acid residues B2; wherein: BI is an amino acid selected from the group consisting of A, I, L, M, F, W, Y, and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S, and T. 24. The isolated or recombinant polynucleotide of any of claims 17-22, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions at least 90% fit the following restrictions: (a) at positions 1, 7, 9, 20, 42, 50, 72, 75, 76, 78, 94, 98, 110, 121 and/or 141 amino acid residues are Z1; (b) at positions 13, 46, 56, 70, 107, 117 and/or 118 amino acid residues Z2; (c) at positions 23, 55, 71, 77, 88 and/or 109 amino acid residues Z3; (d) at positions 16, 21, 41, 73, 85, 99 and/or 111 amino acid residues Z4; (e) at positions 34 and/or 95 amino acid residues Z5; (f) at positions 22, 25, 29, 43, 44, 66, 74, 87, 102, 108, 116, 122, 127, 133, 134, 136 and/or 137 amino acid residues Z6; characterized in that: Zl amino acid selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid selected from the group consisting of F, W and Y; Z3 is an amino acid selected from the group consisting of N, Q, S and T; Z4 is an amino acid selected from the group consisting of R, H and K; Z5 is an amino acid selected from the group consisting of D and E; Z6 is an amino acid selected from the group consisting of C, G and P. 25. The isolated or recombinant polynucleotide of claim 24, characterized in that the amino acid sequence contains at position 36 an amino acid residue selected from the group consisting of Z1 and Z3. 26. Isolated or recombinant polynucleotide from patent claim 24 or patent claim 25, characterized in that the amino acid sequence contains at position 64 an amino acid residue selected from the group consisting of Z1 and Z2. 27. An isolated or recombinant polynucleotide from any of claims 17-26, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions fit at least 80% in the following restrictions: (a) at position 2 amino acid residues I or L; (b) at position 3 amino acid residues E; (c) at position 4 amino acid residues V or I; (d) at position 5 amino acid residues K; (e) at position 6 amino acid residues P; (f) at position 8 amino acid residues N; (g) at position 10 amino acid residues E; (h) at position 11 amino acid residues D or E; (i) at position 12 amino acid residues T; (j) at position 14 amino acid residues E or D; (k) at position 15 amino acid residues L; (1) at position 17 amino acid residues H; (m) at position 18 amino acid residues R, E or K; (n) at position 19 amino acid residues I or V; (o) at position 24 amino acid residues Q; (p) at position 26 amino acid residues M, L, V, or I; (q) at position 27 amino acid residues E; (r) at position 28 amino acid residues A or V; (s) at position 30 amino acid residues M; (t) at position 31 amino acid residues Y or F; (u) at position 32 amino acid residues E or D; (v) at position 33 amino acid residues T or S; (w) at position 35 amino acid residues L; (x) at position 37 amino acid residues R, G, E or Q; (y) at position 39 amino acid residues A or S; (z) at position 40 amino acid residues F or L; (aa) at position 45 amino acid residues Y or F; (ab) at position 47 amino acid residues R or G; (ac) at position 48 amino acid residues G; (ad) at position 49 amino acid residues K, R or Q; (ae) at position 51 amino acid residues I or V; (af) at position 52 amino acid residues S; (ag) at position 53 amino acid residues I or V; (ah) at position 54 amino acid residues A; (ai) at position 57 amino acid residues H or N; (aj) at position 58 are amino acid residues Q, K, R or P; (ak) at position 59 amino acid residues A; (al) at position 60 amino acid residues E; (am) at position 61 amino acid residues H or R; (an) at position 63 amino acid residues E or D; (ao) at position 65 amino acid residues E, P or Q; (ap) at position 67 amino acid residues Q or R; (aq) at position 68 amino acid residues K or E; (ar) at position 69 amino acid residues Q; (as) at position 79 amino acid residues E; (at) at position 80 amino acid residues G; (au) at position 81 amino acid residues Y, H or F; (av) at position 82 amino acid residues R; (aw) at position 83 amino acid residues E or D; (ax) at position 84 amino acid residues Q; (ay) at position 86 amino acid residues A; (az) at position 89 amino acid residues G, T or S; (ba) at position 90 amino acid residues L; (bb) at position 91 amino acid residues L, I or V; (bc) at position 92 amino acid residues R or K; (bd) at position 93 amino acid residues H; (be) at position 96 amino acid residues E or Q; (bf) at position 97 amino acid residues I; (bg) at position 100 amino acid residues K or N; (bh) at position 101 amino acid residues K or R; (bi) at position 103 amino acid residues A or V; (bj) at position 104 amino acid residues D; (bk) at position 105 amino acid residues M, L or I; (bi) at position 106 amino acid residues L; (bm) at position 112 amino acid residues T or A; (bn) at position 113 amino acid residues S or T; (bo) at position 114 amino acid residues A; (bp) at position 115 amino acid residues S; (bq) at position 119 amino acid residues K or R; (br) at position 120 amino acid residues K or R; (bs) at position 123 amino acid residues F or L; (bt) at position 125 amino acid residues E; (bu) at position 126 amino acid residues Q or H; (bv) at position 128 amino acid residues E or D; (bw) at position 129 amino acid residues V or I; (bx) at position 130 amino acid residues F; (by) at position 131 amino acid residues D or E; (bz) at position 132 amino acid residues T; (ca) at position 135 amino acid residues V; (cb) at position 138 amino acid residues H; (cc) at position 139 amino acid residues I; (cd) at position 140 amino acid residues L or M; (ce) at position 142 amino acid residues Y; (cfj at position 143 amino acid residues K or R; (cg) at position 145 amino acid residues L or I; and (ch) at position 146 amino acid residues T. 28. The isolated or recombinant polynucleotide of claim 27, characterized in that the amino acid residues from the amino acid sequence corresponding to the positions specified in (a) - (ch), at least 90% fit within the restrictions of the amino acid residues specified in (a) - (ch). 29. The isolated or recombinant polynucleotide of claim 17, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions at least 80% fit the following restrictions: (a) at positions 9, 76, 94 and 110 amino acid residues A; (b) at positions 29 and 108 amino acid residues C; (c) at position 34 amino acid residues D; (d) at position 95 amino acid residues E; (e) at position 56 amino acid residues F; (f) at positions 43, 44, 66, 74, 87, 102, 116, 122, 127 and 136 amino acid residues G; (g) at position 41 amino acid residues H; (h) at position 7 amino acid residues I; (i) at position 85 amino acid residues K; (j) at position 20, 42, 50, 78 and 121 amino acid residues L; (k) at position 1 and 141 amino acid residues M; (1) at position 23 and 109 amino acid residues N; (m) at positions 22, 25, 133, 134 and 137 amino acid residues P; (n) at position 71 amino acid residues Q; (0) at positions 16, 21, 73, 99 and 111 amino acid residues R; (p) at position 55 amino acid residues S; (q) at position 77 amino acid residues T; (r) at position 107 amino acid residues W; (s) at positions 13, 46, 70 and 118 amino acid residues Y; 30. The isolated or recombinant polypeptide of any patent claim 1-29, characterized in that the amino acid sequence contains one or more amino acid residues from the group consisting of: (a) at position 14 amino acid residues D; (b) at position 18 amino acid residues E; (c) at position 26 amino acid residues M or V; (e) at position 30 amino acid residues I; (f) at position 32 amino acid residues D; (g) at position 36 amino acid residues M or T; (h) at position 37 amino acid residues C; (1) at position 38 amino acid residues D; (j) at position 53 amino acid residues V; (k) at position 58 amino acid residues R; (1) at position 61 amino acid residues R; (m) at position 62 amino acid residues L; (n) at position 64 amino acid residues I or F; (o) at position 65 amino acid residues P; (p) at position 72 amino acid residues I; (q) at position 75 amino acid residues V; (r) at position 88 amino acid residues T; (s) at position 89 amino acid residues G; (t) at position 91 amino acid residues L; (u) at position 98 amino acid residues I; (v) at position 105 amino acid residues I; (w) at position 112 amino acid residues A; (x) at position 124 amino acid residues G or C; (y) at position 128 amino acid residues D; (z) at position 140 amino acid residues M; (aa) at position 143 amino acid residues R; (ab) at position 144 amino acid residues W; 31. The isolated or recombinant polynucleotide of claim 30, characterized in that the amino acid residues from the amino acid sequence corresponding to the positions specified in (a) - (ab), at least 80% fit into the restrictions of the amino acid residues specified in (a) - (ab). 32. An isolated or recombinant polynucleotide from any of claims 17-31, characterized in that the amino acid sequence comprises amino acid residues selected from the group consisting of: (a) at position 41 amino acid residues H; (b) at position 138 amino acid residues H; (c) at position 34 the amino acid residue is N; and (f) at position 55 amino acid residues S. 33. An isolated or recombinant polynucleotide encoding a protein having glyphosate-N-transferase activity, said polynucleotide is selected from the group consisting of SEQ ID NO: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 534, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 620, 622, 624, 626, 628, 630, 632, 634, 636, 638, 640, 642, 644, 646, 648, 650, 652,654, 656, 658, 660, 662, 664, 666, 668, 670, 672, 674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726, 728, 730, 732, 734,736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766,768, 770, 772, 774, 776, 778, 780,782, 784, 786, 788, 790,792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814, 816, 818, 820, 822, 824, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916, 918, 920, 922, 924, 926, 928, 930, 932, 933, 934, 935, 936, 937, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952. 34. The isolated or recombinant polynucleotide of claim 1, characterized in that the polypeptide encoded by said polynucleotide possesses glyphosate-N-transferase activity. 35. The isolated or recombinant polynucleotide of claim 1, characterized in that the polypeptide encoded by said polynucleotide possesses glyphosate-N-transferase activity. 36. The isolated or recombinant polynucleotide of claim 34, characterized in that the polypeptide catalyzes the acetylation of glyphosate with an Ic^/Km of at least lOmM"<1>min-1 for glyphosate. 37. The isolated or recombinant polynucleotide of claim 34, characterized in that the polypeptide catalyzes the acetylation of aminomethylphosphonic acid. 38. Nucleic acid construct containing the isolated or recombinant polynucleotide of claim 1. 39. The nucleic acid construct of claim 38 operably linked to the isolated or recombinant polynucleotide of claim 1, wherein the promoter is heterologous to said polynucleotide and effective to cause sufficient expression of the encoded polypeptides to increase tolerance to glyphosate of a plant cell transformed with said nucleic acid construct. 40. Nucleic acid construct from claim 38, characterized in that the isolated or recombinant polynucleotide sequence from claim 1 functions as a selective marker. 41. The nucleic acid construct of claim 38, characterized in that the construct is a vector. 42. The vector of claim 41 further comprises a second polynucleotide sequence encoding a second polypeptide that causes a defective phenotypic trait when the cell or organism expresses the second polypeptide at an effective level. 43. The vector of claim 42, characterized in that the detectable phenotypic trait functions as a selectable marker. 44. The vector of claim 42, wherein the detectable phenotypic trait is selected from the group consisting of herbicide resistance and a visible marker. 45. The vector of claim 41, characterized in that the vector further comprises a T-DNA sequence. 46. The vector of claim 41, characterized in that the isolated or recombinant polynucleotide is operably linked to a regulatory sequence. 47. The vector of claim 41, characterized in that the vector is a plant transformation vector. 48. A cell comprising at least one isolated or recombinant polynucleotide from claim 1, characterized in that the polynucleotide is heterologous to the cell. 49. The cell of claim 48, characterized in that the isolated recombinant polynucleotide is operably linked to a regulatory sequence. 50. A cell transduced with the vector of claim 41. 51. The cell of claim 49 or 50, characterized in that the cell is a transgenic plant cell. 52. The transgenic plant cell of claim 51, characterized in that the transgenic plant cell expresses an exogenous polypeptide with glyphosate-N-acetyltransferase activity. 53. The transgenic plant cell of claim 51, characterized in that the transgenic plant cell expresses an exogenous polypeptide with glyphosate-N-acetyltransferase activity. 54. A transgenic plant or an explant of a transgenic plant comprising a cell from claim 52. 55. A transgenic plant or explant of a transgenic plant comprising a cell from claim 53. 56. Transgenic plant or transgenic plant explant from patent claim 54, characterized in that said transgenic plant or transgenic plant explant expresses a polypeptide with glyphosate-N-acetyltransferase activity. 57. Transgenic plant or transgenic plant explant from patent claim 55, characterized in that said transgenic plant or transgenic plant explant expresses a polypeptide with glyphosate-N-acetyltransferase activity. 58. Transgenic plant or transgenic plant explant from patent claim 56, indicated that said transgenic plant or transgenic plant explant is a crop plant selected from a group of species (genera) consisting of: Eleusine, Lollium, Bambusa, Brassica, Dactvlis, Sorghum, Pennisetum, Zea, Oryza, Triticum, Secale, Avena, Hordeum, Saccharum, Coix, Glvcine and Gossipum. 59. Transgenic plant or transgenic plant explant from patent claim 57, indicated that said transgenic plant or transgenic plant explant is a crop plant selected from a group of species (genera) consisting of: Eleusine, Lollium, Bambusa, Brassica, Dactvlis, Sorghum, Pennisetum, Zea, Oryza, Triticum, Secale, Avena, Hordeum, Saccharum, Coix, Glvcine and Gossvpium. 60. Transgenic plant or transgenic plant explant from patent claim 56, characterized in that said transgenic plant or transgenic plant explant is Arabidopsis. 61. Transgenic plant or transgenic plant explant from patent claim 57, characterized in that said transgenic plant or transgenic plant explant is Arabidopsis. 62. Transgenic plant or transgenic plant explant from patent claim 56, characterized in that said transgenic plant or transgenic plant explant is Gossvpium. 63. Transgenic plant or transgenic plant explant from patent claim 57, characterized in that said transgenic plant or transgenic plant explant is Gossvpium. 64. The transgenic plant or transgenic plant explant of claim 56, characterized in that said transgenic plant or explant exhibits increased resistance to glyphosate when compared to a wild plant variant of the same species, strain or cultivar. 65. The transgenic plant or transgenic plant explant of claim 57, characterized in that said transgenic plant or explant exhibits increased resistance to glyphosate when compared to a wild plant variant of the same species, strain or cultivar. 66. Seed produced in the plant from patent claim 56. 67. Seed produced in the plant from patent claim 57. 68. A transgenic plant comprising a heterologous gene, said gene being selected from the group consisting of SEQ ID NO: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 534, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 620,622, 624, 626, 628,630, 632, 634, 636, 638, 640, 642,644, 646, 648, 650, 652, 654, 656, 658, 660, 662, 664, 666, 668, 670, 672, 674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726, 728, 730, 732, 734, 736, 738, 740, 742,744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788, 790, 792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814, 816, 818, 820, 822, 824, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900,902, 904, 906, 908,910, 912, 914, 916, 918, 920, 922, 924, 926, 928, 930, 932, 933, 934, 935, 936, 937, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952 encoding a glyphosate-N-acetyltransferase having a kcat/Km of at least 10 mM-lmin-1 for glyphosate, indicated by the plant showing tolerance to glyphosate applied at a level effective to inhibit growth of the same plant lacking the heterologous gene, without a significant reduction in yield due to the use of herbicides. 69. The transgenic plant of claim 68, characterized in that glyphosate-N-acetyltransferase catalyzes the acetylation of aminomethylphosphonic acid. 70. An isolated or recombinant polypeptide comprising: (a) an amino acid sequence that can be optimally aligned with a sequence selected from the group consisting of SEQ ID NO:300, SEQ ID NO:445 and SEQ ID NO.457 to obtain a similarity score of at least 460 using the BLOSUM62 matrix, a break existence "penalty" of 11 and a break spread "penalty" of 1, characterized in that the amino acid sequence contains one or more amino acid residues selected from the group consisting of: (i) at positions 18 and 38, a Z5 amino acid residue; (ii) at position 62, a Z1 amino acid residue; (iii) at position 124, a Z6 amino acid residue; and (iv) at position 144, a Z2 amino acid residue characterized in that: Zl is an amino acid residue selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid residue selected from the group consisting of F, W and Y; Z5 is an amino acid residue selected from the group consisting of D and E; Z6 is an amino acid residue selected from the group consisting of C, G and P; or (b) their complementary nucleotide sequence. 71. The isolated or recombinant polypeptide of claim 70, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions are at least 90% compatible with the following restrictions: (a) at positions 2, 4, 15, 19, 26, 28, 31, 45, 51, 54, 86, 90, 91, 97, 103, 105, 106, 114, 123, 129, 139, and/or 145 amino acid residues of BI; and (b) at positions 3, 5, 8, 10, 11, 14, 17, 24, 27, 32, 37, 47, 48, 49, 52, 57, 58, 61, 63, 68, 69, 79, 80, 82, 83, 89, 92, 100, 101, 104, 119, 120, 125, 126, 128, 131 and/or 143 amino acid residues B2; characterized in that: a BI amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S and T. 72. The isolated or recombinant polypeptide of claim 70, characterized in that the amino acid residues from the amino acid sequence corresponding to the following positions, at least 80% fit the following restrictions: (a) at positions 2, 4, 15, 19, 26, 28, 51, 54, 86, 90, 91, 97, 103, 105, 106, 114, 129, 139, and/or 145 amino acid residues Z1; (b) at positions 31 and/or 45 amino acid residues Z2; (c) at position 8 amino acid residues Z3; (d) at position 89 amino acid residues Z3 or Z6; (e) at positions 82, 92, 101 and/or 120 amino acid residues Z4; (f) at positions 3, 11, 27 and/or 79 amino acid residues Z5; (g) at position 18 amino acid residues Z4 or Z5; (h) at position 123 amino acid residues Z1 or Z2; (i) at positions 12, 33, 35, 39, 53, 59, 112, 132, 135, 140 and/or 146 are amino acid residues Z1 or Z3; (j) at position 30 the amino acid residue is Z1; (k) at position 6 amino acid residues Z6; (1) at position 81 amino acid residues Z2 or Z4; (m) at position 113 amino acid residues Z3; (n) at position 138 amino acid residues Z4; (o) at position 142 amino acid residues Z2; (p) at positions 57 and/or 126 amino acid residues Z3 or Z4; (q) at positions 5, 17 and/or 61 amino acid residues Z4; (r) at position 24 amino acid residues Z3; (s) at position 104 amino acid residues Z5; (t) at positions 52 and/or 69 amino acid residues Z3; (u) at positions 14 and/or 119 amino acid residues Z5; (v) at positions 10, 32, 63 and/or 83 amino acid residues Z5; (w) at positions 48 and/or 80 amino acid residues Z6; (x) at position 40 amino acid residues Z1 or Z2; (y) at position 96 amino acid residues Z3 or Z5; (z) at position 65 amino acid residues Z3, Z4 or Z6; (aa) at positions 84 and/or 115 amino acid residues Z3; (ab) at position 93 amino acid residues Z4; (ac) at position 130 amino acid residues Z2; (ad) at position 58 amino acid residues Z3, Z4 or Z6; (ae) at position 47 amino acid residues Z4 or Z6; (af) at positions 49 and/or 100 amino acid residues Z3 or Z4; (ag) at position 68 amino acid residues Z4 or Z5; (ah) at position 143 amino acid residues Z4; (ai) at position 131 amino acid residues Z5; (aj) at positions 125 and/or 128 amino acid residues Z5; (ak) at position 67 amino acid residues Z3 or Z4; (al) at position 60 amino acid residues Z5; (am) at position 37 amino acid residues Z4 or Z6; characterized in that: Zl amino acid selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid selected from the group consisting of F, W and Y; Z3 is an amino acid selected from the group consisting of N, Q, S and T; Z4 is an amino acid selected from the group consisting of R, H and K; Z5 is an amino acid selected from the group consisting of D and E; Z6 is an amino acid selected from the group consisting of C, G and P. 73. The isolated or recombinant polypeptide of claim 72, characterized in that the amino acid residues in the amino acid sequence corresponding to the positions specified in (a) - (am), at least 90% fit within the restrictions of the amino acid residues specified in (a) - (am). 74. The isolated or recombinant polypeptide of any one of claims 70-73, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions, at least 90% fit the following restrictions: (a) at positions 1, 7, 9, 13, 20, 36, 42, 46, 50, 56, 64, 70, 72, 75, 76, 78, 94, 98, 107, 110, 117, 118, 121 and/or 141 amino acid residues BI; and (b) at positions 16, 21, 22, 23, 25, 29, 34, 41, 43, 44, 55, 66, 71, 73, 74, 77, 85, 87, 88, 95, 99, 102, 108, 109, 111, 116, 122, 127, 133, 134, 136 and/or 137 are amino acid residues B2; characterized in that: a BI amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S, and T. 75. The isolated or recombinant polypeptide of any of claims 70-73, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions, at least 90% fit the following restrictions: (a) at positions 1, 7, 9, 13, 20, 42, 46, 50, 56, 64, 70, 72, 75, 76, 78, 94, 98, 107, 110, 117, 118, 121 and/or 141 amino acid residues BI; and (b) at positions 16, 21, 22, 23, 25, 29, 34, 36, 41, 43, 44, 55, 66, 71, 73, 74, 77, 85, 87, 88, 95, 99, 102, 108, 109, 111, 116, 122, 127, 133, 134, 136 and/or 137 amino acid residues B2; indicated that BI is an amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S, and T. 76. The isolated or recombinant polypeptide of any of claims 70-73, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions at least 90%> fit the following restrictions: (a) at positions 1, 7, 9, 20, 42, 50, 72, 75, 76, 78, 94, 98, 110, 121 and/or 141 amino acid residues Z1; (b) at positions 13, 46, 56, 70, 107, 117 and/or 118 amino acid residues Z2; (c) at positions 23, 55, 71, 77, 88 and/or 109 amino acid residues Z3; (d) at positions 16, 21, 41, 73, 85, 99 and/or 111 amino acid residues Z4; (e) at positions 34 and/or 95 the amino acid residue is Z5; (f) at positions 22, 25, 29, 43, 44, 66, 74, 87, 102, 108, 116, 122, 127, 133, 134, 136 and/or 137 amino acid residues Z6; characterized in that: Z1 is an amino acid selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid selected from the group consisting of F, W and Y; Z3 is an amino acid selected from the group consisting of N, Q, S and T; Z4 is an amino acid selected from the group consisting of R, H and K; Z5 is an amino acid selected from the group consisting of D and E; Z6 is an amino acid selected from the group consisting of C, G and P. 77. The isolated or recombinant polypeptide of claim 76, characterized in that the amino acid sequence contains, at position 36, an amino acid residue selected from the group consisting of Z1 and Z3. 78. The isolated or recombinant polypeptide of claim 76, or claim 77, characterized in that the amino acid sequence contains, at position 64, an amino acid residue selected from the group consisting of Z1 and Z2. 79. The isolated or recombinant polypeptide of any patent claim 70-78, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions at least 80% fit the following restrictions: (a) at position 2 amino acid residues I or L; (b) at position 3 amino acid residues E; (c) at position 4 the amino acid residue is V or I; (d) at position 5 amino acid residues K; (e) at position 6 amino acid residues P; (f) at position 8 amino acid residues N; (g) at position 10 amino acid residues E; (h) at position 11 amino acid residues D or E; (i) at position 12 amino acid residues T; (j) at position 14 amino acid residues E or D; (k) at position 15 amino acid residues L; (1) at position 17 amino acid residues H; (m) at position 18 amino acid residues R, E or K; (n) at position 19 amino acid residues I or V; (o) at position 24 amino acid residues Q; (p) at position 26 amino acid residues M, L, V, or I; (q) at position 27 amino acid residues E; (r) at position 28 amino acid residues A or V; (s) at position 30 amino acid residues M; (t) at position 31 amino acid residues Y or F; (u) at position 32 amino acid residues E or D; (v) at position 33 amino acid residues T or S; (w) at position 35 amino acid residues L; (x) at position 37 amino acid residues R, G, E or Q; (y) at position 39 amino acid residues A or S; (z) at position 40 amino acid residues F or L; (aa) at position 45 amino acid residues Y or F; (ab) at position 47 amino acid residues R or G; (ac) at position 48 amino acid residues G; (ad) at position 49 amino acid residues K, R or Q; (ae) at position 51 amino acid residues I or V; (af) at position 52 amino acid residues S; (ag) at position 53 amino acid residues I or V; (ah) at position 54 amino acid residues A; (ai) at position 57 amino acid residues H or N; (aj) at position 58 are amino acid residues Q, K, R or P; (ak) at position 59 amino acid residues A; (al) at position 60 amino acid residues E; (am) at position 61 amino acid residues H or R; (an) at position 63 amino acid residues E or D; (ao) at position 65 amino acid residues E, P or Q; (ap) at position 67 amino acid residues Q or R; (aq) at position 68 amino acid residues K or E; (ar) at position 69 amino acid residues Q; (as) at position 79 amino acid residues E; (at) at position 80 amino acid residues G; (au) at position 81 the amino acid residue is Y, H or F; (av) at position 82 amino acid residues R; (aw) at position 83 amino acid residues E or D; (ax) at position 84 amino acid residues Q; (ay) at position 86 amino acid residues A; (az) at position 89 amino acid residues G, T or S; (ba) at position 90 amino acid residues L; (bb) at position 91 amino acid residues L, I or V; (bc) at position 92 amino acid residues R or K; (bd) at position 93 amino acid residues H; (be) at position 96 amino acid residues E or Q; (bf) at position 97 amino acid residues I; (bg) at position 100 amino acid residues K or N; (bh) at position 101 amino acid residues K or R; (bi) at position 103 amino acid residues A or V; (bj) at position 104 amino acid residues D; (bk) at position 105 amino acid residues M, L or I; (bi) at position 106 amino acid residues L; (bm) at position 112 amino acid residues T or A; (bn) at position 113 amino acid residues S or T; (bo) at position 114 amino acid residues A; (bp) at position 115 amino acid residues S; (bq) at position 119 amino acid residues K or R; (br) at position 120 amino acid residues K or R; (bs) at position 123 amino acid residues F or L; (bt) at position 125 amino acid residues E; (bu) at position 126 amino acid residues Q or H; (bv) at position 128 amino acid residues E or D; (bw) at position 129 amino acid residues V or I; (bx) at position 130 amino acid residues F; (by) at position 131 amino acid residues D or E; (bz) at position 132 amino acid residues T; (ca) at position 135 amino acid residues V; (cb) at position 138 amino acid residues H; (cc) at position 139 amino acid residues I; (cd) at position 140 amino acid residues L or M; (ce) at position 142 amino acid residues Y; (cf) at position 143 amino acid residues K or R; (cg) at position 145 amino acid residues L or I, and; (ch) at position 146 amino acid residues T; 80. The isolated or recombinant polypeptide of claim 79, characterized in that the amino acid residues in the amino acid sequence corresponding to the positions specified in (a) - (ch), at least 90% fit within the restrictions of the amino acid residues specified in (a) - (ch). 81. The isolated or recombinant polypeptide of claim 70, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions at least 80% fit the following restrictions: (a) at positions 9, 76, 94 and 110 the amino acid residue is A; (b) at positions 29 and 108 amino acid residues C; (c) at position 34 the amino acid residue is D; (d) at position 95 the amino acid residue is E; (e) at position 56 amino acid residues F; (f) at positions 43, 44, 66, 74, 87, 102, 116, 122, 127 and 136 amino acid residues G; (g) at position 41 amino acid residues H; (h) at position 7 amino acid residues I; (i) at position 85 the amino acid residue is K; (j) at position 20, 42, 50, 78 and 121 amino acid residues L; (k) at position 1 and 141 amino acid residues M; (1) at position 23 and 109 amino acid residues N; (m) at positions 22, 25, 133, 134 and 137 amino acid residues P; (n) at position 71 amino acid residues Q; (o) at positions 16, 21, 73, 99 and 111 amino acid residues R; (p) at position 55 amino acid residues S; (q) at position 77 the amino acid residue is T; (r) at position 107 amino acid residues W; (s) at positions 13, 46, 70 and 118 amino acid residues Y; 82. The isolated or recombinant polypeptide of any one of claims 70-78, characterized in that the amino acid sequence contains an amino acid residue from the group consisting of: (a) at position 36 amino acid residues M, L or T; (b) at position 72 amino acid residues L or I; (c) at position 75 amino acid residues M or V; (d) at position 64 amino acid residues L, I or F; (e) at position 88 amino acid residues T or S; (f) at position 117 amino acid residues Y or F; 83. The isolated or recombinant polypeptide of any of claims 70-78, characterized in that the amino acid sequence contains one or more amino acid residues from the group consisting of: (a) at position 14 amino acid residues D; (b) at position 18 amino acid residues E; (c) at position 26 amino acid residues M or V; (e) at position 30 amino acid residues I; (f) at position 32 amino acid residues D; (g) at position 36 amino acid residues M or T; (h) at position 37 amino acid residues C; (i) at position 38 amino acid residues D; (j) at position 53 amino acid residues V; (k) at position 58 amino acid residues R; (1) at position 61 amino acid residues R; (m) at position 62 amino acid residues L; (n) at position 64 amino acid residues I or F; (o) at position 65 amino acid residues P; (p) at position 72 amino acid residues I; (q) at position 75 amino acid residues V; (r) at position 88 amino acid residues T; (s) at position 89 amino acid residues G; (t) at position 91 amino acid residues L; (u) at position 98 amino acid residues I; (v) at position 105 amino acid residues I; (w) at position 112 amino acid residues A; (x) at position 124 amino acid residues G or C; (y) at position 128 amino acid residues D; (z) at position 140 the amino acid residue is M; (aa) at position 143 amino acid residues R; and (ab) at position 144 amino acid residues W; 84. The isolated or recombinant polypeptide of claim 84, characterized in that the amino acid residues in the amino acid sequence corresponding to the positions specified in (a) - (ab), at least 80% fit within the restrictions of the amino acid residues specified in (a) - (ab). 85. The isolated or recombinant polypeptide of any one of claims 70-84, characterized in that the amino acid sequence contains one or more amino acid residues from the group consisting of: (a) at position 41 amino acid residues H; (b) at position 138 amino acid residues H; (c) at position 34 amino acid residues N; and (f) at position 55 amino acid residues S; 86. An isolated or recombinant polypeptide comprising a nucleotide sequence selected from the group consisting of: (a) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:577; (b) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO:578; (c) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO:621; (d) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:579; (e) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:602; (f) a nucleotide sequence encoding an amino acid sequence that is at least 95% identical to SEQ ID NO:697; (g) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO:721; (h) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO:613; (i) a nucleotide sequence encoding an amino acid sequence that is at least 89% identical to SEQ ID NO:677; (j) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO:584; (k) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:707; (1) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO.616; (m) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO:612; (n) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:590; (o) a nucleotide sequence which is complementary to any of the sequences from (a) to (n). 87. The isolated or recombinant polypeptide of claim 86, characterized in that the amino acid sequence contains one or more amino acid residues selected from the group consisting of: (i) at positions 18 and 38, a Z5 amino acid residue; (ii) at position 62, a Z1 amino acid residue; (iii) at position 124, a Z6 amino acid residue; and (iv) at position 144, a Z2 amino acid residue characterized in that: Z1 is an amino acid residue selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid residue selected from the group consisting of F, W and Y; Z5 is an amino acid residue selected from the group consisting of D and E; Z6 is an amino acid residue selected from the group consisting of C, G and P. 88. The isolated or recombinant polypeptide of claim 86, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions at least 90% fit the following restrictions: (a) at positions 2, 4, 15, 19, 26, 28, 31, 45, 51, 54, 86, 90, 91, 97, 103, 105, 106, 114, 129, 139, and/or 145 amino acid residues of BI; and (b) at positions 3, 5, 8, 10, 11, 14, 17, 24, 27, 32, 37, 47, 48, 49, 52, 57, 58, 61, 63, 68, 69, 79, 80, 82, 83, 89, 92, 100, 101, 104, 119, 120, 125, 126, 128, 131 and/or 143 amino acid residues B2; wherein: BI is an amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S and T. 89. The isolated or recombinant polypeptide of claim 86, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions fit at least 80% of the following restrictions: (a) at positions 2, 4, 15, 19, 26, 28, 51, 54, 86, 90, 91, 97, 103, 105, 106, 114, 129, 139, and/or 145 amino acid residues Z1; (b) at positions 31 and/or 45 amino acid residues Z2; (c) at position 8 amino acid residues Z3; (d) at position 89 amino acid residues Z3 or Z6; (e) at positions 82, 92, 101 and/or 120 amino acid residues Z4; (f) at positions 3, 11, 27 and/or 79 amino acid residues Z5; (g) at position 18 amino acid residues Z4 or Z5; (h) at position 123 amino acid residues Z1 or Z2; (i) at positions 12, 33, 35, 39, 53, 59, 112, 132, 135, 140 and/or 146 are amino acid residues Z1 or Z3; (j) at position 30 amino acid residues Zl; (k) at position 6 amino acid residues Z6; (1) at position 81 amino acid residues Z2 or Z4; (m) at position 113 amino acid residues Z3; (n) at position 138 amino acid residues Z4; (o) at position 142 amino acid residues Z2; (p) at positions 57 and/or 126 amino acid residues Z3 or Z4; (q) at positions 5, 17 and/or 61 amino acid residues Z4; (r) at position 24 amino acid residues Z3; (s) at position 104 amino acid residues Z5; (t) at positions 52 and/or 69 amino acid residues Z3; (u) at positions 14 and/or 119 amino acid residues Z5; (v) at positions 10, 32, 63 and/or 83 amino acid residues Z5; (w) at positions 48 and/or 80 amino acid residues Z6; (x) at position 40 amino acid residues Z1 or Z2; (y) at position 96 amino acid residues Z3 or Z5; (z) at position 65 amino acid residues Z3, Z4 or Z6; (aa) at positions 84 and/or 115 amino acid residues Z3; (ab) at position 93 amino acid residues Z4; (ac) at position 130 amino acid residues Z2; (ad) at position 58 amino acid residues Z3, Z4 or Z6; (ae) at position 47 amino acid residues Z4 or Z6; (af) at positions 49 and/or 100 amino acid residues Z3 or Z4; (ag) at position 68 amino acid residues Z4 or Z5; (ah) at position 143 amino acid residues Z4; (ai) at position 131 amino acid residues Z5; (aj) at positions 125 and/or 128 amino acid residues Z5; (ak) at position 67 amino acid residues Z3 or Z4; (al) at position 60 amino acid residues Z5; and (am) at position 37 amino acid residues Z4 or Z6; characterized in that: Zl amino acid selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid selected from the group consisting of F, W and Y; Z3 is an amino acid selected from the group consisting of N, Q, S and T; Z4 is an amino acid selected from the group consisting of R, H and K; Z5 is an amino acid selected from the group consisting of D and E; Z6 is an amino acid selected from the group consisting of C, G and P. 90. The isolated or recombinant polypeptide of claim 89, characterized in that the amino acid residues in the amino acid sequence corresponding to the positions specified in (a) - (am), at least 90% fit within the restrictions of the amino acid residues specified in (a) - (am). 91. The isolated or recombinant polypeptide of claim 89, characterized in that the amino acid residues in the amino acid sequence corresponding to the positions specified in (a) - (am), at least 90% fit the following restrictions: (a) at positions 1, 7, 9, 13, 20, 36, 42, 46, 50, 56, 64, 70, 72, 75, 76, 78, 94, 98, 107, 110, 117, 118, 121 and/or 141 amino acid residues BI; and (b) at positions 16, 21, 22, 23, 25, 29, 34, 41, 43, 44, 55, 66, 71, 73, 74, 77, 85, 87, 88, 95, 99, 102, 108, 109, 111, 116, 122, 127, 133, 134, 136 and/or 137 are amino acid residues B2; indicated that BI is an amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S, and T. 92. The isolated or recombinant polypeptide of any of claims 86-91, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions at least 90% fit the following restrictions: (a) at positions 1, 7, 9, 13, 20, 42, 46, 50, 56, 64, 70, 72, 75, 76, 78, 94, 98, 107, 110, 117, 118, 121 and/or 141 amino acid residues BI; and (b) at positions 16, 21, 22, 23, 25, 29, 34, 36, 41, 43, 44, 55, 66, 71, 73, 74, 77, 85, 87, 88, 95, 99, 102, 108, 109, 111, 116, 122, 127, 133, 134, 136 and/or 137 amino acid residues B2; wherein: BI is an amino acid selected from the group consisting of A, I, L, M, F, W, Y and V; and B2 is an amino acid selected from the group consisting of R, N, D, C, Q, E, G, H, K, P, S, and T. 93. The isolated or recombinant polypeptide of any one of claims 86-91, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions at least 90% fit the following restrictions: (a) at positions 1, 7, 9, 20, 42, 50, 72, 75, 76, 78, 94, 98, 110, 121 and/or 141 amino acid residues Z1; (b) at positions 13, 46, 56, 70, 107, 117 and/or 118 amino acid residues Z2; (c) at positions 23, 55, 71, 77, 88 and/or 109 amino acid residues Z3; (d) at positions 16, 21, 41, 73, 85, 99 and/or 111 amino acid residues Z4; (e) at positions 34 and/or 95 amino acid residues Z5; (f) at positions 22, 25, 29, 43, 44, 66, 74, 87, 102, 108, 116, 122, 127, 133, 134, 136 and/or 137 amino acid residues Z6; characterized in that: Zl amino acid selected from the group consisting of A, I, L, M and V; Z 2 is an amino acid selected from the group consisting of F, W and Y; Z3 is an amino acid selected from the group consisting of N, Q, S and T; Z4 is an amino acid selected from the group consisting of R, H and K; Z5 is an amino acid selected from the group consisting of D and E; Z6 is an amino acid selected from the group consisting of C, G and P. 94. The isolated or recombinant polypeptide of claim 93, characterized in that the amino acid sequence contains at position 36 an amino acid residue selected from the group consisting of Z1 and Z3. 95. Isolated or recombinant polypeptide from claim 93 or claim 94, characterized in that the amino acid sequence contains at position 64 an amino acid residue selected from the group consisting of Z1 and Z2. 96. The isolated or recombinant polypeptide of any of claims 86-95, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions at least 80% fit the following restrictions: (a) at position 2 the amino acid residues are I or L; (b) at position 3 amino acid residues E; (c) at position 4 amino acid residues V or I; (d) at position 5 amino acid residues K; (e) at position 6 amino acid residues P; (f) at position 8 amino acid residues N; (g) at position 10 amino acid residues E; (h) at position 11 amino acid residues D or E; (i) at position 12 the amino acid residue is T; (j) at position 14 amino acid residues E or D; (k) at position 15 the amino acid residue is L; (1) at position 17 the amino acid residue is H; (m) at position 18 amino acid residues R, E or K; (n) at position 19 amino acid residues I or V; (o) at position 24 amino acid residues Q; (p) at position 26 amino acid residues M, L, V, or I; (q) at position 27 amino acid residues E; (r) at position 28 amino acid residues A or V; (s) at position 30 amino acid residues M; (t) at position 31 amino acid residues Y or F; (u) at position 32 amino acid residues E or D; (v) at position 33 amino acid residues T or S; (w) at position 35 amino acid residues L; (x) at position 37 amino acid residues R, G, E or Q; (y) at position 39 amino acid residues A or S; (z) at position 40 amino acid residues F or L; (aa) at position 45 amino acid residues Y or F; (ab) at position 47 amino acid residues R or G; (ac) at position 48 amino acid residues G; (ad) at position 49 amino acid residues K, R or Q; (ae) at position 51 amino acid residues I or V; (af) at position 52 amino acid residues S; (ag) at position 53 amino acid residues I or V; (ah) at position 54 amino acid residues A; (ai) at position 57 amino acid residues H or N; (aj) at position 58 are amino acid residues Q, K, R or P; (ak) at position 59 amino acid residues A; (al) at position 60 amino acid residues E; (am) at position 61 amino acid residues H or R; (an) at position 63 amino acid residues E or D; (ao) at position 65 amino acid residues E, P or Q; (ap) at position 67 amino acid residues Q or R; (aq) at position 68 amino acid residues K or E; (ar) at position 69 amino acid residues Q; (as) at position 79 amino acid residues E; (at) at position 80 amino acid residues G; (au) at position 81 amino acid residues Y, H or F; (av) at position 82 amino acid residues R; (aw) at position 83 amino acid residues E or D; (ax) at position 84 amino acid residues Q; (ay) at position 86 amino acid residues A; (az) at position 89 amino acid residues G, T or S; (ba) at position 90 amino acid residues L; (bb) at position 91 amino acid residues L, I or V; (bc) at position 92 amino acid residues R or K; (bd) at position 93 amino acid residues H; (be) at position 96 amino acid residues E or Q; (bf) at position 97 amino acid residues I; (bg) at position 100 amino acid residues K or N; (bh) at position 101 amino acid residues K or R; (bi) at position 103 amino acid residues A or V; (bj) at position 104 amino acid residues D; (bk) at position 105 amino acid residues M, L or I; (bi) at position 106 amino acid residues L; (bm) at position 112 amino acid residues T or A; (bn) at position 113 amino acid residues S or T; (bo) at position 114 amino acid residues A; (bp) at position 115 amino acid residues S; (bq) at position 119 amino acid residues K or R; (br) at position 120 amino acid residues K or R; (bs) at position 123 amino acid residues F or L; (bt) at position 125 amino acid residues E; (bu) at position 126 amino acid residues Q or H; (bv) at position 128 amino acid residues E or D; (bw) at position 129 amino acid residues V or I; (bx) at position 130 amino acid residues F; (by) at position 131 amino acid residues D or E; (bz) at position 132 amino acid residues T; (ca) at position 135 amino acid residues V; (cb) at position 138 amino acid residues H; (cc) at position 139 amino acid residues I; (cd) at position 140 amino acid residues L or M; (ce) at position 142 amino acid residues Y; (cf) at position 143 amino acid residues K or R; (cg) at position 145 amino acid residues L or I, and; (ch) at position 146 amino acid residues T; 97. The isolated or recombinant polypeptide of claim 96, characterized in that the amino acid residues in the amino acid sequence corresponding to the positions specified in (a) - (ch), at least 90% fit within the restrictions of the amino acid residues specified in (a) - (ch). 98. The isolated or recombinant polypeptide of claim 86, characterized in that the amino acid residues in the amino acid sequence corresponding to the following positions, at least 80% fit the following restrictions: (a) at positions 9, 76, 94 and 110 amino acid residues A; (b) at positions 29 and 108 amino acid residues C; (c) at position 34 amino acid residues D; (d) at position 95 amino acid residues E; (e) at position 56 amino acid residues F; (f) at positions 43, 44, 66, 74, 87, 102, 116, 122, 127 and 136 amino acid residues G; (g) at position 41 amino acid residues H; (h) at position 7 amino acid residues I; (i) at position 85 amino acid residues K; (j) at position 20, 42, 50, 78 and 121 amino acid residues L; (k) at position 1 and 141 amino acid residues M; (1) at position 23 and 109 amino acid residues N; (m) at positions 22, 25, 133, 134 and 137 amino acid residues P; (n) at position 71 amino acid residues Q; (o) at positions 16, 21, 73, 99 and 111 amino acid residues R; (p) at position 55 amino acid residues S; (q) at position 77 amino acid residues T; (r) at position 107 amino acid residues W; (s) at positions 13, 46, 70 and 118 amino acid residues Y; 99. The isolated or recombinant polypeptide of any one of claims 70-98, characterized in that the amino acid sequence contains one or more amino acid residues from the group consisting of: (a) at position 14 amino acid residues D; (b) at position 18 amino acid residues E; (c) at position 26 amino acid residues M or V; (e) at position 30 amino acid residues I; (f) at position 32 amino acid residues D; (g) at position 36 amino acid residues M or T; (h) at position 37 amino acid residues C; (i) at position 38 amino acid residues D; (j) at position 53 amino acid residues V; (k) at position 58 amino acid residues R; (1) at position 61 amino acid residues R; (m) at position 62 amino acid residues L; (n) at position 64 amino acid residues I or F; (o) at position 65 amino acid residues P; (p) at position 72 amino acid residues I; (q) at position 75 amino acid residues V; (r) at position 88 amino acid residues T; (s) at position 89 amino acid residues G; (t) at position 91 amino acid residues L; (u) at position 98 amino acid residues I; (v) at position 105 amino acid residues I; (w) at position 112 amino acid residues A; (x) at position 124 amino acid residues G or C; (y) at position 128 amino acid residues D; (z) at position 140 amino acid residues M; (aa) at position 143 amino acid residues R; and (ab) at position 144 amino acid residues W; 100. The isolated or recombinant polypeptide of claim 99, characterized in that the amino acid residues in the amino acid sequence corresponding to the positions specified in (a) - (ab), at least 80% fit within the restrictions of the amino acid residues specified in (a) - (ab). 101. The isolated or recombinant polypeptide of any one of claims 86-100, characterized in that the amino acid sequence contains one or more amino acid residues from the group consisting of: (a) at position 41 amino acid residues H; (b) at position 138 amino acid residues H; (c) at position 34 amino acid residues N; and (d) at position 55 amino acid residues S. 102. The isolated or recombinant polynucleotide of claim 69, characterized in that the polypeptide catalyzes the acetylation of glyphosate with a kca/Kmin of at least 1OmM"<1>min-1 for glyphosate. 103. The isolated or recombinant polynucleotide of claim 102, characterized in that the polypeptide catalyzes the acetylation of glyphosate with a kcat/Km of at least 100 mM"<1>min-1 for glyphosate. 104. The isolated or recombinant polynucleotide of claim 103, characterized in that the polypeptide catalyzes the acetylation of aminomethylphosphonic acid. 105. A polypeptide having the GAT activity of said polypeptide selected from the group consisting of SEQ ID NO: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597, 598, 599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 665, 667, 669, 671, 673, 675, 677, 679, 681, 683, 685, 687, 689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811, 813, 815, 817, 819, 821, 823, 825, 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909,911, 913, 915, 917, 919, 921, 923, 925, 927,929,931,953,954, 955, 956,957,958, 959,960,961, 962, 963,964,965,966,967,968, 969, 970, 971 and 972 characterized by: (a) Kmza glyphosate of at least 2mM or less (b) Kmza Acetyl CoA of at least 100mM or less; and (c) a kcat equal to or at least about 6/minute. 106. Isolated or recombinant polypeptide possessing glyphosphate-N-acyltransferase activity, said polypeptide is selected from the group consisting of SEQ ID NO: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588,589,590,591,592, 593, 594, 595, 596, 597, 598,599, 600, 601, 602, 603,604,605,606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 665, 667, 669, 671, 673, 675, 677, 679, 681, 683, 685, 687, 689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811, 813, 815, 817, 819, 821, 823,825, 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855,857,859,861,863,865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911,913, 915, 917, 919, 921, 923, 925, 927, 929, 931, 953, 954, 955, 956, 957, 958, 959, 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971 and 972. 107. A method for producing a transgenic plant or plant cell that is resistant to glyphosate comprising: (a) transforming the plant or plant cell with a polynucleotide encoding a glyphosate-N-acetyltransferase of said polynucleotide selected from the group consisting of SEQ ID NO: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 534, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 620, 622, 624, 626, 628, 630, 632, 634, 636, 638, 640, 642, 644, 646, 648, 650, 652, 654, 656, 658, 660, 662, 664, 666, 668, 670, 672, 674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726, 728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788, 790, 792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814, 816, 818, 820, 822, 824, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916, 918, 920, 922, 924, 926, 928, 930, 932, 933, 934, 935, 936, 937, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952; and (b) optionally regenerating the transgenic plant from the transformed plant cell. 108. A method for selecting a plant or plant cell comprising a nucleic acid construct, and comprising: (a) Providing a transgenic plant or plant cell comprising a nucleic acid construct, characterized in that the nucleic acid construct comprises a nucleotide sequence encoding glyphosate-N-acetyltransferase, said nucleotide sequence being selected from the group consisting of SEQ ID NO: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 534, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 620, 622, 624, 626, 628, 630, 632, 634, 636, 638, 640, 642, 644, 646, 648, 650, 652, 654, 656, 658, 660, 662, 664, 666, 668, 670, 672, 674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726, 728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788, 790, 792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814, 816, 818, 820, 822, 824, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916, 918, 920, 922, 924, 926, 928, 930, 932, 933, 934, 935, 936, 937, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952; and (b) growing the transgenic plant or plant cell in the presence of glyphosate under conditions where the glyphosate-N-acetyltransferase is expressed at an effective level and where the transgenic plant or plant cell grows at a growth rate that is substantially greater than the plant or plant cell would grow if it did not contain the nucleic acid construct. 109. A method for selective weed control in a field containing a crop comprising: (a) Planting in the field with seeds of glyphosate tolerant crops or plants resulting from their transformation with a gene encoding glyphosate-N-acetyltransferase, said gene being selected from the group consisting of SEQ ID NO: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 534, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 620, 622, 624, 626, 628, 630, 632, 634, 636, 638, 640, 642, 644, 646, 648, 650, 652, 654, 656, 658, 660, 662, 664, 666, 668, 670, 672, 674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726, 728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788, 790, 792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814, 816, 818, 820, 822, 824, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916, 918, 920, 922, 924, 926, 928, 930, 932, 933, 934, 935, 936, 937, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952; and (b) applying to crops and weeds in the field sufficient amounts of glyphosate to control weeds without significantly affecting the crop. 110. The method of claim 109, wherein the crop is cotton, corn, or soybeans. 110. Transgenic plant or transgenic plant explant having increased tolerance to glyphosate, characterized in that the plant or plant explant expresses a polypeptide with glyphosate-N-acetyltransferase activity, said polypeptide is selected from the group consisting of SEQ ID NO: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597, 598, 599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619,621,623,625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 665, 667, 669, 671, 673, 675, 677,679, 681, 683, 685, 687,689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811, 813, 815, 817, 819, 821, 823, 825, 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887,889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919,921, 923, 925, 927, 929, 931, 953, 954, 955, 956, 957, 958, 959, 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971 and 972; and at least one polypeptide that causes tolerance to glyphosate by an additional mechanism. 112. Transgenic plant or transgenic plant explant, characterized in that the plant or plant explant expresses a polypeptide with glyphosate-N-transferase activity, said polypeptide is selected from the group consisting of SEQ ID NO: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596,597, 598,599,600,601,602,603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659,661,663, 665, 667, 669,671, 673, 675, 677, 679,681,683,685, 687, 689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803,805,807,809,811,813,815,817, 819, 821, 823, 825, 833, 835, 837, 839, 841,843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 929, 931, 953, 954, 955, 956, 957, 958, 959, 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971 and 972; and at least one polypeptide that causes tolerance to the additional herbicide. 113. A transgenic plant or explant of a transgenic plant having encoded tolerance to glyphosate, characterized in that the plant or plant explant expresses a polypeptide with glyphosate-N-transferase activity, said polypeptide being selected from the group consisting of SEQ ID NO: 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597, 598, 599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 665, 667, 669, 671, 673, 675, 677, 679, 681, 683, 685, 687, 689, 691, 693, 695, 697, 699, 701, 703, 705, 707, 709, 711, 713, 715, 717, 719, 721, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811, 813, 815, 817, 819, 821, 823, 825, 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 929, 931, 953, 954, 955, 956, 957, 958, 959, 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971 and 972; and at least one polypeptide that causes tolerance to glyphosate by an additional mechanism, and at least one polypeptide that causes tolerance to an additional herbicide. 114. A method for controlling weeds in a field containing a crop and comprising; (a) Planting a field with seed of a crop or plants transformed with a gene encoding glyphosate-N-acetyltransferase, said gene being selected from the group consisting of SEQ ID NO: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 534, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 620, 622, 624, 626, 628, 630, 632, 634, 636, 638, 640, 642, 644, 646, 648, 650, 652, 654, 656, 658, 660, 662, 664, 666, 668, 670, 672, 674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726, 728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788, 790, 792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814, 816, 818, 820, 822, 824, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916, 918, 920, 922, 924, 926, 928, 930, 932, 933, 934, 935, 936, 937, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952; and at least one gene encoding a polypeptide that causes tolerance to glyphosate by an additional mechanism; and (b) Applying to the crop and weeds in the field an effective dose of glyphosate sufficient to inhibit the growth of weeds in the field, without significantly affecting the crop. 115. A method for selective weed control in a field containing a crop comprising: (a) Planting the field with crop seed or plants transformed with a gene encoding glyphosate-N-acetyltransferase, said gene being selected from the group consisting of SEQ ID NO: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 534, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 620, 622, 624, 626, 628, 630, 632, 634, 636, 638, 640, 642, 644, 646, 648, 650, 652, 654, 656, 658, 660, 662, 664, 666, 668, 670, 672, 674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726, 728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788, 790, 792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814, 816, 818, 820, 822, 824, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916, 918, 920, 922, 924, 926, 928, 930, 932, 933, 934, 935, 936, 937, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952; and at least one gene encoding a polypeptide that causes tolerance to the additional herbicide, and; (b) applying to the crop and weeds in the field simultaneously or in chronologically separate doses of glyphosate and an additional herbicide sufficient to inhibit the growth of the weeds in the field, without significantly affecting the crop. 116. A method for selective weed control in a field containing a crop comprising: (a) Planting the field with crop seed or plants that have been transformed with a gene encoding glyphosate-N-acetyltransferase, said gene being selected from the group consisting of SEQ ID NO: 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532, 533, 534, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 620, 622, 624, 626, 628, 630, 632, 634, 636, 638, 640, 642, 644, 646, 648, 650, 652, 654, 656, 658, 660, 662, 664, 666, 668, 670, 672, 674, 676, 678, 680, 682, 684, 686, 688, 690, 692, 694, 696, 698, 700, 702, 704, 706, 708, 710, 712, 714, 716, 718, 720, 722, 724, 726, 728, 730, 732, 734, 736, 738, 740, 742, 744, 746, 748, 750, 752, 754, 756, 758, 760, 762, 764, 766, 768, 770, 772, 774, 776, 778, 780, 782, 784, 786, 788, 790, 792, 794, 796, 798, 800, 802, 804, 806, 808, 810, 812, 814, 816, 818, 820, 822, 824, 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910, 912, 914, 916, 918, 920, 922, 924, 926, 928, 930, 932, 933, 934, 935, 936, 937, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952; and at least one gene encoding a polypeptide that causes tolerance to glyphosate by an additional mechanism and at least one gene that encodes a polypeptide that causes tolerance to an additional herbicide, and; (b) applying to the crop and weeds in the field simultaneously or in chronologically separate doses of glyphosate and an additional herbicide sufficient to inhibit the growth of the weeds in the field, without significantly affecting the crop. 117. An isolated or recombinant polynucleotide comprising a nucleotide sequence selected from the group consisting of: (a) a nucleotide sequence encoding an amino acid sequence that is at least 96% identical to SEQ ID NO:919; (b) a nucleotide sequence encoding an amino acid sequence that is at least 97% identical to SEQ ID NO:929; (c) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ IDNO:847; (d) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:851; (e) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:853; (f) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:855; (g) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:857; (h) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:861; (i) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:871; (j) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:875; (k) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:881; (1) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO.885; (m) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:887; (n) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:889; (o) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:893; (p) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:897; (q) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ IDNO:899; (r) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:909; (s) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ IDNO:911; (t) a nucleotide sequence encoding an amino acid sequence that is at least 98% identical to SEQ ID NO:837; (u) a nucleotide sequence encoding an amino acid sequence that is at least 99% identical to SEQ ID NO:841; (v) a nucleotide sequence encoding an amino acid sequence that is at least 99% identical to SEQ ID NO:865; (w) a nucleotide sequence encoding an amino acid sequence that is at least 99% identical to SEQ ID NO:869; (x) a nucleotide sequence encoding an amino acid sequence that is at least 99% identical to SEQ ID NO:879. 118. An isolated or recombinant polynucleotide comprising a nucleotide sequence encoding an amino acid sequence that is at least 95% identical to SEQ ID NO:929 and that contains a Gly or Asn residue at the amino acid site corresponding to position 33 in SEQ ID NO:929. 119. An isolated or recombinant polynucleotide encoding a polypeptide possessing glyphosate N-transferase activity, said polynucleotide being selected from the group consisting of SEQ ED NO: 832, 834, 836, 838, 840, 842, 844, 846, 848, 850, 852, 854, 856, 858, 860, 862, 864, 866, 868, 870, 872, 874, 876, 878, 880, 882, 884, 886, 888, 890, 892, 894, 896, 898, 900, 902, 904, 906, 908, 910,912,914,916,918,920,922, 924,926, 928, 930, 932, 933, 934, 935, 936, 937, 938, 939, 940, 941, 942, 943, 944, 945, 947, 949, 951 and 952. 120. An isolated or recombinant polynucleotide comprising an amino acid sequence selected from the group consisting of: (a) an amino acid sequence that is at least 96% identical to SEQ ID NO:919; (b) an amino acid sequence that is at least 97% identical to SEQ ID NO:929; (c) an amino acid sequence that is at least 98% identical to SEQ ID NO:847; (d) an amino acid sequence that is at least 98% identical to SEQ ID NO:851; (e) an amino acid sequence that is at least 98% identical to SEQ ID NO:853; (f) an amino acid sequence that is at least 98% identical to SEQ ID NO:855; (g) an amino acid sequence that is at least 98% identical to SEQ ID NO:857; (h) an amino acid sequence that is at least 98% identical to SEQ ID NO:861; (i) an amino acid sequence that is at least 98% identical to SEQ ID NO:871; (j) an amino acid sequence that is at least 98% identical to SEQ ID NO:875; (k) an amino acid sequence that is at least 98% identical to SEQ ID NO:881; (1) an amino acid sequence that is at least 98% identical to SEQ ID NO:885; (m) an amino acid sequence that is at least 98% identical to SEQ ID NO:887; (n) an amino acid sequence that is at least 98% identical to SEQ ID NO:889; (o) an amino acid sequence that is at least 98% identical to SEQ ID NO:893; (p) an amino acid sequence that is at least 98% identical to SEQ ID NO:897; (q) an amino acid sequence that is at least 98% identical to SEQ ID NO:899; (r) an amino acid sequence that is at least 98% identical to SEQ ID NO:909; (s) an amino acid sequence that is at least 98% identical to SEQ ID NO:911; (t) an amino acid sequence that is at least 98% identical to SEQ ID NO:837; (u) an amino acid sequence that is at least 99% identical to SEQ ID NO:841; (v) an amino acid sequence that is at least 99% identical to SEQ ID NO:865; (w) an amino acid sequence that is at least 99% identical to SEQ ID NO:869; (x) an amino acid sequence that is at least 99% identical to SEQ ID NO:879. 121. An isolated or recombinant polynucleotide comprising an amino acid sequence at least 95% identical to SEQ ID NO:929 and comprising a Gly or Asn residue at an amino acid site corresponding to position 33 in SEQ ID NO:929. 122. An isolated or recombinant polypeptide comprising residues 2-146 of an amino acid sequence selected from the group consisting of SEQ ID NO: 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 929, 931, 953, 954, 955, 956, 957, 958, 959, 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971 and 972. 123. The isolated or recombinant polypeptide of claim 122, comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 929, 931, 953, 954, 955, 956, 957, 958, 959, 960, 961, 962, 963, 964,965,966, 967,968, 969, 970, 971 and 972. 124. A method for increasing expression of a polynucleotide in a plant or plant cell, the method comprising: (a) Obtaining a first polynucleotide comprising a nucleic acid sequence encoding a polypeptide with an amino acid sequence that can be optimally aligned with a sequence selected from the group consisting of SEQ ID NO:300, SEQ ID NO:445 and SEQ ID NO:457 to obtain a similarity score of at least 460 using the BLOSUM62 matrix, a break existence "penalty" of 11 and a break spread "penalty" of 1, the nucleic acid sequence contains the ATG codon of the initial methionine; (b) Insertion of one or two GCG or GCT codons into the nucleic acid sequence immediately downstream and adjacent to the ATG codon of the initial methionine, resulting in a modified polynucleotide; and (c) Transforming the plant or plant cell with the modified polynucleotide, wherein the plant or plant cell transformed with the modified polynucleotide accumulates a greater amount of the encoded polypeptide when compared to the plant or plant cell transformed with the first polynucleotide. 125. The method of claim 124 further comprises identifying one or more codons in the nucleic acid sequence that are commonly used in plants, and replacing codons that are commonly used in plants with codons encoding the same amino acids that are commonly used in plants. 1. An isolated or recombinant polynucleotide, characterized in that it consists of a nucleotide sequence that encodes a polypeptide, which has glyphosate-N-acetyltransferase activity and consists of an amino acid sequence that: (a) is at least 93% identical to the sequence of SEQ ID NO: 803; and/or (b) is at least 94% identical to the sequence of SEQ ID NO: 795. 2. An isolated or recombinant polynucleotide according to claim 1, characterized in that said polynucleotide consists of an amino acid sequence that is identical to the sequences of SEQ ID NO: 803 or SEQ ID NO: 795 at least 95%, 96%, 97%, 98%, or 99%. 3. Isolated or recombinant polynucleotide according to claim 1, characterized in that said polynucleotide consists of the amino acid sequence shown as SEQ ID NO: 621, 623, 625, 627, 629, 631, 633, 635, 637, 639, 641, 643, 645, 647, 649, 651, 653, 655, 657, 659, 661, 663, 673, 675, 677, 679, 681, 683, 685, 687, 689, 691, 693, 701, 705, 715, 723, 725, 727, 729, 731, 733, 735, 737, 739, 741, 743, 745, 747, 749, 751, 753, 755, 757, 759, 761, 763, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 785, 787, 789, 791, 793, 795, 797, 799, 801, 803, 805, 807, 809, 811, 813, 817, 819, 821, 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 929, 931, 946, 948, or 950. 4. Isolated recombinant polynucleotide according to claim 1, characterized in that said polypeptide catalyzes acetylation of glyphosate with kcat/K.m of at least 10 mM"<1>min"<1>for glyphosate, where kcat/Km was measured in the presence of 20 mM HEPES at pH 6.8, 10% ethylene glycol, 0.2 mM acetyl CoA, and without additional KC1 at 23°C. 5. An isolated or recombinant polynucleotide according to claim 4, characterized in that said polynucleotide catalyzes the acetylation of glyphosate with a kcat/Kmod of at least 100 mM"<1>min'<1> for glyphosate. 6. An isolated or recombinant polynucleotide according to claim 1, characterized in that said polypeptide catalyzes acetylation of aminomethylphosphonic acid. 7. An isolated or recombinant polynucleotide according to claim 1, characterized in that said The polypeptide also has glyphosate-N-acetyltransferase activity. 8. The nucleic acid construct of any one of claims 1-7. The nucleic acid construct of claim 8, further comprising a promoter operably linked to said polynucleotide, wherein said promoter is heterologous to said polynucleotide and wherein tolerance to glyphosate of a plant cell transformed with said nucleic acid construct is increased. by a plant cell that has not been transformed with the aforementioned nucleic acid construct. 10. A cell containing at least one polynucleotide according to any of claims 1-7, characterized in that said polynucleotide is heterologous to the cell. 11. A cell according to claim 10, characterized in that said cell is a plant cell. 12. A transgenic plant containing at least one polynucleotide according to any one of claims 1-7, characterized in that said nucleotide is heterologous to the cell. 13. An explant of a transgenic plant containing at least one polynucleotide according to any one of claims 1-7, characterized in that said polynucleotide is heterologous to the cell. 14. Transgenic plant according to claim 12, characterized in that said transgenic plant is a crop plant of a genus selected from the following group: Brassica, Linum, Zea, Glycine, and Gossypium. 15. Transgenic plant according to claim 14, characterized in that said plant exhibits improved tolerance to glyphosate compared to plants of the same species, genus or cultivar that do not contain at least one polynucleotide according to any of claims 1-7. 16. Transgenic plant according to claim 12, characterized in that said plant does not show a reduction in yield after treatment with glyphosate applied at a level effective to inhibit the growth of plants of the same species, genus or cultivar that do not contain at least one polynucleotide according to any of claims 1-7. 17. Transgenic plant according to claim 15, characterized in that said plant further contains at least one polypeptide that contributes to tolerance to an additional herbicide. 18. A transgenic plant according to claim 17, characterized in that at least one said polypeptide contributing to tolerance to an additional herbicide is selected from the group consisting of: (a) sulfonamide-tolerant acetolactate synthase; (b) sulfonamide-tolerant acetohydroxy acid synthase; (c) imidazolinone-tolerant acetolactate synthase; and (d) imidazolinone-tolerant acetohydroxy acid synthase. 19. A seed produced in a plant according to claim 12. 20. A polypeptide having GAT activity, wherein said polypeptide comprises an amino acid sequence which: (a) is at least 93% identical to the sequence of SEQ ID NO: 803; and/or (b) is at least 90% identical to the sequence of SEQ ID NO: 795. 21. Polypeptide according to claim 20, characterized in that said polypeptide has: (a) Kmza glyphosate less than 2.9 mM; and (b) a kcat equal to at least 6 per minute, where said kcat Kms were measured in the presence of 20 mM HEPES at pH 6.8, 10% ethylene glycol, 0.2 mM acetyl CoA, and without additional KCl at 23°C. 22. The polypeptide according to claim 21, characterized in that said polypeptide further comprises a chloroplast transient peptide. 23. Procedure obtaining a transgenic plant resistant to glyphosate, characterized in that it consists of: (a) transforming a plant cell with a polynucleotide according to any one of claims 1-7; (b) selecting a plant cell that is resistant to glyphosate by growing the plant cells in the presence of a concentration of glyphosate that inhibits the growth of plant cells that do not contain the polynucleotide according to any one of claims 1-7; and (c) regenerating a transgenic plant from said plant cell. 24. A method for controlling weeds in a field containing a crop, comprising: (a) planting the field with crop seed or plants tolerant to glyphosate as a result of transformation with a polynucleotide according to any one of claims 1-7; and (b) applying to any crop and weed in the field a sufficient amount of herbicide to control the weed without significantly affecting the crop. 25. The method according to any one of claims 24, characterized in that step (b) is performed before step (a). 26. Procedure according to the request 24, characterized in that said herbicide contains glyphosate. 27. The method according to claim 24, characterized in that said herbicide contains a sulfonyl urea herbicide. 28. The method according to claim 24, characterized in that said herbicide contains glyphosate and sulfonyl urea herbicide. 29. A transgenic plant, characterized in that it contains: (a) a first nucleotide sequence encoding a first polypeptide having glyphosate-N-acetyltransferase activity; and (b) a second nucleotide sequence encoding an HRA mutation of acetolactate synthase, wherein said plant exhibits tolerance to glyphosate compared to a plant of the same species, genus or cultivar that does not contain said first polypeptide. 30. The plant according to claim 29, characterized in that said plant shows no reduction in yield after treatment with glyphosate applied at a level effective to inhibit the growth of a plant of the same species, genus or cultivar containing the first polypeptide. 31. Seeds, indicated thereby obtained from a plant according to claim 29. 32. A method of weed control in a field containing a crop, characterized in that it consists of: (a) planting the field with crop seeds or plants containing: (i) a first nucleotide sequence encoding a first polypeptide having glycosate-N-acetyltransferase activity; and (ii) a second nucleotide sequence encoding an HRA mutation of acetolactate synthase; and (b) applying to any crop and weed in the field a sufficient amount of herbicide to control the weed without significantly affecting the crop. 33. The method according to claim 32, characterized in that step (b) is performed before step (a). 34. The method according to claim 32, characterized in that said herbicide consists of glyphosate. 35. The method according to claim 32, characterized in that said herbicide contains a sulfonylurea herbicide. 36. The method according to claim 35, characterized in that said sulfonylurea herbicide contains at least one of the following chlorimuron, chlorsulfuron, rimsulfuron, rimsulfuron, thiphenylsulfuron or tribenuron. 37. The method according to claim 32, characterized in that said herbicide consists of glyphosate and sulfonylurea herbicides. 38. A method for selective weed control in a field containing a crop, comprising the following steps: (a) seeding the field with crop seeds or plants comprising a first polypeptide having glyphosate N-acetyltransferase activity and a second polypeptide that is an HRA mutation of acetolactate synthase; and (b) applying to the field a sufficient amount of glyphosate and at least one other herbicide to control the weed without significantly affecting the crop, wherein said second herbicide is selected from the group consisting of: (i) chlorimuron; (ii) chlorsulfuron; (iii) rimsulfuron; (iv) thifensulfuron; and (c) tribenuron. 39. The method according to claim 38, characterized in that said second herbicide is tribenuron and where step (b) further consists of applying thifensulfuron to the field. 40. The method according to claim 39, characterized in that step (b) is performed before step (a). 1. An isolated or recombinant polynucleotide containing a nucleotide sequence encoding a polypeptide, characterized in that said polypeptide possesses glyphosate-N-acetyltransferase activity and contains an amino acid sequence that: (a) shares at least 94% identical sequences with SEQ ID NO: 841; and/or (b) contains the amino acid sequence shown in SEQ ED NO: 968. 2. The isolated or recombinant polynucleotide of claim 1, characterized in that said polypeptide contains an amino acid sequence that shares at least 95%, 96%, 97%, 98%, or 99% sequence identity with SEQ ID NO: 841. 3. The isolated or recombinant polynucleotide of claim 1, characterized in that said polypeptide comprises the amino acid sequence shown in SEQ ID NO: 621, 623, 639, 641, 647, 649, 653, 659, 661, 673, 677, 681, 683, 685, 723, 731, 733, 739, 741, 745, 751, 753, 755, 757, 759, 761, 765, 767, 769, 771, 773, 775, 777, 779, 781, 783, 787, 789, 791, 793, 795, 799, 803, 805, 807, 809, 811, 817, 819, 821, 833, 835, 837, 839, 841, 843, 845, 847, 849, 851, 853, 855, 857, 859, 861, 863, 865, 867, 869, 871, 873, 875, 877, 879, 881, 883, 885, 887, 889, 891, 893, 895, 897, 899, 901, 903, 905, 907, 909, 911, 913, 915, 917, 919, 921, 923, 925, 927, 931, 946, 948, and 950. 4. The isolated or recombinant polynucleotide of claim 1, characterized in that said polypeptide catalyzes the acetylation of glyphosate with a kcat/Kmod of at least 10 mM"<1>min"<1> for glyphosate, characterized in that kcat/Kmmeren in the presence of 20 mM HEPES at pH 6.8, 10% ethylene glycol, 0.2 mM acetyl CoA, and no additional KCl at 23°C. 5. The isolated or recombinant polynucleotide of claim 4, characterized in that said polypeptide catalyzes the acetylation of glyphosate with a kcat/Kmod of at least 100 mM"<1>min"<1>for glyphosate. 6. Isolated or recombinant polynucleotide from patent claim 1, characterized in that said polypeptide catalyzes the acetylation of aminomethylphosphonic acid. 7. The isolated or recombinant polynucleotide of claim 1, characterized in that said polypeptide also possesses glyphosate-N-acyltransferase activity. 8. A nucleic acid construct comprising the isolated or recombinant polynucleotide of any one of claims 1-7. 9. The nucleic acid construct of claim 8, further comprising a promoter operably linked to said polynucleotide, indicated that said promoter is heterologous with respect to said polynucleotide and indicated that the tolerance to glyphosate of a plant cell that has been transformed with said nucleic acid construct is increased compared to a plant cell that has not been transformed with said nucleic acid construct. 10. A cell comprising at least one polynucleotide of any one of claims 1-7, characterized in that the polynucleotide is heterologous to the cell. 11. The cell of claim 10, characterized in that the cell is a plant cell. 12. Transgenic plant produced from cells from patent claim 11. 13. An explant of a transgenic plant comprising a cell from claim 11. 14. A transgenic plant from claim 12, characterized in that the transgenic plant is a crop plant within a genus selected from the following group: Brassica, Linum, Zea, Glycine, and Gossypium. 15. The transgenic plant of claim 14, characterized in that said plant exhibits increased tolerance to glyphosate when compared to a plant of the same species, strain or cultivar that does not contain at least one polynucleotide of any of claims 1-7. 16. Transgenic plant from claim 12, characterized in that said plant does not show a reduction in yield after treatment with glyphosate applied at a level effective in inhibiting the growth of a plant of the same species, strain or cultivar that does not contain at least one polynucleotide from any of claim 1-5. 17. The transgenic plant of claim 15, characterized in that said plant further contains at least one polypeptide that provides tolerance to additional herbicide. 18. The transgenic plant of claim 17, characterized in that at least one polypeptide conferring tolerance to an additional herbicide selected from the group consisting of: (a) sulfonamide-tolerant acetolactate synthase is mentioned; (b) sulfonamide-tolerant acetohydroxy acid synthases; (c) imidazolinone-tolerant acetolactate synthases; and (d) imidazolinone-tolerant acetohydroxy acid synthases. 19. The seed produced in the plant of claim 12. 20. A polypeptide possessing GAT activity, characterized in that said polypeptide comprises an amino acid sequence that: (a) shares at least 94% sequence identity with SEQ ID NO: 841; and/or (b) contains the amino acid sequence shown in SEQ ID NO: 968. 21. The polypeptide of claim 20, characterized in that said polypeptide has: (a) Kmza glyphosate less than 2.9 mM; and (b) kcat equal to at least 6 per minute, indicated that said kcat Kms were measured in the presence of 20 mM HEPES at pH 6.8, 10% ethylene glycol, 0.2 mM acetyl CoA, and without additional KCl at 23°C. 22. The polypeptide of claim 21, characterized in that said polypeptide further contains a chloroplast transient peptide. 23. A method for producing a glyphosate-tolerant transgenic plant comprising: (a) transforming a plant cell with the polynucleotide of any one of claims 1-7; (b) selecting a plant cell that is resistant to glyphosate by growing the plant cell in the presence of a concentration of glyphosate that inhibits the growth of the plant cell that does not contain the polynucleotide of any one of claims 1-7; and (c) regenerating a transgenic plant from said plant cell. 24. A method for controlling weeds in a field containing a crop comprising: (a) planting a field with crop seed or plants that are glyphosate tolerant as a result of transformation with the polynucleotide of any one of claims 1-7; and (b) applying to any crop and weed in the field a sufficient amount of herbicide to control the weed without significantly affecting the crop. 25. The method of claim 24, characterized in that step (b) is performed before step (a). 26. The method from claim 24, characterized in that said herbicide contains glyphosate. 27. The method of claim 24, characterized in that said herbicide contains a sulfonylurea herbicide. 28. The method from patent claim 24, characterized in that said herbicide contains glyphosate and sulfonylurea herbicide.