L-Glutamic Acid-Producing Microorganism and a Method for Producing L-Glutamic Acid

Abstract

A coryneform bacterium which has an L-glutamic acid-producing ability and grows at least at the same growth rate as a non-mutated strain or a wild-type strain and has intracellular .alpha.-ketoglutarate dehydrogenase activity which is less than half that of the non-mutated or wild-type strain, and is obtained by introducing a mutation into a coding region or an expression control region of the chromosomal odhA gene encoding the E1o subunit of the .alpha.-ketoglutarate dehydrogenase complex.

Description

[0001] This application claims priority under 35 U.S.C. .sctn.120 to U.S. application Ser. No. 11/222,138, which claims priority under 35 U.S.C. .sctn.119(e) to U.S. provisional application 60/651,229, the entireties of both of which are incorporated by reference.

FIELD OF THE INVENTION

[0002] The present invention relates to an L-glutamic acid-producing microorganism and a method for producing L-glutamic acid using the microorganism. L-glutamic acid is widely used in food industry, for example, as a raw material for production of seasonings.

BRIEF DESCRIPTION OF THE RELATED ART

[0003] L-glutamic acid has been conventionally produced on an industrial scale by fermentative methods using L-glutamic acid-producing coryneform bacteria such as those belonging to the genus Brevibacterium and Corynebacterium. To improve the L-glutamic acid-producing ability of the coryneform bacteria, strains isolated from nature or artificial mutants of such strains are used as the L-glutamic acid-producing coryneform bacteria.

[0004] Various technologies for improving the L-glutamic acid-producing ability by enhancing L-glutamic acid biosynthetic enzyme activity using recombinant DNA techniques have been reported. For example, coryneform bacteria with an amplified citrate synthase gene (JP07-121228B), and coryneform bacteria with an amplified glutamate dehydrogenase gene (EP 955368) have been reported.

[0005] In the production of substances by fermentation, it is necessary to maintain sufficient growth of bacterial cells to sufficiently produce a target substance. Accordingly, it is necessary to breed a strain with enhanced biosynthesis of a target substance without causing a decrease in bacterial growth. In the production of L-glutamic acid, it has been reported that it is advantageous to decrease .alpha.-ketoglutarate dehydrogenase activity (JP06-237779A, and WO95/34672). However, there have been no reports of decreasing the .alpha.-ketoglutarate dehydrogenase activity while maintaining a sufficient level of L-glutamic acid production.

SUMMARY OF THE INVENTION

[0006] An object of the present invention is to provide a technology to improve the L-glutamic acid-producing ability of coryneform bacteria for fermentative production of L-glutamic acid. When the .alpha.-ketoglutarate dehydrogenase gene is disrupted, energy generated through the TCA cycle is decreased, leading to retardation of the bacterial growth. As a result, sufficient yield of L-glutamic acid may not be obtained.

[0007] Therefore, a mutant strain having a decreased ability to degrade L-glutamic acid while maintaining an ordinary growth rate would be useful for efficient production of L-glutamic acid. Mutant strains were obtained that have a decreased .alpha.-ketoglutarate dehydrogenase activity and maintain almost the same growth rate as a wild-type strain, by introducing mutations into a chromosomal odhA gene that encodes the E1o subunits of the .alpha.-ketoglutarate dehydrogenase complex of coryneform bacterium. L-glutamic acid was found to be efficiently produced by using such mutant strains.

[0008] It is an object of the present invention to provide an L-glutamic acid-producing coryneform bacterium, comprising [0009] a) intracellular .alpha.-ketoglutarate dehydrogenase activity which is less than half that of a non-mutated or wild-type strain, and [0010] b) a mutation in a coding region or an expression control region of a chromosomal odhA gene encoding the E1o subunit of the .alpha.-ketoglutarate dehydrogenase complex, wherein said bacterium grows at a rate which is at least about 80% of the growth rate of a non-mutated or wild-type strain.

[0011] It is a further object of the present invention to provide the coryneform bacterium as described above, wherein said odhA gene encodes a protein selected from the group consisting of:

[0012] (A) a protein comprising an amino acid sequence of SEQ ID NO: 10,

[0013] (B) a protein comprising an amino acid sequence of SEQ ID NO: 10,

whereby one or several amino acids in said protein are substituted, deleted, inserted, or added, and wherein said protein has an activity of the E1o subunit of the .alpha.-ketoglutarate dehydrogenase complex.

[0014] (C) a protein comprising amino acids 37 to 1257 of SEQ ID NO: 10, and

[0015] (D) a protein comprising amino acids 37 to 1257 of SEQ ID NO: 10,

whereby one or several amino acids in said protein are substituted, deleted, inserted, or added, and wherein said protein has an activity of the E1o subunit of the .alpha.-ketoglutarate dehydrogenase complex.

[0016] It is a further object of the present invention to provide the coryneform bacterium as described above, wherein said several amino acids are 2 to 20 amino acids.

[0017] It is a further object of the present invention to provide the coryneform bacterium as described above, wherein said odhA gene is selected from the group consisting of:

[0018] (a) a gene comprising nucleotides 443 to 4213 of SEQ ID NO: 9,

[0019] (b) a gene that is able to hybridize under stringent conditions to a polynucleotide comprising nucleotides 443 to 4213 of ID NO: 9 or a probe prepared from a polynucleotide comprising nucleotides 443 to 4213 of SEQ ID NO: 9, and wherein said gene encodes a protein which has the activity of the E1o subunit of the .alpha.-ketoglutarate dehydrogenase complex,

[0020] (c) a gene comprising nucleotides 551 to 4213 of SEQ ID NO: 9, and

[0021] (d) a gene that is able to hybridize under stringent conditions to a polynucleotide comprising nucleotides 551 to 4213 of SEQ ID NO: 9 or a probe prepared from a polynucleotide comprising nucleotides 551 to 4213 of SEQ ID NO: 9, and wherein said gene encodes a protein which has the activity of the E1o subunit of the .alpha.-ketoglutarate dehydrogenase complex.

[0022] It is a further object of the present invention to provide the coryneform bacterium as described above, wherein said mutation is introduced into a region encoding a thiamine pyrophosphate binding region.

[0023] It is a further object of the present invention to provide the coryneform bacterium as described above, wherein said mutation comprises deletion of an amino acid selected from the group consisting of Gly at position 686, Leu at position 687, Gly at position 688, Asn at position 713, Asn at position 714, and combinations thereof in the amino acid sequence shown in SEQ ID NO: 10.

[0024] It is a further object of the present invention to provide the coryneform bacterium as described above, wherein said mutation is introduced into the region comprising nucleotides 2534 to 2548 of SEQ ID NO: 9.

[0025] It is a further object of the present invention to provide the coryneform bacterium as described above, wherein said mutation comprises deletion of one or more amino acids in the region comprising amino acids 698 to 702 of SEQ ID NO: 10.

[0026] It is a further object of the present invention to provide the coryneform bacterium as described above, wherein said mutation comprises replacement of an amino acid selected from the group consisting of Lys at position 698, Leu at position 699, Arg at position 700, Tyr at position 702, and combinations thereof in the amino acid sequence shown in SEQ ID NO: 10.

[0027] It is a further object of the present invention to provide the coryneform bacterium as described above, wherein said mutation is introduced into the region comprising nucleotides 1094 to 1114 of SEQ ID NO: 9.

[0028] It is a further object of the present invention to provide the coryneform bacterium as described above, wherein said mutation comprises deletion of one or more amino acids in the region comprising amino acids 218 to 224 of SEQ ID NO: 10.

[0029] It is a further object of the present invention to provide a method for producing L-glutamic acid comprising:

[0030] a) culturing the coryneform bacterium according to claim 1 in a culture medium and

[0031] b) collecting L-glutamic acid from the culture medium and/or the bacterium.

[0032] It is a further object of the present invention to provide a gene encoding mutant .alpha.-ketoglutarate dehydrogenase selected from the group consisting:

[0033] (a) a gene comprising nucleotides 443 to 4213 of a polynucleotide selected from the group consisting of SEQ ID NO: 11, 13, and 15, or a gene comprising nucleotides 443 to 4210 of a polynucleotide selected from the group consisting of SEQ ID NO: 44, 46, and 48,

[0034] (b) a gene that is able to hybridize under stringent conditions to a polynucleotide comprising nucleotides 443 to 4213 of a polynucleotide selected from the group consisting of SEQ ID NO: 11, 13, and 15, a polynucleotide comprising nucleotides 443 to 4210 of a polynucleotide selected from the group consisting of SEQ ID NO:44, 46, and 48, a probe prepared from nucleotides 443 to 4213 of a polynucleotide selected from the group consisting of SEQ ID NO: 11, 13, and 15, or a probe prepared from nucleotides 443 to 4210 of a polynucleotide selected from the group consisting of SEQ ID NO: 44, 46, and 48, and wherein said gene encodes a protein which has .alpha.-ketoglutarate dehydrogenase activity which is less than half that of a wild-type or non-mutated strain by forming a complex with E2o and E3 subunits,

[0035] (c) a gene comprising nucleotides 551 to 4213 of a polynucleotide selected from the group consisting of SEQ ID NO: 11, 13, and 15, or a gene comprising nucleotides 551 to 4210 of a polynucleotide selected from the group consisting of SEQ ID NO: 44, 46, and 48, and

[0036] (d) a gene that is able to hybridize under stringent conditions to a polynucleotide comprising nucleotides 551 to 4213 of a polynucleotide selected from the group consisting of SEQ ID NO: 11, 13, and 15, a polynucleotide comprising nucleotides 551 to 4210 of a polynucleotide selected from the group consisting of SEQ ID NO: 44, 46, and 48, or a probe prepared from nucleotides 551 to 4213 of a polynucleotide selected from the group consisting of SEQ ID NO: 11, 13, and 15, or a probe prepared from nucleotides 551 to 4210 of a polynucleotide selected from the group consisting of SEQ ID NO: 44, 46, and 48, and wherein said gene encodes a protein which has .alpha.-ketoglutarate dehydrogenase activity which is less than half that of a wild-type or non-mutated strain by forming a complex with E2o and E3 subunits.

[0037] It is a further object of the present invention to provide a mutant .alpha.-ketoglutarate dehydrogenase selected from the group consisting of:

[0038] (a) a protein selected from the group consisting of SEQ ID NO: 12, 14, 16, 45, 47, and 49,

[0039] (b) a protein selected from the group consisting of SEQ ID NO: 12, 14, 16, 45, 47, and 49, whereby one or several amino acids in said protein are substituted, deleted, or added, and wherein said protein exhibits .alpha.-ketoglutarate dehydrogenase activity which is less than half that of a wild-type or non-mutated strain by forming a complex with E2o and E3 subunits,

[0040] (c) a protein comprising amino acids 37 to 1256 of an amino acid sequence selected from the group consisting of SEQ ID NO: 12, 45, 47, and 49, a protein comprising amino acids 37 to 1255 of an amino acid sequence of SEQ ID NO: 14, or a protein comprising amino acids 37 to 1254 of an amino acid sequence of SEQ ID NO: 16, and

[0041] (d) a protein comprising amino acids 37 to 1256 of an amino acid sequence selected from the group consisting of SEQ ID NO: 12, 45, 47, and 49, a protein comprising amino acids 37 to 1255 of an amino acid sequence of SEQ ID NO: 14, or a protein comprising amino acids 37 to 1254 of an amino acid sequence of SEQ ID NO: 16, whereby one or several amino acids in said protein are substituted, deleted, or added, and wherein said protein exhibits .alpha.-ketoglutarate dehydrogenase activity which is less than half that of a wild-type or non-mutated strain by forming a complex with E2o and E3 subunits.

BRIEF DESCRIPTION OF DRAWINGS

[0042] FIG. 1 shows the construction of plasmid pBS3.

[0043] FIG. 2 is shows the construction of plasmid pBS4S.

[0044] FIG. 3 shows the construction of plasmid pBSOAGN.

[0045] FIG. 4 shows the construction of plasmid pBSOA2-2.

[0046] FIG. 5 shows the change in L-glutamic acid concentration when each strain is cultured.

[0047] FIG. 6 shows the growth rate of each strain.

[0048] FIG. 7 shows the change in the amount of residual sugar when each strain is cultured.

DESCRIPTION OF THE PREFERRED EMBODIMENTS

[0049] Hereinafter, the present invention will be described in detail.

[0050] <1> Coryneform Bacterium of the Present Invention

[0051] The coryneform bacterium of the present invention has an L-glutamic acid-producing ability, and grows almost at the same growth rate as a non-mutated strain or a wild-type strain. The corynebacterium of the present invention has intracellular .alpha.-ketoglutarate dehydrogenase (hereinafter, also referred to as ".alpha.-KGDH") activity which is less than half that of a non-mutated strain or the wild-type strain, by introduction of mutations into a coding region or an expression control region of the odhA gene, which encodes the E1o subunit of .alpha.-KGDH complex.

[0052] .alpha.-KGDH is also called oxoglutarate dehydrogenase or 2-oxoglutarate dehydrogenase.

[0053] In the present invention, examples of coryneform bacterium include conventional coryneform bacterium, and also include bacteria that had been classified into the genus Brevibacterium but are currently classified into the genus Corynebacterium (Int. J. Syst. Bacteriol., 41, 255(1991)), as well as the Brevibacterium bacteria that are very close to Corynebacterium bacteria. Examples of such coryneform bacterium include the following.

[0054] Corynebacterium acetoacidophilum

[0055] Corynebacterium acetoglutamicum

[0056] Corynebacterium alkanolyticum

[0057] Corynebacterium callunae

[0058] Corynebacterium glutamicum

[0059] Corynebacterium lilium

[0060] Corynebacterium melassecola

[0061] Corynebacterium thermoaminogenes (Corynebacterium efficiens)

[0062] Corynebacterium herculis

[0063] Brevibacterium divaricatum

[0064] Brevibacterium flavum

[0065] Brevibacterium immariophilum

[0066] Brevibacterium lactofermentum (Corynebacterium glutamicum)

[0067] Brevibacterium roseum

[0068] Brevibacterium saccharolyticum

[0069] Brevibacterium thiogenitalis

[0070] Brevibacterium ammoniagenes

[0071] Brevibacterium album

[0072] Brevibacterium cerinum

[0073] Microbacterium ammoniaphilum

[0074] Specific examples of the coryneform bacteria are as follows.

[0075] Corynebacterium acetoacidophilum ATCC 13870

[0076] Corynebacterium acetoglutamicum ATCC 15806

[0077] Corynebacterium alkanolyticum ATCC21511

[0078] Corynebacterium callunae ATCC15991

[0079] Corynebacterium glutamicum ATCC13020, ATCC13032, ATCC13060, ATCC13869

[0080] Corynebacterium lilium ATCC15990

[0081] Corynebacterium melassecola ATCC17965

[0082] Corynebacterium thermoaminogenes AJ12340 (FERM BP-1539)

[0083] Corynebacterium herculis ATCC13868

[0084] Brevibacterium divaricatum ATCC14020

[0085] Brevibacterium flavum ATCC13826, ATCC14067, AJ12418 (FERM BP-2205)

[0086] Brevibacterium immariophilum ATCC 14068

[0087] Brevibacterium lactofermentum (Corynebacterium glutamicum) ATCC13869

[0088] Brevibacterium roseum ATCC13825

[0089] Brevibacterium saccharolyticum ATCC14066

[0090] Brevibacterium thiogenitalis ATCC19240

[0091] Brevibacterium ammoniagenes ATCC6871, ATCC6872

[0092] Brevibacterium album ATCC15111

[0093] Brevibacterium cerinum ATCC15112

[0094] Microbacterium ammoniaphilum ATCC15354

[0095] These strains are available from the American Type Culture Collection (ATCC, Address: P.O. Box 1549, Manassas, Va. 20108, United States of America). That is, each strain is given a unique registration number which is listed in the catalogue of the ATCC. Strains can be ordered using this registration number. The AJ12340 strain was deposited at National Institute of Bioscience and Human Technology, Agency of Industrial Science and Technology, Ministry of International Trade and Industry (currently International Patent Organism Depositary, National Institute of Advanced Industrial Science and Technology at Tsukuba Central 6, 1-1, Higashi 1-chome, Tsukuba-shi, Ibaraki-ken 305-5466, Japan) on Oct. 27, 1989 under the provisions of the Budapest Treaty and given an accession number of FERM BP-1539. The AJ12418 strain was deposited at National Institute of Bioscience and Human Technology, Agency of Industrial Science and Technology, Ministry of International Trade and Industry on Jan. 5, 1989 under the provisions of the Budapest Treaty and given an accession number of FERM BP-2205.

[0096] In the present invention, "L-glutamic acid-producing ability" means an ability to cause accumulation of a sufficient amount of L-glutamic acid in a medium when the coryneform bacterium of the present invention is cultured in the medium. The L-glutamic acid-producing ability may be either a property of a parent strain from which the coryneform bacterium of the present invention is bred or a property imparted or enhanced by a mutation, gene recombination, etc. Furthermore, the L-glutamic acid-producing ability may be imparted by introducing a mutation into the odhA gene which encodes the E1o subunit of .alpha.-ketoglutarate dehydrogenase complex.

[0097] Examples of the methods for imparting the L-glutamic acid-producing ability include enhancing expression of a gene encoding an L-glutamic acid biosynthetic enzyme. Examples of the enzymes involved in L-glutamic acid biosynthesis include glutamate dehydrogenase, glutamine synthetase, glutamate synthetase, isocitrate dehydrogenase, aconitate hydratase, citrate synthase, phosphoenolpyruvate carboxylase, pyruvate carboxylase, pyruvate dehydrogenase, pyruvate kinase, phosphoenolpyruvate synthase, enolase, phosphoglyceromutase, phosphoglycerate kinase, glyceraldehyde-3-phophate dehydrogenase, triose phosphate isomerase, fructose bisphosphate aldolase, phosphofructokinase, and glucose phosphate isomerase.

[0098] Enhancement of expression of these genes may be achieved by incorporating a DNA fragment containing such a gene into an appropriate plasmid which is able to autonomously replicate in coryneform bacterium, and transforming bacterial cells with the resultant plasmid; integrating such a gene into a chromosome by homologous recombination, conjugation, transposition, etc.; or introducing a mutation into a promoter region of such a gene (WO/0018935).

[0099] When the above-mentioned genes are introduced by a plasmid or integrated on a chromosome, a promoter for expression of the genes may be any promoter so long as it is able to function in coryneform bacteria. Examples of such promoters include lac promoter, trp promoter, trc promoter, PS2 promoter, and pL promoter. A native promoter of the gene may also be used.

[0100] Examples of microorganisms modified so that expression of citrate synthetase gene, phosphoenolpyruvate carboxylase gene, and/or glutamate dehydrogenase gene is enhanced include those microorganisms disclosed in JP2001-333769A (EP1078989A), JP2000-106869A (EP955368A), JP2000-189169A (EP952221A), and JP2001-333769A (EP1078989A).

[0101] The modification for imparting the L-glutamic acid-producing ability includes decreasing or eliminating an activity of an enzyme that catalyzes a reaction for synthesizing a compound other than L-glutamic acid, and branching from an L-glutamic acid biosynthesis pathway. Examples of such enzymes include isocitrate lyase, acetyl phosphate transferase, acetate kinase, acetohydroxy acid synthase, acetolactate synthase, acetyl formate transferase, lactate dehydrogenase, glutamate decarboxylase, and 1-pyrophosphate dehydrogenase.

[0102] To decrease or eliminate the activity of the enzymes as described above, a mutation or deletion which causes a decrease or loss of the activity of the enzymes may be introduced into the genes of the enzymes on the chromosome. This may be achieved by, for example, disrupting the gene encoding the enzyme on the chromosome, or by modifying an expression control sequence such as a promoter and/or Shine Dargarno (SD) sequence of the gene. In addition, the activities of such enzymes may be decreased or eliminated by introducing a missense mutation which causes an amino acid substitution, a nonsense mutation which generates a stop codon, or a frame shift mutation which adds or deletes one or two nucleotides into a coding region, or by deleting a portion of the gene (Journal of biological Chemistry 272:8611-8617 (1997)). Furthermore, the activities of such enzymes may be decreased or eliminated by constructing a gene encoding a mutant enzyme in which its coding region is deleted and replacing a chromosomal gene with the resulting gene by homologous recombination.

[0103] The L-glutamic acid-producing ability may also be imparted by screening a strain resistant to organic acid analogues or respiratory inhibitors, or by screening a strain sensitive to inhibitors of cell wall synthesis. Examples of such methods include imparting resistance to benzopyrone or naphthoquinone (JP56-1889A), imparting resistance to HOQNO (JP56-140895A), imparting resistance to .alpha.-ketomalonic acid (JP57-2689A), imparting resistance to guanidine (JP56-35981A), and imparting sensitivity to penicillin (JP04-88994A).

[0104] Specific examples of such bacteria include the following strains.

[0105] Brevibacterium flavum AJ11355 (FERM P-5007; JP56-1889A)

[0106] Corynebacterium glutamicum AJ11355 (FERM P-5020; JP56-1889A)

[0107] Brevibacterium flavum AJ11217 (FERM P-4318; JP57-2689A)

[0108] Corynebacterium glutamicum AJ11218 (FERM P-4319; JP57-2689A)

[0109] Brevibacterium flavum AJ11564 (FERM P-5472; JP56-140895A)

[0110] Brevibacterium flavum AJ11439 (FERM P-5136; JP56-35981A)

[0111] Corynebacterium glutamicum H7684 (FERM BP-3004; JP04-88994A)

[0112] The coryneform bacterium of the present invention can be obtained from coryneform bacterium having the L-glutamic acid-producing ability as described above by introducing a mutation into a chromosomal odhA gene which encodes the E1o subunit of the .alpha.-KGDH complex, and selecting those strains that grow almost at the same growth rate as a non-mutated strain or a wild-type strain, and exhibits .alpha.-KGDH activity less than half that of the non-mutated strain or wild-type strain. Alternatively, such a mutation may be introduced into the odhA gene first, followed by imparting an L-amino acid-producing ability.

[0113] In the present invention, .alpha.-KGDH activity means an activity catalyzing a reaction of oxidative decarboxylation of .alpha.-ketoglutarate (2-oxoglutarate) to generate succinyl-CoA. The above-mentioned reaction is catalyzed by the .alpha.-KGDH complex, which includes three kinds of subunits, i.e., .alpha.-ketoglutarate dehydrogenase (E1o, EC1.2.4.2), dihydrolipoamide-S-succinyltransferase (E2o, EC:2.3.1.61), and dihydrolipoamide dehydrogenase (E3, EC:1.8.1.4). That is, these three subunits catalyze each of the following reactions:

[0114] E1o Subunit: 2-oxoglutarate+[dihydrolipoyllysine-residue succinyltransferase]lipoyllysine=[dihydrolipoyllysine-residue succinyltransferase]S-succinyldihydrolipoyllysine+CO.sub.2

[0115] E2o Subunit: CoA+enzymeN6-(S-succinyldihydrolipoyl)lysine=succinyl-CoA+enzymeN6-(dihyd- rolipoyl)lysine

[0116] E3 Subunit: protein N6-(dihydrolipoyl)lysine+NAD.sup.+=protein N6-(lipoyl)lysine+NADH+H.sup.+

[0117] The activity of the ".alpha.-KGDH complex" means an activity catalyzing the total reaction of the above three reactions.

[0118] In Escherichia coli, these three subunits form a complex.

[0119] In the case of coryneform bacterium, the E1o subunit is encoded by the odhA gene and the E3 subunit is encoded by the lpd gene (GenBank Accession NO. Y16642; SEQ ID NO: 17). It is controversial whether the E2o subunit is encoded by the odhA gene as a bifunctional protein together with the E1o subunit (Usuda et al., Microbiology 1996 142, 3347-3354), or encoded by a separate gene registered as an accession No. NCg12126 of NC.sub.--003450 (SEQ ID NO: 27) in the GenBank database. Thus, the odhA gene may encode the E2o subunit in addition to the E1o subunit.

[0120] The coryneform bacteria of the present invention have a mutation in the chromosomal odhA gene. The odhA gene includes, for example, a gene having a nucleotide sequence encoding the amino acid sequence shown in SEQ ID NO: 10. The odhA gene also includes a gene having a nucleotide sequence encoding the amino acid sequence shown in SEQ ID NO: 51. In addition, it is possible that the "gtg" at positions 551 to 553 in the nucleotide sequence of SEQ ID NO: 9 may be translated as Met and translation may be initiated at this codon, even though it is a codon for Val. Therefore, the odhA gene also includes a gene having a nucleotide sequence encoding the amino acid sequence of amino acids 37 to 1257 of SEQ ID NO: 10. Furthermore, the odhA gene may also be a gene encoding a protein that has an amino acid sequence shown in SEQ ID NO: 10 or 51, or amino acid sequence of amino acids 37 to 1257 of SEQ ID NO: 10, including substitution, deletion, insertion or addition of one or several amino acids so long as it exhibits an activity of the E1o subunit of the .alpha.-KGDH complex. The activity of the E1o subunit itself can be determined by the method of Massey et al. (Biochim. Biophys. Acta 38, 447-460). "Several" as used herein is preferably 2 to 20, more preferably 2 to 10, and particularly preferably 2 to 5.

[0121] More specifically, the odhA gene preferably has a nucleotide sequence of nucleotides 443 to 4213 of SEQ ID NO: 9, or a nucleotide sequence of nucleotides 551 to 4213 of SEQ ID NO: 9. The odhA gene may have a nucleotide sequence shown in SEQ ID NO: 50. Furthermore, since the nucleotide sequences of the odhA genes may differ between the species or strains of the coryneform bacteria, the odhA gene may be a gene that hybridizes with a polynucleotide having a nucleotide sequence of nucleotides 443 to 4213 of SEQ ID NO: 9, a polynucleotide having a nucleotide sequence shown in SEQ ID NO: 50, or a nucleotide sequence of nucleotides 551 to 4213 of SEQ ID NO: 9, or a probe prepared from the nucleotide sequences under stringent conditions so long as the gene encodes a protein that exhibits the activity of the E1o subunit of the .alpha.-KGDH complex. The "stringent conditions" as used herein are conditions under which a so-called specific hybrid is formed, and a non-specific hybrid is not formed. It is difficult to clearly express this condition by using any numerical value. However, examples of stringent conditions include those under which DNAs hybridize to each other at a salt concentration with washing typical of Southern hybridization, i.e., washing once or preferably 2-3 times under 1.times.SSC, 0.1% SDS at 60.degree. C., preferably 0.1.times.SSC, 0.1% SDS at 60.degree. C., more preferably 0.1.times.SSC, 0.1% SDS at 68.degree. C.

[0122] In the present invention, "a mutation is introduced into a chromosomal odhA gene" includes the case where the odhA gene on a chromosome is replaced by a mutant odhA gene to generate substantially the same condition in which a mutation is directly introduced into the chromosomal odhA gene.

[0123] The above-mentioned mutation may be introduced not only in the coding region but also in the expression controlling region of the odhA gene. The expression controlling region includes, for example, a promoter, SD sequence, and operator. The expression controlling region of the odhA gene includes a nucleotide sequence of nucleotides 1 to 442 of SEQ ID NO: 9. The expression controlling sequence of the odhA gene may also be identified by genetic analysis software such as GENETYX or by the method disclosed in Goldstein et al. (Prokaryotic promoters in biotechnology. Biotechnol. Annu. Rev., 1995, 1, 105-128).

[0124] The ".alpha.-KGDH activity less than half that of a non-mutated or wild-type strain" preferably means that the .alpha.-KGDH activity per unit cell (per unit weight of protein) of the coryneform bacterium of the present invention cultured for 4 hours is less than half the activity of a non-mutated or wild-type strain of coryneform bacteria cultured under the same conditions. Examples of coryneform bacterium having such decreased .alpha.-KGDH activity include a bacterium in which the number of .alpha.-KGDH molecules per cell is decreased and a bacterium in which the activity per .alpha.-KGDH molecule is decreased. Examples of a wild-type coryneform bacterium used as a control include Brevibacterium lactofermentum ATCC13869 strain. The intracellular .alpha.-KGDH activity of the coryneform bacterium of the present invention is preferably less than 40%, more preferably less than 30% that of the activity of a non-mutated or wild-type strain. Although .alpha.-KGDH activity may be decreased to an undetectable level, it is preferable that the activity is not completely eliminated. The .alpha.-KGDH activity (activity of .alpha.-KGDH complex) can be measured by the method of Shiio et al. (Isamu Shiio and Kyoko Ujigawa-Takeda, Agric. Biol. Chem., 44(8), 1897-1904, 1980).

[0125] As a result of the decrease of intracellular .alpha.-KGDH activity, the L-glutamic acid-producing ability of the coryneform bacterium is improved. In the present invention, "L-glutamic acid-producing ability is improved" preferably means that when the strain of coryneform bacterium into which a mutation has been introduced into odhA gene is cultured in a medium, the amount of L-glutamic acid which accumulates in the medium by the mutant coryneform bacterium is larger than that which accumulates by the wild-type or non-mutated strain, or the rate of L-glutamic acid production by the mutant coryneform bacterium is higher than that of the wild-type or non-mutated strain.

[0126] The phrase "the bacterium grows almost at the same growth rate compared to a wild-type strain or non-mutated strain" preferably means the bacterium of the present invention grows almost at the same growth rate as a wild-type strain such as Brevibacterium lactofermentum ATCC13869. Here, "almost at the same growth rate" means 80% or more, more preferably 90%, or more preferably 95% or more of the growth rate of a wild-type or non-mutated strain. It is not necessary that the coryneform bacterium of the present invention grows almost at the same growth rate as a wild-type or non-mutated strain at any culture temperature. That is, coryneform bacterium which exhibits a sufficient growth rate at low temperatures but exhibits a decreased growth rate at high temperatures such as GN-2-2 strain as shown in the Examples is also included in the coryneform bacterium of the present invention.

[0127] The growth rates of the strain of the present invention and the wild-type or non-mutated strain can be compared, for example, by inoculating the same number of cells of each strain in a medium and comparing viable cell numbers after a predetermined time. When a liquid medium is used, the viable cell number can be calculated based on, for example, optical density (OD) at a wavelength of 600 nm or weight of bacterial cells after a predetermined time. When a solid medium such as a plate medium is used, the viable cell numbers can be calculated based on the number of colonies that appeared after a predetermined time.

[0128] Examples of the method of introducing a mutation into the odhA gene on the chromosome include using X-rays or ultraviolet rays to irradiate the coryneform bacterium, and treating the coryneform bacterium with a mutagen such as N-methyl-N'-nitro-N-nitrosoguanidine. Mutation may also be introduced into the odhA gene on the chromosome by preparing a mutant odhA gene, and replacing the chromosomal odhA gene with such a mutant odhA gene by a homologous recombination technique. Such a mutant odhA gene may be prepared by error-prone PCR, DNA shuffling, or StEP-PCR (Firth A E, Patrick W M; Bioinformatics. 2005 Jun. 2; Statistics of protein library construction.), or overlap-extension PCR (Urban, A., Neukirchen, S. and Jaeger, K. E., A rapid and efficient method for site-directed mutagenesis using one-step overlap extension PCR. Nucleic Acids Res, 25, 2227-8. (1997)).

[0129] Homologous recombination may be performed by a method called "Red-driven integration" in which a linear DNA is used (Datsenko, K. A., PNAS, 97(12), 6640-6645, 2000) or by a method using a plasmid having a temperature-sensitive replication origin (U.S. Pat. No. 6,303,383, and JP05-007491A). Introduction of a mutation into a chromosomal odhA gene may also be performed by using a plasmid which is not replicable in cells of coryneform bacteria or a plasmid capable of transferring to coryneform bacteria by conjugation.

[0130] Examples of such a temperature-sensitive plasmid for Coryneform bacteria include p48K and pSFKT2 (JP2000-262288A), pHSC4 (France Patent Laid-open Publication No. 2667875, 1992 and JP5-7491A), pBS5T, and so forth. These plasmids can autonomously replicate at least at a temperature of 25.degree. C., but cannot autonomously replicate at a temperature of 37.degree. C. in Coryneform bacteria. The AJ12571 strain harboring pHSC4 was deposited at National Institute of Bioscience and Human Technology, Agency of Industrial Science and Technology, Ministry of International Trade and Industry (currently International Patent Organism Depositary, National Institute of Advanced Industrial Science and Technology at Tsukuba Central 6, 1-1, Higashi 1-chome, Tsukuba-shi, Ibaraki-ken 305-5466, Japan) on Aug. 26, 1991 under the provisions of the Budapest Treaty and given an accession number of FERM BP-3524.

[0131] A plasmid which is not replicable in the cells of coryneform bacteria is preferably one replicable in cells of Escherichia bacteria, and examples thereof include pHSG299 (Takara Bio) and pHSG399 (Takara Bio). Examples of a plasmid capable of transferring to coryneform bacteria by conjugation include pK19mobsacB (J. Bacteriology 174:5462-65(1992)).

[0132] A mutant odhA gene is inserted into a temperature-sensitive plasmid or a plasmid which is not replicable in coryneform bacteria, and the obtained recombinant plasmids are used to transform coryneform bacteria. Transformation can be performed by conventional methods. For example, a method of treating recipient cells with calcium chloride so as to increase the permeability of DNA, which has been reported for Escherichia coli (Mandel, M. and Higa, A., J. Mol. Biol., 53, 159 (1970)), and a method of using competent cells prepared from growing cells to introduce a DNA, which has been reported for Bacillus subtilis (Duncan, C. H., Wilson, G. A. and Young, F. E., Gene, 1, 153 (1977)) can be employed. In addition to these methods, a method of introducing a recombinant DNA into protoplast- or spheroplast-like recipient cells, which have been reported to be applicable to Bacillus subtilis, actinomycetes, and yeasts (Chang, S. and Choen, S. N., Molec. Gen. Genet., 168, 111 (1979); Bibb, M. J., Ward, J. M. and Hopwood, O. A., Nature, 274,398 (1978); Hinnen, A., Hicks, J. B. and Fink, G. R., Proc. Natl. Sci., USA, 75, 1929 (1978)), can be employed. In addition, transformation of Coryneform bacteria can also be performed by the electric pulse method (Sugimoto et al., JP2-207791A).

[0133] In the case of using a plasmid which is not capable in cells of coryneform bacteria, a wild-type odhA gene on a chromosome is replaced with the mutant odhA gene on the plasmid.

[0134] In the case of using a temperature-sensitive plasmid, the transformant strain is cultured at a temperature at which the temperature sensitive replication origin does not function (e.g. 25.degree. C.) to obtain a strain into which the plasmid is introduced. Then, the transformant is cultured at a high temperature to eliminate the temperature-sensitive plasmid, and spread over a plate medium containing an antibiotic drug such as kanamycin. Although strains from which the plasmid is eliminated cannot grow on a plate containing such an antibiotic drug, a few strains in which the chromosomal odhA gene is replaced with the mutant odhA gene can grow and appear as colonies.

[0135] In such a strain in which the recombinant DNA containing the mutant odhA gene is integrated into the chromosomal DNA as described above, the recombinant DNA causes recombination with the odhA gene that originally exists on the chromosome, and the fusion genes of the chromosomal odhA gene and the mutant odhA gene are inserted into the chromosome so that the other portions of the recombinant DNA (vector segment, temperature sensitive replication origin and drug resistance marker) are present between the fusion genes. Then, in order to leave only the mutant odhA gene on the chromosomal DNA, one copy of the odhA gene is eliminated together with the vector segment (including the temperature sensitive replication origin and the drug resistance marker) from the chromosomal DNA. In this case, the normal odhA gene is left on the chromosomal DNA and the mutant odhA gene is excised from the chromosomal DNA, or to the contrary, the mutant odhA gene is left on the chromosomal DNA and the normal odhA gene is excised from the chromosome DNA. Then, a strain in which only the mutant odhA gene is left on the chromosome can be selected using PCR, Southern hybridization, or the like.

[0136] Homologous recombination may be performed using a sacB gene encoding levan sucrase as a marker for recombination. The sacB gene encoding levan sucrase is used to efficiently select strains in which a chromosomal odhA gene is replaced by the mutant odhA gene and a vector portion is cured from a chromosome (Schafer, A. et al., Gene 145 (1994) 69-73). That is, in the case of the coryneform bacteria, when levan sucrase is expressed, levan generated by assimilation of sucrose becomes lethal for the bacteria and hence the bacteria cannot grow. Therefore, by culturing on a sucrose-containing plate, strains in which substitution occurs between the mutant odhA gene in the vector and a chromosomal odhA gene and from which the other portions of the vector are cured can be selected.

[0137] Examples of the sacB gene include the following: [0138] Bacillus subillus: sacB GenBank Accession Number X02730 (SEQ ID NO: 19) [0139] Bacillus amyloliqufaciens: sacB GenBank Accession Number X52988 [0140] Zymomonas mobilis: sacB GenBank Accession Number L33402 [0141] Bacillus stearothermophilus: surB GenBank Accession Number U34874 [0142] Lactobacillus sanfranciscensis: frfA GenBank Accession Number AJ508391

[0143] Acetobacter xylinus: lsxA GenBank Accession Number AB034152 [0144] Gluconacetobacter diazotrophicus: lsdA GenBank Accession Number L41732

[0145] <2> The Mutant odhA Gene of the Present Invention

[0146] The mutation to be introduced into the chromosomal odhA gene is not particularly limited so long as it is a mutation which decreases the .alpha.-KGDH activity to be less than half of the .alpha.-KGDH activity of a non-mutated strain or wild-type strain, but does not cause retardation of the growth of the bacterium. Specific examples of the mutation include the following.

[0147] (1) Mutation in the Thiamine Pyrophosphate Binding Region

[0148] This mutation is introduced into the binding region of thiamine pyrophosphate, which is a coenzyme. Thiamine pyrophosphate binding region means a region corresponding to that encoded by nucleotides 2498 to 2584 of the odhA gene (SEQ ID NO: 9). The amino acid sequence of the region is shown as amino acids 686 to 714 in SEQ ID NO: 10. Examples of a mutation in this region include one that causes a deletion of one or more amino acid residues selected from Gly at position 686, Leu at position 687, Gly at position 688, Asn at position 713, and Asn at position 714.

[0149] The mutation in the thiamine pyrophosphate binding region may also be introduced in the region of nucleotides 2534 to 2548 of the odhA gene (SEQ ID NO: 9). This mutation is named a GN type mutation. The GN type mutation is preferably a mutation that causes deletion and/or substitution of one or more amino acid residues selected from Lys at position 698, Leu at position 699, Arg at position 700, Gly at position 701, and Tyr at position 702 in SEQ ID NO: 10. An example of such a mutation is that which deletes Gly at position 701 in SEQ ID NO: 10. Examples of the mutant odhA gene having this mutation include a gene having a nucleotide sequence of nucleotides 443 to 4213 of SEQ ID NO: 13, and genes having a nucleotide sequence of nucleotides 443 to 4210 of SEQ ID NOS: 44, 46 or 48, and the mutant .alpha.-KGDH proteins encoded by these genes are shown in SEQ ID NOS: 14, 45, 47, and 49. Examples of the mutant odhA gene having this mutation also include a gene having a nucleotide sequence of nucleotides 551 to 4213 of SEQ ID NO: 13, and genes having a nucleotide sequence of nucleotides 551 to 4210 of SEQ ID NOS: 44, 46, or 48, and the mutant .alpha.-KGDH proteins encoded by these genes are shown in amino acids 37 to 1255 of SEQ ID NO: 14, and amino acids 37 to 1256 of SEQ ID NOS: 45, 47, and 49. In the nucleotide sequence of SEQ ID NO: 13, a mutation which deletes "t" at position 2538 and "ggcta" at positions 2543 to 2547 of SEQ ID NO: 9 is introduced.

[0150] Furthermore, mutant odhA genes having a mutation which results in replacement of one or more amino acid residues selected from Lys at position 698, Leu at position 699, Arg at position 700, and Tyr at position 702 with another amino acid in SEQ ID NO: 10 are also preferable. The "another amino acid" is not particularly limited so long as it is different from the original amino acid, and selected from natural amino acids such as Lys, Glu, Thr, Val, Leu, Ile, Ser, Asp, Asn, Gln, Arg, Cys, Met, Phe, Trp, Tyr, Gly, Ala, Pro, and His. However, it is preferable that Lys at position 698 is replaced by amino acids other than basic amino acids such as Arg and His, Leu at position 699 is replaced by amino acids other than hydrophobic aliphatic amino acids such as Ile and Val, Arg at position 700 is replaced by amino acids other than basic amino acids such as Lys and His, Tyr at position 702 is replaced by amino acids other than hydroxy amino acids such as Ser and Thr. It is particularly preferable that Lys at position 698 is replaced by hydrophobic aliphatic amino acid such as Ile, Leu, or Val, Leu at position 699 is replaced by hydroxyl amino acid such as Ser, Thr or Tyr, Arg at position 700 is replaced by sulfur-containing amino acid such as Cys or Met, Tyr at position 702 is replaced by hydrophobic aliphatic amino acid such as Ile, Leu, or Val.

[0151] A GN-type mutation may cause both the deletion of Gly at position 701 and replacement of one or more amino acid residues selected from Lys at position 698, Leu at position 699, Arg at position 700, and Tyr at position 702 in SEQ ID NO: 10. Examples of such mutant odhA gene include genes having a nucleotide sequence of nucleotides 443 to 4210 of SEQ ID NOS: 44,46, and 48. Amino acid sequences of mutant .alpha.-KGDH proteins encoded by these mutant odhA genes are shown in SEQ ID NOS: 45, 47, and 49. Examples of such a mutant odhA gene also include genes having nucleotide sequence of nucleotides 551 to 4210 of SEQ ID NOS: 44, 46, and 48. Amino acid sequences of mutant .alpha.-KGDH proteins encoded by these mutant odhA genes are shown in amino acids 37 to 1256 of SEQ ID NOS: 45, 47, and 49. However, the mutant odhA gene having a mutation in the thiamine pyrophosphate binding region is not limited to these examples.

[0152] (2) 2-2 Type Mutation

[0153] This type of mutation is preferably a mutation introduced into the region of nucleotides 1094 to 1114 of the odhA gene (SEQ ID NO: 9) which causes deletion and/or substitution of one or more amino acid residues selected from Asp at position 218, Val at position 219, Ile at position 220, Asp at position 221, Gly at position 222, Lys at position 223, and Pro at position 224 in SEQ ID NO: 10. The 2-2 type mutation is preferably a mutation which deletes Asp at position 218 in SEQ ID NO: 10. Examples of the odhA gene having this mutation include an odhA gene having a nucleotide sequence of nucleotides 443 to 4213 of SEQ ID NO: 11, or an odhA gene having a nucleotide sequence of nucleotides 551 to 4213 of SEQ ID NO: 11. The amino acid sequences of the mutant .alpha.-KGDH encoded by these genes are shown in SEQ ID NO: 12 or amino acid numbers 37 to 1256 of SEQ ID NO: 12, respectively. The nucleotide sequence of SEQ ID NO: 11 has the mutations to delete "gacgt" at 1094 to 1098 and replaces "ag" at 1110 to 1111 with "ggcc" in the nucleotide sequence shown in SEQ ID NO: 9. The 2-2 type mutation is also preferably a mutation which replaces one or more amino acids selected from Val at position 219, Ile at position 220, Asp at position 221, Gly at position 222, and Lys at position 223. Although the amino acids which replace these amino acids are not particularly limited, Val at position 219 is preferably replaced with an amino acid other than an aliphatic hydrophobic amino acid such as Ile and Leu, Ile at position 220 is preferably replaced with an amino acid other than an aliphatic hydrophobic amino acid such as Leu, Asp at position 221 is preferably replaced with an amino acid other than an acidic amino acid such as Glu, and Gly at position 222 is preferably replaced with an amino acid other than a simple amino acid such as Ala. More preferably, Val at position 219, Ile at position 220, and Asp at position 221 are replaced with basic amino acids such as His, Arg and Lys, Gly at 222 is replaced with an amino acid having amide-containing side chain such as Asp and Gln, and Lys at position 223 is replaced with an amino acid such as Gly and Ala.

[0154] However, mutant odhA gene having 2-2 type mutation is not limited to these examples.

[0155] (3) GN2-2 Type Mutation

[0156] This mutation includes both the GN type mutation and the 2-2 type mutation. Examples of the odhA gene having this mutation include an odhA gene having a nucleotide sequence of nucleotides 443 to 4213 of SEQ ID NO: 15, or an odhA gene having a nucleotide sequence of nucleotides 551 to 4213 of SEQ ID NO: 15. The amino acid sequences of the mutant .alpha.-KGDH encoded by these genes are shown in SEQ ID NO: 16 or amino acids 37 to 1254 of SEQ ID NO: 16, respectively. However, the mutant odhA gene having a GN2-2 type mutation is not limited to these examples.

[0157] Other kinds of mutant odhA genes used in the present invention may be screened by using a yggB mutant strain, such as ATCC13869-L as described in Example 5 shown below. That is, a random mutation is introduced into the odhA gene and used to transform the yggB mutant strain. A strain which grows almost at the same growth rate as a wild-type strain or a non-mutated strain and exhibits .alpha.-KGDH activity which is less than half that of the wild-type strain or non-mutated strain is selected from the transformants, followed by sequence determination. Thereby, mutant odhA genes can be obtained.

[0158] A mutant E1o subunit of the .alpha.-KGDH complex encoded by the above-described mutant odhA gene is a protein which has .alpha.-KGDH activity which is less than half that of a wild-type or non-mutated strain by forming a complex with the E2o and E3 subunits of the .alpha.-KGDH complex, and does not cause severe growth retardation of a coryneform bacterium when it is expressed in the coryneform bacterium.

[0159] Such properties of the mutant E1o subunit are considered to be maintained even if one or several amino acids other than the specific amino acids replaced in the above-described GN type or 2-2 type mutants, for example, amino acids that do not influence the enzymatic activity are replaced by other amino acids. Therefore, in the above-mentioned amino acid sequences of the mutant E1o subunit protein (e.g., SEQ ID NOS: 12, 14, 16, 45, 47 and 49 or amino acids 37 to 1256 of SEQ ID NOS: 12, 45, 47 and 49, amino acids 37 to 1255 of SEQ ID NO: 14 and amino acids 37 to 1254 of SEQ ID NO: 16), one or several amino acids other than the specific amino acids substituted in the GN type or 2-2 type mutants may be replaced, so long as the encoded protein exhibits .alpha.-KGDH activity less than half of a wild-type .alpha.-KGDH complex by forming a complex together with .alpha.-KGDH E2o subunit and E3 subunit proteins. Here, "several" means preferably 2 to 20, more preferably 2 to 10, and particularly preferably 2 to 5. Such amino acid substitution may be one caused by a naturally occurring mutation arising from individual difference and difference in species of bacterium from which odhA gene is derived. For example, mutant odhA gene having a nucleotide sequence encoding amino acid sequence of SEQ ID NO: 51 whereby amino acids corresponding to the above-mentioned GN-type mutation or 2-2 type mutation are deleted and/or substituted can also be used in the present invention. Such amino acids corresponding to the GN-type mutation or 2-2 type mutation in the amino acid sequence of SEQ ID NO: 51 can be easily identified by aligning the amino acid sequences of SEQ ID NOS: 10 and 51.

[0160] The above-mentioned substitution is preferably a conservative substitution. In the case of aromatic amino acids, conservative substitutions are referred to substitutions between phe, trp, and tyr for each other. In the case of hydrophobic amino acids, conservative substitutions are referred to substitutions between leu, ile, and val for each other. In the case of polar amino acids, conservative substitutions are referred to substitutions between gln and asn for each other. In the case of basic amino acids, conservative substitutions are referred to substitutions between arg, lys, and his for each other. In the case of acidic amino acids, conservative substitutions are substitutions between asp and glu for each other. In the case of hydroxyl group-containing amino acids, conservative substitutions are referred to substitutions between ser and thr for each other. The conservative substitutions also include: substitution of ser or thr for ala, substitution of gln, his, or lys for arg; substitution of glu, gln, lys, his, or asp for asn; substitution of asn, glu, or gln for asp; substitution of ser or ala for cys; substitution of asn, glu, lys, his, asp, or arg for gln; substitution of asn, gln, lys, or asp for glu; substitution of val for gly; substitution of asn, lys, gln, arg, or tyr for his; substitution of leu, met, val, or phe for ile; substitution of ile, met, val, or phe for leu; substitution of asn, glu, gln, his, or arg for lys; substitution of ile, leu, val or phe for met; substitution of trp, tyr, met, ile, or leu for phe; substitution of thr or ala for ser; substitution of ser or ala for thr; substitution of phe or tyr for trp; substitution of his, phe, or tip for tyr; and substitution of met, ile, or leu for val.

[0161] When the E1o subunit and E2o subunit are encoded by a single odhA gene, the .alpha.-KGDH complex may include the protein of SEQ ID NO: 10 (or amino acids 37 to 1257 of SEQ ID NO: 10) and the protein of SEQ ID NO: 18. When the E1o subunit is encoded by the odhA gene and the E2o subunit is encoded by the gene of SEQ ID NO: 27, the .alpha.-KGDH complex may include the protein of SEQ ID NO: 10, the protein of SEQ ID NO: 18, and the protein of SEQ ID NO: 28.

[0162] A mutant odhA gene of the present invention is a gene encoding the above-mentioned mutant .alpha.-KGDH E1o subunit. The mutant odhA gene of the present invention may be genes that hybridize with a polynucleotide each having the nucleotide sequence of nucleotides 443 to 4213 of SEQ ID NO: 11, 13, or 15, a polynucleotide each having the nucleotide sequence of nucleotides 443 to 4210 of SEQ ID NO: 44, 46 or 48, or with the nucleotide sequence of nucleotide numbers of 551 to 4213 of SEQ ID NO: 11, 13, 15, or with the nucleotide sequence of nucleotides 551 to 4210 of SEQ ID NO: 44, 46, or 48, or with a probe prepared from the sequences under stringent conditions so long as the gene encodes a protein that exhibits .alpha.-KGDH activity less than half that of a wild-type .alpha.-KGDH complex by forming a complex together with the E2o subunit and E3 subunit proteins. Examples of stringent conditions include those under which DNAs hybridize to each other at a salt concentration with washing typical of Southern hybridization, i.e., washing once or preferably 2-3 times under 1.times.SSC, 0.1% SDS at 60.degree. C., preferably 0.1.times.SSC, 0.1% SDS at 60.degree. C., more preferably 0.1.times.SSC, 0.1% SDS at 68.degree. C.

[0163] <3> Method of Producing L-Glutamic Acid

[0164] L-glutamic acid can be produced by culturing the coryneform bacterium of the present invention in a medium to cause accumulation of L-glutamic acid in the medium and/or in the bacterial cells, and collecting the L-glutamic acid from the medium and/or the bacterial cells. In the production method of the present invention, L-glutamic acid is produced preferably by culturing the coryneform bacterium of the present invention, for example, at 25 to 40.degree. C. for 8 to 120 hours. If a strain which exhibits a sufficient growth rate at low temperatures but exhibits decreased growth rate at high temperatures such as the GN-2-2 strain shown in the Examples is used for L-glutamic acid production, it is preferable to culture such a strain at a low temperature such as 25 to 30.degree. C. for 8 to 30 hours so that the strain can grow; and then incubate the obtained bacterial cells at high temperature such as 34 to 40.degree. C. for 16 to 48 hours so that the strain can produce L-glutamic acid.

[0165] The culture medium may be an ordinary medium that contains a carbon source, a nitrogen source, an inorganic salt, and optionally organic micronutrients such as amino acids and vitamins. Either a synthetic medium or a natural medium may be used. Any kinds of the carbon source and nitrogen source may be used so long as they can be utilized by the strain to be cultured.

[0166] Saccharides such as glucose, glycerol, fructose, sucrose, maltose, mannose, galactose, starch hydrolysate, and molasses may be used as the carbon source. In addition, organic acids such as acetic acid and citric acid, and alcohols such as ethanol may also be used alone or in combination as a carbon source. Ammonia, ammonium salts such as ammonium sulfate, ammonium carbonate, ammonium chloride, ammonium phosphate, and ammonium acetate, nitrates, and the like may be used as the nitrogen source. Amino acids, vitamins, fatty acids, nucleic acids, substances containing peptone, casamino acid, yeast extract, and soybean protein decomposition products may be used in a slight amount as the organic nutrients. When an auxotrophic mutant strain that requires an amino acid etc. for growth is used, such a required nutrient is preferably added. Phosphates, magnesium salts, calcium salts, iron salts, manganese salts, and the like can be used as inorganic salts.

[0167] Preferably, aerobic culturing is performed by controlling the fermentation temperature and adjusting the pH of the culture medium to 3 to 9. When the pH decreases during the culture, the medium is neutralized by adding alkali such as calcium carbonate or ammonia gas. Culture for about 10 to about 120 hours results in accumulation of a considerable amount of L-glutamic acid in the medium.

[0168] Furthermore, the culture may be performed by using a liquid medium adjusted to conditions under which the produced L-glutamic acid crystallizes and precipitates. The conditions under which L-glutamic acid crystallizes include pH 5.0 to 4.0, preferably pH 4.5 to 4.0, more preferably pH 4.3 to 4.0, particularly preferably pH 4.0 (EP1233069, EP1233070).

[0169] Collection of L-glutamic acid from the medium after completion of the culture may be performed by conventional methods. L-glutamic acid may be collected, for example, by removing bacterial cells from the medium and concentrating L-glutamic acid or by using ion exchange chromatography. When the culture is performed under conditions under which L-glutamic acid crystallizes and precipitates, the crystallized L-glutamic acid can be collected, for example, by centrifugation or filtration. In this case, L-glutamic acid dissolved in the medium may also be collected after crystallization of the dissolved L-glutamic acid.

EXAMPLES

[0170] Hereinafter, the present invention will be more specifically explained by referring to the following non-limiting examples.

Example 1

[0171] <1> Construction of a Vector Carrying the sacB Gene

[0172] (A) Construction of pBS3

[0173] A sacB gene (SEQ ID NO: 19) was obtained by PCR using a chromosomal DNA of Bacillus subtilis as a template and the oligonucleotides of SEQ ID NOS: 21 and 22 as primers. The PCR was performed using LAtaq (available from TaKaRa) according to the program of one cycle of pre-denaturation at 94.degree. C. for 5 minutes; and 25 cycles of denaturation at 94.degree. C. for 30 seconds, annealing at 49.degree. C. for 30 seconds, and elongation at 72.degree. C. for 2 minutes. The obtained PCR product was purified by a conventional method, and then digested with Bg1II and BamHI and blunt-ended. The fragment was inserted into pHSG299 which had been digested with AvaII and blunt-ended. The resulting DNA was used to transform competent cells of Escherichia coli JM109 (available from Takara Bio). Then, the transformed bacterial cells were applied onto an LB agar plate containing 25 .mu.g/ml of kanamycin (hereinafter, abbreviated as "Km"), and incubated for one night. Thereafter, colonies that appeared were selected as transformants. Plasmids were isolated from the obtained transformants and the plasmid having an insert of the object PCR product was named pBS3. FIG. 1 shows the procedure for constructing pBS3.

[0174] (B) Construction of pBS4S

[0175] The SmaI recognition site in the kanamycin-resistant gene on pBS3 was destroyed by nucleotide substitution using cross-over PCR without causing amino acid substitution. First, PCR was performed using pBS3 as a template and synthetic DNAs of SEQ ID NOS: 23 and 24 as primers to obtain an N-terminal fragment of the kanamycin-resistant gene. On the other hand, to obtain a C-terminal fragment of kanamycin-resistant gene, PCR was performed using pBS3 as a template and synthetic DNAs of SEQ ID NOS: 25 and 26 as primers. The PCR was performed using Pyrobest DNA Polymerase (available from Takara Bio) according to the program of pre-denaturation at 98.degree. C. for 5 minutes; and 25 cycles of denaturation at 98.degree. C. for 10 seconds, annealing at 57.degree. C. for 30 seconds, and elongation at 72.degree. C. for 1 minute. SEQ ID NOS: 24 and 25 are partially complementary to each other and do not contain the SmaI recognition site. Then, to obtain a full-length fragment of the mutant kanamycin-resistant gene without the SmaI recognition site, the above-mentioned N-terminal and C-terminal gene products were mixed with each other in substantially equimolar amounts. PCR was performed using the gene products as a template and synthetic DNAs of SEQ ID NOS: 23 and 26 as primers to obtain a mutation-introduced Km resistant gene. The PCR was performed using Pyrobest DNA Polymerase (available from Takara Bio) according to the program of pre-denaturation at 98.degree. C. for 5 minutes; and 25 cycles of denaturation at 98.degree. C. for 10 seconds, annealing at 57.degree. C. for 30 seconds, and elongation at 72.degree. C. for 1.5 minutes.

[0176] The PCR product was purified by a conventional method, and then digested with BanII and then inserted into the above-described BanII recognition site of pBS3. The resulting plasmid was used to transform competent cells of Escherichia coli JM109 (available from Takara Bio). That is, the transformed bacterial cells were applied onto LB agar medium containing 25 .mu.g/ml of kanamycin, and incubated for one night. Thereafter, colonies that appeared were selected as transformants. Plasmids were isolated from the obtained transformants and the plasmid having an insert of the object PCR product was named pBS4S. FIG. 2 shows the procedure for constructing pBS4S.

[0177] <2> Introduction of odhA Mutation (GN-Type) into C. Glutamicum ATCC13869 Strain

[0178] The sequence of odhA that encodes .alpha.-ketoglutarate dehydrogenase of coryneform bacteria has already been reported (Microbiology 142, 3347-3354 (1996), GenBank accession No. D84102).

[0179] Analysis of the nucleotide sequence of the L-glutamic acid-producing bacterium strain GN which the inventors of the present invention had succeeded in breeding revealed that this strain has deletions of the nucleotides 2538 and 2543 to 2547 in the nucleotide sequence of the odhA gene (SEQ ID NO: 9) as shown in Table 1. In Table 1, amino acid sequence of mutant E1o subunit encoded by the mutant odhA gene is also shown. TABLE-US-00001 TABLE 1 Strain Nucleotide sequence of odhA gene ATCC13869 GCT AAG CTG CGT GGC TAC GAC GTC GGA GGC ACC ATC OAGN GCT AAG C-G CGT --- --C GAC GTC GGA GGC ACC ATC Amino acid sequence of Elo subunit ATCC13869 Ala Lys Leu Arg Gly Tyr Asp Val Gly Gly Thr Ile OAGN Ala Lys Arg Val --- --- Asp Val Gly Gly Thr Ile

[0180] Then, this mutant odhA gene was introduced into C. glutamicum 2256 strain (ATCC13869) and evaluated. At first, a plasmid for introducing these mutations into C. glutamicum 2256 strain (ATCC13869) was prepared. A chromosomal DNA was extracted from the above-mentioned GN strain using Bacterial Genomic DNA Purif. Kit (manufactured by MS Technosystems Co., Ltd.) and PCR was performed using the obtained chromosomal DNA as a template and oligonucleotides of SEQ ID NOS: 1 and 2 as primers. PCR was performed using Pyrobest polymerase (available from Takara Bio) according to the program of 30 cycles of denaturation at 98.degree. C. for 10 seconds, annealing at 50.degree. C. for 30 seconds, and elongation at 72.degree. C. for 3 minutes to amplify a fragment of about 2.75 kb. The primers contain a BamHI recognition sequence at the 5'-end and are designed to amplify the region of nucleotide numbers 1521 to 4270 of the sequence of GenBank accession No. D84102. The amplified fragment was digested with BamHI and ligated to pBS4S vector digested with BamHI (Ligation kit Ver. 2, using a product available from Takara Bio), and thereby plasmid pBSOAGN was obtained (FIG. 3 shows the construction procedure).

[0181] pBSOAGN was introduced into C. glutamicum ATCC13869 strain by an electric pulse method (JP02-207791A) and the obtained bacterial cells were applied to CM-Dex agar medium (5 g/l glucose, 10 g/l polypeptone, 10 g/l yeast extract, 1 g/l KH.sub.2PO.sub.4, 0.4 g/l MgSO.sub.4.7H.sub.2O, 0.01 g/l FeSO.sub.4.7H.sub.2O, 0.01 g/l MnSO.sub.4.4-5H.sub.2O, 3 g/l urea, 1.2 g/l soybean protein hydrolysate, and 20 g/l agar, pH adjusted to 7.5) containing 25 .mu.g/ml of kanamycin. After culturing at 25.degree. C., it was confirmed by using PCR that the colonies which appeared were once recombinant strains in which pBSOAGN was incorporated by homologous recombination on the chromosome. The PCR was performed using the chromosomal DNA of a candidate strain as template and an oligonucleotide having a nucleotide sequence specific to the sequence of pBS4S (SEQ ID NO: 3) and an oligonucleotide having a nucleotide sequence specific to the sequence on the chromosome (SEQ ID NO: 4) as primers. That is, since the sequence of pBS4S is absent on the chromosome of a non-recombinant strain, no fragment is amplified by PCR if the candidate strain is not a recombinant strain. The obtained once recombinant strains were cultured at 25.degree. C. for one day in CM-Dex liquid medium containing 25 .mu.g/ml kanamycin and the obtained culture was diluted appropriately and applied onto S10 plate which has a composition of the above-mentioned CM-Dex medium whereby 5 g/l glucose is replaced by 10 g/l of sucrose. Several strains that grew on the S10 plate and showed kanamycin sensitivity were selected, and then the nucleotide sequence of the odhA sequence was confirmed by the method of Sanger (J. Mol. Biol., 143, 161 (1980)). The nucleotide sequence was analyzed by genetic Analyzer ABI310 (manufactured by Applied Biosystems) using BigDye terminator sequencing kit (manufactured by Applied Biyosystems). The thus obtained strain carrying the GN-type mutant odhA gene was named ATCC13869 OAGN.

[0182] <3> Introduction of the 2-2 Type Mutant odhA Gene into C. Glutamicum ATCC13869 Strain

[0183] Analysis of the nucleotide sequence of the L-glutamic acid-producing "2-2" strain which the inventors of the present invention had succeeded in breeding revealed that the strain contains deletions of the nucleotides 1094 to 1098 and replacement of "ag" at 1110 to 1111 with "ggcc" in the odhA gene (SEQ ID NO: 9) as shown in Table 2. In Table 2, amino acid sequence of mutant E1o subunit encoded by the mutant odhA gene is also shown. TABLE-US-00002 TABLE 2 Strain Nucleotide sequence of odhA gene ATCC13869 AAC TCC TAC GAC GTC ATC GAC GGC AAG CCA ACC CTG OA2-2 AAC TCC TAC --- CAT CGA CGG CAG GCC CCA ACC CTG Strain Amino acid sequence of Elo subunit ATCC13869 Asn Ser Tyr Asp Val Ile Asp Gly Lys Pro Thr Leu OA2-2 Asn Ser Tyr --- His Arg Arg Gln Ala Pro Thr Leu

[0184] Then, this mutant odhA gene was introduced into C. glutamicum 2256 strain (ATCC13869) and evaluated. At first, a plasmid for introducing these mutations into C. glutamicum 2256 was prepared. A chromosomal DNA was isolated from the 2-2 strain using Bacterial Genomic DNA Purif. Kit (manufactured by MS Technosystems Co., Ltd.) and PCR was performed using this chromosomal DNA as a template and oligonucleotides of SEQ ID NOS: 5 and 6 as primers. PCR was performed using TaKaRa Ex Taq (available from Takara Bio) according to the program of 25 cycles of denaturation at 94.degree. C. for 30 seconds, annealing at 55.degree. C. for 10 seconds, and elongation at 72.degree. C. for 2 minutes to amplify a fragment of about 2.0 kb. The primers contain a BamHI recognition sequence at the 5'-end and designed to amplify the region of nucleotides 51 to 2150 of the nucleotide sequence of GenBank accession No. D84102. The amplified fragment was digested with BamHI and ligated to pBS4S vector digested with BamHI using Ligation kit Ver. 2 of Takara Bio, and thereby the plasmid pBSOA2-2 was obtained (FIG. 4 shows the construction diagram). The same procedure described in Example 1<2> was performed to obtain a strain carrying the 2-2 type mutant odhA gene (ATCC13869 OA2-2 strain).

[0185] <4> Introduction of 2-2 Type Mutation into GN Type odhA Gene of ATCC13869 OAGN Strain

[0186] According to the same procedures as described in Example 1<2>, the plasmid pBSOA2-2 constructed in Example 1<3> was introduced into ATCC13869 OAGN strain prepared in Example 1<2> to obtain ATCC13869 strain carrying both the GN type and 2-2 type mutations in odhA gene. Hereinafter, a double mutation consisting of 2-2 type mutation and GN type mutation is also called GN2-2 mutation.

[0187] Although the mutant strains were prepared using mutant odhA genes amplified by PCR using a chromosomal DNA from the GN strain or 2-2 strain as a template in Example 1<2> to <4>, they can also be prepared by using mutant odhA genes obtained by site-directed mutagenesis technique such as those using Mutan-Super Express Km kit (Takara Bio). For example, a plasmid having a similar structure to pBSOAGN prepared in Example 1<2> can be obtained as follows. That is, an odhA gene fragment is prepared by PCR using synthetic DNAs of SEQ ID NOS: 2 and 5 as primers and a chromosomal DNA of a wild-type odhA gene as a template, and the resultant PCR fragment is cloned into the BamHI recognition site of plasmid pKF19k attached to Mutan-Super Express Km kit. Next, another PCR is performed using a template of the obtained plasmid and primers of a synthetic DNA of SEQ ID NO: 7 having phosphorylated 5'-end and the selection primer attached to Mutan-Super Express Km kit. Transformation of sup.sup.0 E. coli, for example, MV1184 strain (available from Takara Bio) with the obtained PCR product results in construction of a plasmid containing the mutant odhA gene fragment. Finally, the fragment is digested with BamHI and inserted into the pBS4S vector, and thereby a plasmid similar to pBSOAGN can be constructed.

[0188] Similarly, to obtain odhA gene containing the 2-2 type mutation, a plasmid similar to pBSOA2-2 can be constructed by using the synthetic DNA of SEQ ID NO: 8 having phosphorylated 5'-end instead of the synthetic DNA of SEQ ID NO: 7 having phosphorylated 5'-end in the procedure as described above.

[0189] Furthermore, to obtain odhA gene containing GN2-2 double mutations, a fragment containing the GN-type mutation is excised or PCR-amplified from the above-described plasmid similar to pBSOAGN and used to replace the corresponding fragment on the above-described plasmid similar to pBSOA2-2.

Example 2

[0190] Comparison of the Ability of Strains ATCC13869 OAGN, OA2-2, and OAGN2-2 to Degrade Glutamic Acid

[0191] While strains carrying a wild-type odhA gene can assimilate L-glutamic acid in a medium, the strains in which the activity of .alpha.-KGDH is weakened or eliminated due to the odhA mutation is presumed to also have a decreased ability to degrade glutamic acid. Then, the ability to degrade glutamic acid was determined using each of the odhA mutant strains ATCC13869 OAGN, OA2-2, and OAGN2-2 prepared in Example 1<2> to <4>. Each strain was cultured on a CM-Dex plate for one day at 25.degree. C. and then inoculated into a liquid medium composed of 20 g/l sodium glutamate, 2.64 g/l (NH.sub.4).sub.2SO.sub.4, 0.5 g/l KH.sub.2PO.sub.4, 0.5 g/l K.sub.2HPO.sub.4, 0.25 g/l MgSO.sub.4.7H.sub.2O, 0.01 g/l FeSO.sub.4.7H.sub.2O, 0.01 g/l MnSO.sub.4.4-5H.sub.2O, 0.01 g/l CaCl.sub.2, 0.02 mg/l CuSO.sub.4, 40 g/l MOPS, 0.03 g/l protocatechinic acid, 200 .mu.g/l vitamin B1, and 300 .mu.g/l biotin (adjusted to pH 6.7 with NaOH), followed by culturing at 25.degree. C. and 34.degree. C. for 50 hours. The amounts of glutamic acid at the starting point, and after 25 hours and 50 hours of the culture were measured, respectively and the amounts of degraded glutamic acid were compared between the strains cultured at 25.degree. C. and 34.degree. C. Table 3 shows the results. In particular, the GN2-2 mutant strain exhibited a significant decrease in the amount of degraded glutamic acid, especially when the culture temperature was 34.degree. C. These results suggest that introduction of the GN2-2 mutation can efficiently reduce the .alpha.-KGDH activity and a strain having this mutation is preferably used in L-glutamic acid production. TABLE-US-00003 TABLE 3 Amount of degraded glutamic acid 25 Hours 50 Hours Strains 25.degree. C. 34.degree. C. 25.degree. C. 34.degree. C. ATCC13869 15 15 15.4 15.4 OAGN 3.8 5.8 9.4 10.0 OA2-2 11.7 15.1 15.4 15.4 OAGN2-2 0.7 0.5 4.9 1.0 (Unit: g/l)

Example 3

[0192] Comparison of the .alpha.-KGDH Activity of ATCC13869 OAGN, OA2-2, and OAGN2-2 Strains

[0193] The .alpha.-KGDH activity of the strains ATCC13869 OAGN, OA2-2, and OAGN2-2 was measured using the culture broth collected after 4 hours from the start of the culture in Example 4 as described below. The activity was measured according to the method described in Agric. Biol. Chem., 44(8), p 1897 (1980). Specifically, after bacterial cells were washed with 0.2% sodium chloride, they were suspended in a buffer solution of 100 mM TES-NaOH (pH 7.5) containing 30% glycerol. The bacterial cells were sonicated using Bioruptor (Olympus) and then centrifuged to remove non-ruptured bacterial cells, followed by gel filtration with the same buffer using Sephadex-G25 (Amersham Pharmacia). The thus obtained preparation was used as a crude enzyme solution. The crude enzyme solution was added to a reaction system containing 100 mM TES-NaOH (pH 7.7), 5 mM MgCl.sub.2, 0.2 mM CoA, 0.3 mM cocarboxylase, 1 mM .alpha.-ketoglutaric acid, 3 mM L-cysteine, and 1 mM acetylpyridine-adenine-dinucleotide and absorption at 365 nm at 31.5.degree. C. was measured using Hitachi spectrophotometer U-2001. In the measurement of the protein concentration in the crude enzyme solution, protein Assay (Bio-Rad) was used. Bovine serum albumin was used as a standard protein.

[0194] Table 4 shows the results of the measurement of the .alpha.-KGDH activity. Introduction of the GN type mutation, 2-2 type mutation, and GN2-2 type mutation leads to a decrease in the .alpha.-KGDH as compared to ATCC13869. In particular, in the case of GN2-2 type mutation-introduced strain, a considerable decrease in the activity was observed. This indicates that the GN type mutation, 2-2 type mutation, and GN2-2 type mutation are mutations that reduce the .alpha.-KGDH activity. TABLE-US-00004 TABLE 4 .alpha.-KGDH activity Strains Culture temperature 25.degree. C. Culture temperature 34.degree. C. ATCC13869 0.036 0.021 OAGN 0.001 0.002 OA2-2 0.007 0.009 OAGN2-2 0.001> 0.001> (Unit: .DELTA.Abs/min/mg protein)

Example 4

[0195] Comparison of L-Glutamic Acid-Producing Ability of the Strains ATCC13869 OAGN, OA2-2, and OAGN2-2

[0196] The L-glutamic acid-producing ability of the strains ATCC13869 OAGN, OA2-2, and OAGN2-2 were examined in a jar fermenter culture. First, the above-mentioned four strains were cultured on a CM-Dex agar medium at 25.degree. C. for one day and the obtained bacterial cells were inoculated in 300 ml of a sterilized seed medium containing 60 g/l glucose, 1.54 g/l H.sub.3PO.sub.4, 1.45 g/l KOH, 0.9 g/l MgSO.sub.4.7H.sub.2O, 0.01 g/l FeSO.sub.4.7H.sub.2O, 670 .mu.g/l vitamin B1, 3,200 .mu.g/l biotin, 0.28 g/l DL-Met, 1.54 g/l soybean protein hydrolysate, and 0.1 ml/l defoaming agent AZ-20R, and cultured until the sugar was completely consumed. During the culture, the medium was stirred with aeration of 1/1 VVM so that the concentration of dissolved oxygen was maintained not less than 5%. The pH during the culture was controlled to pH 7.2 with ammonia gas. Then, 30 ml of the obtained seed culture was inoculated in 270 ml of a main culture medium containing 80 g/l glucose, 3.46 g/l KH.sub.2PO.sub.4, 1.0 g/l MgSO.sub.4.7H.sub.2O, 0.01 g/l FeSO.sub.4.7H.sub.2O, 0.01 g/l MnSO.sub.4.4-5H.sub.2O, 230 .mu.g/l vitamin B1, 525 .mu.g/l biotin, 0.35 g/l soybean protein hydrolysate, and 0.2 ml/l defoaming agent AZ-20R, and cultured at 25.degree. C. or 34.degree. C. During the culture, aeration was performed as described above. The pH during the culturing was controlled at pH 7.3 with ammonia gas.

[0197] Table 5 shows amount of accumulated L-glutamic acid after about 7.5 hours from the start of the culture. FIGS. 5, 6, and 7 show time courses of L-glutamic acid accumulation, bacterial cell amount, and residual sugar, respectively. ATCC13869 strain did not accumulate L-glutamic acid, whereas OAGN and OAGN2-2 mutant strains accumulated L-glutamic acid. In particular, when these strains were cultured at 34.degree. C., the amounts of accumulated L-glutamic acid significantly increased. Each mutation-introduced strain showed almost the same growth rate as the wild-type strain.

[0198] From these results, it was confirmed that the GN type mutation, 2-2 type mutation, and GN2-2 type mutation are effective to increase L-glutamic acid production. Among these mutations, GN2-2 type mutation was found to have the most significant effect on the L-glutamic acid production. TABLE-US-00005 TABLE 5 Amount of produced L-glutamic acid (Glu) of odhA mutation-introduced strains 25.degree. C. 34.degree. C. Strains Glu (g/L) Glu (g/L) ATCC13869 0.24 0.13 OAGN 0.18 1.88 OA2-2 0.59 4.70 OAGN2-2 0.38 5.13

Example 5

[0199] Screening of odhA Mutant Strains Using a yggB Mutant Strain

[0200] <Construction of L30 Type yggB Mutant Strain>

[0201] At first, a mutant strain having a mutation in the yggB gene was constructed from ATCC13869 strain. The L30 type mutation is a mutation which replaces "C" at position 1768 with "T" in the yggB gene (SEQ ID NO: 29). The mutant yggB gene having the L30 type mutation is shown in SEQ ID NO: 31 and the amino acid sequence encoded by the gene is shown in SEQ ID NO: 32. The mutant yggB gene was constructed by the same method as in Example 1. That is, a fragment encoding the N-terminus portion of the yggB gene was prepared by PCR using primers of SEQ ID NOS: 33 and 34 and a template of chromosomal DNA of the ATCC13869 strain. In a similar way, a fragment encoding the C-terminus portion of the yggB gene was prepared by PCR using primers of SEQ ID NOS: 35 and 36 and a template of chromosomal DNA of the ATCC13869 strain. Subsequently, a fragment of the yggB gene including the L30 type mutation was obtained by PCR using primers of SEQ ID NOS: 37 and 35 and a template of a mixture of equal amounts of the N-terminus fragment and C-terminus fragment. The obtained PCR product is digested by SacI and ligated to SacI-digested pBS4S, and thereby the plasmid for introducing the mutation is obtained (pBS4 yggB-L). The obtained pBS4 yggB-L was integrated into the chromosome of the ATCC13869 strain and then cured from the strain according to a similar method as in Example 1. The nucleotide sequence of yggB gene of the obtained kanamycin-resistant strain is determined and the strain in which yggB gene is replaced with L30 type was selected. The strain having yggB gene of SEQ ID NO: 31 was named ATCC13869-L strain. This strain can be used in the screening of odhA mutant genes.

[0202] <Construction of the yggB, odhA Double Mutant Strain>

[0203] Then, each of the mutations shown in Table 6 was introduced into the chromosomal odhA gene of ATCC13869-L strain. In Table 6, nucleotide sequences of the region corresponding to nucleotides 2528 to 2562 of SEQ ID NO: 9 of each strain are shown. In Table 7, amino acid sequences of the region corresponding to amino acids 696 to 707 of SEQ ID NO: 10 of each strain are shown.

[0204] The L30sucA8 strain in which odhA gene having nucleotide sequence of SEQ ID NO: 42 is introduced can be obtained as follows. The mutant odhA gene fragment is prepared by PCR using primers of SEQ ID NOS: 2 and 5. The obtained fragment is digested with BamHI and ligated to the BamHI site of plasmid pKF19m which is attached to Mutan-Super Express Km (Takara Bio). Then, PCR is performed using a primer of SEQ ID NO: 38 having a phosphorylated 5'-end and the selection primer of Mutan-Super Express Km, and the obtained PCR product is used to transform sup0-E. coli strain such as MV1184 strain to obtain a plasmid containing the mutant odhA fragment. This fragment is inserted into the pBS4S plasmid and the obtained plasmid is used to transform ATCC13869-L strain according to a similar method as in Example 1 to thereby obtain a strain in which the plasmid is integrated into its chromosome. Then, a strain which is resistant to sucrose and sensitive to kanamycin is selected from these strains. The nucleotide sequence of odhA gene of the selected strains is determined and the strain in which function of .alpha.-KGDH is deficient by frameshift mutation in odhA gene is selected as ATCC13869-L30sucA8 (odhA8) strain. The other odhA mutant strains can be obtained by the similar procedures using the yggB mutant strain.

[0205] sucA801 strain in which a mutant odhA gene having a nucleotide sequence of SEQ ID NO: 44 is introduced can be obtained by a similar method as described above in which a primer of SEQ ID NO: 39 having a phosphorylated 5'-end is used instead of a primer of SEQ ID NO: 38.

[0206] sucA805 strain in which a mutant odhA gene having a nucleotide sequence of SEQ ID NO: 46 is introduced can be obtained by a similar method as described above in which a primer of SEQ ID NO: 40 having a phosphorylated 5'-end is used instead of a primer of SEQ ID NO: 38.

[0207] sucA77 strain in which a mutant odhA gene having a nucleotide sequence of SEQ ID NO: 48 is introduced can be obtained by a similar method as described above in which a primer of SEQ ID NO: 41 having a phosphorylated 5'-end is used instead of a primer of SEQ ID NO: 38.

[0208] The L30sucA8 strain does not have intracellular .alpha.-KGDH because the sucA8 mutation is a frame-shift mutation which causes immature truncation of .alpha.-KGDH protein. On the other hand, sucA801 strain, sucA805 strain, and sucA77 strain have decreased but some .alpha.-KGDH activity because these mutations are not frame-shift mutations and do not cause immature truncation of .alpha.-KGDH protein. TABLE-US-00006 TABLE 6 partial nucleotide acid sequence of the odhA mutant genes Strains Nucleotide sequence of the odhA gene ATCC13869-L CTG GCT AAG CTG CGT GGC TAC GAC GTC GGA GGC ACC L30sucA8 CTG GCT AAG CTG CGT C GAC GTC GGA GGC ACC L30sucA801 CTG GCT AAG CTG CGT CTC GAC GTC GGA GGC ACC L30sucA805 CTG GCT AAA AGC TGC GTC GAC GTC GGA GGC ACC L30sucA77 CTG GCT ATA AGC TGC GTC GAC GTC GGA GGC ACC

[0209] TABLE-US-00007 TABLE 7 amino acid sequence of the odhA mutants Strains Amino acid sequence of the Elo subunit Wild Leu Ala Lys Leu Arg Gly Tyr Asp Val Gly Gly Thr L30sucA8 (sucA) Leu Ala Lys Leu Arg Arg Arg Arg Arg His L30sucA801 Leu Ala Lys Leu Arg Leu Asp Val Gly Gly Thr L30sucA805 Leu Ala Lys Ser Cys Val Asp Val Gly Gly Thr L30sucA77 Leu Ala Ile Ser Cys Val Asp Val Gly Gly Thr

[0210] <L-Glutamic Acid Production Using Strains Carrying each of the Mutant odhA Genes>

[0211] L-glutamic acid productivity of the obtained odhA mutant strains was evaluated by culturing these strains in Sakaguchi flask. Each of the strains listed in Table 6 was cultured at 31.5.degree. C. overnight on CM-Dex agar medium, and then 1/6 of the culture was transferred to 20 ml of a medium containing 60 g/l glucose, 22.5 g/l (NH.sub.4).sub.2SO.sub.4, 1 g/l KH.sub.2PO.sub.4, 0.4 g/l MgSO.sub.4.7H.sub.2O, 0.01 g/l FeSO.sub.4.7H.sub.2O, 0.01 g/l MnSO.sub.4.4-5H.sub.2O, 200 .mu.g/l vitamin B1, 0.48 g/l soybean protein hydrolysate, and 300 .mu.g/l biotin (adjusted to pH 8.0 with KOH), added with CaCO.sub.3 and cultured with stirring at 115 rpm at 31.5.degree. C. The amount of accumulated L-glutamic acid after 19 hours of culture was shown in Table 8. The sucA801, sucA805, and sucA77 strains exhibited higher L-glutamic acid productivity than the ATCC13869-L strain carrying a wild-type odhA gene and the sucA8 strain carrying odhA gene with a frame-shift mutation. These results showed that L-glutamic acid is efficiently produced by regulating KGDH activity by introducing mutations into the proximate of thiamine pyrophosphate binding region of the odhA gene. TABLE-US-00008 TABLE 8 L-glutamic acid production by odhA mutant strains Strain L-glutamic acid (g/L) ATCC13869-L 4.9 L30sucA8 19.8 L30sucA801 22.1 L30sucA805 23.8 L30sucA77 21.6

[0212] While the invention has been described in detail with reference to preferred embodiments thereof, it will be apparent to one skilled in the art that various changes can be made, and equivalents employed, without departing from the scope of the invention. Each of the aforementioned documents, including the foreign priority document, JP2004-264458, is incorporated by reference herein in its entirety.

Sequence CWU 1

1

51 1 40 DNA Artificial sequence primer 1 gccgggatcc tccggtgaat tcctgcgtac catgtctcgc 40 2 40 DNA Artificial sequence primer 2 gccgggatcc ctgtgtgatt cacactgcat aaggccctct 40 3 24 DNA Artificial sequence primer 3 gcttccggct cgtatgttgt gtgg 24 4 20 DNA Artificial sequence primer 4 gatcgtgacc gcacagattc 20 5 40 DNA Artificial sequence primer 5 gccgggatcc ccatcgccgc catccctgat ggtttcaatc 40 6 40 DNA Artificial sequence primer 6 gccgggatcc ggccctggcc tgcggcggtg tcgatggcgg 40 7 33 DNA Artificial sequence primer 7 gctaagcgcg tcgacgtcgg aggcaccatc cac 33 8 42 DNA Artificial sequence primer 8 ctcctaccat cgacggcagg ccccaaccct gatcgtgcct ga 42 9 4394 DNA Corynebacterium glutamicum CDS (443)..(4213) 9 gtcgacaagc aaaatcgaag cggcagcacg ccgcgtcgga gccttaaacg ccatcgccgc 60 catccctgat ggtttcaatc atcaagtcgg tgaacgcggg cgcaacctgt catccggaca 120 gcgccaactg atcgcgctgg cgcgcgccga actcatcgag ccttccatca tgcttctcga 180 cgaagccacc tccaccctcg accccgccac cgaagccgtt atcctcaacg cctccgatcg 240 agtcactaag ggacgcacca gcatcatcgt cgcgcaccgc ttggcaaccg ctaaaagggc 300 cgaccgtatt cttgttgttg aacaaggacg tatcattgag gacggatctc acgacgcgtt 360 gttgtctgct aacggcacct acgcccgcat gtggcattta atggcctgac acgttatttt 420 taggagaact gtcaacaaat ta atg cta caa ctg ggg ctt agg cat aat cag 472 Met Leu Gln Leu Gly Leu Arg His Asn Gln 1 5 10 cca acg acc aac gtt aca gtg gat aaa ata aag ctc aat aaa ccc tca 520 Pro Thr Thr Asn Val Thr Val Asp Lys Ile Lys Leu Asn Lys Pro Ser 15 20 25 aga agc aag gaa aag agg cga gta cct gcc gtg agc agc gct agt act 568 Arg Ser Lys Glu Lys Arg Arg Val Pro Ala Val Ser Ser Ala Ser Thr 30 35 40 ttc ggc cag aat gcg tgg ctg gta gac gag atg ttc cag cag ttc cag 616 Phe Gly Gln Asn Ala Trp Leu Val Asp Glu Met Phe Gln Gln Phe Gln 45 50 55 aag gac ccc aag tcc gtg gac aag gaa tgg aga gaa ctc ttt gag gcg 664 Lys Asp Pro Lys Ser Val Asp Lys Glu Trp Arg Glu Leu Phe Glu Ala 60 65 70 cag ggg gga cca aat gct acc ccc gct aca aca gaa gca cag cct tca 712 Gln Gly Gly Pro Asn Ala Thr Pro Ala Thr Thr Glu Ala Gln Pro Ser 75 80 85 90 gcg ccc aag gag tct gcg aaa cca gca cca aag gct gcc cct gca gcc 760 Ala Pro Lys Glu Ser Ala Lys Pro Ala Pro Lys Ala Ala Pro Ala Ala 95 100 105 aag gca gca ccg cgc gta gaa acc aag ccg gcc gcc aag acc gcc cct 808 Lys Ala Ala Pro Arg Val Glu Thr Lys Pro Ala Ala Lys Thr Ala Pro 110 115 120 aag gcc aag gag tcc tca gtg cca cag caa cct aag ctt ccg gag cca 856 Lys Ala Lys Glu Ser Ser Val Pro Gln Gln Pro Lys Leu Pro Glu Pro 125 130 135 gga caa acc cca atc agg ggt att ttc aag tcc atc gcg aag aac atg 904 Gly Gln Thr Pro Ile Arg Gly Ile Phe Lys Ser Ile Ala Lys Asn Met 140 145 150 gat atc tcc ctg gaa atc cca acc gca acc tcg gtt cgc gat atg cca 952 Asp Ile Ser Leu Glu Ile Pro Thr Ala Thr Ser Val Arg Asp Met Pro 155 160 165 170 gct cgc ctc atg ttc gaa aac cgc gcg atg gtc aac gat cag ctc aag 1000 Ala Arg Leu Met Phe Glu Asn Arg Ala Met Val Asn Asp Gln Leu Lys 175 180 185 cgc acc cgc ggt ggc aag atc tcc ttc acc cac atc att ggc tac gcc 1048 Arg Thr Arg Gly Gly Lys Ile Ser Phe Thr His Ile Ile Gly Tyr Ala 190 195 200 atg gtg aag gca gtc atg gct cac ccg gac atg aac aac tcc tac gac 1096 Met Val Lys Ala Val Met Ala His Pro Asp Met Asn Asn Ser Tyr Asp 205 210 215 gtc atc gac ggc aag cca acc ctg atc gtg cct gag cac atc aac ctg 1144 Val Ile Asp Gly Lys Pro Thr Leu Ile Val Pro Glu His Ile Asn Leu 220 225 230 ggc ctt gcc atc gac ctt cct cag aag gac ggc tcc cgc gca ctt gtc 1192 Gly Leu Ala Ile Asp Leu Pro Gln Lys Asp Gly Ser Arg Ala Leu Val 235 240 245 250 gta gca gcc atc aag gaa acc gag aag atg aac ttc tcc gag ttc ctc 1240 Val Ala Ala Ile Lys Glu Thr Glu Lys Met Asn Phe Ser Glu Phe Leu 255 260 265 gca gca tac gaa gac atc gtg aca cgc tcc cgc aag ggc aag ctc acc 1288 Ala Ala Tyr Glu Asp Ile Val Thr Arg Ser Arg Lys Gly Lys Leu Thr 270 275 280 atg gat gac tac cag ggc gtt acc gtt tcc ttg acc aac cca ggt ggc 1336 Met Asp Asp Tyr Gln Gly Val Thr Val Ser Leu Thr Asn Pro Gly Gly 285 290 295 atc ggt acc cgc cac tct gtc cca cgt ctg acc aag ggc cag ggc acc 1384 Ile Gly Thr Arg His Ser Val Pro Arg Leu Thr Lys Gly Gln Gly Thr 300 305 310 atc atc ggt gtc ggt tcc atg gat tac cca gca gag ttc cag ggc gct 1432 Ile Ile Gly Val Gly Ser Met Asp Tyr Pro Ala Glu Phe Gln Gly Ala 315 320 325 330 tcc gaa gac cgc ctt gca gag ctc ggc gtt gga aag ctt gtc acc atc 1480 Ser Glu Asp Arg Leu Ala Glu Leu Gly Val Gly Lys Leu Val Thr Ile 335 340 345 acc tcc acc tac gat cac cgc gtg atc cag ggt gct gtg tcc ggt gaa 1528 Thr Ser Thr Tyr Asp His Arg Val Ile Gln Gly Ala Val Ser Gly Glu 350 355 360 ttc ctg cgt acc atg tct cgc ctg ctc acc gat gat tcc ttc tgg gat 1576 Phe Leu Arg Thr Met Ser Arg Leu Leu Thr Asp Asp Ser Phe Trp Asp 365 370 375 gag atc ttc gac gca atg aac gtt cct tac acc cca atg cgt tgg gca 1624 Glu Ile Phe Asp Ala Met Asn Val Pro Tyr Thr Pro Met Arg Trp Ala 380 385 390 cag gac gtt cca aac acc ggt gtt gat aag aac acc cgc gtc atg cag 1672 Gln Asp Val Pro Asn Thr Gly Val Asp Lys Asn Thr Arg Val Met Gln 395 400 405 410 ctc att gag gca tac cgc tcc cgt gga cac ctc atc gct gac acc aac 1720 Leu Ile Glu Ala Tyr Arg Ser Arg Gly His Leu Ile Ala Asp Thr Asn 415 420 425 cca ctt tca tgg gtt cag cct ggc atg cca gtt cca gac cac cgc gac 1768 Pro Leu Ser Trp Val Gln Pro Gly Met Pro Val Pro Asp His Arg Asp 430 435 440 ctc gac atc gag acc cac agc ctg acc atc tgg gat ctg gac cgt acc 1816 Leu Asp Ile Glu Thr His Ser Leu Thr Ile Trp Asp Leu Asp Arg Thr 445 450 455 ttc agc gtc ggt ggc ttc ggc ggc aag gag acc atg acc ctg cgc gag 1864 Phe Ser Val Gly Gly Phe Gly Gly Lys Glu Thr Met Thr Leu Arg Glu 460 465 470 gta ctg tcc cgc ctg cgc gct gcc tac acc ttg aag gtc ggc tcc gaa 1912 Val Leu Ser Arg Leu Arg Ala Ala Tyr Thr Leu Lys Val Gly Ser Glu 475 480 485 490 tac acc cac atc ctg gac cgc gac gag cgc acc tgg ctg cag gac cgc 1960 Tyr Thr His Ile Leu Asp Arg Asp Glu Arg Thr Trp Leu Gln Asp Arg 495 500 505 ctc gaa gcc gga atg cca aag cca acc cag gca gag cag aag tac atc 2008 Leu Glu Ala Gly Met Pro Lys Pro Thr Gln Ala Glu Gln Lys Tyr Ile 510 515 520 ctg cag aag ctg aac gcc gca gag gct ttc gag aac ttc ctg cag acc 2056 Leu Gln Lys Leu Asn Ala Ala Glu Ala Phe Glu Asn Phe Leu Gln Thr 525 530 535 aag tac gtc ggc cag aag cgc ttc tcc ctc gaa ggt gca gaa gct ctc 2104 Lys Tyr Val Gly Gln Lys Arg Phe Ser Leu Glu Gly Ala Glu Ala Leu 540 545 550 atc cca ctg atg gac tcc gcc atc gac acc gcc gca ggc cag ggc ctc 2152 Ile Pro Leu Met Asp Ser Ala Ile Asp Thr Ala Ala Gly Gln Gly Leu 555 560 565 570 gac gaa gtt gtc atc ggt atg cca cac cgt ggt cgc ctc aac gtg ctg 2200 Asp Glu Val Val Ile Gly Met Pro His Arg Gly Arg Leu Asn Val Leu 575 580 585 ttc aac atc gtg ggc aag cca ctg gca tcc atc ttc aac gag ttt gaa 2248 Phe Asn Ile Val Gly Lys Pro Leu Ala Ser Ile Phe Asn Glu Phe Glu 590 595 600 ggc caa atg gag cag ggc cag atc ggt ggc tcc ggt gac gtg aag tac 2296 Gly Gln Met Glu Gln Gly Gln Ile Gly Gly Ser Gly Asp Val Lys Tyr 605 610 615 cac ctc ggt tcc gaa ggc cag cac ctg cag atg ttc ggc gac ggc gag 2344 His Leu Gly Ser Glu Gly Gln His Leu Gln Met Phe Gly Asp Gly Glu 620 625 630 atc aag gtc tcc ctg act gct aac ccg tcc cac ctg gaa gct gtt aac 2392 Ile Lys Val Ser Leu Thr Ala Asn Pro Ser His Leu Glu Ala Val Asn 635 640 645 650 cca gtg atg gaa ggt atc gtc cgc gca aag cag gac tac ctg gac aag 2440 Pro Val Met Glu Gly Ile Val Arg Ala Lys Gln Asp Tyr Leu Asp Lys 655 660 665 ggc gta gac ggc aag act gtt gtg cca ctg ctg ctc cac ggt gac gct 2488 Gly Val Asp Gly Lys Thr Val Val Pro Leu Leu Leu His Gly Asp Ala 670 675 680 gca ttc gca ggc ctg ggc atc gtg cca gaa acc atc aac ctg gct aag 2536 Ala Phe Ala Gly Leu Gly Ile Val Pro Glu Thr Ile Asn Leu Ala Lys 685 690 695 ctg cgt ggc tac gac gtc gga ggc acc atc cac atc gtg gtg aac aac 2584 Leu Arg Gly Tyr Asp Val Gly Gly Thr Ile His Ile Val Val Asn Asn 700 705 710 cag atc ggc ttc acc acc acc cca gac tcc agc cgc tcc atg cac tac 2632 Gln Ile Gly Phe Thr Thr Thr Pro Asp Ser Ser Arg Ser Met His Tyr 715 720 725 730 gca acc gac tac gcc aag gca ttc ggc tgc cca gtc ttc cac gtc aat 2680 Ala Thr Asp Tyr Ala Lys Ala Phe Gly Cys Pro Val Phe His Val Asn 735 740 745 ggt gat gac cca gag gca gtt gtc tgg gtt ggc cag ctg gca acc gag 2728 Gly Asp Asp Pro Glu Ala Val Val Trp Val Gly Gln Leu Ala Thr Glu 750 755 760 tac cgt cgt cgc ttc ggc aag gac gtc ttc atc gac ctc gtt tgc tac 2776 Tyr Arg Arg Arg Phe Gly Lys Asp Val Phe Ile Asp Leu Val Cys Tyr 765 770 775 cgc ctc cgc ggc cac aac gaa gct gat gat cct tcc atg acc cag cca 2824 Arg Leu Arg Gly His Asn Glu Ala Asp Asp Pro Ser Met Thr Gln Pro 780 785 790 aag atg tat gag ctc atc acc ggc cgc gag acc gtt cgt gct cag tac 2872 Lys Met Tyr Glu Leu Ile Thr Gly Arg Glu Thr Val Arg Ala Gln Tyr 795 800 805 810 acc gaa gac ctg ctc gga cgt gga gac ctc tcc aac gaa gat gca gaa 2920 Thr Glu Asp Leu Leu Gly Arg Gly Asp Leu Ser Asn Glu Asp Ala Glu 815 820 825 gca gtc gtc cgc gac ttc cac gac cag atg gaa tct gtg ttc aac gaa 2968 Ala Val Val Arg Asp Phe His Asp Gln Met Glu Ser Val Phe Asn Glu 830 835 840 gtc aag gaa ggc ggc aag aag cag gct gag gca cag acc ggc atc acc 3016 Val Lys Glu Gly Gly Lys Lys Gln Ala Glu Ala Gln Thr Gly Ile Thr 845 850 855 ggc tcc cag aag ctt cca cac ggc ctt gag acc aac atc tcc cgt gaa 3064 Gly Ser Gln Lys Leu Pro His Gly Leu Glu Thr Asn Ile Ser Arg Glu 860 865 870 gag ctc ctg gaa ctg gga cag gct ttc gcc aac acc cca gaa ggc ttc 3112 Glu Leu Leu Glu Leu Gly Gln Ala Phe Ala Asn Thr Pro Glu Gly Phe 875 880 885 890 aac tac cac cca cgt gtg gct cca gtt gct aag aag cgc gtc tcc tct 3160 Asn Tyr His Pro Arg Val Ala Pro Val Ala Lys Lys Arg Val Ser Ser 895 900 905 gtc acc gaa ggt ggc atc gac tgg gca tgg ggc gag ctc ctc gcc ttc 3208 Val Thr Glu Gly Gly Ile Asp Trp Ala Trp Gly Glu Leu Leu Ala Phe 910 915 920 ggt tcc ctg gct aac tcc ggc cgc ttg gtt cgc ctt gca ggt gaa gat 3256 Gly Ser Leu Ala Asn Ser Gly Arg Leu Val Arg Leu Ala Gly Glu Asp 925 930 935 tcc cgc cgc ggt acc ttc acc cag cgc cac gca gtt gcc atc gac cca 3304 Ser Arg Arg Gly Thr Phe Thr Gln Arg His Ala Val Ala Ile Asp Pro 940 945 950 gcg acc gct gaa gag ttc aac cca ctc cac gag ctt gca cag tcc aag 3352 Ala Thr Ala Glu Glu Phe Asn Pro Leu His Glu Leu Ala Gln Ser Lys 955 960 965 970 ggc aac aac ggt aag ttc ctg gtc tac aac tcc gca ctg acc gag tac 3400 Gly Asn Asn Gly Lys Phe Leu Val Tyr Asn Ser Ala Leu Thr Glu Tyr 975 980 985 gca ggc atg ggc ttc gag tac ggc tac tcc gta gga aac gaa gac tcc 3448 Ala Gly Met Gly Phe Glu Tyr Gly Tyr Ser Val Gly Asn Glu Asp Ser 990 995 1000 gtc gtt gca tgg gaa gca cag ttc ggc gac ttc gcc aac ggc gct 3493 Val Val Ala Trp Glu Ala Gln Phe Gly Asp Phe Ala Asn Gly Ala 1005 1010 1015 cag acc atc atc gat gag tac gtc tcc tca ggc gaa gct aag tgg 3538 Gln Thr Ile Ile Asp Glu Tyr Val Ser Ser Gly Glu Ala Lys Trp 1020 1025 1030 ggc cag acc tcc aag ctg atc ctt ctg ctg cct cac ggc tac gaa 3583 Gly Gln Thr Ser Lys Leu Ile Leu Leu Leu Pro His Gly Tyr Glu 1035 1040 1045 ggc cag ggc cca gac cac tct tcc gca cgt atc gag cgc ttc ctg 3628 Gly Gln Gly Pro Asp His Ser Ser Ala Arg Ile Glu Arg Phe Leu 1050 1055 1060 cag ctg tgc gct gag ggt tcc atg act gtt gct cag cca tcc acc 3673 Gln Leu Cys Ala Glu Gly Ser Met Thr Val Ala Gln Pro Ser Thr 1065 1070 1075 cca gca aac cac ttc cac ctg ctg cgt cgt cac gct ctg tcc gac 3718 Pro Ala Asn His Phe His Leu Leu Arg Arg His Ala Leu Ser Asp 1080 1085 1090 ctg aag cgt cca ctg gtt atc ttc acc ccg aag tcc atg ctg cgt 3763 Leu Lys Arg Pro Leu Val Ile Phe Thr Pro Lys Ser Met Leu Arg 1095 1100 1105 aac aag gct gct gcc tcc gca cca gaa gac ttc act gag gtc acc 3808 Asn Lys Ala Ala Ala Ser Ala Pro Glu Asp Phe Thr Glu Val Thr 1110 1115 1120 aag ttc caa tcc gtg atc gac gat cca aac gtt gca gat gca gcc 3853 Lys Phe Gln Ser Val Ile Asp Asp Pro Asn Val Ala Asp Ala Ala 1125 1130 1135 aag gtg aag aag gtc atg ctg gtc tcc ggc aag ctg tac tac gaa 3898 Lys Val Lys Lys Val Met Leu Val Ser Gly Lys Leu Tyr Tyr Glu 1140 1145 1150 ttg gca aag cgc aag gag aag gac gga cgc gac gac atc gcg atc 3943 Leu Ala Lys Arg Lys Glu Lys Asp Gly Arg Asp Asp Ile Ala Ile 1155 1160 1165 gtt cgt atc gaa atg ctc cac cca att ccg ttc aac cgc atc tcc 3988 Val Arg Ile Glu Met Leu His Pro Ile Pro Phe Asn Arg Ile Ser 1170 1175 1180 gag gct ctt gcc ggc tac cct aac gct gag gaa gtc ctc ttc gtt 4033 Glu Ala Leu Ala Gly Tyr Pro Asn Ala Glu Glu Val Leu Phe Val 1185 1190 1195 cag gat gag cca gca aac cag ggc cca tgg ccg ttc tac cag gag 4078 Gln Asp Glu Pro Ala Asn Gln Gly Pro Trp Pro Phe Tyr Gln Glu 1200 1205 1210 cac ctc cca gag ctg atc ccg aac atg cca aag atg cgc cgc gtt 4123 His Leu Pro Glu Leu Ile Pro Asn Met Pro Lys Met Arg Arg Val 1215 1220 1225 tcc cgc cgc gct cag tcc tcc acc gca act ggt gtt gct aag gtg 4168 Ser Arg Arg Ala Gln Ser Ser Thr Ala Thr Gly Val Ala Lys Val 1230 1235 1240 cac cag ctg gag gag aag cag ctt atc gac gag gct ttc gag gct 4213 His Gln Leu Glu Glu Lys Gln Leu Ile Asp Glu Ala Phe Glu Ala 1245 1250 1255 taagtcttta tagtcctgca ctagcctaga gggccttatg cagtgtgaat cacacagcat 4273 aaggcccttt ttgctgccgt ggttgcctaa ggtggaaggc atgaaacgaa tctgtgcggt 4333 cacgatctct tcagtacttt tgctaagtgg ctgctcctcc acttccacca cgcagctcga 4393 g 4394 10 1257 PRT Corynebacterium glutamicum 10 Met Leu Gln Leu Gly Leu Arg His Asn Gln Pro Thr Thr Asn Val Thr 1 5 10 15 Val Asp Lys Ile Lys Leu Asn Lys Pro Ser Arg Ser Lys Glu Lys Arg 20 25 30 Arg Val Pro Ala Val Ser Ser Ala Ser Thr Phe Gly Gln Asn Ala Trp 35 40 45 Leu Val Asp Glu Met Phe Gln Gln Phe Gln Lys Asp Pro Lys Ser Val 50 55 60 Asp Lys Glu Trp Arg Glu Leu Phe Glu Ala Gln Gly Gly Pro Asn Ala 65 70 75 80 Thr Pro Ala Thr Thr Glu Ala Gln Pro Ser Ala Pro Lys Glu Ser Ala 85 90 95 Lys Pro Ala Pro Lys Ala Ala Pro Ala Ala Lys Ala Ala Pro Arg Val 100 105 110 Glu Thr Lys Pro Ala Ala Lys Thr Ala Pro Lys Ala Lys Glu Ser Ser 115 120 125 Val Pro Gln Gln Pro Lys Leu Pro Glu Pro Gly Gln Thr Pro Ile Arg 130 135 140 Gly Ile Phe Lys Ser Ile Ala Lys Asn Met Asp Ile

Ser Leu Glu Ile 145 150 155 160 Pro Thr Ala Thr Ser Val Arg Asp Met Pro Ala Arg Leu Met Phe Glu 165 170 175 Asn Arg Ala Met Val Asn Asp Gln Leu Lys Arg Thr Arg Gly Gly Lys 180 185 190 Ile Ser Phe Thr His Ile Ile Gly Tyr Ala Met Val Lys Ala Val Met 195 200 205 Ala His Pro Asp Met Asn Asn Ser Tyr Asp Val Ile Asp Gly Lys Pro 210 215 220 Thr Leu Ile Val Pro Glu His Ile Asn Leu Gly Leu Ala Ile Asp Leu 225 230 235 240 Pro Gln Lys Asp Gly Ser Arg Ala Leu Val Val Ala Ala Ile Lys Glu 245 250 255 Thr Glu Lys Met Asn Phe Ser Glu Phe Leu Ala Ala Tyr Glu Asp Ile 260 265 270 Val Thr Arg Ser Arg Lys Gly Lys Leu Thr Met Asp Asp Tyr Gln Gly 275 280 285 Val Thr Val Ser Leu Thr Asn Pro Gly Gly Ile Gly Thr Arg His Ser 290 295 300 Val Pro Arg Leu Thr Lys Gly Gln Gly Thr Ile Ile Gly Val Gly Ser 305 310 315 320 Met Asp Tyr Pro Ala Glu Phe Gln Gly Ala Ser Glu Asp Arg Leu Ala 325 330 335 Glu Leu Gly Val Gly Lys Leu Val Thr Ile Thr Ser Thr Tyr Asp His 340 345 350 Arg Val Ile Gln Gly Ala Val Ser Gly Glu Phe Leu Arg Thr Met Ser 355 360 365 Arg Leu Leu Thr Asp Asp Ser Phe Trp Asp Glu Ile Phe Asp Ala Met 370 375 380 Asn Val Pro Tyr Thr Pro Met Arg Trp Ala Gln Asp Val Pro Asn Thr 385 390 395 400 Gly Val Asp Lys Asn Thr Arg Val Met Gln Leu Ile Glu Ala Tyr Arg 405 410 415 Ser Arg Gly His Leu Ile Ala Asp Thr Asn Pro Leu Ser Trp Val Gln 420 425 430 Pro Gly Met Pro Val Pro Asp His Arg Asp Leu Asp Ile Glu Thr His 435 440 445 Ser Leu Thr Ile Trp Asp Leu Asp Arg Thr Phe Ser Val Gly Gly Phe 450 455 460 Gly Gly Lys Glu Thr Met Thr Leu Arg Glu Val Leu Ser Arg Leu Arg 465 470 475 480 Ala Ala Tyr Thr Leu Lys Val Gly Ser Glu Tyr Thr His Ile Leu Asp 485 490 495 Arg Asp Glu Arg Thr Trp Leu Gln Asp Arg Leu Glu Ala Gly Met Pro 500 505 510 Lys Pro Thr Gln Ala Glu Gln Lys Tyr Ile Leu Gln Lys Leu Asn Ala 515 520 525 Ala Glu Ala Phe Glu Asn Phe Leu Gln Thr Lys Tyr Val Gly Gln Lys 530 535 540 Arg Phe Ser Leu Glu Gly Ala Glu Ala Leu Ile Pro Leu Met Asp Ser 545 550 555 560 Ala Ile Asp Thr Ala Ala Gly Gln Gly Leu Asp Glu Val Val Ile Gly 565 570 575 Met Pro His Arg Gly Arg Leu Asn Val Leu Phe Asn Ile Val Gly Lys 580 585 590 Pro Leu Ala Ser Ile Phe Asn Glu Phe Glu Gly Gln Met Glu Gln Gly 595 600 605 Gln Ile Gly Gly Ser Gly Asp Val Lys Tyr His Leu Gly Ser Glu Gly 610 615 620 Gln His Leu Gln Met Phe Gly Asp Gly Glu Ile Lys Val Ser Leu Thr 625 630 635 640 Ala Asn Pro Ser His Leu Glu Ala Val Asn Pro Val Met Glu Gly Ile 645 650 655 Val Arg Ala Lys Gln Asp Tyr Leu Asp Lys Gly Val Asp Gly Lys Thr 660 665 670 Val Val Pro Leu Leu Leu His Gly Asp Ala Ala Phe Ala Gly Leu Gly 675 680 685 Ile Val Pro Glu Thr Ile Asn Leu Ala Lys Leu Arg Gly Tyr Asp Val 690 695 700 Gly Gly Thr Ile His Ile Val Val Asn Asn Gln Ile Gly Phe Thr Thr 705 710 715 720 Thr Pro Asp Ser Ser Arg Ser Met His Tyr Ala Thr Asp Tyr Ala Lys 725 730 735 Ala Phe Gly Cys Pro Val Phe His Val Asn Gly Asp Asp Pro Glu Ala 740 745 750 Val Val Trp Val Gly Gln Leu Ala Thr Glu Tyr Arg Arg Arg Phe Gly 755 760 765 Lys Asp Val Phe Ile Asp Leu Val Cys Tyr Arg Leu Arg Gly His Asn 770 775 780 Glu Ala Asp Asp Pro Ser Met Thr Gln Pro Lys Met Tyr Glu Leu Ile 785 790 795 800 Thr Gly Arg Glu Thr Val Arg Ala Gln Tyr Thr Glu Asp Leu Leu Gly 805 810 815 Arg Gly Asp Leu Ser Asn Glu Asp Ala Glu Ala Val Val Arg Asp Phe 820 825 830 His Asp Gln Met Glu Ser Val Phe Asn Glu Val Lys Glu Gly Gly Lys 835 840 845 Lys Gln Ala Glu Ala Gln Thr Gly Ile Thr Gly Ser Gln Lys Leu Pro 850 855 860 His Gly Leu Glu Thr Asn Ile Ser Arg Glu Glu Leu Leu Glu Leu Gly 865 870 875 880 Gln Ala Phe Ala Asn Thr Pro Glu Gly Phe Asn Tyr His Pro Arg Val 885 890 895 Ala Pro Val Ala Lys Lys Arg Val Ser Ser Val Thr Glu Gly Gly Ile 900 905 910 Asp Trp Ala Trp Gly Glu Leu Leu Ala Phe Gly Ser Leu Ala Asn Ser 915 920 925 Gly Arg Leu Val Arg Leu Ala Gly Glu Asp Ser Arg Arg Gly Thr Phe 930 935 940 Thr Gln Arg His Ala Val Ala Ile Asp Pro Ala Thr Ala Glu Glu Phe 945 950 955 960 Asn Pro Leu His Glu Leu Ala Gln Ser Lys Gly Asn Asn Gly Lys Phe 965 970 975 Leu Val Tyr Asn Ser Ala Leu Thr Glu Tyr Ala Gly Met Gly Phe Glu 980 985 990 Tyr Gly Tyr Ser Val Gly Asn Glu Asp Ser Val Val Ala Trp Glu Ala 995 1000 1005 Gln Phe Gly Asp Phe Ala Asn Gly Ala Gln Thr Ile Ile Asp Glu 1010 1015 1020 Tyr Val Ser Ser Gly Glu Ala Lys Trp Gly Gln Thr Ser Lys Leu 1025 1030 1035 Ile Leu Leu Leu Pro His Gly Tyr Glu Gly Gln Gly Pro Asp His 1040 1045 1050 Ser Ser Ala Arg Ile Glu Arg Phe Leu Gln Leu Cys Ala Glu Gly 1055 1060 1065 Ser Met Thr Val Ala Gln Pro Ser Thr Pro Ala Asn His Phe His 1070 1075 1080 Leu Leu Arg Arg His Ala Leu Ser Asp Leu Lys Arg Pro Leu Val 1085 1090 1095 Ile Phe Thr Pro Lys Ser Met Leu Arg Asn Lys Ala Ala Ala Ser 1100 1105 1110 Ala Pro Glu Asp Phe Thr Glu Val Thr Lys Phe Gln Ser Val Ile 1115 1120 1125 Asp Asp Pro Asn Val Ala Asp Ala Ala Lys Val Lys Lys Val Met 1130 1135 1140 Leu Val Ser Gly Lys Leu Tyr Tyr Glu Leu Ala Lys Arg Lys Glu 1145 1150 1155 Lys Asp Gly Arg Asp Asp Ile Ala Ile Val Arg Ile Glu Met Leu 1160 1165 1170 His Pro Ile Pro Phe Asn Arg Ile Ser Glu Ala Leu Ala Gly Tyr 1175 1180 1185 Pro Asn Ala Glu Glu Val Leu Phe Val Gln Asp Glu Pro Ala Asn 1190 1195 1200 Gln Gly Pro Trp Pro Phe Tyr Gln Glu His Leu Pro Glu Leu Ile 1205 1210 1215 Pro Asn Met Pro Lys Met Arg Arg Val Ser Arg Arg Ala Gln Ser 1220 1225 1230 Ser Thr Ala Thr Gly Val Ala Lys Val His Gln Leu Glu Glu Lys 1235 1240 1245 Gln Leu Ile Asp Glu Ala Phe Glu Ala 1250 1255 11 4391 DNA Corynebacterium glutamicum CDS (443)..(4213) 11 gtcgacaagc aaaatcgaag cggcagcacg ccgcgtcgga gccttaaacg ccatcgccgc 60 catccctgat ggtttcaatc atcaagtcgg tgaacgcggg cgcaacctgt catccggaca 120 gcgccaactg atcgcgctgg cgcgcgccga actcatcgag ccttccatca tgcttctcga 180 cgaagccacc tccaccctcg accccgccac cgaagccgtt atcctcaacg cctccgatcg 240 agtcactaag ggacgcacca gcatcatcgt cgcgcaccgc ttggcaaccg ctaaaagggc 300 cgaccgtatt cttgttgttg aacaaggacg tatcattgag gacggatctc acgacgcgtt 360 gttgtctgct aacggcacct acgcccgcat gtggcattta atggcctgac acgttatttt 420 taggagaact gtcaacaaat ta atg cta caa ctg ggg ctt agg cat aat cag 472 Met Leu Gln Leu Gly Leu Arg His Asn Gln 1 5 10 cca acg acc aac gtt aca gtg gat aaa ata aag ctc aat aaa ccc tca 520 Pro Thr Thr Asn Val Thr Val Asp Lys Ile Lys Leu Asn Lys Pro Ser 15 20 25 aga agc aag gaa aag agg cga gta cct gcc gtg agc agc gct agt act 568 Arg Ser Lys Glu Lys Arg Arg Val Pro Ala Val Ser Ser Ala Ser Thr 30 35 40 ttc ggc cag aat gcg tgg ctg gta gac gag atg ttc cag cag ttc cag 616 Phe Gly Gln Asn Ala Trp Leu Val Asp Glu Met Phe Gln Gln Phe Gln 45 50 55 aag gac ccc aag tcc gtg gac aag gaa tgg aga gaa ctc ttt gag gcg 664 Lys Asp Pro Lys Ser Val Asp Lys Glu Trp Arg Glu Leu Phe Glu Ala 60 65 70 cag ggg gga cca aat gct acc ccc gct aca aca gaa gca cag cct tca 712 Gln Gly Gly Pro Asn Ala Thr Pro Ala Thr Thr Glu Ala Gln Pro Ser 75 80 85 90 gcg ccc aag gag tct gcg aaa cca gca cca aag gct gcc cct gca gcc 760 Ala Pro Lys Glu Ser Ala Lys Pro Ala Pro Lys Ala Ala Pro Ala Ala 95 100 105 aag gca gca ccg cgc gta gaa acc aag ccg gcc gcc aag acc gcc cct 808 Lys Ala Ala Pro Arg Val Glu Thr Lys Pro Ala Ala Lys Thr Ala Pro 110 115 120 aag gcc aag gag tcc tca gtg cca cag caa cct aag ctt ccg gag cca 856 Lys Ala Lys Glu Ser Ser Val Pro Gln Gln Pro Lys Leu Pro Glu Pro 125 130 135 gga caa acc cca atc agg ggt att ttc aag tcc atc gcg aag aac atg 904 Gly Gln Thr Pro Ile Arg Gly Ile Phe Lys Ser Ile Ala Lys Asn Met 140 145 150 gat atc tcc ctg gaa atc cca acc gca acc tcg gtt cgc gat atg cca 952 Asp Ile Ser Leu Glu Ile Pro Thr Ala Thr Ser Val Arg Asp Met Pro 155 160 165 170 gct cgc ctc atg ttc gaa aac cgc gcg atg gtc aac gat cag ctc aag 1000 Ala Arg Leu Met Phe Glu Asn Arg Ala Met Val Asn Asp Gln Leu Lys 175 180 185 cgc acc cgc ggt ggc aag atc tcc ttc acc cac atc att ggc tac gcc 1048 Arg Thr Arg Gly Gly Lys Ile Ser Phe Thr His Ile Ile Gly Tyr Ala 190 195 200 atg gtg aag gca gtc atg gct cac ccg gac atg aac aac tcc tac cat 1096 Met Val Lys Ala Val Met Ala His Pro Asp Met Asn Asn Ser Tyr His 205 210 215 cga cgg cag gcc cca acc ctg atc gtg cct gag cac atc aac ctg ggc 1144 Arg Arg Gln Ala Pro Thr Leu Ile Val Pro Glu His Ile Asn Leu Gly 220 225 230 ctt gcc atc gac ctt cct cag aag gac ggc tcc cgc gca ctt gtc gta 1192 Leu Ala Ile Asp Leu Pro Gln Lys Asp Gly Ser Arg Ala Leu Val Val 235 240 245 250 gca gcc atc aag gaa acc gag aag atg aac ttc tcc gag ttc ctc gca 1240 Ala Ala Ile Lys Glu Thr Glu Lys Met Asn Phe Ser Glu Phe Leu Ala 255 260 265 gca tac gaa gac atc gtg aca cgc tcc cgc aag ggc aag ctc acc atg 1288 Ala Tyr Glu Asp Ile Val Thr Arg Ser Arg Lys Gly Lys Leu Thr Met 270 275 280 gat gac tac cag ggc gtt acc gtt tcc ttg acc aac cca ggt ggc atc 1336 Asp Asp Tyr Gln Gly Val Thr Val Ser Leu Thr Asn Pro Gly Gly Ile 285 290 295 ggt acc cgc cac tct gtc cca cgt ctg acc aag ggc cag ggc acc atc 1384 Gly Thr Arg His Ser Val Pro Arg Leu Thr Lys Gly Gln Gly Thr Ile 300 305 310 atc ggt gtc ggt tcc atg gat tac cca gca gag ttc cag ggc gct tcc 1432 Ile Gly Val Gly Ser Met Asp Tyr Pro Ala Glu Phe Gln Gly Ala Ser 315 320 325 330 gaa gac cgc ctt gca gag ctc ggc gtt gga aag ctt gtc acc atc acc 1480 Glu Asp Arg Leu Ala Glu Leu Gly Val Gly Lys Leu Val Thr Ile Thr 335 340 345 tcc acc tac gat cac cgc gtg atc cag ggt gct gtg tcc ggt gaa ttc 1528 Ser Thr Tyr Asp His Arg Val Ile Gln Gly Ala Val Ser Gly Glu Phe 350 355 360 ctg cgt acc atg tct cgc ctg ctc acc gat gat tcc ttc tgg gat gag 1576 Leu Arg Thr Met Ser Arg Leu Leu Thr Asp Asp Ser Phe Trp Asp Glu 365 370 375 atc ttc gac gca atg aac gtt cct tac acc cca atg cgt tgg gca cag 1624 Ile Phe Asp Ala Met Asn Val Pro Tyr Thr Pro Met Arg Trp Ala Gln 380 385 390 gac gtt cca aac acc ggt gtt gat aag aac acc cgc gtc atg cag ctc 1672 Asp Val Pro Asn Thr Gly Val Asp Lys Asn Thr Arg Val Met Gln Leu 395 400 405 410 att gag gca tac cgc tcc cgt gga cac ctc atc gct gac acc aac cca 1720 Ile Glu Ala Tyr Arg Ser Arg Gly His Leu Ile Ala Asp Thr Asn Pro 415 420 425 ctt tca tgg gtt cag cct ggc atg cca gtt cca gac cac cgc gac ctc 1768 Leu Ser Trp Val Gln Pro Gly Met Pro Val Pro Asp His Arg Asp Leu 430 435 440 gac atc gag acc cac agc ctg acc atc tgg gat ctg gac cgt acc ttc 1816 Asp Ile Glu Thr His Ser Leu Thr Ile Trp Asp Leu Asp Arg Thr Phe 445 450 455 agc gtc ggt ggc ttc ggc ggc aag gag acc atg acc ctg cgc gag gta 1864 Ser Val Gly Gly Phe Gly Gly Lys Glu Thr Met Thr Leu Arg Glu Val 460 465 470 ctg tcc cgc ctg cgc gct gcc tac acc ttg aag gtc ggc tcc gaa tac 1912 Leu Ser Arg Leu Arg Ala Ala Tyr Thr Leu Lys Val Gly Ser Glu Tyr 475 480 485 490 acc cac atc ctg gac cgc gac gag cgc acc tgg ctg cag gac cgc ctc 1960 Thr His Ile Leu Asp Arg Asp Glu Arg Thr Trp Leu Gln Asp Arg Leu 495 500 505 gaa gcc gga atg cca aag cca acc cag gca gag cag aag tac atc ctg 2008 Glu Ala Gly Met Pro Lys Pro Thr Gln Ala Glu Gln Lys Tyr Ile Leu 510 515 520 cag aag ctg aac gcc gca gag gct ttc gag aac ttc ctg cag acc aag 2056 Gln Lys Leu Asn Ala Ala Glu Ala Phe Glu Asn Phe Leu Gln Thr Lys 525 530 535 tac gtc ggc cag aag cgc ttc tcc ctc gaa ggt gca gaa gct ctc atc 2104 Tyr Val Gly Gln Lys Arg Phe Ser Leu Glu Gly Ala Glu Ala Leu Ile 540 545 550 cca ctg atg gac tcc gcc atc gac acc gcc gca ggc cag ggc ctc gac 2152 Pro Leu Met Asp Ser Ala Ile Asp Thr Ala Ala Gly Gln Gly Leu Asp 555 560 565 570 gaa gtt gtc atc ggt atg cca cac cgt ggt cgc ctc aac gtg ctg ttc 2200 Glu Val Val Ile Gly Met Pro His Arg Gly Arg Leu Asn Val Leu Phe 575 580 585 aac atc gtg ggc aag cca ctg gca tcc atc ttc aac gag ttt gaa ggc 2248 Asn Ile Val Gly Lys Pro Leu Ala Ser Ile Phe Asn Glu Phe Glu Gly 590 595 600 caa atg gag cag ggc cag atc ggt ggc tcc ggt gac gtg aag tac cac 2296 Gln Met Glu Gln Gly Gln Ile Gly Gly Ser Gly Asp Val Lys Tyr His 605 610 615 ctc ggt tcc gaa ggc cag cac ctg cag atg ttc ggc gac ggc gag atc 2344 Leu Gly Ser Glu Gly Gln His Leu Gln Met Phe Gly Asp Gly Glu Ile 620 625 630 aag gtc tcc ctg act gct aac ccg tcc cac ctg gaa gct gtt aac cca 2392 Lys Val Ser Leu Thr Ala Asn Pro Ser His Leu Glu Ala Val Asn Pro 635 640 645 650 gtg atg gaa ggt atc gtc cgc gca aag cag gac tac ctg gac aag ggc 2440 Val Met Glu Gly Ile Val Arg Ala Lys Gln Asp Tyr Leu Asp Lys Gly 655 660 665 gta gac ggc aag act gtt gtg cca ctg ctg ctc cac ggt gac gct gca 2488 Val Asp Gly Lys Thr Val Val Pro Leu Leu Leu His Gly Asp Ala Ala 670 675 680 ttc gca ggc ctg ggc atc gtg cca gaa acc atc aac ctg gct aag ctg 2536 Phe Ala Gly Leu Gly Ile Val Pro Glu Thr Ile Asn Leu Ala Lys Leu 685 690 695 cgt ggc tac gac gtc gga ggc acc atc cac atc gtg gtg aac aac cag 2584 Arg Gly Tyr Asp Val Gly Gly Thr Ile His Ile Val Val Asn Asn Gln 700 705 710 atc ggc ttc acc acc acc cca gac tcc agc cgc tcc atg cac tac gca 2632 Ile Gly Phe Thr Thr Thr Pro Asp Ser Ser Arg Ser Met His Tyr Ala 715 720 725 730 acc gac tac gcc aag gca ttc ggc tgc cca gtc ttc cac gtc aat ggt 2680 Thr Asp Tyr Ala Lys Ala Phe Gly Cys Pro Val Phe His Val Asn Gly 735 740 745 gat gac cca gag gca gtt gtc tgg gtt ggc cag ctg gca acc gag tac 2728 Asp Asp Pro Glu Ala Val Val Trp Val Gly Gln Leu Ala Thr Glu Tyr 750 755 760 cgt cgt cgc ttc ggc aag gac gtc ttc atc gac ctc gtt tgc tac cgc 2776 Arg Arg Arg Phe Gly Lys Asp Val Phe Ile Asp Leu Val Cys Tyr Arg 765

770 775 ctc cgc ggc cac aac gaa gct gat gat cct tcc atg acc cag cca aag 2824 Leu Arg Gly His Asn Glu Ala Asp Asp Pro Ser Met Thr Gln Pro Lys 780 785 790 atg tat gag ctc atc acc ggc cgc gag acc gtt cgt gct cag tac acc 2872 Met Tyr Glu Leu Ile Thr Gly Arg Glu Thr Val Arg Ala Gln Tyr Thr 795 800 805 810 gaa gac ctg ctc gga cgt gga gac ctc tcc aac gaa gat gca gaa gca 2920 Glu Asp Leu Leu Gly Arg Gly Asp Leu Ser Asn Glu Asp Ala Glu Ala 815 820 825 gtc gtc cgc gac ttc cac gac cag atg gaa tct gtg ttc aac gaa gtc 2968 Val Val Arg Asp Phe His Asp Gln Met Glu Ser Val Phe Asn Glu Val 830 835 840 aag gaa ggc ggc aag aag cag gct gag gca cag acc ggc atc acc ggc 3016 Lys Glu Gly Gly Lys Lys Gln Ala Glu Ala Gln Thr Gly Ile Thr Gly 845 850 855 tcc cag aag ctt cca cac ggc ctt gag acc aac atc tcc cgt gaa gag 3064 Ser Gln Lys Leu Pro His Gly Leu Glu Thr Asn Ile Ser Arg Glu Glu 860 865 870 ctc ctg gaa ctg gga cag gct ttc gcc aac acc cca gaa ggc ttc aac 3112 Leu Leu Glu Leu Gly Gln Ala Phe Ala Asn Thr Pro Glu Gly Phe Asn 875 880 885 890 tac cac cca cgt gtg gct cca gtt gct aag aag cgc gtc tcc tct gtc 3160 Tyr His Pro Arg Val Ala Pro Val Ala Lys Lys Arg Val Ser Ser Val 895 900 905 acc gaa ggt ggc atc gac tgg gca tgg ggc gag ctc ctc gcc ttc ggt 3208 Thr Glu Gly Gly Ile Asp Trp Ala Trp Gly Glu Leu Leu Ala Phe Gly 910 915 920 tcc ctg gct aac tcc ggc cgc ttg gtt cgc ctt gca ggt gaa gat tcc 3256 Ser Leu Ala Asn Ser Gly Arg Leu Val Arg Leu Ala Gly Glu Asp Ser 925 930 935 cgc cgc ggt acc ttc acc cag cgc cac gca gtt gcc atc gac cca gcg 3304 Arg Arg Gly Thr Phe Thr Gln Arg His Ala Val Ala Ile Asp Pro Ala 940 945 950 acc gct gaa gag ttc aac cca ctc cac gag ctt gca cag tcc aag ggc 3352 Thr Ala Glu Glu Phe Asn Pro Leu His Glu Leu Ala Gln Ser Lys Gly 955 960 965 970 aac aac ggt aag ttc ctg gtc tac aac tcc gca ctg acc gag tac gca 3400 Asn Asn Gly Lys Phe Leu Val Tyr Asn Ser Ala Leu Thr Glu Tyr Ala 975 980 985 ggc atg ggc ttc gag tac ggc tac tcc gta gga aac gaa gac tcc gtc 3448 Gly Met Gly Phe Glu Tyr Gly Tyr Ser Val Gly Asn Glu Asp Ser Val 990 995 1000 gtt gca tgg gaa gca cag ttc ggc gac ttc gcc aac ggc gct cag 3493 Val Ala Trp Glu Ala Gln Phe Gly Asp Phe Ala Asn Gly Ala Gln 1005 1010 1015 acc atc atc gat gag tac gtc tcc tca ggc gaa gct aag tgg ggc 3538 Thr Ile Ile Asp Glu Tyr Val Ser Ser Gly Glu Ala Lys Trp Gly 1020 1025 1030 cag acc tcc aag ctg atc ctt ctg ctg cct cac ggc tac gaa ggc 3583 Gln Thr Ser Lys Leu Ile Leu Leu Leu Pro His Gly Tyr Glu Gly 1035 1040 1045 cag ggc cca gac cac tct tcc gca cgt atc gag cgc ttc ctg cag 3628 Gln Gly Pro Asp His Ser Ser Ala Arg Ile Glu Arg Phe Leu Gln 1050 1055 1060 ctg tgc gct gag ggt tcc atg act gtt gct cag cca tcc acc cca 3673 Leu Cys Ala Glu Gly Ser Met Thr Val Ala Gln Pro Ser Thr Pro 1065 1070 1075 gca aac cac ttc cac ctg ctg cgt cgt cac gct ctg tcc gac ctg 3718 Ala Asn His Phe His Leu Leu Arg Arg His Ala Leu Ser Asp Leu 1080 1085 1090 aag cgt cca ctg gtt atc ttc acc ccg aag tcc atg ctg cgt aac 3763 Lys Arg Pro Leu Val Ile Phe Thr Pro Lys Ser Met Leu Arg Asn 1095 1100 1105 aag gct gct gcc tcc gca cca gaa gac ttc act gag gtc acc aag 3808 Lys Ala Ala Ala Ser Ala Pro Glu Asp Phe Thr Glu Val Thr Lys 1110 1115 1120 ttc caa tcc gtg atc gac gat cca aac gtt gca gat gca gcc aag 3853 Phe Gln Ser Val Ile Asp Asp Pro Asn Val Ala Asp Ala Ala Lys 1125 1130 1135 gtg aag aag gtc atg ctg gtc tcc ggc aag ctg tac tac gaa ttg 3898 Val Lys Lys Val Met Leu Val Ser Gly Lys Leu Tyr Tyr Glu Leu 1140 1145 1150 gca aag cgc aag gag aag gac gga cgc gac gac atc gcg atc gtt 3943 Ala Lys Arg Lys Glu Lys Asp Gly Arg Asp Asp Ile Ala Ile Val 1155 1160 1165 cgt atc gaa atg ctc cac cca att ccg ttc aac cgc atc tcc gag 3988 Arg Ile Glu Met Leu His Pro Ile Pro Phe Asn Arg Ile Ser Glu 1170 1175 1180 gct ctt gcc ggc tac cct aac gct gag gaa gtc ctc ttc gtt cag 4033 Ala Leu Ala Gly Tyr Pro Asn Ala Glu Glu Val Leu Phe Val Gln 1185 1190 1195 gat gag cca gca aac cag ggc cca tgg ccg ttc tac cag gag cac 4078 Asp Glu Pro Ala Asn Gln Gly Pro Trp Pro Phe Tyr Gln Glu His 1200 1205 1210 ctc cca gag ctg atc ccg aac atg cca aag atg cgc cgc gtt tcc 4123 Leu Pro Glu Leu Ile Pro Asn Met Pro Lys Met Arg Arg Val Ser 1215 1220 1225 cgc cgc gct cag tcc tcc acc gca act ggt gtt gct aag gtg cac 4168 Arg Arg Ala Gln Ser Ser Thr Ala Thr Gly Val Ala Lys Val His 1230 1235 1240 cag ctg gag gag aag cag ctt atc gac gag gct ttc gag gct taa 4213 Gln Leu Glu Glu Lys Gln Leu Ile Asp Glu Ala Phe Glu Ala 1245 1250 1255 gtctttatag tcctgcacta gcctagaggg ccttatgcag tgtgaatcac acagcataag 4273 gccctttttg ctgccgtggt tgcctaaggt ggaaggcatg aaacgaatct gtgcggtcac 4333 gatctcttca gtacttttgc taagtggctg ctcctccact tccaccacgc agctcgag 4391 12 1256 PRT Corynebacterium glutamicum 12 Met Leu Gln Leu Gly Leu Arg His Asn Gln Pro Thr Thr Asn Val Thr 1 5 10 15 Val Asp Lys Ile Lys Leu Asn Lys Pro Ser Arg Ser Lys Glu Lys Arg 20 25 30 Arg Val Pro Ala Val Ser Ser Ala Ser Thr Phe Gly Gln Asn Ala Trp 35 40 45 Leu Val Asp Glu Met Phe Gln Gln Phe Gln Lys Asp Pro Lys Ser Val 50 55 60 Asp Lys Glu Trp Arg Glu Leu Phe Glu Ala Gln Gly Gly Pro Asn Ala 65 70 75 80 Thr Pro Ala Thr Thr Glu Ala Gln Pro Ser Ala Pro Lys Glu Ser Ala 85 90 95 Lys Pro Ala Pro Lys Ala Ala Pro Ala Ala Lys Ala Ala Pro Arg Val 100 105 110 Glu Thr Lys Pro Ala Ala Lys Thr Ala Pro Lys Ala Lys Glu Ser Ser 115 120 125 Val Pro Gln Gln Pro Lys Leu Pro Glu Pro Gly Gln Thr Pro Ile Arg 130 135 140 Gly Ile Phe Lys Ser Ile Ala Lys Asn Met Asp Ile Ser Leu Glu Ile 145 150 155 160 Pro Thr Ala Thr Ser Val Arg Asp Met Pro Ala Arg Leu Met Phe Glu 165 170 175 Asn Arg Ala Met Val Asn Asp Gln Leu Lys Arg Thr Arg Gly Gly Lys 180 185 190 Ile Ser Phe Thr His Ile Ile Gly Tyr Ala Met Val Lys Ala Val Met 195 200 205 Ala His Pro Asp Met Asn Asn Ser Tyr His Arg Arg Gln Ala Pro Thr 210 215 220 Leu Ile Val Pro Glu His Ile Asn Leu Gly Leu Ala Ile Asp Leu Pro 225 230 235 240 Gln Lys Asp Gly Ser Arg Ala Leu Val Val Ala Ala Ile Lys Glu Thr 245 250 255 Glu Lys Met Asn Phe Ser Glu Phe Leu Ala Ala Tyr Glu Asp Ile Val 260 265 270 Thr Arg Ser Arg Lys Gly Lys Leu Thr Met Asp Asp Tyr Gln Gly Val 275 280 285 Thr Val Ser Leu Thr Asn Pro Gly Gly Ile Gly Thr Arg His Ser Val 290 295 300 Pro Arg Leu Thr Lys Gly Gln Gly Thr Ile Ile Gly Val Gly Ser Met 305 310 315 320 Asp Tyr Pro Ala Glu Phe Gln Gly Ala Ser Glu Asp Arg Leu Ala Glu 325 330 335 Leu Gly Val Gly Lys Leu Val Thr Ile Thr Ser Thr Tyr Asp His Arg 340 345 350 Val Ile Gln Gly Ala Val Ser Gly Glu Phe Leu Arg Thr Met Ser Arg 355 360 365 Leu Leu Thr Asp Asp Ser Phe Trp Asp Glu Ile Phe Asp Ala Met Asn 370 375 380 Val Pro Tyr Thr Pro Met Arg Trp Ala Gln Asp Val Pro Asn Thr Gly 385 390 395 400 Val Asp Lys Asn Thr Arg Val Met Gln Leu Ile Glu Ala Tyr Arg Ser 405 410 415 Arg Gly His Leu Ile Ala Asp Thr Asn Pro Leu Ser Trp Val Gln Pro 420 425 430 Gly Met Pro Val Pro Asp His Arg Asp Leu Asp Ile Glu Thr His Ser 435 440 445 Leu Thr Ile Trp Asp Leu Asp Arg Thr Phe Ser Val Gly Gly Phe Gly 450 455 460 Gly Lys Glu Thr Met Thr Leu Arg Glu Val Leu Ser Arg Leu Arg Ala 465 470 475 480 Ala Tyr Thr Leu Lys Val Gly Ser Glu Tyr Thr His Ile Leu Asp Arg 485 490 495 Asp Glu Arg Thr Trp Leu Gln Asp Arg Leu Glu Ala Gly Met Pro Lys 500 505 510 Pro Thr Gln Ala Glu Gln Lys Tyr Ile Leu Gln Lys Leu Asn Ala Ala 515 520 525 Glu Ala Phe Glu Asn Phe Leu Gln Thr Lys Tyr Val Gly Gln Lys Arg 530 535 540 Phe Ser Leu Glu Gly Ala Glu Ala Leu Ile Pro Leu Met Asp Ser Ala 545 550 555 560 Ile Asp Thr Ala Ala Gly Gln Gly Leu Asp Glu Val Val Ile Gly Met 565 570 575 Pro His Arg Gly Arg Leu Asn Val Leu Phe Asn Ile Val Gly Lys Pro 580 585 590 Leu Ala Ser Ile Phe Asn Glu Phe Glu Gly Gln Met Glu Gln Gly Gln 595 600 605 Ile Gly Gly Ser Gly Asp Val Lys Tyr His Leu Gly Ser Glu Gly Gln 610 615 620 His Leu Gln Met Phe Gly Asp Gly Glu Ile Lys Val Ser Leu Thr Ala 625 630 635 640 Asn Pro Ser His Leu Glu Ala Val Asn Pro Val Met Glu Gly Ile Val 645 650 655 Arg Ala Lys Gln Asp Tyr Leu Asp Lys Gly Val Asp Gly Lys Thr Val 660 665 670 Val Pro Leu Leu Leu His Gly Asp Ala Ala Phe Ala Gly Leu Gly Ile 675 680 685 Val Pro Glu Thr Ile Asn Leu Ala Lys Leu Arg Gly Tyr Asp Val Gly 690 695 700 Gly Thr Ile His Ile Val Val Asn Asn Gln Ile Gly Phe Thr Thr Thr 705 710 715 720 Pro Asp Ser Ser Arg Ser Met His Tyr Ala Thr Asp Tyr Ala Lys Ala 725 730 735 Phe Gly Cys Pro Val Phe His Val Asn Gly Asp Asp Pro Glu Ala Val 740 745 750 Val Trp Val Gly Gln Leu Ala Thr Glu Tyr Arg Arg Arg Phe Gly Lys 755 760 765 Asp Val Phe Ile Asp Leu Val Cys Tyr Arg Leu Arg Gly His Asn Glu 770 775 780 Ala Asp Asp Pro Ser Met Thr Gln Pro Lys Met Tyr Glu Leu Ile Thr 785 790 795 800 Gly Arg Glu Thr Val Arg Ala Gln Tyr Thr Glu Asp Leu Leu Gly Arg 805 810 815 Gly Asp Leu Ser Asn Glu Asp Ala Glu Ala Val Val Arg Asp Phe His 820 825 830 Asp Gln Met Glu Ser Val Phe Asn Glu Val Lys Glu Gly Gly Lys Lys 835 840 845 Gln Ala Glu Ala Gln Thr Gly Ile Thr Gly Ser Gln Lys Leu Pro His 850 855 860 Gly Leu Glu Thr Asn Ile Ser Arg Glu Glu Leu Leu Glu Leu Gly Gln 865 870 875 880 Ala Phe Ala Asn Thr Pro Glu Gly Phe Asn Tyr His Pro Arg Val Ala 885 890 895 Pro Val Ala Lys Lys Arg Val Ser Ser Val Thr Glu Gly Gly Ile Asp 900 905 910 Trp Ala Trp Gly Glu Leu Leu Ala Phe Gly Ser Leu Ala Asn Ser Gly 915 920 925 Arg Leu Val Arg Leu Ala Gly Glu Asp Ser Arg Arg Gly Thr Phe Thr 930 935 940 Gln Arg His Ala Val Ala Ile Asp Pro Ala Thr Ala Glu Glu Phe Asn 945 950 955 960 Pro Leu His Glu Leu Ala Gln Ser Lys Gly Asn Asn Gly Lys Phe Leu 965 970 975 Val Tyr Asn Ser Ala Leu Thr Glu Tyr Ala Gly Met Gly Phe Glu Tyr 980 985 990 Gly Tyr Ser Val Gly Asn Glu Asp Ser Val Val Ala Trp Glu Ala Gln 995 1000 1005 Phe Gly Asp Phe Ala Asn Gly Ala Gln Thr Ile Ile Asp Glu Tyr 1010 1015 1020 Val Ser Ser Gly Glu Ala Lys Trp Gly Gln Thr Ser Lys Leu Ile 1025 1030 1035 Leu Leu Leu Pro His Gly Tyr Glu Gly Gln Gly Pro Asp His Ser 1040 1045 1050 Ser Ala Arg Ile Glu Arg Phe Leu Gln Leu Cys Ala Glu Gly Ser 1055 1060 1065 Met Thr Val Ala Gln Pro Ser Thr Pro Ala Asn His Phe His Leu 1070 1075 1080 Leu Arg Arg His Ala Leu Ser Asp Leu Lys Arg Pro Leu Val Ile 1085 1090 1095 Phe Thr Pro Lys Ser Met Leu Arg Asn Lys Ala Ala Ala Ser Ala 1100 1105 1110 Pro Glu Asp Phe Thr Glu Val Thr Lys Phe Gln Ser Val Ile Asp 1115 1120 1125 Asp Pro Asn Val Ala Asp Ala Ala Lys Val Lys Lys Val Met Leu 1130 1135 1140 Val Ser Gly Lys Leu Tyr Tyr Glu Leu Ala Lys Arg Lys Glu Lys 1145 1150 1155 Asp Gly Arg Asp Asp Ile Ala Ile Val Arg Ile Glu Met Leu His 1160 1165 1170 Pro Ile Pro Phe Asn Arg Ile Ser Glu Ala Leu Ala Gly Tyr Pro 1175 1180 1185 Asn Ala Glu Glu Val Leu Phe Val Gln Asp Glu Pro Ala Asn Gln 1190 1195 1200 Gly Pro Trp Pro Phe Tyr Gln Glu His Leu Pro Glu Leu Ile Pro 1205 1210 1215 Asn Met Pro Lys Met Arg Arg Val Ser Arg Arg Ala Gln Ser Ser 1220 1225 1230 Thr Ala Thr Gly Val Ala Lys Val His Gln Leu Glu Glu Lys Gln 1235 1240 1245 Leu Ile Asp Glu Ala Phe Glu Ala 1250 1255 13 4388 DNA Corynebacterium glutamicum CDS (443)..(4213) 13 gtcgacaagc aaaatcgaag cggcagcacg ccgcgtcgga gccttaaacg ccatcgccgc 60 catccctgat ggtttcaatc atcaagtcgg tgaacgcggg cgcaacctgt catccggaca 120 gcgccaactg atcgcgctgg cgcgcgccga actcatcgag ccttccatca tgcttctcga 180 cgaagccacc tccaccctcg accccgccac cgaagccgtt atcctcaacg cctccgatcg 240 agtcactaag ggacgcacca gcatcatcgt cgcgcaccgc ttggcaaccg ctaaaagggc 300 cgaccgtatt cttgttgttg aacaaggacg tatcattgag gacggatctc acgacgcgtt 360 gttgtctgct aacggcacct acgcccgcat gtggcattta atggcctgac acgttatttt 420 taggagaact gtcaacaaat ta atg cta caa ctg ggg ctt agg cat aat cag 472 Met Leu Gln Leu Gly Leu Arg His Asn Gln 1 5 10 cca acg acc aac gtt aca gtg gat aaa ata aag ctc aat aaa ccc tca 520 Pro Thr Thr Asn Val Thr Val Asp Lys Ile Lys Leu Asn Lys Pro Ser 15 20 25 aga agc aag gaa aag agg cga gta cct gcc gtg agc agc gct agt act 568 Arg Ser Lys Glu Lys Arg Arg Val Pro Ala Val Ser Ser Ala Ser Thr 30 35 40 ttc ggc cag aat gcg tgg ctg gta gac gag atg ttc cag cag ttc cag 616 Phe Gly Gln Asn Ala Trp Leu Val Asp Glu Met Phe Gln Gln Phe Gln 45 50 55 aag gac ccc aag tcc gtg gac aag gaa tgg aga gaa ctc ttt gag gcg 664 Lys Asp Pro Lys Ser Val Asp Lys Glu Trp Arg Glu Leu Phe Glu Ala 60 65 70 cag ggg gga cca aat gct acc ccc gct aca aca gaa gca cag cct tca 712 Gln Gly Gly Pro Asn Ala Thr Pro Ala Thr Thr Glu Ala Gln Pro Ser 75 80 85 90 gcg ccc aag gag tct gcg aaa cca gca cca aag gct gcc cct gca gcc 760 Ala Pro Lys Glu Ser Ala Lys Pro Ala Pro Lys Ala Ala Pro Ala Ala 95 100 105 aag gca gca ccg cgc gta gaa acc aag ccg gcc gcc aag acc gcc cct 808 Lys Ala Ala Pro Arg Val Glu Thr Lys Pro Ala Ala Lys Thr Ala Pro 110 115 120 aag gcc aag gag tcc tca gtg cca cag caa cct aag ctt ccg gag cca 856 Lys Ala Lys Glu Ser Ser Val Pro Gln Gln Pro Lys Leu Pro Glu Pro 125 130 135 gga caa acc cca atc agg ggt att ttc aag tcc atc gcg aag aac atg 904 Gly Gln Thr Pro Ile Arg Gly Ile Phe Lys Ser Ile Ala Lys Asn Met 140 145 150 gat atc tcc ctg gaa atc cca acc gca acc tcg gtt cgc gat atg cca 952 Asp Ile Ser Leu Glu Ile Pro Thr Ala Thr Ser Val Arg Asp Met Pro

155 160 165 170 gct cgc ctc atg ttc gaa aac cgc gcg atg gtc aac gat cag ctc aag 1000 Ala Arg Leu Met Phe Glu Asn Arg Ala Met Val Asn Asp Gln Leu Lys 175 180 185 cgc acc cgc ggt ggc aag atc tcc ttc acc cac atc att ggc tac gcc 1048 Arg Thr Arg Gly Gly Lys Ile Ser Phe Thr His Ile Ile Gly Tyr Ala 190 195 200 atg gtg aag gca gtc atg gct cac ccg gac atg aac aac tcc tac gac 1096 Met Val Lys Ala Val Met Ala His Pro Asp Met Asn Asn Ser Tyr Asp 205 210 215 gtc atc gac ggc aag cca acc ctg atc gtg cct gag cac atc aac ctg 1144 Val Ile Asp Gly Lys Pro Thr Leu Ile Val Pro Glu His Ile Asn Leu 220 225 230 ggc ctt gcc atc gac ctt cct cag aag gac ggc tcc cgc gca ctt gtc 1192 Gly Leu Ala Ile Asp Leu Pro Gln Lys Asp Gly Ser Arg Ala Leu Val 235 240 245 250 gta gca gcc atc aag gaa acc gag aag atg aac ttc tcc gag ttc ctc 1240 Val Ala Ala Ile Lys Glu Thr Glu Lys Met Asn Phe Ser Glu Phe Leu 255 260 265 gca gca tac gaa gac atc gtg aca cgc tcc cgc aag ggc aag ctc acc 1288 Ala Ala Tyr Glu Asp Ile Val Thr Arg Ser Arg Lys Gly Lys Leu Thr 270 275 280 atg gat gac tac cag ggc gtt acc gtt tcc ttg acc aac cca ggt ggc 1336 Met Asp Asp Tyr Gln Gly Val Thr Val Ser Leu Thr Asn Pro Gly Gly 285 290 295 atc ggt acc cgc cac tct gtc cca cgt ctg acc aag ggc cag ggc acc 1384 Ile Gly Thr Arg His Ser Val Pro Arg Leu Thr Lys Gly Gln Gly Thr 300 305 310 atc atc ggt gtc ggt tcc atg gat tac cca gca gag ttc cag ggc gct 1432 Ile Ile Gly Val Gly Ser Met Asp Tyr Pro Ala Glu Phe Gln Gly Ala 315 320 325 330 tcc gaa gac cgc ctt gca gag ctc ggc gtt gga aag ctt gtc acc atc 1480 Ser Glu Asp Arg Leu Ala Glu Leu Gly Val Gly Lys Leu Val Thr Ile 335 340 345 acc tcc acc tac gat cac cgc gtg atc cag ggt gct gtg tcc ggt gaa 1528 Thr Ser Thr Tyr Asp His Arg Val Ile Gln Gly Ala Val Ser Gly Glu 350 355 360 ttc ctg cgt acc atg tct cgc ctg ctc acc gat gat tcc ttc tgg gat 1576 Phe Leu Arg Thr Met Ser Arg Leu Leu Thr Asp Asp Ser Phe Trp Asp 365 370 375 gag atc ttc gac gca atg aac gtt cct tac acc cca atg cgt tgg gca 1624 Glu Ile Phe Asp Ala Met Asn Val Pro Tyr Thr Pro Met Arg Trp Ala 380 385 390 cag gac gtt cca aac acc ggt gtt gat aag aac acc cgc gtc atg cag 1672 Gln Asp Val Pro Asn Thr Gly Val Asp Lys Asn Thr Arg Val Met Gln 395 400 405 410 ctc att gag gca tac cgc tcc cgt gga cac ctc atc gct gac acc aac 1720 Leu Ile Glu Ala Tyr Arg Ser Arg Gly His Leu Ile Ala Asp Thr Asn 415 420 425 cca ctt tca tgg gtt cag cct ggc atg cca gtt cca gac cac cgc gac 1768 Pro Leu Ser Trp Val Gln Pro Gly Met Pro Val Pro Asp His Arg Asp 430 435 440 ctc gac atc gag acc cac agc ctg acc atc tgg gat ctg gac cgt acc 1816 Leu Asp Ile Glu Thr His Ser Leu Thr Ile Trp Asp Leu Asp Arg Thr 445 450 455 ttc agc gtc ggt ggc ttc ggc ggc aag gag acc atg acc ctg cgc gag 1864 Phe Ser Val Gly Gly Phe Gly Gly Lys Glu Thr Met Thr Leu Arg Glu 460 465 470 gta ctg tcc cgc ctg cgc gct gcc tac acc ttg aag gtc ggc tcc gaa 1912 Val Leu Ser Arg Leu Arg Ala Ala Tyr Thr Leu Lys Val Gly Ser Glu 475 480 485 490 tac acc cac atc ctg gac cgc gac gag cgc acc tgg ctg cag gac cgc 1960 Tyr Thr His Ile Leu Asp Arg Asp Glu Arg Thr Trp Leu Gln Asp Arg 495 500 505 ctc gaa gcc gga atg cca aag cca acc cag gca gag cag aag tac atc 2008 Leu Glu Ala Gly Met Pro Lys Pro Thr Gln Ala Glu Gln Lys Tyr Ile 510 515 520 ctg cag aag ctg aac gcc gca gag gct ttc gag aac ttc ctg cag acc 2056 Leu Gln Lys Leu Asn Ala Ala Glu Ala Phe Glu Asn Phe Leu Gln Thr 525 530 535 aag tac gtc ggc cag aag cgc ttc tcc ctc gaa ggt gca gaa gct ctc 2104 Lys Tyr Val Gly Gln Lys Arg Phe Ser Leu Glu Gly Ala Glu Ala Leu 540 545 550 atc cca ctg atg gac tcc gcc atc gac acc gcc gca ggc cag ggc ctc 2152 Ile Pro Leu Met Asp Ser Ala Ile Asp Thr Ala Ala Gly Gln Gly Leu 555 560 565 570 gac gaa gtt gtc atc ggt atg cca cac cgt ggt cgc ctc aac gtg ctg 2200 Asp Glu Val Val Ile Gly Met Pro His Arg Gly Arg Leu Asn Val Leu 575 580 585 ttc aac atc gtg ggc aag cca ctg gca tcc atc ttc aac gag ttt gaa 2248 Phe Asn Ile Val Gly Lys Pro Leu Ala Ser Ile Phe Asn Glu Phe Glu 590 595 600 ggc caa atg gag cag ggc cag atc ggt ggc tcc ggt gac gtg aag tac 2296 Gly Gln Met Glu Gln Gly Gln Ile Gly Gly Ser Gly Asp Val Lys Tyr 605 610 615 cac ctc ggt tcc gaa ggc cag cac ctg cag atg ttc ggc gac ggc gag 2344 His Leu Gly Ser Glu Gly Gln His Leu Gln Met Phe Gly Asp Gly Glu 620 625 630 atc aag gtc tcc ctg act gct aac ccg tcc cac ctg gaa gct gtt aac 2392 Ile Lys Val Ser Leu Thr Ala Asn Pro Ser His Leu Glu Ala Val Asn 635 640 645 650 cca gtg atg gaa ggt atc gtc cgc gca aag cag gac tac ctg gac aag 2440 Pro Val Met Glu Gly Ile Val Arg Ala Lys Gln Asp Tyr Leu Asp Lys 655 660 665 ggc gta gac ggc aag act gtt gtg cca ctg ctg ctc cac ggt gac gct 2488 Gly Val Asp Gly Lys Thr Val Val Pro Leu Leu Leu His Gly Asp Ala 670 675 680 gca ttc gca ggc ctg ggc atc gtg cca gaa acc atc aac ctg gct aag 2536 Ala Phe Ala Gly Leu Gly Ile Val Pro Glu Thr Ile Asn Leu Ala Lys 685 690 695 cgc gtc gac gtc gga ggc acc atc cac atc gtg gtg aac aac cag atc 2584 Arg Val Asp Val Gly Gly Thr Ile His Ile Val Val Asn Asn Gln Ile 700 705 710 ggc ttc acc acc acc cca gac tcc agc cgc tcc atg cac tac gca acc 2632 Gly Phe Thr Thr Thr Pro Asp Ser Ser Arg Ser Met His Tyr Ala Thr 715 720 725 730 gac tac gcc aag gca ttc ggc tgc cca gtc ttc cac gtc aat ggt gat 2680 Asp Tyr Ala Lys Ala Phe Gly Cys Pro Val Phe His Val Asn Gly Asp 735 740 745 gac cca gag gca gtt gtc tgg gtt ggc cag ctg gca acc gag tac cgt 2728 Asp Pro Glu Ala Val Val Trp Val Gly Gln Leu Ala Thr Glu Tyr Arg 750 755 760 cgt cgc ttc ggc aag gac gtc ttc atc gac ctc gtt tgc tac cgc ctc 2776 Arg Arg Phe Gly Lys Asp Val Phe Ile Asp Leu Val Cys Tyr Arg Leu 765 770 775 cgc ggc cac aac gaa gct gat gat cct tcc atg acc cag cca aag atg 2824 Arg Gly His Asn Glu Ala Asp Asp Pro Ser Met Thr Gln Pro Lys Met 780 785 790 tat gag ctc atc acc ggc cgc gag acc gtt cgt gct cag tac acc gaa 2872 Tyr Glu Leu Ile Thr Gly Arg Glu Thr Val Arg Ala Gln Tyr Thr Glu 795 800 805 810 gac ctg ctc gga cgt gga gac ctc tcc aac gaa gat gca gaa gca gtc 2920 Asp Leu Leu Gly Arg Gly Asp Leu Ser Asn Glu Asp Ala Glu Ala Val 815 820 825 gtc cgc gac ttc cac gac cag atg gaa tct gtg ttc aac gaa gtc aag 2968 Val Arg Asp Phe His Asp Gln Met Glu Ser Val Phe Asn Glu Val Lys 830 835 840 gaa ggc ggc aag aag cag gct gag gca cag acc ggc atc acc ggc tcc 3016 Glu Gly Gly Lys Lys Gln Ala Glu Ala Gln Thr Gly Ile Thr Gly Ser 845 850 855 cag aag ctt cca cac ggc ctt gag acc aac atc tcc cgt gaa gag ctc 3064 Gln Lys Leu Pro His Gly Leu Glu Thr Asn Ile Ser Arg Glu Glu Leu 860 865 870 ctg gaa ctg gga cag gct ttc gcc aac acc cca gaa ggc ttc aac tac 3112 Leu Glu Leu Gly Gln Ala Phe Ala Asn Thr Pro Glu Gly Phe Asn Tyr 875 880 885 890 cac cca cgt gtg gct cca gtt gct aag aag cgc gtc tcc tct gtc acc 3160 His Pro Arg Val Ala Pro Val Ala Lys Lys Arg Val Ser Ser Val Thr 895 900 905 gaa ggt ggc atc gac tgg gca tgg ggc gag ctc ctc gcc ttc ggt tcc 3208 Glu Gly Gly Ile Asp Trp Ala Trp Gly Glu Leu Leu Ala Phe Gly Ser 910 915 920 ctg gct aac tcc ggc cgc ttg gtt cgc ctt gca ggt gaa gat tcc cgc 3256 Leu Ala Asn Ser Gly Arg Leu Val Arg Leu Ala Gly Glu Asp Ser Arg 925 930 935 cgc ggt acc ttc acc cag cgc cac gca gtt gcc atc gac cca gcg acc 3304 Arg Gly Thr Phe Thr Gln Arg His Ala Val Ala Ile Asp Pro Ala Thr 940 945 950 gct gaa gag ttc aac cca ctc cac gag ctt gca cag tcc aag ggc aac 3352 Ala Glu Glu Phe Asn Pro Leu His Glu Leu Ala Gln Ser Lys Gly Asn 955 960 965 970 aac ggt aag ttc ctg gtc tac aac tcc gca ctg acc gag tac gca ggc 3400 Asn Gly Lys Phe Leu Val Tyr Asn Ser Ala Leu Thr Glu Tyr Ala Gly 975 980 985 atg ggc ttc gag tac ggc tac tcc gta gga aac gaa gac tcc gtc gtt 3448 Met Gly Phe Glu Tyr Gly Tyr Ser Val Gly Asn Glu Asp Ser Val Val 990 995 1000 gca tgg gaa gca cag ttc ggc gac ttc gcc aac ggc gct cag acc 3493 Ala Trp Glu Ala Gln Phe Gly Asp Phe Ala Asn Gly Ala Gln Thr 1005 1010 1015 atc atc gat gag tac gtc tcc tca ggc gaa gct aag tgg ggc cag 3538 Ile Ile Asp Glu Tyr Val Ser Ser Gly Glu Ala Lys Trp Gly Gln 1020 1025 1030 acc tcc aag ctg atc ctt ctg ctg cct cac ggc tac gaa ggc cag 3583 Thr Ser Lys Leu Ile Leu Leu Leu Pro His Gly Tyr Glu Gly Gln 1035 1040 1045 ggc cca gac cac tct tcc gca cgt atc gag cgc ttc ctg cag ctg 3628 Gly Pro Asp His Ser Ser Ala Arg Ile Glu Arg Phe Leu Gln Leu 1050 1055 1060 tgc gct gag ggt tcc atg act gtt gct cag cca tcc acc cca gca 3673 Cys Ala Glu Gly Ser Met Thr Val Ala Gln Pro Ser Thr Pro Ala 1065 1070 1075 aac cac ttc cac ctg ctg cgt cgt cac gct ctg tcc gac ctg aag 3718 Asn His Phe His Leu Leu Arg Arg His Ala Leu Ser Asp Leu Lys 1080 1085 1090 cgt cca ctg gtt atc ttc acc ccg aag tcc atg ctg cgt aac aag 3763 Arg Pro Leu Val Ile Phe Thr Pro Lys Ser Met Leu Arg Asn Lys 1095 1100 1105 gct gct gcc tcc gca cca gaa gac ttc act gag gtc acc aag ttc 3808 Ala Ala Ala Ser Ala Pro Glu Asp Phe Thr Glu Val Thr Lys Phe 1110 1115 1120 caa tcc gtg atc gac gat cca aac gtt gca gat gca gcc aag gtg 3853 Gln Ser Val Ile Asp Asp Pro Asn Val Ala Asp Ala Ala Lys Val 1125 1130 1135 aag aag gtc atg ctg gtc tcc ggc aag ctg tac tac gaa ttg gca 3898 Lys Lys Val Met Leu Val Ser Gly Lys Leu Tyr Tyr Glu Leu Ala 1140 1145 1150 aag cgc aag gag aag gac gga cgc gac gac atc gcg atc gtt cgt 3943 Lys Arg Lys Glu Lys Asp Gly Arg Asp Asp Ile Ala Ile Val Arg 1155 1160 1165 atc gaa atg ctc cac cca att ccg ttc aac cgc atc tcc gag gct 3988 Ile Glu Met Leu His Pro Ile Pro Phe Asn Arg Ile Ser Glu Ala 1170 1175 1180 ctt gcc ggc tac cct aac gct gag gaa gtc ctc ttc gtt cag gat 4033 Leu Ala Gly Tyr Pro Asn Ala Glu Glu Val Leu Phe Val Gln Asp 1185 1190 1195 gag cca gca aac cag ggc cca tgg ccg ttc tac cag gag cac ctc 4078 Glu Pro Ala Asn Gln Gly Pro Trp Pro Phe Tyr Gln Glu His Leu 1200 1205 1210 cca gag ctg atc ccg aac atg cca aag atg cgc cgc gtt tcc cgc 4123 Pro Glu Leu Ile Pro Asn Met Pro Lys Met Arg Arg Val Ser Arg 1215 1220 1225 cgc gct cag tcc tcc acc gca act ggt gtt gct aag gtg cac cag 4168 Arg Ala Gln Ser Ser Thr Ala Thr Gly Val Ala Lys Val His Gln 1230 1235 1240 ctg gag gag aag cag ctt atc gac gag gct ttc gag gct taa gtc 4213 Leu Glu Glu Lys Gln Leu Ile Asp Glu Ala Phe Glu Ala Val 1245 1250 1255 tttatagtcc tgcactagcc tagagggcct tatgcagtgt gaatcacaca gcataaggcc 4273 ctttttgctg ccgtggttgc ctaaggtgga aggcatgaaa cgaatctgtg cggtcacgat 4333 ctcttcagta cttttgctaa gtggctgctc ctccacttcc accacgcagc tcgag 4388 14 1255 PRT Corynebacterium glutamicum 14 Met Leu Gln Leu Gly Leu Arg His Asn Gln Pro Thr Thr Asn Val Thr 1 5 10 15 Val Asp Lys Ile Lys Leu Asn Lys Pro Ser Arg Ser Lys Glu Lys Arg 20 25 30 Arg Val Pro Ala Val Ser Ser Ala Ser Thr Phe Gly Gln Asn Ala Trp 35 40 45 Leu Val Asp Glu Met Phe Gln Gln Phe Gln Lys Asp Pro Lys Ser Val 50 55 60 Asp Lys Glu Trp Arg Glu Leu Phe Glu Ala Gln Gly Gly Pro Asn Ala 65 70 75 80 Thr Pro Ala Thr Thr Glu Ala Gln Pro Ser Ala Pro Lys Glu Ser Ala 85 90 95 Lys Pro Ala Pro Lys Ala Ala Pro Ala Ala Lys Ala Ala Pro Arg Val 100 105 110 Glu Thr Lys Pro Ala Ala Lys Thr Ala Pro Lys Ala Lys Glu Ser Ser 115 120 125 Val Pro Gln Gln Pro Lys Leu Pro Glu Pro Gly Gln Thr Pro Ile Arg 130 135 140 Gly Ile Phe Lys Ser Ile Ala Lys Asn Met Asp Ile Ser Leu Glu Ile 145 150 155 160 Pro Thr Ala Thr Ser Val Arg Asp Met Pro Ala Arg Leu Met Phe Glu 165 170 175 Asn Arg Ala Met Val Asn Asp Gln Leu Lys Arg Thr Arg Gly Gly Lys 180 185 190 Ile Ser Phe Thr His Ile Ile Gly Tyr Ala Met Val Lys Ala Val Met 195 200 205 Ala His Pro Asp Met Asn Asn Ser Tyr Asp Val Ile Asp Gly Lys Pro 210 215 220 Thr Leu Ile Val Pro Glu His Ile Asn Leu Gly Leu Ala Ile Asp Leu 225 230 235 240 Pro Gln Lys Asp Gly Ser Arg Ala Leu Val Val Ala Ala Ile Lys Glu 245 250 255 Thr Glu Lys Met Asn Phe Ser Glu Phe Leu Ala Ala Tyr Glu Asp Ile 260 265 270 Val Thr Arg Ser Arg Lys Gly Lys Leu Thr Met Asp Asp Tyr Gln Gly 275 280 285 Val Thr Val Ser Leu Thr Asn Pro Gly Gly Ile Gly Thr Arg His Ser 290 295 300 Val Pro Arg Leu Thr Lys Gly Gln Gly Thr Ile Ile Gly Val Gly Ser 305 310 315 320 Met Asp Tyr Pro Ala Glu Phe Gln Gly Ala Ser Glu Asp Arg Leu Ala 325 330 335 Glu Leu Gly Val Gly Lys Leu Val Thr Ile Thr Ser Thr Tyr Asp His 340 345 350 Arg Val Ile Gln Gly Ala Val Ser Gly Glu Phe Leu Arg Thr Met Ser 355 360 365 Arg Leu Leu Thr Asp Asp Ser Phe Trp Asp Glu Ile Phe Asp Ala Met 370 375 380 Asn Val Pro Tyr Thr Pro Met Arg Trp Ala Gln Asp Val Pro Asn Thr 385 390 395 400 Gly Val Asp Lys Asn Thr Arg Val Met Gln Leu Ile Glu Ala Tyr Arg 405 410 415 Ser Arg Gly His Leu Ile Ala Asp Thr Asn Pro Leu Ser Trp Val Gln 420 425 430 Pro Gly Met Pro Val Pro Asp His Arg Asp Leu Asp Ile Glu Thr His 435 440 445 Ser Leu Thr Ile Trp Asp Leu Asp Arg Thr Phe Ser Val Gly Gly Phe 450 455 460 Gly Gly Lys Glu Thr Met Thr Leu Arg Glu Val Leu Ser Arg Leu Arg 465 470 475 480 Ala Ala Tyr Thr Leu Lys Val Gly Ser Glu Tyr Thr His Ile Leu Asp 485 490 495 Arg Asp Glu Arg Thr Trp Leu Gln Asp Arg Leu Glu Ala Gly Met Pro 500 505 510 Lys Pro Thr Gln Ala Glu Gln Lys Tyr Ile Leu Gln Lys Leu Asn Ala 515 520 525 Ala Glu Ala Phe Glu Asn Phe Leu Gln Thr Lys Tyr Val Gly Gln Lys 530 535 540 Arg Phe Ser Leu Glu Gly Ala Glu Ala Leu Ile Pro Leu Met Asp Ser 545 550 555 560 Ala Ile Asp Thr Ala Ala Gly Gln Gly Leu Asp Glu Val Val Ile Gly 565 570 575 Met Pro His Arg Gly Arg Leu Asn Val Leu Phe Asn Ile Val Gly Lys 580 585 590 Pro Leu Ala Ser Ile Phe Asn Glu Phe Glu Gly Gln Met Glu Gln Gly 595 600 605 Gln Ile Gly Gly Ser Gly Asp Val Lys Tyr His Leu Gly Ser Glu Gly 610 615 620 Gln His Leu Gln Met Phe Gly Asp Gly Glu Ile Lys Val Ser Leu Thr

625 630 635 640 Ala Asn Pro Ser His Leu Glu Ala Val Asn Pro Val Met Glu Gly Ile 645 650 655 Val Arg Ala Lys Gln Asp Tyr Leu Asp Lys Gly Val Asp Gly Lys Thr 660 665 670 Val Val Pro Leu Leu Leu His Gly Asp Ala Ala Phe Ala Gly Leu Gly 675 680 685 Ile Val Pro Glu Thr Ile Asn Leu Ala Lys Arg Val Asp Val Gly Gly 690 695 700 Thr Ile His Ile Val Val Asn Asn Gln Ile Gly Phe Thr Thr Thr Pro 705 710 715 720 Asp Ser Ser Arg Ser Met His Tyr Ala Thr Asp Tyr Ala Lys Ala Phe 725 730 735 Gly Cys Pro Val Phe His Val Asn Gly Asp Asp Pro Glu Ala Val Val 740 745 750 Trp Val Gly Gln Leu Ala Thr Glu Tyr Arg Arg Arg Phe Gly Lys Asp 755 760 765 Val Phe Ile Asp Leu Val Cys Tyr Arg Leu Arg Gly His Asn Glu Ala 770 775 780 Asp Asp Pro Ser Met Thr Gln Pro Lys Met Tyr Glu Leu Ile Thr Gly 785 790 795 800 Arg Glu Thr Val Arg Ala Gln Tyr Thr Glu Asp Leu Leu Gly Arg Gly 805 810 815 Asp Leu Ser Asn Glu Asp Ala Glu Ala Val Val Arg Asp Phe His Asp 820 825 830 Gln Met Glu Ser Val Phe Asn Glu Val Lys Glu Gly Gly Lys Lys Gln 835 840 845 Ala Glu Ala Gln Thr Gly Ile Thr Gly Ser Gln Lys Leu Pro His Gly 850 855 860 Leu Glu Thr Asn Ile Ser Arg Glu Glu Leu Leu Glu Leu Gly Gln Ala 865 870 875 880 Phe Ala Asn Thr Pro Glu Gly Phe Asn Tyr His Pro Arg Val Ala Pro 885 890 895 Val Ala Lys Lys Arg Val Ser Ser Val Thr Glu Gly Gly Ile Asp Trp 900 905 910 Ala Trp Gly Glu Leu Leu Ala Phe Gly Ser Leu Ala Asn Ser Gly Arg 915 920 925 Leu Val Arg Leu Ala Gly Glu Asp Ser Arg Arg Gly Thr Phe Thr Gln 930 935 940 Arg His Ala Val Ala Ile Asp Pro Ala Thr Ala Glu Glu Phe Asn Pro 945 950 955 960 Leu His Glu Leu Ala Gln Ser Lys Gly Asn Asn Gly Lys Phe Leu Val 965 970 975 Tyr Asn Ser Ala Leu Thr Glu Tyr Ala Gly Met Gly Phe Glu Tyr Gly 980 985 990 Tyr Ser Val Gly Asn Glu Asp Ser Val Val Ala Trp Glu Ala Gln Phe 995 1000 1005 Gly Asp Phe Ala Asn Gly Ala Gln Thr Ile Ile Asp Glu Tyr Val 1010 1015 1020 Ser Ser Gly Glu Ala Lys Trp Gly Gln Thr Ser Lys Leu Ile Leu 1025 1030 1035 Leu Leu Pro His Gly Tyr Glu Gly Gln Gly Pro Asp His Ser Ser 1040 1045 1050 Ala Arg Ile Glu Arg Phe Leu Gln Leu Cys Ala Glu Gly Ser Met 1055 1060 1065 Thr Val Ala Gln Pro Ser Thr Pro Ala Asn His Phe His Leu Leu 1070 1075 1080 Arg Arg His Ala Leu Ser Asp Leu Lys Arg Pro Leu Val Ile Phe 1085 1090 1095 Thr Pro Lys Ser Met Leu Arg Asn Lys Ala Ala Ala Ser Ala Pro 1100 1105 1110 Glu Asp Phe Thr Glu Val Thr Lys Phe Gln Ser Val Ile Asp Asp 1115 1120 1125 Pro Asn Val Ala Asp Ala Ala Lys Val Lys Lys Val Met Leu Val 1130 1135 1140 Ser Gly Lys Leu Tyr Tyr Glu Leu Ala Lys Arg Lys Glu Lys Asp 1145 1150 1155 Gly Arg Asp Asp Ile Ala Ile Val Arg Ile Glu Met Leu His Pro 1160 1165 1170 Ile Pro Phe Asn Arg Ile Ser Glu Ala Leu Ala Gly Tyr Pro Asn 1175 1180 1185 Ala Glu Glu Val Leu Phe Val Gln Asp Glu Pro Ala Asn Gln Gly 1190 1195 1200 Pro Trp Pro Phe Tyr Gln Glu His Leu Pro Glu Leu Ile Pro Asn 1205 1210 1215 Met Pro Lys Met Arg Arg Val Ser Arg Arg Ala Gln Ser Ser Thr 1220 1225 1230 Ala Thr Gly Val Ala Lys Val His Gln Leu Glu Glu Lys Gln Leu 1235 1240 1245 Ile Asp Glu Ala Phe Glu Ala 1250 1255 15 4385 DNA Corynebacterium glutamicum CDS (443)..(4213) 15 gtcgacaagc aaaatcgaag cggcagcacg ccgcgtcgga gccttaaacg ccatcgccgc 60 catccctgat ggtttcaatc atcaagtcgg tgaacgcggg cgcaacctgt catccggaca 120 gcgccaactg atcgcgctgg cgcgcgccga actcatcgag ccttccatca tgcttctcga 180 cgaagccacc tccaccctcg accccgccac cgaagccgtt atcctcaacg cctccgatcg 240 agtcactaag ggacgcacca gcatcatcgt cgcgcaccgc ttggcaaccg ctaaaagggc 300 cgaccgtatt cttgttgttg aacaaggacg tatcattgag gacggatctc acgacgcgtt 360 gttgtctgct aacggcacct acgcccgcat gtggcattta atggcctgac acgttatttt 420 taggagaact gtcaacaaat ta atg cta caa ctg ggg ctt agg cat aat cag 472 Met Leu Gln Leu Gly Leu Arg His Asn Gln 1 5 10 cca acg acc aac gtt aca gtg gat aaa ata aag ctc aat aaa ccc tca 520 Pro Thr Thr Asn Val Thr Val Asp Lys Ile Lys Leu Asn Lys Pro Ser 15 20 25 aga agc aag gaa aag agg cga gta cct gcc gtg agc agc gct agt act 568 Arg Ser Lys Glu Lys Arg Arg Val Pro Ala Val Ser Ser Ala Ser Thr 30 35 40 ttc ggc cag aat gcg tgg ctg gta gac gag atg ttc cag cag ttc cag 616 Phe Gly Gln Asn Ala Trp Leu Val Asp Glu Met Phe Gln Gln Phe Gln 45 50 55 aag gac ccc aag tcc gtg gac aag gaa tgg aga gaa ctc ttt gag gcg 664 Lys Asp Pro Lys Ser Val Asp Lys Glu Trp Arg Glu Leu Phe Glu Ala 60 65 70 cag ggg gga cca aat gct acc ccc gct aca aca gaa gca cag cct tca 712 Gln Gly Gly Pro Asn Ala Thr Pro Ala Thr Thr Glu Ala Gln Pro Ser 75 80 85 90 gcg ccc aag gag tct gcg aaa cca gca cca aag gct gcc cct gca gcc 760 Ala Pro Lys Glu Ser Ala Lys Pro Ala Pro Lys Ala Ala Pro Ala Ala 95 100 105 aag gca gca ccg cgc gta gaa acc aag ccg gcc gcc aag acc gcc cct 808 Lys Ala Ala Pro Arg Val Glu Thr Lys Pro Ala Ala Lys Thr Ala Pro 110 115 120 aag gcc aag gag tcc tca gtg cca cag caa cct aag ctt ccg gag cca 856 Lys Ala Lys Glu Ser Ser Val Pro Gln Gln Pro Lys Leu Pro Glu Pro 125 130 135 gga caa acc cca atc agg ggt att ttc aag tcc atc gcg aag aac atg 904 Gly Gln Thr Pro Ile Arg Gly Ile Phe Lys Ser Ile Ala Lys Asn Met 140 145 150 gat atc tcc ctg gaa atc cca acc gca acc tcg gtt cgc gat atg cca 952 Asp Ile Ser Leu Glu Ile Pro Thr Ala Thr Ser Val Arg Asp Met Pro 155 160 165 170 gct cgc ctc atg ttc gaa aac cgc gcg atg gtc aac gat cag ctc aag 1000 Ala Arg Leu Met Phe Glu Asn Arg Ala Met Val Asn Asp Gln Leu Lys 175 180 185 cgc acc cgc ggt ggc aag atc tcc ttc acc cac atc att ggc tac gcc 1048 Arg Thr Arg Gly Gly Lys Ile Ser Phe Thr His Ile Ile Gly Tyr Ala 190 195 200 atg gtg aag gca gtc atg gct cac ccg gac atg aac aac tcc tac cat 1096 Met Val Lys Ala Val Met Ala His Pro Asp Met Asn Asn Ser Tyr His 205 210 215 cga cgg cag gcc cca acc ctg atc gtg cct gag cac atc aac ctg ggc 1144 Arg Arg Gln Ala Pro Thr Leu Ile Val Pro Glu His Ile Asn Leu Gly 220 225 230 ctt gcc atc gac ctt cct cag aag gac ggc tcc cgc gca ctt gtc gta 1192 Leu Ala Ile Asp Leu Pro Gln Lys Asp Gly Ser Arg Ala Leu Val Val 235 240 245 250 gca gcc atc aag gaa acc gag aag atg aac ttc tcc gag ttc ctc gca 1240 Ala Ala Ile Lys Glu Thr Glu Lys Met Asn Phe Ser Glu Phe Leu Ala 255 260 265 gca tac gaa gac atc gtg aca cgc tcc cgc aag ggc aag ctc acc atg 1288 Ala Tyr Glu Asp Ile Val Thr Arg Ser Arg Lys Gly Lys Leu Thr Met 270 275 280 gat gac tac cag ggc gtt acc gtt tcc ttg acc aac cca ggt ggc atc 1336 Asp Asp Tyr Gln Gly Val Thr Val Ser Leu Thr Asn Pro Gly Gly Ile 285 290 295 ggt acc cgc cac tct gtc cca cgt ctg acc aag ggc cag ggc acc atc 1384 Gly Thr Arg His Ser Val Pro Arg Leu Thr Lys Gly Gln Gly Thr Ile 300 305 310 atc ggt gtc ggt tcc atg gat tac cca gca gag ttc cag ggc gct tcc 1432 Ile Gly Val Gly Ser Met Asp Tyr Pro Ala Glu Phe Gln Gly Ala Ser 315 320 325 330 gaa gac cgc ctt gca gag ctc ggc gtt gga aag ctt gtc acc atc acc 1480 Glu Asp Arg Leu Ala Glu Leu Gly Val Gly Lys Leu Val Thr Ile Thr 335 340 345 tcc acc tac gat cac cgc gtg atc cag ggt gct gtg tcc ggt gaa ttc 1528 Ser Thr Tyr Asp His Arg Val Ile Gln Gly Ala Val Ser Gly Glu Phe 350 355 360 ctg cgt acc atg tct cgc ctg ctc acc gat gat tcc ttc tgg gat gag 1576 Leu Arg Thr Met Ser Arg Leu Leu Thr Asp Asp Ser Phe Trp Asp Glu 365 370 375 atc ttc gac gca atg aac gtt cct tac acc cca atg cgt tgg gca cag 1624 Ile Phe Asp Ala Met Asn Val Pro Tyr Thr Pro Met Arg Trp Ala Gln 380 385 390 gac gtt cca aac acc ggt gtt gat aag aac acc cgc gtc atg cag ctc 1672 Asp Val Pro Asn Thr Gly Val Asp Lys Asn Thr Arg Val Met Gln Leu 395 400 405 410 att gag gca tac cgc tcc cgt gga cac ctc atc gct gac acc aac cca 1720 Ile Glu Ala Tyr Arg Ser Arg Gly His Leu Ile Ala Asp Thr Asn Pro 415 420 425 ctt tca tgg gtt cag cct ggc atg cca gtt cca gac cac cgc gac ctc 1768 Leu Ser Trp Val Gln Pro Gly Met Pro Val Pro Asp His Arg Asp Leu 430 435 440 gac atc gag acc cac agc ctg acc atc tgg gat ctg gac cgt acc ttc 1816 Asp Ile Glu Thr His Ser Leu Thr Ile Trp Asp Leu Asp Arg Thr Phe 445 450 455 agc gtc ggt ggc ttc ggc ggc aag gag acc atg acc ctg cgc gag gta 1864 Ser Val Gly Gly Phe Gly Gly Lys Glu Thr Met Thr Leu Arg Glu Val 460 465 470 ctg tcc cgc ctg cgc gct gcc tac acc ttg aag gtc ggc tcc gaa tac 1912 Leu Ser Arg Leu Arg Ala Ala Tyr Thr Leu Lys Val Gly Ser Glu Tyr 475 480 485 490 acc cac atc ctg gac cgc gac gag cgc acc tgg ctg cag gac cgc ctc 1960 Thr His Ile Leu Asp Arg Asp Glu Arg Thr Trp Leu Gln Asp Arg Leu 495 500 505 gaa gcc gga atg cca aag cca acc cag gca gag cag aag tac atc ctg 2008 Glu Ala Gly Met Pro Lys Pro Thr Gln Ala Glu Gln Lys Tyr Ile Leu 510 515 520 cag aag ctg aac gcc gca gag gct ttc gag aac ttc ctg cag acc aag 2056 Gln Lys Leu Asn Ala Ala Glu Ala Phe Glu Asn Phe Leu Gln Thr Lys 525 530 535 tac gtc ggc cag aag cgc ttc tcc ctc gaa ggt gca gaa gct ctc atc 2104 Tyr Val Gly Gln Lys Arg Phe Ser Leu Glu Gly Ala Glu Ala Leu Ile 540 545 550 cca ctg atg gac tcc gcc atc gac acc gcc gca ggc cag ggc ctc gac 2152 Pro Leu Met Asp Ser Ala Ile Asp Thr Ala Ala Gly Gln Gly Leu Asp 555 560 565 570 gaa gtt gtc atc ggt atg cca cac cgt ggt cgc ctc aac gtg ctg ttc 2200 Glu Val Val Ile Gly Met Pro His Arg Gly Arg Leu Asn Val Leu Phe 575 580 585 aac atc gtg ggc aag cca ctg gca tcc atc ttc aac gag ttt gaa ggc 2248 Asn Ile Val Gly Lys Pro Leu Ala Ser Ile Phe Asn Glu Phe Glu Gly 590 595 600 caa atg gag cag ggc cag atc ggt ggc tcc ggt gac gtg aag tac cac 2296 Gln Met Glu Gln Gly Gln Ile Gly Gly Ser Gly Asp Val Lys Tyr His 605 610 615 ctc ggt tcc gaa ggc cag cac ctg cag atg ttc ggc gac ggc gag atc 2344 Leu Gly Ser Glu Gly Gln His Leu Gln Met Phe Gly Asp Gly Glu Ile 620 625 630 aag gtc tcc ctg act gct aac ccg tcc cac ctg gaa gct gtt aac cca 2392 Lys Val Ser Leu Thr Ala Asn Pro Ser His Leu Glu Ala Val Asn Pro 635 640 645 650 gtg atg gaa ggt atc gtc cgc gca aag cag gac tac ctg gac aag ggc 2440 Val Met Glu Gly Ile Val Arg Ala Lys Gln Asp Tyr Leu Asp Lys Gly 655 660 665 gta gac ggc aag act gtt gtg cca ctg ctg ctc cac ggt gac gct gca 2488 Val Asp Gly Lys Thr Val Val Pro Leu Leu Leu His Gly Asp Ala Ala 670 675 680 ttc gca ggc ctg ggc atc gtg cca gaa acc atc aac ctg gct aag cgc 2536 Phe Ala Gly Leu Gly Ile Val Pro Glu Thr Ile Asn Leu Ala Lys Arg 685 690 695 gtc gac gtc gga ggc acc atc cac atc gtg gtg aac aac cag atc ggc 2584 Val Asp Val Gly Gly Thr Ile His Ile Val Val Asn Asn Gln Ile Gly 700 705 710 ttc acc acc acc cca gac tcc agc cgc tcc atg cac tac gca acc gac 2632 Phe Thr Thr Thr Pro Asp Ser Ser Arg Ser Met His Tyr Ala Thr Asp 715 720 725 730 tac gcc aag gca ttc ggc tgc cca gtc ttc cac gtc aat ggt gat gac 2680 Tyr Ala Lys Ala Phe Gly Cys Pro Val Phe His Val Asn Gly Asp Asp 735 740 745 cca gag gca gtt gtc tgg gtt ggc cag ctg gca acc gag tac cgt cgt 2728 Pro Glu Ala Val Val Trp Val Gly Gln Leu Ala Thr Glu Tyr Arg Arg 750 755 760 cgc ttc ggc aag gac gtc ttc atc gac ctc gtt tgc tac cgc ctc cgc 2776 Arg Phe Gly Lys Asp Val Phe Ile Asp Leu Val Cys Tyr Arg Leu Arg 765 770 775 ggc cac aac gaa gct gat gat cct tcc atg acc cag cca aag atg tat 2824 Gly His Asn Glu Ala Asp Asp Pro Ser Met Thr Gln Pro Lys Met Tyr 780 785 790 gag ctc atc acc ggc cgc gag acc gtt cgt gct cag tac acc gaa gac 2872 Glu Leu Ile Thr Gly Arg Glu Thr Val Arg Ala Gln Tyr Thr Glu Asp 795 800 805 810 ctg ctc gga cgt gga gac ctc tcc aac gaa gat gca gaa gca gtc gtc 2920 Leu Leu Gly Arg Gly Asp Leu Ser Asn Glu Asp Ala Glu Ala Val Val 815 820 825 cgc gac ttc cac gac cag atg gaa tct gtg ttc aac gaa gtc aag gaa 2968 Arg Asp Phe His Asp Gln Met Glu Ser Val Phe Asn Glu Val Lys Glu 830 835 840 ggc ggc aag aag cag gct gag gca cag acc ggc atc acc ggc tcc cag 3016 Gly Gly Lys Lys Gln Ala Glu Ala Gln Thr Gly Ile Thr Gly Ser Gln 845 850 855 aag ctt cca cac ggc ctt gag acc aac atc tcc cgt gaa gag ctc ctg 3064 Lys Leu Pro His Gly Leu Glu Thr Asn Ile Ser Arg Glu Glu Leu Leu 860 865 870 gaa ctg gga cag gct ttc gcc aac acc cca gaa ggc ttc aac tac cac 3112 Glu Leu Gly Gln Ala Phe Ala Asn Thr Pro Glu Gly Phe Asn Tyr His 875 880 885 890 cca cgt gtg gct cca gtt gct aag aag cgc gtc tcc tct gtc acc gaa 3160 Pro Arg Val Ala Pro Val Ala Lys Lys Arg Val Ser Ser Val Thr Glu 895 900 905 ggt ggc atc gac tgg gca tgg ggc gag ctc ctc gcc ttc ggt tcc ctg 3208 Gly Gly Ile Asp Trp Ala Trp Gly Glu Leu Leu Ala Phe Gly Ser Leu 910 915 920 gct aac tcc ggc cgc ttg gtt cgc ctt gca ggt gaa gat tcc cgc cgc 3256 Ala Asn Ser Gly Arg Leu Val Arg Leu Ala Gly Glu Asp Ser Arg Arg 925 930 935 ggt acc ttc acc cag cgc cac gca gtt gcc atc gac cca gcg acc gct 3304 Gly Thr Phe Thr Gln Arg His Ala Val Ala Ile Asp Pro Ala Thr Ala 940 945 950 gaa gag ttc aac cca ctc cac gag ctt gca cag tcc aag ggc aac aac 3352 Glu Glu Phe Asn Pro Leu His Glu Leu Ala Gln Ser Lys Gly Asn Asn 955 960 965 970 ggt aag ttc ctg gtc tac aac tcc gca ctg acc gag tac gca ggc atg 3400 Gly Lys Phe Leu Val Tyr Asn Ser Ala Leu Thr Glu Tyr Ala Gly Met 975 980 985 ggc ttc gag tac ggc tac tcc gta gga aac gaa gac tcc gtc gtt gca 3448 Gly Phe Glu Tyr Gly Tyr Ser Val Gly Asn Glu Asp Ser Val Val Ala 990 995 1000 tgg gaa gca cag ttc ggc gac ttc gcc aac ggc gct cag acc atc 3493 Trp Glu Ala Gln Phe Gly Asp Phe Ala Asn Gly Ala Gln Thr Ile 1005 1010 1015 atc gat gag tac gtc tcc tca ggc gaa gct aag tgg ggc cag acc 3538 Ile Asp Glu Tyr Val Ser Ser Gly Glu Ala Lys Trp Gly Gln Thr 1020 1025 1030 tcc aag ctg atc ctt ctg ctg cct cac ggc tac gaa ggc cag ggc 3583 Ser Lys Leu Ile Leu Leu Leu Pro His Gly Tyr Glu Gly Gln Gly 1035 1040 1045 cca gac cac tct tcc gca cgt atc gag cgc ttc ctg cag ctg tgc 3628 Pro Asp His Ser Ser Ala Arg Ile Glu Arg Phe Leu Gln Leu Cys 1050 1055 1060 gct gag ggt tcc atg act gtt gct cag cca tcc acc cca gca aac 3673 Ala Glu Gly Ser Met Thr Val Ala Gln

Pro Ser Thr Pro Ala Asn 1065 1070 1075 cac ttc cac ctg ctg cgt cgt cac gct ctg tcc gac ctg aag cgt 3718 His Phe His Leu Leu Arg Arg His Ala Leu Ser Asp Leu Lys Arg 1080 1085 1090 cca ctg gtt atc ttc acc ccg aag tcc atg ctg cgt aac aag gct 3763 Pro Leu Val Ile Phe Thr Pro Lys Ser Met Leu Arg Asn Lys Ala 1095 1100 1105 gct gcc tcc gca cca gaa gac ttc act gag gtc acc aag ttc caa 3808 Ala Ala Ser Ala Pro Glu Asp Phe Thr Glu Val Thr Lys Phe Gln 1110 1115 1120 tcc gtg atc gac gat cca aac gtt gca gat gca gcc aag gtg aag 3853 Ser Val Ile Asp Asp Pro Asn Val Ala Asp Ala Ala Lys Val Lys 1125 1130 1135 aag gtc atg ctg gtc tcc ggc aag ctg tac tac gaa ttg gca aag 3898 Lys Val Met Leu Val Ser Gly Lys Leu Tyr Tyr Glu Leu Ala Lys 1140 1145 1150 cgc aag gag aag gac gga cgc gac gac atc gcg atc gtt cgt atc 3943 Arg Lys Glu Lys Asp Gly Arg Asp Asp Ile Ala Ile Val Arg Ile 1155 1160 1165 gaa atg ctc cac cca att ccg ttc aac cgc atc tcc gag gct ctt 3988 Glu Met Leu His Pro Ile Pro Phe Asn Arg Ile Ser Glu Ala Leu 1170 1175 1180 gcc ggc tac cct aac gct gag gaa gtc ctc ttc gtt cag gat gag 4033 Ala Gly Tyr Pro Asn Ala Glu Glu Val Leu Phe Val Gln Asp Glu 1185 1190 1195 cca gca aac cag ggc cca tgg ccg ttc tac cag gag cac ctc cca 4078 Pro Ala Asn Gln Gly Pro Trp Pro Phe Tyr Gln Glu His Leu Pro 1200 1205 1210 gag ctg atc ccg aac atg cca aag atg cgc cgc gtt tcc cgc cgc 4123 Glu Leu Ile Pro Asn Met Pro Lys Met Arg Arg Val Ser Arg Arg 1215 1220 1225 gct cag tcc tcc acc gca act ggt gtt gct aag gtg cac cag ctg 4168 Ala Gln Ser Ser Thr Ala Thr Gly Val Ala Lys Val His Gln Leu 1230 1235 1240 gag gag aag cag ctt atc gac gag gct ttc gag gct taa gtc ttt 4213 Glu Glu Lys Gln Leu Ile Asp Glu Ala Phe Glu Ala Val Phe 1245 1250 1255 atagtcctgc actagcctag agggccttat gcagtgtgaa tcacacagca taaggccctt 4273 tttgctgccg tggttgccta aggtggaagg catgaaacga atctgtgcgg tcacgatctc 4333 ttcagtactt ttgctaagtg gctgctcctc cacttccacc acgcagctcg ag 4385 16 1254 PRT Corynebacterium glutamicum 16 Met Leu Gln Leu Gly Leu Arg His Asn Gln Pro Thr Thr Asn Val Thr 1 5 10 15 Val Asp Lys Ile Lys Leu Asn Lys Pro Ser Arg Ser Lys Glu Lys Arg 20 25 30 Arg Val Pro Ala Val Ser Ser Ala Ser Thr Phe Gly Gln Asn Ala Trp 35 40 45 Leu Val Asp Glu Met Phe Gln Gln Phe Gln Lys Asp Pro Lys Ser Val 50 55 60 Asp Lys Glu Trp Arg Glu Leu Phe Glu Ala Gln Gly Gly Pro Asn Ala 65 70 75 80 Thr Pro Ala Thr Thr Glu Ala Gln Pro Ser Ala Pro Lys Glu Ser Ala 85 90 95 Lys Pro Ala Pro Lys Ala Ala Pro Ala Ala Lys Ala Ala Pro Arg Val 100 105 110 Glu Thr Lys Pro Ala Ala Lys Thr Ala Pro Lys Ala Lys Glu Ser Ser 115 120 125 Val Pro Gln Gln Pro Lys Leu Pro Glu Pro Gly Gln Thr Pro Ile Arg 130 135 140 Gly Ile Phe Lys Ser Ile Ala Lys Asn Met Asp Ile Ser Leu Glu Ile 145 150 155 160 Pro Thr Ala Thr Ser Val Arg Asp Met Pro Ala Arg Leu Met Phe Glu 165 170 175 Asn Arg Ala Met Val Asn Asp Gln Leu Lys Arg Thr Arg Gly Gly Lys 180 185 190 Ile Ser Phe Thr His Ile Ile Gly Tyr Ala Met Val Lys Ala Val Met 195 200 205 Ala His Pro Asp Met Asn Asn Ser Tyr His Arg Arg Gln Ala Pro Thr 210 215 220 Leu Ile Val Pro Glu His Ile Asn Leu Gly Leu Ala Ile Asp Leu Pro 225 230 235 240 Gln Lys Asp Gly Ser Arg Ala Leu Val Val Ala Ala Ile Lys Glu Thr 245 250 255 Glu Lys Met Asn Phe Ser Glu Phe Leu Ala Ala Tyr Glu Asp Ile Val 260 265 270 Thr Arg Ser Arg Lys Gly Lys Leu Thr Met Asp Asp Tyr Gln Gly Val 275 280 285 Thr Val Ser Leu Thr Asn Pro Gly Gly Ile Gly Thr Arg His Ser Val 290 295 300 Pro Arg Leu Thr Lys Gly Gln Gly Thr Ile Ile Gly Val Gly Ser Met 305 310 315 320 Asp Tyr Pro Ala Glu Phe Gln Gly Ala Ser Glu Asp Arg Leu Ala Glu 325 330 335 Leu Gly Val Gly Lys Leu Val Thr Ile Thr Ser Thr Tyr Asp His Arg 340 345 350 Val Ile Gln Gly Ala Val Ser Gly Glu Phe Leu Arg Thr Met Ser Arg 355 360 365 Leu Leu Thr Asp Asp Ser Phe Trp Asp Glu Ile Phe Asp Ala Met Asn 370 375 380 Val Pro Tyr Thr Pro Met Arg Trp Ala Gln Asp Val Pro Asn Thr Gly 385 390 395 400 Val Asp Lys Asn Thr Arg Val Met Gln Leu Ile Glu Ala Tyr Arg Ser 405 410 415 Arg Gly His Leu Ile Ala Asp Thr Asn Pro Leu Ser Trp Val Gln Pro 420 425 430 Gly Met Pro Val Pro Asp His Arg Asp Leu Asp Ile Glu Thr His Ser 435 440 445 Leu Thr Ile Trp Asp Leu Asp Arg Thr Phe Ser Val Gly Gly Phe Gly 450 455 460 Gly Lys Glu Thr Met Thr Leu Arg Glu Val Leu Ser Arg Leu Arg Ala 465 470 475 480 Ala Tyr Thr Leu Lys Val Gly Ser Glu Tyr Thr His Ile Leu Asp Arg 485 490 495 Asp Glu Arg Thr Trp Leu Gln Asp Arg Leu Glu Ala Gly Met Pro Lys 500 505 510 Pro Thr Gln Ala Glu Gln Lys Tyr Ile Leu Gln Lys Leu Asn Ala Ala 515 520 525 Glu Ala Phe Glu Asn Phe Leu Gln Thr Lys Tyr Val Gly Gln Lys Arg 530 535 540 Phe Ser Leu Glu Gly Ala Glu Ala Leu Ile Pro Leu Met Asp Ser Ala 545 550 555 560 Ile Asp Thr Ala Ala Gly Gln Gly Leu Asp Glu Val Val Ile Gly Met 565 570 575 Pro His Arg Gly Arg Leu Asn Val Leu Phe Asn Ile Val Gly Lys Pro 580 585 590 Leu Ala Ser Ile Phe Asn Glu Phe Glu Gly Gln Met Glu Gln Gly Gln 595 600 605 Ile Gly Gly Ser Gly Asp Val Lys Tyr His Leu Gly Ser Glu Gly Gln 610 615 620 His Leu Gln Met Phe Gly Asp Gly Glu Ile Lys Val Ser Leu Thr Ala 625 630 635 640 Asn Pro Ser His Leu Glu Ala Val Asn Pro Val Met Glu Gly Ile Val 645 650 655 Arg Ala Lys Gln Asp Tyr Leu Asp Lys Gly Val Asp Gly Lys Thr Val 660 665 670 Val Pro Leu Leu Leu His Gly Asp Ala Ala Phe Ala Gly Leu Gly Ile 675 680 685 Val Pro Glu Thr Ile Asn Leu Ala Lys Arg Val Asp Val Gly Gly Thr 690 695 700 Ile His Ile Val Val Asn Asn Gln Ile Gly Phe Thr Thr Thr Pro Asp 705 710 715 720 Ser Ser Arg Ser Met His Tyr Ala Thr Asp Tyr Ala Lys Ala Phe Gly 725 730 735 Cys Pro Val Phe His Val Asn Gly Asp Asp Pro Glu Ala Val Val Trp 740 745 750 Val Gly Gln Leu Ala Thr Glu Tyr Arg Arg Arg Phe Gly Lys Asp Val 755 760 765 Phe Ile Asp Leu Val Cys Tyr Arg Leu Arg Gly His Asn Glu Ala Asp 770 775 780 Asp Pro Ser Met Thr Gln Pro Lys Met Tyr Glu Leu Ile Thr Gly Arg 785 790 795 800 Glu Thr Val Arg Ala Gln Tyr Thr Glu Asp Leu Leu Gly Arg Gly Asp 805 810 815 Leu Ser Asn Glu Asp Ala Glu Ala Val Val Arg Asp Phe His Asp Gln 820 825 830 Met Glu Ser Val Phe Asn Glu Val Lys Glu Gly Gly Lys Lys Gln Ala 835 840 845 Glu Ala Gln Thr Gly Ile Thr Gly Ser Gln Lys Leu Pro His Gly Leu 850 855 860 Glu Thr Asn Ile Ser Arg Glu Glu Leu Leu Glu Leu Gly Gln Ala Phe 865 870 875 880 Ala Asn Thr Pro Glu Gly Phe Asn Tyr His Pro Arg Val Ala Pro Val 885 890 895 Ala Lys Lys Arg Val Ser Ser Val Thr Glu Gly Gly Ile Asp Trp Ala 900 905 910 Trp Gly Glu Leu Leu Ala Phe Gly Ser Leu Ala Asn Ser Gly Arg Leu 915 920 925 Val Arg Leu Ala Gly Glu Asp Ser Arg Arg Gly Thr Phe Thr Gln Arg 930 935 940 His Ala Val Ala Ile Asp Pro Ala Thr Ala Glu Glu Phe Asn Pro Leu 945 950 955 960 His Glu Leu Ala Gln Ser Lys Gly Asn Asn Gly Lys Phe Leu Val Tyr 965 970 975 Asn Ser Ala Leu Thr Glu Tyr Ala Gly Met Gly Phe Glu Tyr Gly Tyr 980 985 990 Ser Val Gly Asn Glu Asp Ser Val Val Ala Trp Glu Ala Gln Phe Gly 995 1000 1005 Asp Phe Ala Asn Gly Ala Gln Thr Ile Ile Asp Glu Tyr Val Ser 1010 1015 1020 Ser Gly Glu Ala Lys Trp Gly Gln Thr Ser Lys Leu Ile Leu Leu 1025 1030 1035 Leu Pro His Gly Tyr Glu Gly Gln Gly Pro Asp His Ser Ser Ala 1040 1045 1050 Arg Ile Glu Arg Phe Leu Gln Leu Cys Ala Glu Gly Ser Met Thr 1055 1060 1065 Val Ala Gln Pro Ser Thr Pro Ala Asn His Phe His Leu Leu Arg 1070 1075 1080 Arg His Ala Leu Ser Asp Leu Lys Arg Pro Leu Val Ile Phe Thr 1085 1090 1095 Pro Lys Ser Met Leu Arg Asn Lys Ala Ala Ala Ser Ala Pro Glu 1100 1105 1110 Asp Phe Thr Glu Val Thr Lys Phe Gln Ser Val Ile Asp Asp Pro 1115 1120 1125 Asn Val Ala Asp Ala Ala Lys Val Lys Lys Val Met Leu Val Ser 1130 1135 1140 Gly Lys Leu Tyr Tyr Glu Leu Ala Lys Arg Lys Glu Lys Asp Gly 1145 1150 1155 Arg Asp Asp Ile Ala Ile Val Arg Ile Glu Met Leu His Pro Ile 1160 1165 1170 Pro Phe Asn Arg Ile Ser Glu Ala Leu Ala Gly Tyr Pro Asn Ala 1175 1180 1185 Glu Glu Val Leu Phe Val Gln Asp Glu Pro Ala Asn Gln Gly Pro 1190 1195 1200 Trp Pro Phe Tyr Gln Glu His Leu Pro Glu Leu Ile Pro Asn Met 1205 1210 1215 Pro Lys Met Arg Arg Val Ser Arg Arg Ala Gln Ser Ser Thr Ala 1220 1225 1230 Thr Gly Val Ala Lys Val His Gln Leu Glu Glu Lys Gln Leu Ile 1235 1240 1245 Asp Glu Ala Phe Glu Ala 1250 17 1800 DNA Corynebacterium glutamicum CDS (211)..(1620) 17 gatcctccgc attcagtaat ctttcccaca gcatcggctt gttctaaaac agcacggtgc 60 ttagaccgta cataaaacac ctgcatttct gtgcccattt gggcccggat gtgggtgttt 120 ttcattttct tccactctaa aattaagtat ggaaaaccaa ccgcacccgg atgcacgaca 180 atgacccact aaacacgtat ccttgaatgc gtg act gaa cat tat gac gta gta 234 Met Thr Glu His Tyr Asp Val Val 1 5 gta ctc gga gcc ggc ccc ggt ggc tat gtc tcc gcc atc cgt gca gcg 282 Val Leu Gly Ala Gly Pro Gly Gly Tyr Val Ser Ala Ile Arg Ala Ala 10 15 20 cag ctt ggc aag aag gtt gct gta att gag aag cag tac tgg ggt ggt 330 Gln Leu Gly Lys Lys Val Ala Val Ile Glu Lys Gln Tyr Trp Gly Gly 25 30 35 40 gtt tgc cta aac gtg ggc tgc att cct tcc aag tct ctg atc aaa aac 378 Val Cys Leu Asn Val Gly Cys Ile Pro Ser Lys Ser Leu Ile Lys Asn 45 50 55 gct gaa gtt gcc cat acc ttt acc cat gag aag aag acc ttc ggc atc 426 Ala Glu Val Ala His Thr Phe Thr His Glu Lys Lys Thr Phe Gly Ile 60 65 70 aat ggc gaa gtg acc ttc aac tat gag gat gct cac aag cgt tcc cgt 474 Asn Gly Glu Val Thr Phe Asn Tyr Glu Asp Ala His Lys Arg Ser Arg 75 80 85 ggc gtt tcc gac aag atc gtt gga ggc gtt cat tac ttg atg aag aag 522 Gly Val Ser Asp Lys Ile Val Gly Gly Val His Tyr Leu Met Lys Lys 90 95 100 aac aag atc atc gaa att cat ggt ctt gga aac ttc aag gat gct aag 570 Asn Lys Ile Ile Glu Ile His Gly Leu Gly Asn Phe Lys Asp Ala Lys 105 110 115 120 act ctt gag gtc acc gac ggt aag gat gct ggc aag acc atc acc ttt 618 Thr Leu Glu Val Thr Asp Gly Lys Asp Ala Gly Lys Thr Ile Thr Phe 125 130 135 gat gac tgc atc atc gca acc ggt tcg gta gtc aac acc ctc cgt ggc 666 Asp Asp Cys Ile Ile Ala Thr Gly Ser Val Val Asn Thr Leu Arg Gly 140 145 150 gtt gac ttc tca gag aac gtt gtg tct ttt gaa gag cag att ctt aac 714 Val Asp Phe Ser Glu Asn Val Val Ser Phe Glu Glu Gln Ile Leu Asn 155 160 165 cct gtt gcg cca aag aag atg gtc att gtt ggt gca ggc gca att gga 762 Pro Val Ala Pro Lys Lys Met Val Ile Val Gly Ala Gly Ala Ile Gly 170 175 180 atg gaa ttc gcc tac gtt ctt ggt aac tac ggt gta gat gta acc gtc 810 Met Glu Phe Ala Tyr Val Leu Gly Asn Tyr Gly Val Asp Val Thr Val 185 190 195 200 atc gag ttc atg gat cgt gtg ctt cca aat gaa gat gct gaa gtc tcc 858 Ile Glu Phe Met Asp Arg Val Leu Pro Asn Glu Asp Ala Glu Val Ser 205 210 215 aag gtt att gca aag gcc tac aag aag atg ggc gtt aag ctt ctt cct 906 Lys Val Ile Ala Lys Ala Tyr Lys Lys Met Gly Val Lys Leu Leu Pro 220 225 230 ggc cat gca acc act gct gtt cgg gac aac ggt gac ttt gtc gag gtt 954 Gly His Ala Thr Thr Ala Val Arg Asp Asn Gly Asp Phe Val Glu Val 235 240 245 gat tac cag aag aag ggc tct gac aag aca gag act ctt act gtt gat 1002 Asp Tyr Gln Lys Lys Gly Ser Asp Lys Thr Glu Thr Leu Thr Val Asp 250 255 260 cga gtc atg gtt tcc gtt ggt ttc cgt cca cgc gtt gag gga ttt ggt 1050 Arg Val Met Val Ser Val Gly Phe Arg Pro Arg Val Glu Gly Phe Gly 265 270 275 280 ctt gaa aac act ggc gtt aag ctc acc gag cgt ggc gca atc gag atc 1098 Leu Glu Asn Thr Gly Val Lys Leu Thr Glu Arg Gly Ala Ile Glu Ile 285 290 295 gat gat tac atg cgt acc aac gtc gat ggc att tac gcc atc ggt gac 1146 Asp Asp Tyr Met Arg Thr Asn Val Asp Gly Ile Tyr Ala Ile Gly Asp 300 305 310 gtg acc gcc aag ctt cag ctt gct cac gtc gca gaa gca cag ggc att 1194 Val Thr Ala Lys Leu Gln Leu Ala His Val Ala Glu Ala Gln Gly Ile 315 320 325 gtt gcc gca gag act att gct ggt gca gaa act cag act ctt ggt gat 1242 Val Ala Ala Glu Thr Ile Ala Gly Ala Glu Thr Gln Thr Leu Gly Asp 330 335 340 tac atg atg atg cca cgt gca acc ttc tgc aac cca cag gtt tct tcc 1290 Tyr Met Met Met Pro Arg Ala Thr Phe Cys Asn Pro Gln Val Ser Ser 345 350 355 360 ttt ggt tac acc gaa gag cag gcc aag gag aag tgg cca gat cgt gag 1338 Phe Gly Tyr Thr Glu Glu Gln Ala Lys Glu Lys Trp Pro Asp Arg Glu 365 370 375 atc aag gtt gct tcc ctc cca ttc tct gca aac ggt aaa gca gtt ggc 1386 Ile Lys Val Ala Ser Leu Pro Phe Ser Ala Asn Gly Lys Ala Val Gly 380 385 390 ctg gca gaa act gat ggt ttc gca aag atc gtt gct gat gca gaa ttc 1434 Leu Ala Glu Thr Asp Gly Phe Ala Lys Ile Val Ala Asp Ala Glu Phe 395 400 405 ggt gag ctg ctc ggt gca cac ctg gtt gga gca aat gca tca gag ctc 1482 Gly Glu Leu Leu Gly Ala His Leu Val Gly Ala Asn Ala Ser Glu Leu 410 415 420 atc aat gaa ttg gtg ctt gct cag aac tgg gat ctc acc act gaa gag 1530 Ile Asn Glu Leu Val Leu Ala Gln Asn Trp Asp Leu Thr Thr Glu Glu 425 430 435 440 atc tct cgt agc gtc cat att cac cca acg cta tct gag gca gtt aag 1578 Ile Ser Arg Ser Val His Ile His Pro Thr Leu Ser Glu Ala Val Lys 445 450 455 gaa gct gca cac ggt atc tct gga cac atg atc aac ttc tag 1620 Glu Ala Ala His Gly Ile Ser Gly His Met Ile Asn Phe 460 465 aatccacctc gttggccctg tttctgtatg gaaacagggc caaaaccgat tttcaatcca 1680 aaccgagtgc tggttagtgc tcatactcac acaaactttt cgattatcaa agagaattat 1740 ttctaaaatt cggtatcgtc taagaaatga gtttgccaat agctcagcat caaaatgctg 1800 18 469 PRT Corynebacterium

glutamicum 18 Met Thr Glu His Tyr Asp Val Val Val Leu Gly Ala Gly Pro Gly Gly 1 5 10 15 Tyr Val Ser Ala Ile Arg Ala Ala Gln Leu Gly Lys Lys Val Ala Val 20 25 30 Ile Glu Lys Gln Tyr Trp Gly Gly Val Cys Leu Asn Val Gly Cys Ile 35 40 45 Pro Ser Lys Ser Leu Ile Lys Asn Ala Glu Val Ala His Thr Phe Thr 50 55 60 His Glu Lys Lys Thr Phe Gly Ile Asn Gly Glu Val Thr Phe Asn Tyr 65 70 75 80 Glu Asp Ala His Lys Arg Ser Arg Gly Val Ser Asp Lys Ile Val Gly 85 90 95 Gly Val His Tyr Leu Met Lys Lys Asn Lys Ile Ile Glu Ile His Gly 100 105 110 Leu Gly Asn Phe Lys Asp Ala Lys Thr Leu Glu Val Thr Asp Gly Lys 115 120 125 Asp Ala Gly Lys Thr Ile Thr Phe Asp Asp Cys Ile Ile Ala Thr Gly 130 135 140 Ser Val Val Asn Thr Leu Arg Gly Val Asp Phe Ser Glu Asn Val Val 145 150 155 160 Ser Phe Glu Glu Gln Ile Leu Asn Pro Val Ala Pro Lys Lys Met Val 165 170 175 Ile Val Gly Ala Gly Ala Ile Gly Met Glu Phe Ala Tyr Val Leu Gly 180 185 190 Asn Tyr Gly Val Asp Val Thr Val Ile Glu Phe Met Asp Arg Val Leu 195 200 205 Pro Asn Glu Asp Ala Glu Val Ser Lys Val Ile Ala Lys Ala Tyr Lys 210 215 220 Lys Met Gly Val Lys Leu Leu Pro Gly His Ala Thr Thr Ala Val Arg 225 230 235 240 Asp Asn Gly Asp Phe Val Glu Val Asp Tyr Gln Lys Lys Gly Ser Asp 245 250 255 Lys Thr Glu Thr Leu Thr Val Asp Arg Val Met Val Ser Val Gly Phe 260 265 270 Arg Pro Arg Val Glu Gly Phe Gly Leu Glu Asn Thr Gly Val Lys Leu 275 280 285 Thr Glu Arg Gly Ala Ile Glu Ile Asp Asp Tyr Met Arg Thr Asn Val 290 295 300 Asp Gly Ile Tyr Ala Ile Gly Asp Val Thr Ala Lys Leu Gln Leu Ala 305 310 315 320 His Val Ala Glu Ala Gln Gly Ile Val Ala Ala Glu Thr Ile Ala Gly 325 330 335 Ala Glu Thr Gln Thr Leu Gly Asp Tyr Met Met Met Pro Arg Ala Thr 340 345 350 Phe Cys Asn Pro Gln Val Ser Ser Phe Gly Tyr Thr Glu Glu Gln Ala 355 360 365 Lys Glu Lys Trp Pro Asp Arg Glu Ile Lys Val Ala Ser Leu Pro Phe 370 375 380 Ser Ala Asn Gly Lys Ala Val Gly Leu Ala Glu Thr Asp Gly Phe Ala 385 390 395 400 Lys Ile Val Ala Asp Ala Glu Phe Gly Glu Leu Leu Gly Ala His Leu 405 410 415 Val Gly Ala Asn Ala Ser Glu Leu Ile Asn Glu Leu Val Leu Ala Gln 420 425 430 Asn Trp Asp Leu Thr Thr Glu Glu Ile Ser Arg Ser Val His Ile His 435 440 445 Pro Thr Leu Ser Glu Ala Val Lys Glu Ala Ala His Gly Ile Ser Gly 450 455 460 His Met Ile Asn Phe 465 19 2014 DNA Bacillus subtilis CDS (464)..(1885) 19 gatccttttt aacccatcac atatacctgc cgttcactat tatttagtga aatgagatat 60 tatgatattt tctgaattgt gattaaaaag gcaactttat gcccatgcaa cagaaactat 120 aaaaaataca gagaatgaaa agaaacagat agatttttta gttctttagg cccgtagtct 180 gcaaatcctt ttatgatttt ctatcaaaca aaagaggaaa atagaccagt tgcaatccaa 240 acgagagtct aatagaatga ggtcgaaaag taaatcgcgc gggtttgtta ctgataaagc 300 aggcaagacc taaaatgtgt aaagggcaaa gtgtatactt tggcgtcacc ccttacatat 360 tttaggtctt tttttattgt gcgtaactaa cttgccatct tcaaacagga gggctggaag 420 aagcagaccg ctaacacagt acataaaaaa ggagacatga acg atg aac atc aaa 475 Met Asn Ile Lys 1 aag ttt gca aaa caa gca aca gta tta acc ttt act acc gca ctg ctg 523 Lys Phe Ala Lys Gln Ala Thr Val Leu Thr Phe Thr Thr Ala Leu Leu 5 10 15 20 gca gga ggc gca act caa gcg ttt gcg aaa gaa acg aac caa aag cca 571 Ala Gly Gly Ala Thr Gln Ala Phe Ala Lys Glu Thr Asn Gln Lys Pro 25 30 35 tat aag gaa aca tac ggc att tcc cat att aca cgc cat gat atg ctg 619 Tyr Lys Glu Thr Tyr Gly Ile Ser His Ile Thr Arg His Asp Met Leu 40 45 50 caa atc cct gaa cag caa aaa aat gaa aaa tat caa gtt cct gaa ttc 667 Gln Ile Pro Glu Gln Gln Lys Asn Glu Lys Tyr Gln Val Pro Glu Phe 55 60 65 gat tcg tcc aca att aaa aat atc tct tct gca aaa ggc ctg gac gtt 715 Asp Ser Ser Thr Ile Lys Asn Ile Ser Ser Ala Lys Gly Leu Asp Val 70 75 80 tgg gac agc tgg cca tta caa aac gct gac ggc act gtc gca aac tat 763 Trp Asp Ser Trp Pro Leu Gln Asn Ala Asp Gly Thr Val Ala Asn Tyr 85 90 95 100 cac ggc tac cac atc gtc ttt gca tta gcc gga gat cct aaa aat gcg 811 His Gly Tyr His Ile Val Phe Ala Leu Ala Gly Asp Pro Lys Asn Ala 105 110 115 gat gac aca tcg att tac atg ttc tat caa aaa gtc ggc gaa act tct 859 Asp Asp Thr Ser Ile Tyr Met Phe Tyr Gln Lys Val Gly Glu Thr Ser 120 125 130 att gac agc tgg aaa aac gct ggc cgc gtc ttt aaa gac agc gac aaa 907 Ile Asp Ser Trp Lys Asn Ala Gly Arg Val Phe Lys Asp Ser Asp Lys 135 140 145 ttc gat gca aat gat tct atc cta aaa gac caa aca caa gaa tgg tca 955 Phe Asp Ala Asn Asp Ser Ile Leu Lys Asp Gln Thr Gln Glu Trp Ser 150 155 160 ggt tca gcc aca ttt aca tct gac gga aaa atc cgt tta ttc tac act 1003 Gly Ser Ala Thr Phe Thr Ser Asp Gly Lys Ile Arg Leu Phe Tyr Thr 165 170 175 180 gat ttc tcc ggt aaa cat tac ggc aaa caa aca ctg aca act gca caa 1051 Asp Phe Ser Gly Lys His Tyr Gly Lys Gln Thr Leu Thr Thr Ala Gln 185 190 195 gtt aac gta tca gca tca gac agc tct ttg aac atc aac ggt gta gag 1099 Val Asn Val Ser Ala Ser Asp Ser Ser Leu Asn Ile Asn Gly Val Glu 200 205 210 gat tat aaa tca atc ttt gac ggt gac gga aaa acg tat caa aat gta 1147 Asp Tyr Lys Ser Ile Phe Asp Gly Asp Gly Lys Thr Tyr Gln Asn Val 215 220 225 cag cag ttc atc gat gaa ggc aac tac agc tca ggc gac aac cat acg 1195 Gln Gln Phe Ile Asp Glu Gly Asn Tyr Ser Ser Gly Asp Asn His Thr 230 235 240 ctg aga gat cct cac tac gta gaa gat aaa ggc cac aaa tac tta gta 1243 Leu Arg Asp Pro His Tyr Val Glu Asp Lys Gly His Lys Tyr Leu Val 245 250 255 260 ttt gaa gca aac act gga act gaa gat ggc tac caa ggc gaa gaa tct 1291 Phe Glu Ala Asn Thr Gly Thr Glu Asp Gly Tyr Gln Gly Glu Glu Ser 265 270 275 tta ttt aac aaa gca tac tat ggc aaa agc aca tca ttc ttc cgt caa 1339 Leu Phe Asn Lys Ala Tyr Tyr Gly Lys Ser Thr Ser Phe Phe Arg Gln 280 285 290 gaa agt caa aaa ctt ctg caa agc gat aaa aaa cgc acg gct gag tta 1387 Glu Ser Gln Lys Leu Leu Gln Ser Asp Lys Lys Arg Thr Ala Glu Leu 295 300 305 gca aac ggc gct ctc ggt atg att gag cta aac gat gat tac aca ctg 1435 Ala Asn Gly Ala Leu Gly Met Ile Glu Leu Asn Asp Asp Tyr Thr Leu 310 315 320 aaa aaa gtg atg aaa ccg ctg att gca tct aac aca gta aca gat gaa 1483 Lys Lys Val Met Lys Pro Leu Ile Ala Ser Asn Thr Val Thr Asp Glu 325 330 335 340 att gaa cgc gcg aac gtc ttt aaa atg aac ggc aaa tgg tac ctg ttc 1531 Ile Glu Arg Ala Asn Val Phe Lys Met Asn Gly Lys Trp Tyr Leu Phe 345 350 355 act gac tcc cgc gga tca aaa atg acg att gac ggc att acg tct aac 1579 Thr Asp Ser Arg Gly Ser Lys Met Thr Ile Asp Gly Ile Thr Ser Asn 360 365 370 gat att tac atg ctt ggt tat gtt tct aat tct tta act ggc cca tac 1627 Asp Ile Tyr Met Leu Gly Tyr Val Ser Asn Ser Leu Thr Gly Pro Tyr 375 380 385 aag ccg ctg aac aaa act ggc ctt gtg tta aaa atg gat ctt gat cct 1675 Lys Pro Leu Asn Lys Thr Gly Leu Val Leu Lys Met Asp Leu Asp Pro 390 395 400 aac gat gta acc ttt act tac tca cac ttc gct gta cct caa gcg aaa 1723 Asn Asp Val Thr Phe Thr Tyr Ser His Phe Ala Val Pro Gln Ala Lys 405 410 415 420 gga aac aat gtc gtg att aca agc tat atg aca aac aga gga ttc tac 1771 Gly Asn Asn Val Val Ile Thr Ser Tyr Met Thr Asn Arg Gly Phe Tyr 425 430 435 gca gac aaa caa tca acg ttt gcg cca agc ttc ctg ctg aac atc aaa 1819 Ala Asp Lys Gln Ser Thr Phe Ala Pro Ser Phe Leu Leu Asn Ile Lys 440 445 450 ggc aag aaa aca tct gtt gtc aaa gac agc atc ctt gaa caa gga caa 1867 Gly Lys Lys Thr Ser Val Val Lys Asp Ser Ile Leu Glu Gln Gly Gln 455 460 465 tta aca gtt aac aaa taa aaacgcaaaa gaaaatgccg atatcctatt 1915 Leu Thr Val Asn Lys 470 ggcattttct tttatttctt atcaacataa aggtgaatcc catatgaact atataaaagc 1975 aggcaaatgg ctaaccgtat tcctaacctt ttgaagatc 2014 20 473 PRT Bacillus subtilis 20 Met Asn Ile Lys Lys Phe Ala Lys Gln Ala Thr Val Leu Thr Phe Thr 1 5 10 15 Thr Ala Leu Leu Ala Gly Gly Ala Thr Gln Ala Phe Ala Lys Glu Thr 20 25 30 Asn Gln Lys Pro Tyr Lys Glu Thr Tyr Gly Ile Ser His Ile Thr Arg 35 40 45 His Asp Met Leu Gln Ile Pro Glu Gln Gln Lys Asn Glu Lys Tyr Gln 50 55 60 Val Pro Glu Phe Asp Ser Ser Thr Ile Lys Asn Ile Ser Ser Ala Lys 65 70 75 80 Gly Leu Asp Val Trp Asp Ser Trp Pro Leu Gln Asn Ala Asp Gly Thr 85 90 95 Val Ala Asn Tyr His Gly Tyr His Ile Val Phe Ala Leu Ala Gly Asp 100 105 110 Pro Lys Asn Ala Asp Asp Thr Ser Ile Tyr Met Phe Tyr Gln Lys Val 115 120 125 Gly Glu Thr Ser Ile Asp Ser Trp Lys Asn Ala Gly Arg Val Phe Lys 130 135 140 Asp Ser Asp Lys Phe Asp Ala Asn Asp Ser Ile Leu Lys Asp Gln Thr 145 150 155 160 Gln Glu Trp Ser Gly Ser Ala Thr Phe Thr Ser Asp Gly Lys Ile Arg 165 170 175 Leu Phe Tyr Thr Asp Phe Ser Gly Lys His Tyr Gly Lys Gln Thr Leu 180 185 190 Thr Thr Ala Gln Val Asn Val Ser Ala Ser Asp Ser Ser Leu Asn Ile 195 200 205 Asn Gly Val Glu Asp Tyr Lys Ser Ile Phe Asp Gly Asp Gly Lys Thr 210 215 220 Tyr Gln Asn Val Gln Gln Phe Ile Asp Glu Gly Asn Tyr Ser Ser Gly 225 230 235 240 Asp Asn His Thr Leu Arg Asp Pro His Tyr Val Glu Asp Lys Gly His 245 250 255 Lys Tyr Leu Val Phe Glu Ala Asn Thr Gly Thr Glu Asp Gly Tyr Gln 260 265 270 Gly Glu Glu Ser Leu Phe Asn Lys Ala Tyr Tyr Gly Lys Ser Thr Ser 275 280 285 Phe Phe Arg Gln Glu Ser Gln Lys Leu Leu Gln Ser Asp Lys Lys Arg 290 295 300 Thr Ala Glu Leu Ala Asn Gly Ala Leu Gly Met Ile Glu Leu Asn Asp 305 310 315 320 Asp Tyr Thr Leu Lys Lys Val Met Lys Pro Leu Ile Ala Ser Asn Thr 325 330 335 Val Thr Asp Glu Ile Glu Arg Ala Asn Val Phe Lys Met Asn Gly Lys 340 345 350 Trp Tyr Leu Phe Thr Asp Ser Arg Gly Ser Lys Met Thr Ile Asp Gly 355 360 365 Ile Thr Ser Asn Asp Ile Tyr Met Leu Gly Tyr Val Ser Asn Ser Leu 370 375 380 Thr Gly Pro Tyr Lys Pro Leu Asn Lys Thr Gly Leu Val Leu Lys Met 385 390 395 400 Asp Leu Asp Pro Asn Asp Val Thr Phe Thr Tyr Ser His Phe Ala Val 405 410 415 Pro Gln Ala Lys Gly Asn Asn Val Val Ile Thr Ser Tyr Met Thr Asn 420 425 430 Arg Gly Phe Tyr Ala Asp Lys Gln Ser Thr Phe Ala Pro Ser Phe Leu 435 440 445 Leu Asn Ile Lys Gly Lys Lys Thr Ser Val Val Lys Asp Ser Ile Leu 450 455 460 Glu Gln Gly Gln Leu Thr Val Asn Lys 465 470 21 24 DNA Artificial sequence primer 21 cgggatcctt tttaacccat caca 24 22 29 DNA Artificial sequence primer 22 gaagatcttc aaaaggttag gaatacggt 29 23 23 DNA Artificial sequence primer 23 ccttttgaag atcgaccagt tgg 23 24 44 DNA Artificial sequence primer 24 tacctggaat gctgttttcc cagggatcgc agtggtgagt aacc 44 25 28 DNA Artificial sequence primer 25 cctgggaaaa cagcattcca ggtattag 28 26 23 DNA Artificial sequence primer 26 tgcaggtcga ctctagagga tcc 23 27 2028 DNA Corynebacterium glutamicum CDS (1)..(2028) 27 atg gcg ttc tcc gta gag atg ccc gag ctg ggc gaa tca gta acc gaa 48 Met Ala Phe Ser Val Glu Met Pro Glu Leu Gly Glu Ser Val Thr Glu 1 5 10 15 ggc acg atc acc cag tgg ttg aag tct gtt ggt gac act gtt gag gta 96 Gly Thr Ile Thr Gln Trp Leu Lys Ser Val Gly Asp Thr Val Glu Val 20 25 30 gat gag ccg ttg ctc gag gtc tca act gac aag gtc gac acc gag att 144 Asp Glu Pro Leu Leu Glu Val Ser Thr Asp Lys Val Asp Thr Glu Ile 35 40 45 ccc tct cct gtc gcc ggt gtc atc cta gag att aag gct gaa gag gat 192 Pro Ser Pro Val Ala Gly Val Ile Leu Glu Ile Lys Ala Glu Glu Asp 50 55 60 gac acc gtc gac gtc ggc ggt gtc att gca ata atc ggc gat gct gat 240 Asp Thr Val Asp Val Gly Gly Val Ile Ala Ile Ile Gly Asp Ala Asp 65 70 75 80 gag act cct gcc aac gaa gct cct gcc gac gag gca cca gct cct gcc 288 Glu Thr Pro Ala Asn Glu Ala Pro Ala Asp Glu Ala Pro Ala Pro Ala 85 90 95 gaa gag gaa gaa cca gtt aag gaa gag cca aag aag gag gca gct cct 336 Glu Glu Glu Glu Pro Val Lys Glu Glu Pro Lys Lys Glu Ala Ala Pro 100 105 110 gaa gct cca gca gca act ggc gcc gca acc gat gtg gaa atg cca gaa 384 Glu Ala Pro Ala Ala Thr Gly Ala Ala Thr Asp Val Glu Met Pro Glu 115 120 125 ctc ggc gaa tcc gtc acc gaa ggc acc att acc cag tgg ctc aag gct 432 Leu Gly Glu Ser Val Thr Glu Gly Thr Ile Thr Gln Trp Leu Lys Ala 130 135 140 gtc ggc gac acc gtc gaa gta gac gaa cca ctt ctt gag gtc tcc acc 480 Val Gly Asp Thr Val Glu Val Asp Glu Pro Leu Leu Glu Val Ser Thr 145 150 155 160 gac aag gtc gac acc gaa atc cca tcc cca gta gca ggc acc atc gtg 528 Asp Lys Val Asp Thr Glu Ile Pro Ser Pro Val Ala Gly Thr Ile Val 165 170 175 gag atc ctt gca gac gaa gac gac acc gtc gac gtc ggc gca gtc atc 576 Glu Ile Leu Ala Asp Glu Asp Asp Thr Val Asp Val Gly Ala Val Ile 180 185 190 gcc cgc atc ggt gac gca aac gca gct gca gca cct gcc gaa gag gaa 624 Ala Arg Ile Gly Asp Ala Asn Ala Ala Ala Ala Pro Ala Glu Glu Glu 195 200 205 gca gct cct gcc gaa gag gaa gaa cca gtt aag gaa gag cca aag aag 672 Ala Ala Pro Ala Glu Glu Glu Glu Pro Val Lys Glu Glu Pro Lys Lys 210 215 220 gag gca gct cct gaa gct cca gca gca act ggc gcc gca acc gat gtg 720 Glu Ala Ala Pro Glu Ala Pro Ala Ala Thr Gly Ala Ala Thr Asp Val 225 230 235 240 gaa atg cca gaa ctc ggc gaa tcc gtc acc gaa ggc acc att acc cag 768 Glu Met Pro Glu Leu Gly Glu Ser Val Thr Glu Gly Thr Ile Thr Gln 245 250 255 tgg ctc aag gct gtc ggc gac acc gtc gaa gta gac gaa cca ctt ctt 816 Trp Leu Lys Ala Val Gly Asp Thr Val Glu Val Asp Glu Pro Leu Leu 260 265 270 gag gtc tcc acc gac aag gtc gac acc gaa atc cca tcc cca gta gca 864 Glu Val Ser Thr Asp Lys Val Asp Thr Glu Ile Pro Ser Pro Val Ala 275 280 285 ggc acc atc gtg gag atc ctt gca gac gaa gac gac acc gtc gac gtc 912 Gly Thr Ile Val Glu Ile Leu Ala Asp Glu Asp Asp Thr Val Asp Val 290 295 300 ggc gca gtc atc gcc cgc atc ggt gac gca aac gca gct gca gca cct 960 Gly Ala Val Ile Ala Arg Ile Gly Asp Ala Asn Ala Ala Ala Ala Pro 305 310 315 320 gcc gaa gag gaa gca gct cct gcc gaa gag gag gaa cca gtt aag gaa 1008 Ala Glu Glu Glu Ala Ala

Pro Ala Glu Glu Glu Glu Pro Val Lys Glu 325 330 335 gag cca aag aag gaa gag ccc aag aag gaa gag ccc aag aag gaa gca 1056 Glu Pro Lys Lys Glu Glu Pro Lys Lys Glu Glu Pro Lys Lys Glu Ala 340 345 350 gct act aca cct gct gcg gca tcc gca act gtg tcc gct tct ggc gac 1104 Ala Thr Thr Pro Ala Ala Ala Ser Ala Thr Val Ser Ala Ser Gly Asp 355 360 365 aac gtt cca tac gtc acc cca ctg gtg cgc aag ctt gct gaa aag cac 1152 Asn Val Pro Tyr Val Thr Pro Leu Val Arg Lys Leu Ala Glu Lys His 370 375 380 ggc gtt gac ttg aac acc gtg acc ggt acc ggt atc ggt ggc cgt atc 1200 Gly Val Asp Leu Asn Thr Val Thr Gly Thr Gly Ile Gly Gly Arg Ile 385 390 395 400 cgc aag cag gat gtt ttg gct gct gcg aac ggc gag gct gca cct gct 1248 Arg Lys Gln Asp Val Leu Ala Ala Ala Asn Gly Glu Ala Ala Pro Ala 405 410 415 gag gct gct gct cct gtt tcc gct tgg tcc act aag tct gtt gac cct 1296 Glu Ala Ala Ala Pro Val Ser Ala Trp Ser Thr Lys Ser Val Asp Pro 420 425 430 gag aag gct aag ctc cgt ggt acc act cag aag gtc aac cgc atc cgt 1344 Glu Lys Ala Lys Leu Arg Gly Thr Thr Gln Lys Val Asn Arg Ile Arg 435 440 445 gag atc acc gcg atg aag acc gtc gag gct ctg cag att tct gct cag 1392 Glu Ile Thr Ala Met Lys Thr Val Glu Ala Leu Gln Ile Ser Ala Gln 450 455 460 ctc acc cag ctg cac gag gtc gat atg act cgc gtt gct gag ctg cgt 1440 Leu Thr Gln Leu His Glu Val Asp Met Thr Arg Val Ala Glu Leu Arg 465 470 475 480 aag aag aac aag ccc gcg ttc atc gag aag cac ggt gtg aac ctc act 1488 Lys Lys Asn Lys Pro Ala Phe Ile Glu Lys His Gly Val Asn Leu Thr 485 490 495 tac ctg cca ttc ttc gtg aag gca gtt gtc gag gct ttg gtt tcc cat 1536 Tyr Leu Pro Phe Phe Val Lys Ala Val Val Glu Ala Leu Val Ser His 500 505 510 cca aac gtc aac gcg tct ttc aac gcg aag acc aag gag atg acc tac 1584 Pro Asn Val Asn Ala Ser Phe Asn Ala Lys Thr Lys Glu Met Thr Tyr 515 520 525 cac tcc tcc gtt aac ctc tcc atc gct gtt gat acc cca gct ggt ctg 1632 His Ser Ser Val Asn Leu Ser Ile Ala Val Asp Thr Pro Ala Gly Leu 530 535 540 ttg acc cca gtc att cac gat gct cag gat ctc tcc atc cca gag atc 1680 Leu Thr Pro Val Ile His Asp Ala Gln Asp Leu Ser Ile Pro Glu Ile 545 550 555 560 gca aag gca att gtt gac ctg gct gat cgt tca cgc aac aac aag ctg 1728 Ala Lys Ala Ile Val Asp Leu Ala Asp Arg Ser Arg Asn Asn Lys Leu 565 570 575 aag cca aac gat ctg tcc ggt ggc acc ttc acc atc acc aac att ggt 1776 Lys Pro Asn Asp Leu Ser Gly Gly Thr Phe Thr Ile Thr Asn Ile Gly 580 585 590 tct gaa ggc gca ctg tct gat acc cca atc ctg gtt cca cca cag gct 1824 Ser Glu Gly Ala Leu Ser Asp Thr Pro Ile Leu Val Pro Pro Gln Ala 595 600 605 ggc atc ttg ggc acc ggc gcg atc gtg aag cgt cca gtt gtc atc acc 1872 Gly Ile Leu Gly Thr Gly Ala Ile Val Lys Arg Pro Val Val Ile Thr 610 615 620 gag gat gga att gat tcc atc gcg atc cgt cag atg gtc ttc cta cca 1920 Glu Asp Gly Ile Asp Ser Ile Ala Ile Arg Gln Met Val Phe Leu Pro 625 630 635 640 ctg acc tac gac cac cag gtt gta gat ggc gca gat gct ggt cgc ttc 1968 Leu Thr Tyr Asp His Gln Val Val Asp Gly Ala Asp Ala Gly Arg Phe 645 650 655 ctg acc acc atc aag gac cgc ctt gag acc gct aac ttc gaa ggc gat 2016 Leu Thr Thr Ile Lys Asp Arg Leu Glu Thr Ala Asn Phe Glu Gly Asp 660 665 670 ctg cag ctc taa 2028 Leu Gln Leu 675 28 675 PRT Corynebacterium glutamicum 28 Met Ala Phe Ser Val Glu Met Pro Glu Leu Gly Glu Ser Val Thr Glu 1 5 10 15 Gly Thr Ile Thr Gln Trp Leu Lys Ser Val Gly Asp Thr Val Glu Val 20 25 30 Asp Glu Pro Leu Leu Glu Val Ser Thr Asp Lys Val Asp Thr Glu Ile 35 40 45 Pro Ser Pro Val Ala Gly Val Ile Leu Glu Ile Lys Ala Glu Glu Asp 50 55 60 Asp Thr Val Asp Val Gly Gly Val Ile Ala Ile Ile Gly Asp Ala Asp 65 70 75 80 Glu Thr Pro Ala Asn Glu Ala Pro Ala Asp Glu Ala Pro Ala Pro Ala 85 90 95 Glu Glu Glu Glu Pro Val Lys Glu Glu Pro Lys Lys Glu Ala Ala Pro 100 105 110 Glu Ala Pro Ala Ala Thr Gly Ala Ala Thr Asp Val Glu Met Pro Glu 115 120 125 Leu Gly Glu Ser Val Thr Glu Gly Thr Ile Thr Gln Trp Leu Lys Ala 130 135 140 Val Gly Asp Thr Val Glu Val Asp Glu Pro Leu Leu Glu Val Ser Thr 145 150 155 160 Asp Lys Val Asp Thr Glu Ile Pro Ser Pro Val Ala Gly Thr Ile Val 165 170 175 Glu Ile Leu Ala Asp Glu Asp Asp Thr Val Asp Val Gly Ala Val Ile 180 185 190 Ala Arg Ile Gly Asp Ala Asn Ala Ala Ala Ala Pro Ala Glu Glu Glu 195 200 205 Ala Ala Pro Ala Glu Glu Glu Glu Pro Val Lys Glu Glu Pro Lys Lys 210 215 220 Glu Ala Ala Pro Glu Ala Pro Ala Ala Thr Gly Ala Ala Thr Asp Val 225 230 235 240 Glu Met Pro Glu Leu Gly Glu Ser Val Thr Glu Gly Thr Ile Thr Gln 245 250 255 Trp Leu Lys Ala Val Gly Asp Thr Val Glu Val Asp Glu Pro Leu Leu 260 265 270 Glu Val Ser Thr Asp Lys Val Asp Thr Glu Ile Pro Ser Pro Val Ala 275 280 285 Gly Thr Ile Val Glu Ile Leu Ala Asp Glu Asp Asp Thr Val Asp Val 290 295 300 Gly Ala Val Ile Ala Arg Ile Gly Asp Ala Asn Ala Ala Ala Ala Pro 305 310 315 320 Ala Glu Glu Glu Ala Ala Pro Ala Glu Glu Glu Glu Pro Val Lys Glu 325 330 335 Glu Pro Lys Lys Glu Glu Pro Lys Lys Glu Glu Pro Lys Lys Glu Ala 340 345 350 Ala Thr Thr Pro Ala Ala Ala Ser Ala Thr Val Ser Ala Ser Gly Asp 355 360 365 Asn Val Pro Tyr Val Thr Pro Leu Val Arg Lys Leu Ala Glu Lys His 370 375 380 Gly Val Asp Leu Asn Thr Val Thr Gly Thr Gly Ile Gly Gly Arg Ile 385 390 395 400 Arg Lys Gln Asp Val Leu Ala Ala Ala Asn Gly Glu Ala Ala Pro Ala 405 410 415 Glu Ala Ala Ala Pro Val Ser Ala Trp Ser Thr Lys Ser Val Asp Pro 420 425 430 Glu Lys Ala Lys Leu Arg Gly Thr Thr Gln Lys Val Asn Arg Ile Arg 435 440 445 Glu Ile Thr Ala Met Lys Thr Val Glu Ala Leu Gln Ile Ser Ala Gln 450 455 460 Leu Thr Gln Leu His Glu Val Asp Met Thr Arg Val Ala Glu Leu Arg 465 470 475 480 Lys Lys Asn Lys Pro Ala Phe Ile Glu Lys His Gly Val Asn Leu Thr 485 490 495 Tyr Leu Pro Phe Phe Val Lys Ala Val Val Glu Ala Leu Val Ser His 500 505 510 Pro Asn Val Asn Ala Ser Phe Asn Ala Lys Thr Lys Glu Met Thr Tyr 515 520 525 His Ser Ser Val Asn Leu Ser Ile Ala Val Asp Thr Pro Ala Gly Leu 530 535 540 Leu Thr Pro Val Ile His Asp Ala Gln Asp Leu Ser Ile Pro Glu Ile 545 550 555 560 Ala Lys Ala Ile Val Asp Leu Ala Asp Arg Ser Arg Asn Asn Lys Leu 565 570 575 Lys Pro Asn Asp Leu Ser Gly Gly Thr Phe Thr Ile Thr Asn Ile Gly 580 585 590 Ser Glu Gly Ala Leu Ser Asp Thr Pro Ile Leu Val Pro Pro Gln Ala 595 600 605 Gly Ile Leu Gly Thr Gly Ala Ile Val Lys Arg Pro Val Val Ile Thr 610 615 620 Glu Asp Gly Ile Asp Ser Ile Ala Ile Arg Gln Met Val Phe Leu Pro 625 630 635 640 Leu Thr Tyr Asp His Gln Val Val Asp Gly Ala Asp Ala Gly Arg Phe 645 650 655 Leu Thr Thr Ile Lys Asp Arg Leu Glu Thr Ala Asn Phe Glu Gly Asp 660 665 670 Leu Gln Leu 675 29 3481 DNA Corynebacterium glutamicum CDS (1437)..(3035) yggB 29 gatcttgccg atttcggcag gatcaatgtc ggcgtgaatg atcttggcat caggtgcgaa 60 agtgtcaacg tcaccggtga cgcggtcatc aaagcgggag ccgatagcaa tcagcaggtc 120 gctgcgctgc agtgcaccaa cagcggacac agtgccatgc atgcctggca tacccatgtg 180 cagctcgtgg gactctggga aggttcccag cgccatcaat gtggtgacaa ctggaatgcc 240 ggtgtgctca gcgaacgcac gaagctcttc gtgggcatca gccttgataa cgccgccgcc 300 aacgtaaagg acaggcttct tagactcacc gatcagtttg acagcctgct caatctgtcg 360 agcatgcggt gttgaaactg ggcggtagcc tggcaggtcg atctttggtg gccagacgaa 420 atccaattca gcgttctgaa catccttggg gatatccact agaacaggac cagggcgacc 480 agtaatcgcg aggtggaatg cctcagccaa tgcctgtgga atgtcgttgg ggttggtgac 540 catgaagttg tgcttggtca ctggcatggt gatgccgcgg atatcggctt cctggaaagc 600 atcggtaccc agcaggctac ttccgacctg gccggtgatg gcaaccatgg gaacggagtc 660 caagtttgca tcagcgattg gggtaaccaa gttggttgcg cctgggccag aggttgcaat 720 gcagacgcca acgcgtccag taacctgcgc gtagccggtt gctgcgtggc ctgcgccctg 780 ctcgtggcgc actaggacgt ggcgcacctt tgtggaggaa tagagcgggt catacaccgg 840 tagcaccgca ccaccaggaa taccgaacac gatgtcggcg ttaagctcct cgagcgatcg 900 aacaattgcc tgtgcacctg tcatccgctc aggggcggcg gatcgaccac ggcttgcaac 960 cgtggcggga gtgggctgtt gagaagctgc cacattcacg actttctggc tcctttacta 1020 aataaggatt ttcacaggac ccgtccaagc caagccgatt tcaactcagc ctaaagacaa 1080 agccctcatt taaaattgtt ccgacgcgga tgcgtgtgca cgcagtgcga cagatgtctg 1140 ttgcaaagtt ggctacttgg gtcataacca acaagaaagc cctcgttcca acactgtggt 1200 gagtgttgtc gagggcgctt gacgagacga cttggaaggc cgttacggca ggcgccgcgc 1260 ggttactact acaagtcgaa taatggtcat ggtgtgtcat gctacacaca tcgagtttcc 1320 aattccacaa cgcacgaaaa ttcccacccc caaaactccc ccacttcggt taaggaatca 1380 ggattctcac aaagttcagg caggctcccg ctacttttca gcgctaatct tggctc atg 1439 Met 1 att tta ggc gta ccc att caa tat ttg ctc tat tca ttg tgg aat tgg 1487 Ile Leu Gly Val Pro Ile Gln Tyr Leu Leu Tyr Ser Leu Trp Asn Trp 5 10 15 att gtc gat acc ggt ttt gat gta gca att atc ctg gtc ttg gcg ttt 1535 Ile Val Asp Thr Gly Phe Asp Val Ala Ile Ile Leu Val Leu Ala Phe 20 25 30 ttg att cca cgt atc ggc cga ctg gcc atg cgt att atc aag cag cga 1583 Leu Ile Pro Arg Ile Gly Arg Leu Ala Met Arg Ile Ile Lys Gln Arg 35 40 45 gtg gag tct gca gcc gat gcg gac acc act aag aac cag ctc gcg ttc 1631 Val Glu Ser Ala Ala Asp Ala Asp Thr Thr Lys Asn Gln Leu Ala Phe 50 55 60 65 gct ggc gtt ggc gtt tat atc gcg caa att gtg gcg ttt ttc atg ctt 1679 Ala Gly Val Gly Val Tyr Ile Ala Gln Ile Val Ala Phe Phe Met Leu 70 75 80 gcc gtc tcc gcg atg cag gct ttt ggt ttc tct ctc gcg ggc gct gcg 1727 Ala Val Ser Ala Met Gln Ala Phe Gly Phe Ser Leu Ala Gly Ala Ala 85 90 95 att ccg gca acc att gcg tca gct gcc att ggt ctt ggt gcg cag tcg 1775 Ile Pro Ala Thr Ile Ala Ser Ala Ala Ile Gly Leu Gly Ala Gln Ser 100 105 110 att gtt gcg gac ttc ttg gcc gga ttt ttc atc ctg acg gaa aag caa 1823 Ile Val Ala Asp Phe Leu Ala Gly Phe Phe Ile Leu Thr Glu Lys Gln 115 120 125 ttc ggc gtg ggt gac tgg gtg cgc ttt gag ggc aac ggc atc gtt gtt 1871 Phe Gly Val Gly Asp Trp Val Arg Phe Glu Gly Asn Gly Ile Val Val 130 135 140 145 gaa ggc acc gtc att gag atc acc atg cgc gcg acc aaa att cgc acg 1919 Glu Gly Thr Val Ile Glu Ile Thr Met Arg Ala Thr Lys Ile Arg Thr 150 155 160 att gca caa gag acc gtg atc atc ccg aac tcc acg gcg aaa gtg tgc 1967 Ile Ala Gln Glu Thr Val Ile Ile Pro Asn Ser Thr Ala Lys Val Cys 165 170 175 atc aac aat tct aat aac tgg tcg cgt gcg gtt gtc gtt att ccg atc 2015 Ile Asn Asn Ser Asn Asn Trp Ser Arg Ala Val Val Val Ile Pro Ile 180 185 190 ccc atg ttg ggt tct gaa aac atc aca gat gtc atc gcg cgc tct gaa 2063 Pro Met Leu Gly Ser Glu Asn Ile Thr Asp Val Ile Ala Arg Ser Glu 195 200 205 gct gcg act cgt cgc gca ctt ggc cag gag aaa atc gca ccg gaa atc 2111 Ala Ala Thr Arg Arg Ala Leu Gly Gln Glu Lys Ile Ala Pro Glu Ile 210 215 220 225 ctc ggt gaa ctc gat gtg cac cca gcc acg gaa gtc aca ccg cca acg 2159 Leu Gly Glu Leu Asp Val His Pro Ala Thr Glu Val Thr Pro Pro Thr 230 235 240 gtg gtc ggc atg ccg tgg atg gtc acc atg cgt ttc ctc gtg caa gtc 2207 Val Val Gly Met Pro Trp Met Val Thr Met Arg Phe Leu Val Gln Val 245 250 255 acc gcc ggc aat caa tgg ctg gtc gaa cgc gcc atc cgc aca gaa atc 2255 Thr Ala Gly Asn Gln Trp Leu Val Glu Arg Ala Ile Arg Thr Glu Ile 260 265 270 atc aac gaa ttc tgg gaa gaa tac ggc agc gca acc act aca tcg gga 2303 Ile Asn Glu Phe Trp Glu Glu Tyr Gly Ser Ala Thr Thr Thr Ser Gly 275 280 285 acc ctc att gat tcc tta cac gtt gag cat gaa gag cca aag acc tcg 2351 Thr Leu Ile Asp Ser Leu His Val Glu His Glu Glu Pro Lys Thr Ser 290 295 300 305 ctt atc gac gcc tcc ccc cag gct ctt aag gaa ccg aag ccg gag gct 2399 Leu Ile Asp Ala Ser Pro Gln Ala Leu Lys Glu Pro Lys Pro Glu Ala 310 315 320 gcg gcg acg gtt gca tcg cta gct gca tcg tct aac gac gat gca gac 2447 Ala Ala Thr Val Ala Ser Leu Ala Ala Ser Ser Asn Asp Asp Ala Asp 325 330 335 aat gca gac gcc tcg gcg atc aat gca ggc aat cca gag aag gaa ctt 2495 Asn Ala Asp Ala Ser Ala Ile Asn Ala Gly Asn Pro Glu Lys Glu Leu 340 345 350 gat tcc gat gtg ctg gaa caa gaa ctc tcc agc gaa gaa ccg gaa gaa 2543 Asp Ser Asp Val Leu Glu Gln Glu Leu Ser Ser Glu Glu Pro Glu Glu 355 360 365 aca gca aaa cca gat cac tct ctc cga ggc ttc ttc cgc act gat tac 2591 Thr Ala Lys Pro Asp His Ser Leu Arg Gly Phe Phe Arg Thr Asp Tyr 370 375 380 385 tac cca aat cgg tgg cag aag atc ctg tcg ttt ggc gga cgt gtc cgc 2639 Tyr Pro Asn Arg Trp Gln Lys Ile Leu Ser Phe Gly Gly Arg Val Arg 390 395 400 atg agc act tcc ctg ttg ttg ggt gcg ctg ctc ttg ctg tca cta ttt 2687 Met Ser Thr Ser Leu Leu Leu Gly Ala Leu Leu Leu Leu Ser Leu Phe 405 410 415 aag gtc atg act gtg gaa cca agt gag aat tgg caa aac tcc agt gga 2735 Lys Val Met Thr Val Glu Pro Ser Glu Asn Trp Gln Asn Ser Ser Gly 420 425 430 tgg ctg tca cca agc act gcc acc tca act gcg gtg acc acc tcc gaa 2783 Trp Leu Ser Pro Ser Thr Ala Thr Ser Thr Ala Val Thr Thr Ser Glu 435 440 445 act tcc gcg cca gca agc acg cct tcg atg aca gtg ccc act acg gtg 2831 Thr Ser Ala Pro Ala Ser Thr Pro Ser Met Thr Val Pro Thr Thr Val 450 455 460 465 gag gag acc cca acg atg gaa tct agc gtc gaa acg cag cag gaa acc 2879 Glu Glu Thr Pro Thr Met Glu Ser Ser Val Glu Thr Gln Gln Glu Thr 470 475 480 tca acc cct gca acc gca acg ccc cag cga gcc gac acc atc gaa ccg 2927 Ser Thr Pro Ala Thr Ala Thr Pro Gln Arg Ala Asp Thr Ile Glu Pro 485 490 495 acc gag gaa gcc acg tcg cag gag gaa acg act gca tcg cag acg cag 2975 Thr Glu Glu Ala Thr Ser Gln Glu Glu Thr Thr Ala Ser Gln Thr Gln 500 505 510 tct cca gca gtg gaa gca cca acc gcg gtc caa gaa aca gtt gcg ccg 3023 Ser Pro Ala Val Glu Ala Pro Thr Ala Val Gln Glu Thr Val Ala Pro 515 520 525 acg tcc acc cct taggacgctg attacagacg tgtcccattt ctttactact 3075 Thr Ser Thr Pro 530 attggaaatt atgagttcag acgcagaaaa ggcatccgtg gagctttccg aaaaatttca 3135 cccagaacgc acccatattt tgggcgccgt tgtttttggc ctgatctcat tattagtcat 3195 cggcgcagcc cctcagtacc tgttttggct gctcgcgctc cctgtcatct tcggttactg 3255 ggttctaaaa tcatccacga tcgttgatga acagggcatc accgcaaact acgccttcaa 3315 gggcaaaaag gttgtggcct gggaagacct cgcaggaatc ggattcaagg gtgcccgcac 3375 tttcgctcgc accacctccg atgcagaagt caccctcccc ggcgtcacct tcaactccct 3435 tccccgcctt gaagctgctt cccacggccg catccccgat gcgatc 3481 30 533 PRT Corynebacterium glutamicum 30 Met Ile Leu Gly Val Pro

Ile Gln Tyr Leu Leu Tyr Ser Leu Trp Asn 1 5 10 15 Trp Ile Val Asp Thr Gly Phe Asp Val Ala Ile Ile Leu Val Leu Ala 20 25 30 Phe Leu Ile Pro Arg Ile Gly Arg Leu Ala Met Arg Ile Ile Lys Gln 35 40 45 Arg Val Glu Ser Ala Ala Asp Ala Asp Thr Thr Lys Asn Gln Leu Ala 50 55 60 Phe Ala Gly Val Gly Val Tyr Ile Ala Gln Ile Val Ala Phe Phe Met 65 70 75 80 Leu Ala Val Ser Ala Met Gln Ala Phe Gly Phe Ser Leu Ala Gly Ala 85 90 95 Ala Ile Pro Ala Thr Ile Ala Ser Ala Ala Ile Gly Leu Gly Ala Gln 100 105 110 Ser Ile Val Ala Asp Phe Leu Ala Gly Phe Phe Ile Leu Thr Glu Lys 115 120 125 Gln Phe Gly Val Gly Asp Trp Val Arg Phe Glu Gly Asn Gly Ile Val 130 135 140 Val Glu Gly Thr Val Ile Glu Ile Thr Met Arg Ala Thr Lys Ile Arg 145 150 155 160 Thr Ile Ala Gln Glu Thr Val Ile Ile Pro Asn Ser Thr Ala Lys Val 165 170 175 Cys Ile Asn Asn Ser Asn Asn Trp Ser Arg Ala Val Val Val Ile Pro 180 185 190 Ile Pro Met Leu Gly Ser Glu Asn Ile Thr Asp Val Ile Ala Arg Ser 195 200 205 Glu Ala Ala Thr Arg Arg Ala Leu Gly Gln Glu Lys Ile Ala Pro Glu 210 215 220 Ile Leu Gly Glu Leu Asp Val His Pro Ala Thr Glu Val Thr Pro Pro 225 230 235 240 Thr Val Val Gly Met Pro Trp Met Val Thr Met Arg Phe Leu Val Gln 245 250 255 Val Thr Ala Gly Asn Gln Trp Leu Val Glu Arg Ala Ile Arg Thr Glu 260 265 270 Ile Ile Asn Glu Phe Trp Glu Glu Tyr Gly Ser Ala Thr Thr Thr Ser 275 280 285 Gly Thr Leu Ile Asp Ser Leu His Val Glu His Glu Glu Pro Lys Thr 290 295 300 Ser Leu Ile Asp Ala Ser Pro Gln Ala Leu Lys Glu Pro Lys Pro Glu 305 310 315 320 Ala Ala Ala Thr Val Ala Ser Leu Ala Ala Ser Ser Asn Asp Asp Ala 325 330 335 Asp Asn Ala Asp Ala Ser Ala Ile Asn Ala Gly Asn Pro Glu Lys Glu 340 345 350 Leu Asp Ser Asp Val Leu Glu Gln Glu Leu Ser Ser Glu Glu Pro Glu 355 360 365 Glu Thr Ala Lys Pro Asp His Ser Leu Arg Gly Phe Phe Arg Thr Asp 370 375 380 Tyr Tyr Pro Asn Arg Trp Gln Lys Ile Leu Ser Phe Gly Gly Arg Val 385 390 395 400 Arg Met Ser Thr Ser Leu Leu Leu Gly Ala Leu Leu Leu Leu Ser Leu 405 410 415 Phe Lys Val Met Thr Val Glu Pro Ser Glu Asn Trp Gln Asn Ser Ser 420 425 430 Gly Trp Leu Ser Pro Ser Thr Ala Thr Ser Thr Ala Val Thr Thr Ser 435 440 445 Glu Thr Ser Ala Pro Ala Ser Thr Pro Ser Met Thr Val Pro Thr Thr 450 455 460 Val Glu Glu Thr Pro Thr Met Glu Ser Ser Val Glu Thr Gln Gln Glu 465 470 475 480 Thr Ser Thr Pro Ala Thr Ala Thr Pro Gln Arg Ala Asp Thr Ile Glu 485 490 495 Pro Thr Glu Glu Ala Thr Ser Gln Glu Glu Thr Thr Ala Ser Gln Thr 500 505 510 Gln Ser Pro Ala Val Glu Ala Pro Thr Ala Val Gln Glu Thr Val Ala 515 520 525 Pro Thr Ser Thr Pro 530 31 3481 DNA Corynebacterium glutamicum CDS (1437)..(3035) 31 gatcttgccg atttcggcag gatcaatgtc ggcgtgaatg atcttggcat caggtgcgaa 60 agtgtcaacg tcaccggtga cgcggtcatc aaagcgggag ccgatagcaa tcagcaggtc 120 gctgcgctgc agtgcaccaa cagcggacac agtgccatgc atgcctggca tacccatgtg 180 cagctcgtgg gactctggga aggttcccag cgccatcaat gtggtgacaa ctggaatgcc 240 ggtgtgctca gcgaacgcac gaagctcttc gtgggcatca gccttgataa cgccgccgcc 300 aacgtaaagg acaggcttct tagactcacc gatcagtttg acagcctgct caatctgtcg 360 agcatgcggt gttgaaactg ggcggtagcc tggcaggtcg atctttggtg gccagacgaa 420 atccaattca gcgttctgaa catccttggg gatatccact agaacaggac cagggcgacc 480 agtaatcgcg aggtggaatg cctcagccaa tgcctgtgga atgtcgttgg ggttggtgac 540 catgaagttg tgcttggtca ctggcatggt gatgccgcgg atatcggctt cctggaaagc 600 atcggtaccc agcaggctac ttccgacctg gccggtgatg gcaaccatgg gaacggagtc 660 caagtttgca tcagcgattg gggtaaccaa gttggttgcg cctgggccag aggttgcaat 720 gcagacgcca acgcgtccag taacctgcgc gtagccggtt gctgcgtggc ctgcgccctg 780 ctcgtggcgc actaggacgt ggcgcacctt tgtggaggaa tagagcgggt catacaccgg 840 tagcaccgca ccaccaggaa taccgaacac gatgtcggcg ttaagctcct cgagcgatcg 900 aacaattgcc tgtgcacctg tcatccgctc aggggcggcg gatcgaccac ggcttgcaac 960 cgtggcggga gtgggctgtt gagaagctgc cacattcacg actttctggc tcctttacta 1020 aataaggatt ttcacaggac ccgtccaagc caagccgatt tcaactcagc ctaaagacaa 1080 agccctcatt taaaattgtt ccgacgcgga tgcgtgtgca cgcagtgcga cagatgtctg 1140 ttgcaaagtt ggctacttgg gtcataacca acaagaaagc cctcgttcca acactgtggt 1200 gagtgttgtc gagggcgctt gacgagacga cttggaaggc cgttacggca ggcgccgcgc 1260 ggttactact acaagtcgaa taatggtcat ggtgtgtcat gctacacaca tcgagtttcc 1320 aattccacaa cgcacgaaaa ttcccacccc caaaactccc ccacttcggt taaggaatca 1380 ggattctcac aaagttcagg caggctcccg ctacttttca gcgctaatct tggctc atg 1439 Met 1 att tta ggc gta ccc att caa tat ttg ctc tat tca ttg tgg aat tgg 1487 Ile Leu Gly Val Pro Ile Gln Tyr Leu Leu Tyr Ser Leu Trp Asn Trp 5 10 15 att gtc gat acc ggt ttt gat gta gca att atc ctg gtc ttg gcg ttt 1535 Ile Val Asp Thr Gly Phe Asp Val Ala Ile Ile Leu Val Leu Ala Phe 20 25 30 ttg att cca cgt atc ggc cga ctg gcc atg cgt att atc aag cag cga 1583 Leu Ile Pro Arg Ile Gly Arg Leu Ala Met Arg Ile Ile Lys Gln Arg 35 40 45 gtg gag tct gca gcc gat gcg gac acc act aag aac cag ctc gcg ttc 1631 Val Glu Ser Ala Ala Asp Ala Asp Thr Thr Lys Asn Gln Leu Ala Phe 50 55 60 65 gct ggc gtt ggc gtt tat atc gcg caa att gtg gcg ttt ttc atg ctt 1679 Ala Gly Val Gly Val Tyr Ile Ala Gln Ile Val Ala Phe Phe Met Leu 70 75 80 gcc gtc tcc gcg atg cag gct ttt ggt ttc tct ctc gcg ggc gct gcg 1727 Ala Val Ser Ala Met Gln Ala Phe Gly Phe Ser Leu Ala Gly Ala Ala 85 90 95 att ccg gca acc att gcg tca gct gcc att ggt ctt ggt gtg cag tcg 1775 Ile Pro Ala Thr Ile Ala Ser Ala Ala Ile Gly Leu Gly Val Gln Ser 100 105 110 att gtt gcg gac ttc ttg gcc gga ttt ttc atc ctg acg gaa aag caa 1823 Ile Val Ala Asp Phe Leu Ala Gly Phe Phe Ile Leu Thr Glu Lys Gln 115 120 125 ttc ggc gtg ggt gac tgg gtg cgc ttt gag ggc aac ggc atc gtt gtt 1871 Phe Gly Val Gly Asp Trp Val Arg Phe Glu Gly Asn Gly Ile Val Val 130 135 140 145 gaa ggc acc gtc att gag atc acc atg cgc gcg acc aaa att cgc acg 1919 Glu Gly Thr Val Ile Glu Ile Thr Met Arg Ala Thr Lys Ile Arg Thr 150 155 160 att gca caa gag acc gtg atc atc ccg aac tcc acg gcg aaa gtg tgc 1967 Ile Ala Gln Glu Thr Val Ile Ile Pro Asn Ser Thr Ala Lys Val Cys 165 170 175 atc aac aat tct aat aac tgg tcg cgt gcg gtt gtc gtt att ccg atc 2015 Ile Asn Asn Ser Asn Asn Trp Ser Arg Ala Val Val Val Ile Pro Ile 180 185 190 ccc atg ttg ggt tct gaa aac atc aca gat gtc atc gcg cgc tct gaa 2063 Pro Met Leu Gly Ser Glu Asn Ile Thr Asp Val Ile Ala Arg Ser Glu 195 200 205 gct gcg act cgt cgc gca ctt ggc cag gag aaa atc gca ccg gaa atc 2111 Ala Ala Thr Arg Arg Ala Leu Gly Gln Glu Lys Ile Ala Pro Glu Ile 210 215 220 225 ctc ggt gaa ctc gat gtg cac cca gcc acg gaa gtc aca ccg cca acg 2159 Leu Gly Glu Leu Asp Val His Pro Ala Thr Glu Val Thr Pro Pro Thr 230 235 240 gtg gtc ggc atg ccg tgg atg gtc acc atg cgt ttc ctc gtg caa gtc 2207 Val Val Gly Met Pro Trp Met Val Thr Met Arg Phe Leu Val Gln Val 245 250 255 acc gcc ggc aat caa tgg ctg gtc gaa cgc gcc atc cgc aca gaa atc 2255 Thr Ala Gly Asn Gln Trp Leu Val Glu Arg Ala Ile Arg Thr Glu Ile 260 265 270 atc aac gaa ttc tgg gaa gaa tac ggc agc gca acc act aca tcg gga 2303 Ile Asn Glu Phe Trp Glu Glu Tyr Gly Ser Ala Thr Thr Thr Ser Gly 275 280 285 acc ctc att gat tcc tta cac gtt gag cat gaa gag cca aag acc tcg 2351 Thr Leu Ile Asp Ser Leu His Val Glu His Glu Glu Pro Lys Thr Ser 290 295 300 305 ctt atc gac gcc tcc ccc cag gct ctt aag gaa ccg aag ccg gag gct 2399 Leu Ile Asp Ala Ser Pro Gln Ala Leu Lys Glu Pro Lys Pro Glu Ala 310 315 320 gcg gcg acg gtt gca tcg cta gct gca tcg tct aac gac gat gca gac 2447 Ala Ala Thr Val Ala Ser Leu Ala Ala Ser Ser Asn Asp Asp Ala Asp 325 330 335 aat gca gac gcc tcg gcg atc aat gca ggc aat cca gag aag gaa ctt 2495 Asn Ala Asp Ala Ser Ala Ile Asn Ala Gly Asn Pro Glu Lys Glu Leu 340 345 350 gat tcc gat gtg ctg gaa caa gaa ctc tcc agc gaa gaa ccg gaa gaa 2543 Asp Ser Asp Val Leu Glu Gln Glu Leu Ser Ser Glu Glu Pro Glu Glu 355 360 365 aca gca aaa cca gat cac tct ctc cga ggc ttc ttc cgc act gat tac 2591 Thr Ala Lys Pro Asp His Ser Leu Arg Gly Phe Phe Arg Thr Asp Tyr 370 375 380 385 tac cca aat cgg tgg cag aag atc ctg tcg ttt ggc gga cgt gtc cgc 2639 Tyr Pro Asn Arg Trp Gln Lys Ile Leu Ser Phe Gly Gly Arg Val Arg 390 395 400 atg agc act tcc ctg ttg ttg ggt gcg ctg ctc ttg ctg tca cta ttt 2687 Met Ser Thr Ser Leu Leu Leu Gly Ala Leu Leu Leu Leu Ser Leu Phe 405 410 415 aag gtc atg act gtg gaa cca agt gag aat tgg caa aac tcc agt gga 2735 Lys Val Met Thr Val Glu Pro Ser Glu Asn Trp Gln Asn Ser Ser Gly 420 425 430 tgg ctg tca cca agc act gcc acc tca act gcg gtg acc acc tcc gaa 2783 Trp Leu Ser Pro Ser Thr Ala Thr Ser Thr Ala Val Thr Thr Ser Glu 435 440 445 act tcc gcg cca gca agc acg cct tcg atg aca gtg ccc act acg gtg 2831 Thr Ser Ala Pro Ala Ser Thr Pro Ser Met Thr Val Pro Thr Thr Val 450 455 460 465 gag gag acc cca acg atg gaa tct agc gtc gaa acg cag cag gaa acc 2879 Glu Glu Thr Pro Thr Met Glu Ser Ser Val Glu Thr Gln Gln Glu Thr 470 475 480 tca acc cct gca acc gca acg ccc cag cga gcc gac acc atc gaa ccg 2927 Ser Thr Pro Ala Thr Ala Thr Pro Gln Arg Ala Asp Thr Ile Glu Pro 485 490 495 acc gag gaa gcc acg tcg cag gag gaa acg act gca tcg cag acg cag 2975 Thr Glu Glu Ala Thr Ser Gln Glu Glu Thr Thr Ala Ser Gln Thr Gln 500 505 510 tct cca gca gtg gaa gca cca acc gcg gtc caa gaa aca gtt gcg ccg 3023 Ser Pro Ala Val Glu Ala Pro Thr Ala Val Gln Glu Thr Val Ala Pro 515 520 525 acg tcc acc cct taggacgctg attacagacg tgtcccattt ctttactact 3075 Thr Ser Thr Pro 530 attggaaatt atgagttcag acgcagaaaa ggcatccgtg gagctttccg aaaaatttca 3135 cccagaacgc acccatattt tgggcgccgt tgtttttggc ctgatctcat tattagtcat 3195 cggcgcagcc cctcagtacc tgttttggct gctcgcgctc cctgtcatct tcggttactg 3255 ggttctaaaa tcatccacga tcgttgatga acagggcatc accgcaaact acgccttcaa 3315 gggcaaaaag gttgtggcct gggaagacct cgcaggaatc ggattcaagg gtgcccgcac 3375 tttcgctcgc accacctccg atgcagaagt caccctcccc ggcgtcacct tcaactccct 3435 tccccgcctt gaagctgctt cccacggccg catccccgat gcgatc 3481 32 533 PRT Corynebacterium glutamicum 32 Met Ile Leu Gly Val Pro Ile Gln Tyr Leu Leu Tyr Ser Leu Trp Asn 1 5 10 15 Trp Ile Val Asp Thr Gly Phe Asp Val Ala Ile Ile Leu Val Leu Ala 20 25 30 Phe Leu Ile Pro Arg Ile Gly Arg Leu Ala Met Arg Ile Ile Lys Gln 35 40 45 Arg Val Glu Ser Ala Ala Asp Ala Asp Thr Thr Lys Asn Gln Leu Ala 50 55 60 Phe Ala Gly Val Gly Val Tyr Ile Ala Gln Ile Val Ala Phe Phe Met 65 70 75 80 Leu Ala Val Ser Ala Met Gln Ala Phe Gly Phe Ser Leu Ala Gly Ala 85 90 95 Ala Ile Pro Ala Thr Ile Ala Ser Ala Ala Ile Gly Leu Gly Val Gln 100 105 110 Ser Ile Val Ala Asp Phe Leu Ala Gly Phe Phe Ile Leu Thr Glu Lys 115 120 125 Gln Phe Gly Val Gly Asp Trp Val Arg Phe Glu Gly Asn Gly Ile Val 130 135 140 Val Glu Gly Thr Val Ile Glu Ile Thr Met Arg Ala Thr Lys Ile Arg 145 150 155 160 Thr Ile Ala Gln Glu Thr Val Ile Ile Pro Asn Ser Thr Ala Lys Val 165 170 175 Cys Ile Asn Asn Ser Asn Asn Trp Ser Arg Ala Val Val Val Ile Pro 180 185 190 Ile Pro Met Leu Gly Ser Glu Asn Ile Thr Asp Val Ile Ala Arg Ser 195 200 205 Glu Ala Ala Thr Arg Arg Ala Leu Gly Gln Glu Lys Ile Ala Pro Glu 210 215 220 Ile Leu Gly Glu Leu Asp Val His Pro Ala Thr Glu Val Thr Pro Pro 225 230 235 240 Thr Val Val Gly Met Pro Trp Met Val Thr Met Arg Phe Leu Val Gln 245 250 255 Val Thr Ala Gly Asn Gln Trp Leu Val Glu Arg Ala Ile Arg Thr Glu 260 265 270 Ile Ile Asn Glu Phe Trp Glu Glu Tyr Gly Ser Ala Thr Thr Thr Ser 275 280 285 Gly Thr Leu Ile Asp Ser Leu His Val Glu His Glu Glu Pro Lys Thr 290 295 300 Ser Leu Ile Asp Ala Ser Pro Gln Ala Leu Lys Glu Pro Lys Pro Glu 305 310 315 320 Ala Ala Ala Thr Val Ala Ser Leu Ala Ala Ser Ser Asn Asp Asp Ala 325 330 335 Asp Asn Ala Asp Ala Ser Ala Ile Asn Ala Gly Asn Pro Glu Lys Glu 340 345 350 Leu Asp Ser Asp Val Leu Glu Gln Glu Leu Ser Ser Glu Glu Pro Glu 355 360 365 Glu Thr Ala Lys Pro Asp His Ser Leu Arg Gly Phe Phe Arg Thr Asp 370 375 380 Tyr Tyr Pro Asn Arg Trp Gln Lys Ile Leu Ser Phe Gly Gly Arg Val 385 390 395 400 Arg Met Ser Thr Ser Leu Leu Leu Gly Ala Leu Leu Leu Leu Ser Leu 405 410 415 Phe Lys Val Met Thr Val Glu Pro Ser Glu Asn Trp Gln Asn Ser Ser 420 425 430 Gly Trp Leu Ser Pro Ser Thr Ala Thr Ser Thr Ala Val Thr Thr Ser 435 440 445 Glu Thr Ser Ala Pro Ala Ser Thr Pro Ser Met Thr Val Pro Thr Thr 450 455 460 Val Glu Glu Thr Pro Thr Met Glu Ser Ser Val Glu Thr Gln Gln Glu 465 470 475 480 Thr Ser Thr Pro Ala Thr Ala Thr Pro Gln Arg Ala Asp Thr Ile Glu 485 490 495 Pro Thr Glu Glu Ala Thr Ser Gln Glu Glu Thr Thr Ala Ser Gln Thr 500 505 510 Gln Ser Pro Ala Val Glu Ala Pro Thr Ala Val Gln Glu Thr Val Ala 515 520 525 Pro Thr Ser Thr Pro 530 33 20 DNA Artificial sequence yggB N-terminus primer 33 ggctgttgag aagctgccac 20 34 29 DNA Artificial sequence yggB N-terminus primer2 34 ccgcaacaat cgactgcaca ccaagacca 29 35 28 DNA Artificial sequence yggB C-terminus primer1 35 gggagctcca cggcatgccg accaccgt 28 36 29 DNA Artificial sequence yggB C-terminus primer2 36 tggtcttggt gtgcagtcga ttgttgcgg 29 37 28 DNA Artificial sequence yggB 2nd primer 37 gggagctcga ctttctggct cctttact 28 38 28 DNA Artificial sequence sucA8primer 38 ctgcgtcgac gtcggaggca ccatccac 28 39 30 DNA Artificial sequence sucA801primer 39 ctgcgtctcg acgtcggagg caccatccac 30 40 36 DNA Artificial sequence sucA805primer 40 gctaaaagct gcgtcgacgt cggaggcacc atccac 36 41 36 DNA Artificial sequence Synthetic DNA 41 gctataagct gcgtcgacgt cggaggcacc atccac 36 42 4389 DNA Corynebacterium glutamicum CDS (443)..(2542) 42 gtcgacaagc aaaatcgaag cggcagcacg ccgcgtcgga gccttaaacg ccatcgccgc 60 catccctgat ggtttcaatc atcaagtcgg tgaacgcggg cgcaacctgt catccggaca 120 gcgccaactg atcgcgctgg cgcgcgccga actcatcgag ccttccatca tgcttctcga 180 cgaagccacc

tccaccctcg accccgccac cgaagccgtt atcctcaacg cctccgatcg 240 agtcactaag ggacgcacca gcatcatcgt cgcgcaccgc ttggcaaccg ctaaaagggc 300 cgaccgtatt cttgttgttg aacaaggacg tatcattgag gacggatctc acgacgcgtt 360 gttgtctgct aacggcacct acgcccgcat gtggcattta atggcctgac acgttatttt 420 taggagaact gtcaacaaat ta atg cta caa ctg ggg ctt agg cat aat cag 472 Met Leu Gln Leu Gly Leu Arg His Asn Gln 1 5 10 cca acg acc aac gtt aca gtg gat aaa ata aag ctc aat aaa ccc tca 520 Pro Thr Thr Asn Val Thr Val Asp Lys Ile Lys Leu Asn Lys Pro Ser 15 20 25 aga agc aag gaa aag agg cga gta cct gcc gtg agc agc gct agt act 568 Arg Ser Lys Glu Lys Arg Arg Val Pro Ala Val Ser Ser Ala Ser Thr 30 35 40 ttc ggc cag aat gcg tgg ctg gta gac gag atg ttc cag cag ttc cag 616 Phe Gly Gln Asn Ala Trp Leu Val Asp Glu Met Phe Gln Gln Phe Gln 45 50 55 aag gac ccc aag tcc gtg gac aag gaa tgg aga gaa ctc ttt gag gcg 664 Lys Asp Pro Lys Ser Val Asp Lys Glu Trp Arg Glu Leu Phe Glu Ala 60 65 70 cag ggg gga cca aat gct acc ccc gct aca aca gaa gca cag cct tca 712 Gln Gly Gly Pro Asn Ala Thr Pro Ala Thr Thr Glu Ala Gln Pro Ser 75 80 85 90 gcg ccc aag gag tct gcg aaa cca gca cca aag gct gcc cct gca gcc 760 Ala Pro Lys Glu Ser Ala Lys Pro Ala Pro Lys Ala Ala Pro Ala Ala 95 100 105 aag gca gca ccg cgc gta gaa acc aag ccg gcc gcc aag acc gcc cct 808 Lys Ala Ala Pro Arg Val Glu Thr Lys Pro Ala Ala Lys Thr Ala Pro 110 115 120 aag gcc aag gag tcc tca gtg cca cag caa cct aag ctt ccg gag cca 856 Lys Ala Lys Glu Ser Ser Val Pro Gln Gln Pro Lys Leu Pro Glu Pro 125 130 135 gga caa acc cca atc agg ggt att ttc aag tcc atc gcg aag aac atg 904 Gly Gln Thr Pro Ile Arg Gly Ile Phe Lys Ser Ile Ala Lys Asn Met 140 145 150 gat atc tcc ctg gaa atc cca acc gca acc tcg gtt cgc gat atg cca 952 Asp Ile Ser Leu Glu Ile Pro Thr Ala Thr Ser Val Arg Asp Met Pro 155 160 165 170 gct cgc ctc atg ttc gaa aac cgc gcg atg gtc aac gat cag ctc aag 1000 Ala Arg Leu Met Phe Glu Asn Arg Ala Met Val Asn Asp Gln Leu Lys 175 180 185 cgc acc cgc ggt ggc aag atc tcc ttc acc cac atc att ggc tac gcc 1048 Arg Thr Arg Gly Gly Lys Ile Ser Phe Thr His Ile Ile Gly Tyr Ala 190 195 200 atg gtg aag gca gtc atg gct cac ccg gac atg aac aac tcc tac gac 1096 Met Val Lys Ala Val Met Ala His Pro Asp Met Asn Asn Ser Tyr Asp 205 210 215 gtc atc gac ggc aag cca acc ctg atc gtg cct gag cac atc aac ctg 1144 Val Ile Asp Gly Lys Pro Thr Leu Ile Val Pro Glu His Ile Asn Leu 220 225 230 ggc ctt gcc atc gac ctt cct cag aag gac ggc tcc cgc gca ctt gtc 1192 Gly Leu Ala Ile Asp Leu Pro Gln Lys Asp Gly Ser Arg Ala Leu Val 235 240 245 250 gta gca gcc atc aag gaa acc gag aag atg aac ttc tcc gag ttc ctc 1240 Val Ala Ala Ile Lys Glu Thr Glu Lys Met Asn Phe Ser Glu Phe Leu 255 260 265 gca gca tac gaa gac atc gtg aca cgc tcc cgc aag ggc aag ctc acc 1288 Ala Ala Tyr Glu Asp Ile Val Thr Arg Ser Arg Lys Gly Lys Leu Thr 270 275 280 atg gat gac tac cag ggc gtt acc gtt tcc ttg acc aac cca ggt ggc 1336 Met Asp Asp Tyr Gln Gly Val Thr Val Ser Leu Thr Asn Pro Gly Gly 285 290 295 atc ggt acc cgc cac tct gtc cca cgt ctg acc aag ggc cag ggc acc 1384 Ile Gly Thr Arg His Ser Val Pro Arg Leu Thr Lys Gly Gln Gly Thr 300 305 310 atc atc ggt gtc ggt tcc atg gat tac cca gca gag ttc cag ggc gct 1432 Ile Ile Gly Val Gly Ser Met Asp Tyr Pro Ala Glu Phe Gln Gly Ala 315 320 325 330 tcc gaa gac cgc ctt gca gag ctc ggc gtt gga aag ctt gtc acc atc 1480 Ser Glu Asp Arg Leu Ala Glu Leu Gly Val Gly Lys Leu Val Thr Ile 335 340 345 acc tcc acc tac gat cac cgc gtg atc cag ggt gct gtg tcc ggt gaa 1528 Thr Ser Thr Tyr Asp His Arg Val Ile Gln Gly Ala Val Ser Gly Glu 350 355 360 ttc ctg cgt acc atg tct cgc ctg ctc acc gat gat tcc ttc tgg gat 1576 Phe Leu Arg Thr Met Ser Arg Leu Leu Thr Asp Asp Ser Phe Trp Asp 365 370 375 gag atc ttc gac gca atg aac gtt cct tac acc cca atg cgt tgg gca 1624 Glu Ile Phe Asp Ala Met Asn Val Pro Tyr Thr Pro Met Arg Trp Ala 380 385 390 cag gac gtt cca aac acc ggt gtt gat aag aac acc cgc gtc atg cag 1672 Gln Asp Val Pro Asn Thr Gly Val Asp Lys Asn Thr Arg Val Met Gln 395 400 405 410 ctc att gag gca tac cgc tcc cgt gga cac ctc atc gct gac acc aac 1720 Leu Ile Glu Ala Tyr Arg Ser Arg Gly His Leu Ile Ala Asp Thr Asn 415 420 425 cca ctt tca tgg gtt cag cct ggc atg cca gtt cca gac cac cgc gac 1768 Pro Leu Ser Trp Val Gln Pro Gly Met Pro Val Pro Asp His Arg Asp 430 435 440 ctc gac atc gag acc cac agc ctg acc atc tgg gat ctg gac cgt acc 1816 Leu Asp Ile Glu Thr His Ser Leu Thr Ile Trp Asp Leu Asp Arg Thr 445 450 455 ttc agc gtc ggt ggc ttc ggc ggc aag gag acc atg acc ctg cgc gag 1864 Phe Ser Val Gly Gly Phe Gly Gly Lys Glu Thr Met Thr Leu Arg Glu 460 465 470 gta ctg tcc cgc ctg cgc gct gcc tac acc ttg aag gtc ggc tcc gaa 1912 Val Leu Ser Arg Leu Arg Ala Ala Tyr Thr Leu Lys Val Gly Ser Glu 475 480 485 490 tac acc cac atc ctg gac cgc gac gag cgc acc tgg ctg cag gac cgc 1960 Tyr Thr His Ile Leu Asp Arg Asp Glu Arg Thr Trp Leu Gln Asp Arg 495 500 505 ctc gaa gcc gga atg cca aag cca acc cag gca gag cag aag tac atc 2008 Leu Glu Ala Gly Met Pro Lys Pro Thr Gln Ala Glu Gln Lys Tyr Ile 510 515 520 ctg cag aag ctg aac gcc gca gag gct ttc gag aac ttc ctg cag acc 2056 Leu Gln Lys Leu Asn Ala Ala Glu Ala Phe Glu Asn Phe Leu Gln Thr 525 530 535 aag tac gtc ggc cag aag cgc ttc tcc ctc gaa ggt gca gaa gct ctc 2104 Lys Tyr Val Gly Gln Lys Arg Phe Ser Leu Glu Gly Ala Glu Ala Leu 540 545 550 atc cca ctg atg gac tcc gcc atc gac acc gcc gca ggc cag ggc ctc 2152 Ile Pro Leu Met Asp Ser Ala Ile Asp Thr Ala Ala Gly Gln Gly Leu 555 560 565 570 gac gaa gtt gtc atc ggt atg cca cac cgt ggt cgc ctc aac gtg ctg 2200 Asp Glu Val Val Ile Gly Met Pro His Arg Gly Arg Leu Asn Val Leu 575 580 585 ttc aac atc gtg ggc aag cca ctg gca tcc atc ttc aac gag ttt gaa 2248 Phe Asn Ile Val Gly Lys Pro Leu Ala Ser Ile Phe Asn Glu Phe Glu 590 595 600 ggc caa atg gag cag ggc cag atc ggt ggc tcc ggt gac gtg aag tac 2296 Gly Gln Met Glu Gln Gly Gln Ile Gly Gly Ser Gly Asp Val Lys Tyr 605 610 615 cac ctc ggt tcc gaa ggc cag cac ctg cag atg ttc ggc gac ggc gag 2344 His Leu Gly Ser Glu Gly Gln His Leu Gln Met Phe Gly Asp Gly Glu 620 625 630 atc aag gtc tcc ctg act gct aac ccg tcc cac ctg gaa gct gtt aac 2392 Ile Lys Val Ser Leu Thr Ala Asn Pro Ser His Leu Glu Ala Val Asn 635 640 645 650 cca gtg atg gaa ggt atc gtc cgc gca aag cag gac tac ctg gac aag 2440 Pro Val Met Glu Gly Ile Val Arg Ala Lys Gln Asp Tyr Leu Asp Lys 655 660 665 ggc gta gac ggc aag act gtt gtg cca ctg ctg ctc cac ggt gac gct 2488 Gly Val Asp Gly Lys Thr Val Val Pro Leu Leu Leu His Gly Asp Ala 670 675 680 gca ttc gca ggc ctg ggc atc gtg cca gaa acc atc aac ctg gct aag 2536 Ala Phe Ala Gly Leu Gly Ile Val Pro Glu Thr Ile Asn Leu Ala Lys 685 690 695 ctg cgt cgacgtcgga ggcaccatcc acatcgtggt gaacaaccag atcggcttca 2592 Leu Arg 700 ccaccacccc agactccagc cgctccatgc actacgcaac cgactacgcc aaggcattcg 2652 gctgcccagt cttccacgtc aatggtgatg acccagaggc agttgtctgg gttggccagc 2712 tggcaaccga gtaccgtcgt cgcttcggca aggacgtctt catcgacctc gtttgctacc 2772 gcctccgcgg ccacaacgaa gctgatgatc cttccatgac ccagccaaag atgtatgagc 2832 tcatcaccgg ccgcgagacc gttcgtgctc agtacaccga agacctgctc ggacgtggag 2892 acctctccaa cgaagatgca gaagcagtcg tccgcgactt ccacgaccag atggaatctg 2952 tgttcaacga agtcaaggaa ggcggcaaga agcaggctga ggcacagacc ggcatcaccg 3012 gctcccagaa gcttccacac ggccttgaga ccaacatctc ccgtgaagag ctcctggaac 3072 tgggacaggc tttcgccaac accccagaag gcttcaacta ccacccacgt gtggctccag 3132 ttgctaagaa gcgcgtctcc tctgtcaccg aaggtggcat cgactgggca tggggcgagc 3192 tcctcgcctt cggttccctg gctaactccg gccgcttggt tcgccttgca ggtgaagatt 3252 cccgccgcgg taccttcacc cagcgccacg cagttgccat cgacccagcg accgctgaag 3312 agttcaaccc actccacgag cttgcacagt ccaagggcaa caacggtaag ttcctggtct 3372 acaactccgc actgaccgag tacgcaggca tgggcttcga gtacggctac tccgtaggaa 3432 acgaagactc cgtcgttgca tgggaagcac agttcggcga cttcgccaac ggcgctcaga 3492 ccatcatcga tgagtacgtc tcctcaggcg aagctaagtg gggccagacc tccaagctga 3552 tccttctgct gcctcacggc tacgaaggcc agggcccaga ccactcttcc gcacgtatcg 3612 agcgcttcct gcagctgtgc gctgagggtt ccatgactgt tgctcagcca tccaccccag 3672 caaaccactt ccacctgctg cgtcgtcacg ctctgtccga cctgaagcgt ccactggtta 3732 tcttcacccc gaagtccatg ctgcgtaaca aggctgctgc ctccgcacca gaagacttca 3792 ctgaggtcac caagttccaa tccgtgatcg acgatccaaa cgttgcagat gcagccaagg 3852 tgaagaaggt catgctggtc tccggcaagc tgtactacga attggcaaag cgcaaggaga 3912 aggacggacg cgacgacatc gcgatcgttc gtatcgaaat gctccaccca attccgttca 3972 accgcatctc cgaggctctt gccggctacc ctaacgctga ggaagtcctc ttcgttcagg 4032 atgagccagc aaaccagggc ccatggccgt tctaccagga gcacctccca gagctgatcc 4092 cgaacatgcc aaagatgcgc cgcgtttccc gccgcgctca gtcctccacc gcaactggtg 4152 ttgctaaggt gcaccagctg gaggagaagc agcttatcga cgaggctttc gaggcttaag 4212 tctttatagt cctgcactag cctagagggc cttatgcagt gtgaatcaca cagcataagg 4272 ccctttttgc tgccgtggtt gcctaaggtg gaaggcatga aacgaatctg tgcggtcacg 4332 atctcttcag tacttttgct aagtggctgc tcctccactt ccaccacgca gctcgag 4389 43 700 PRT Corynebacterium glutamicum 43 Met Leu Gln Leu Gly Leu Arg His Asn Gln Pro Thr Thr Asn Val Thr 1 5 10 15 Val Asp Lys Ile Lys Leu Asn Lys Pro Ser Arg Ser Lys Glu Lys Arg 20 25 30 Arg Val Pro Ala Val Ser Ser Ala Ser Thr Phe Gly Gln Asn Ala Trp 35 40 45 Leu Val Asp Glu Met Phe Gln Gln Phe Gln Lys Asp Pro Lys Ser Val 50 55 60 Asp Lys Glu Trp Arg Glu Leu Phe Glu Ala Gln Gly Gly Pro Asn Ala 65 70 75 80 Thr Pro Ala Thr Thr Glu Ala Gln Pro Ser Ala Pro Lys Glu Ser Ala 85 90 95 Lys Pro Ala Pro Lys Ala Ala Pro Ala Ala Lys Ala Ala Pro Arg Val 100 105 110 Glu Thr Lys Pro Ala Ala Lys Thr Ala Pro Lys Ala Lys Glu Ser Ser 115 120 125 Val Pro Gln Gln Pro Lys Leu Pro Glu Pro Gly Gln Thr Pro Ile Arg 130 135 140 Gly Ile Phe Lys Ser Ile Ala Lys Asn Met Asp Ile Ser Leu Glu Ile 145 150 155 160 Pro Thr Ala Thr Ser Val Arg Asp Met Pro Ala Arg Leu Met Phe Glu 165 170 175 Asn Arg Ala Met Val Asn Asp Gln Leu Lys Arg Thr Arg Gly Gly Lys 180 185 190 Ile Ser Phe Thr His Ile Ile Gly Tyr Ala Met Val Lys Ala Val Met 195 200 205 Ala His Pro Asp Met Asn Asn Ser Tyr Asp Val Ile Asp Gly Lys Pro 210 215 220 Thr Leu Ile Val Pro Glu His Ile Asn Leu Gly Leu Ala Ile Asp Leu 225 230 235 240 Pro Gln Lys Asp Gly Ser Arg Ala Leu Val Val Ala Ala Ile Lys Glu 245 250 255 Thr Glu Lys Met Asn Phe Ser Glu Phe Leu Ala Ala Tyr Glu Asp Ile 260 265 270 Val Thr Arg Ser Arg Lys Gly Lys Leu Thr Met Asp Asp Tyr Gln Gly 275 280 285 Val Thr Val Ser Leu Thr Asn Pro Gly Gly Ile Gly Thr Arg His Ser 290 295 300 Val Pro Arg Leu Thr Lys Gly Gln Gly Thr Ile Ile Gly Val Gly Ser 305 310 315 320 Met Asp Tyr Pro Ala Glu Phe Gln Gly Ala Ser Glu Asp Arg Leu Ala 325 330 335 Glu Leu Gly Val Gly Lys Leu Val Thr Ile Thr Ser Thr Tyr Asp His 340 345 350 Arg Val Ile Gln Gly Ala Val Ser Gly Glu Phe Leu Arg Thr Met Ser 355 360 365 Arg Leu Leu Thr Asp Asp Ser Phe Trp Asp Glu Ile Phe Asp Ala Met 370 375 380 Asn Val Pro Tyr Thr Pro Met Arg Trp Ala Gln Asp Val Pro Asn Thr 385 390 395 400 Gly Val Asp Lys Asn Thr Arg Val Met Gln Leu Ile Glu Ala Tyr Arg 405 410 415 Ser Arg Gly His Leu Ile Ala Asp Thr Asn Pro Leu Ser Trp Val Gln 420 425 430 Pro Gly Met Pro Val Pro Asp His Arg Asp Leu Asp Ile Glu Thr His 435 440 445 Ser Leu Thr Ile Trp Asp Leu Asp Arg Thr Phe Ser Val Gly Gly Phe 450 455 460 Gly Gly Lys Glu Thr Met Thr Leu Arg Glu Val Leu Ser Arg Leu Arg 465 470 475 480 Ala Ala Tyr Thr Leu Lys Val Gly Ser Glu Tyr Thr His Ile Leu Asp 485 490 495 Arg Asp Glu Arg Thr Trp Leu Gln Asp Arg Leu Glu Ala Gly Met Pro 500 505 510 Lys Pro Thr Gln Ala Glu Gln Lys Tyr Ile Leu Gln Lys Leu Asn Ala 515 520 525 Ala Glu Ala Phe Glu Asn Phe Leu Gln Thr Lys Tyr Val Gly Gln Lys 530 535 540 Arg Phe Ser Leu Glu Gly Ala Glu Ala Leu Ile Pro Leu Met Asp Ser 545 550 555 560 Ala Ile Asp Thr Ala Ala Gly Gln Gly Leu Asp Glu Val Val Ile Gly 565 570 575 Met Pro His Arg Gly Arg Leu Asn Val Leu Phe Asn Ile Val Gly Lys 580 585 590 Pro Leu Ala Ser Ile Phe Asn Glu Phe Glu Gly Gln Met Glu Gln Gly 595 600 605 Gln Ile Gly Gly Ser Gly Asp Val Lys Tyr His Leu Gly Ser Glu Gly 610 615 620 Gln His Leu Gln Met Phe Gly Asp Gly Glu Ile Lys Val Ser Leu Thr 625 630 635 640 Ala Asn Pro Ser His Leu Glu Ala Val Asn Pro Val Met Glu Gly Ile 645 650 655 Val Arg Ala Lys Gln Asp Tyr Leu Asp Lys Gly Val Asp Gly Lys Thr 660 665 670 Val Val Pro Leu Leu Leu His Gly Asp Ala Ala Phe Ala Gly Leu Gly 675 680 685 Ile Val Pro Glu Thr Ile Asn Leu Ala Lys Leu Arg 690 695 700 44 4391 DNA Corynebacterium glutamicum CDS (443)..(4210) sucA801 44 gtcgacaagc aaaatcgaag cggcagcacg ccgcgtcgga gccttaaacg ccatcgccgc 60 catccctgat ggtttcaatc atcaagtcgg tgaacgcggg cgcaacctgt catccggaca 120 gcgccaactg atcgcgctgg cgcgcgccga actcatcgag ccttccatca tgcttctcga 180 cgaagccacc tccaccctcg accccgccac cgaagccgtt atcctcaacg cctccgatcg 240 agtcactaag ggacgcacca gcatcatcgt cgcgcaccgc ttggcaaccg ctaaaagggc 300 cgaccgtatt cttgttgttg aacaaggacg tatcattgag gacggatctc acgacgcgtt 360 gttgtctgct aacggcacct acgcccgcat gtggcattta atggcctgac acgttatttt 420 taggagaact gtcaacaaat ta atg cta caa ctg ggg ctt agg cat aat cag 472 Met Leu Gln Leu Gly Leu Arg His Asn Gln 1 5 10 cca acg acc aac gtt aca gtg gat aaa ata aag ctc aat aaa ccc tca 520 Pro Thr Thr Asn Val Thr Val Asp Lys Ile Lys Leu Asn Lys Pro Ser 15 20 25 aga agc aag gaa aag agg cga gta cct gcc gtg agc agc gct agt act 568 Arg Ser Lys Glu Lys Arg Arg Val Pro Ala Val Ser Ser Ala Ser Thr 30 35 40 ttc ggc cag aat gcg tgg ctg gta gac gag atg ttc cag cag ttc cag 616 Phe Gly Gln Asn Ala Trp Leu Val Asp Glu Met Phe Gln Gln Phe Gln 45 50 55 aag gac ccc aag tcc gtg gac aag gaa tgg aga gaa ctc ttt gag gcg 664 Lys Asp Pro Lys Ser Val Asp Lys Glu Trp Arg Glu Leu Phe Glu Ala 60 65 70 cag ggg gga cca aat gct acc ccc gct aca aca gaa gca cag cct tca 712 Gln Gly Gly Pro Asn Ala Thr Pro Ala Thr Thr Glu Ala Gln Pro Ser 75 80 85 90 gcg ccc aag gag tct gcg aaa cca gca cca aag gct gcc cct gca gcc 760 Ala Pro Lys Glu Ser Ala Lys Pro Ala Pro Lys Ala Ala Pro Ala Ala 95 100 105 aag gca

gca ccg cgc gta gaa acc aag ccg gcc gcc aag acc gcc cct 808 Lys Ala Ala Pro Arg Val Glu Thr Lys Pro Ala Ala Lys Thr Ala Pro 110 115 120 aag gcc aag gag tcc tca gtg cca cag caa cct aag ctt ccg gag cca 856 Lys Ala Lys Glu Ser Ser Val Pro Gln Gln Pro Lys Leu Pro Glu Pro 125 130 135 gga caa acc cca atc agg ggt att ttc aag tcc atc gcg aag aac atg 904 Gly Gln Thr Pro Ile Arg Gly Ile Phe Lys Ser Ile Ala Lys Asn Met 140 145 150 gat atc tcc ctg gaa atc cca acc gca acc tcg gtt cgc gat atg cca 952 Asp Ile Ser Leu Glu Ile Pro Thr Ala Thr Ser Val Arg Asp Met Pro 155 160 165 170 gct cgc ctc atg ttc gaa aac cgc gcg atg gtc aac gat cag ctc aag 1000 Ala Arg Leu Met Phe Glu Asn Arg Ala Met Val Asn Asp Gln Leu Lys 175 180 185 cgc acc cgc ggt ggc aag atc tcc ttc acc cac atc att ggc tac gcc 1048 Arg Thr Arg Gly Gly Lys Ile Ser Phe Thr His Ile Ile Gly Tyr Ala 190 195 200 atg gtg aag gca gtc atg gct cac ccg gac atg aac aac tcc tac gac 1096 Met Val Lys Ala Val Met Ala His Pro Asp Met Asn Asn Ser Tyr Asp 205 210 215 gtc atc gac ggc aag cca acc ctg atc gtg cct gag cac atc aac ctg 1144 Val Ile Asp Gly Lys Pro Thr Leu Ile Val Pro Glu His Ile Asn Leu 220 225 230 ggc ctt gcc atc gac ctt cct cag aag gac ggc tcc cgc gca ctt gtc 1192 Gly Leu Ala Ile Asp Leu Pro Gln Lys Asp Gly Ser Arg Ala Leu Val 235 240 245 250 gta gca gcc atc aag gaa acc gag aag atg aac ttc tcc gag ttc ctc 1240 Val Ala Ala Ile Lys Glu Thr Glu Lys Met Asn Phe Ser Glu Phe Leu 255 260 265 gca gca tac gaa gac atc gtg aca cgc tcc cgc aag ggc aag ctc acc 1288 Ala Ala Tyr Glu Asp Ile Val Thr Arg Ser Arg Lys Gly Lys Leu Thr 270 275 280 atg gat gac tac cag ggc gtt acc gtt tcc ttg acc aac cca ggt ggc 1336 Met Asp Asp Tyr Gln Gly Val Thr Val Ser Leu Thr Asn Pro Gly Gly 285 290 295 atc ggt acc cgc cac tct gtc cca cgt ctg acc aag ggc cag ggc acc 1384 Ile Gly Thr Arg His Ser Val Pro Arg Leu Thr Lys Gly Gln Gly Thr 300 305 310 atc atc ggt gtc ggt tcc atg gat tac cca gca gag ttc cag ggc gct 1432 Ile Ile Gly Val Gly Ser Met Asp Tyr Pro Ala Glu Phe Gln Gly Ala 315 320 325 330 tcc gaa gac cgc ctt gca gag ctc ggc gtt gga aag ctt gtc acc atc 1480 Ser Glu Asp Arg Leu Ala Glu Leu Gly Val Gly Lys Leu Val Thr Ile 335 340 345 acc tcc acc tac gat cac cgc gtg atc cag ggt gct gtg tcc ggt gaa 1528 Thr Ser Thr Tyr Asp His Arg Val Ile Gln Gly Ala Val Ser Gly Glu 350 355 360 ttc ctg cgt acc atg tct cgc ctg ctc acc gat gat tcc ttc tgg gat 1576 Phe Leu Arg Thr Met Ser Arg Leu Leu Thr Asp Asp Ser Phe Trp Asp 365 370 375 gag atc ttc gac gca atg aac gtt cct tac acc cca atg cgt tgg gca 1624 Glu Ile Phe Asp Ala Met Asn Val Pro Tyr Thr Pro Met Arg Trp Ala 380 385 390 cag gac gtt cca aac acc ggt gtt gat aag aac acc cgc gtc atg cag 1672 Gln Asp Val Pro Asn Thr Gly Val Asp Lys Asn Thr Arg Val Met Gln 395 400 405 410 ctc att gag gca tac cgc tcc cgt gga cac ctc atc gct gac acc aac 1720 Leu Ile Glu Ala Tyr Arg Ser Arg Gly His Leu Ile Ala Asp Thr Asn 415 420 425 cca ctt tca tgg gtt cag cct ggc atg cca gtt cca gac cac cgc gac 1768 Pro Leu Ser Trp Val Gln Pro Gly Met Pro Val Pro Asp His Arg Asp 430 435 440 ctc gac atc gag acc cac agc ctg acc atc tgg gat ctg gac cgt acc 1816 Leu Asp Ile Glu Thr His Ser Leu Thr Ile Trp Asp Leu Asp Arg Thr 445 450 455 ttc agc gtc ggt ggc ttc ggc ggc aag gag acc atg acc ctg cgc gag 1864 Phe Ser Val Gly Gly Phe Gly Gly Lys Glu Thr Met Thr Leu Arg Glu 460 465 470 gta ctg tcc cgc ctg cgc gct gcc tac acc ttg aag gtc ggc tcc gaa 1912 Val Leu Ser Arg Leu Arg Ala Ala Tyr Thr Leu Lys Val Gly Ser Glu 475 480 485 490 tac acc cac atc ctg gac cgc gac gag cgc acc tgg ctg cag gac cgc 1960 Tyr Thr His Ile Leu Asp Arg Asp Glu Arg Thr Trp Leu Gln Asp Arg 495 500 505 ctc gaa gcc gga atg cca aag cca acc cag gca gag cag aag tac atc 2008 Leu Glu Ala Gly Met Pro Lys Pro Thr Gln Ala Glu Gln Lys Tyr Ile 510 515 520 ctg cag aag ctg aac gcc gca gag gct ttc gag aac ttc ctg cag acc 2056 Leu Gln Lys Leu Asn Ala Ala Glu Ala Phe Glu Asn Phe Leu Gln Thr 525 530 535 aag tac gtc ggc cag aag cgc ttc tcc ctc gaa ggt gca gaa gct ctc 2104 Lys Tyr Val Gly Gln Lys Arg Phe Ser Leu Glu Gly Ala Glu Ala Leu 540 545 550 atc cca ctg atg gac tcc gcc atc gac acc gcc gca ggc cag ggc ctc 2152 Ile Pro Leu Met Asp Ser Ala Ile Asp Thr Ala Ala Gly Gln Gly Leu 555 560 565 570 gac gaa gtt gtc atc ggt atg cca cac cgt ggt cgc ctc aac gtg ctg 2200 Asp Glu Val Val Ile Gly Met Pro His Arg Gly Arg Leu Asn Val Leu 575 580 585 ttc aac atc gtg ggc aag cca ctg gca tcc atc ttc aac gag ttt gaa 2248 Phe Asn Ile Val Gly Lys Pro Leu Ala Ser Ile Phe Asn Glu Phe Glu 590 595 600 ggc caa atg gag cag ggc cag atc ggt ggc tcc ggt gac gtg aag tac 2296 Gly Gln Met Glu Gln Gly Gln Ile Gly Gly Ser Gly Asp Val Lys Tyr 605 610 615 cac ctc ggt tcc gaa ggc cag cac ctg cag atg ttc ggc gac ggc gag 2344 His Leu Gly Ser Glu Gly Gln His Leu Gln Met Phe Gly Asp Gly Glu 620 625 630 atc aag gtc tcc ctg act gct aac ccg tcc cac ctg gaa gct gtt aac 2392 Ile Lys Val Ser Leu Thr Ala Asn Pro Ser His Leu Glu Ala Val Asn 635 640 645 650 cca gtg atg gaa ggt atc gtc cgc gca aag cag gac tac ctg gac aag 2440 Pro Val Met Glu Gly Ile Val Arg Ala Lys Gln Asp Tyr Leu Asp Lys 655 660 665 ggc gta gac ggc aag act gtt gtg cca ctg ctg ctc cac ggt gac gct 2488 Gly Val Asp Gly Lys Thr Val Val Pro Leu Leu Leu His Gly Asp Ala 670 675 680 gca ttc gca ggc ctg ggc atc gtg cca gaa acc atc aac ctg gct aag 2536 Ala Phe Ala Gly Leu Gly Ile Val Pro Glu Thr Ile Asn Leu Ala Lys 685 690 695 ctg cgt ctc gac gtc gga ggc acc atc cac atc gtg gtg aac aac cag 2584 Leu Arg Leu Asp Val Gly Gly Thr Ile His Ile Val Val Asn Asn Gln 700 705 710 atc ggc ttc acc acc acc cca gac tcc agc cgc tcc atg cac tac gca 2632 Ile Gly Phe Thr Thr Thr Pro Asp Ser Ser Arg Ser Met His Tyr Ala 715 720 725 730 acc gac tac gcc aag gca ttc ggc tgc cca gtc ttc cac gtc aat ggt 2680 Thr Asp Tyr Ala Lys Ala Phe Gly Cys Pro Val Phe His Val Asn Gly 735 740 745 gat gac cca gag gca gtt gtc tgg gtt ggc cag ctg gca acc gag tac 2728 Asp Asp Pro Glu Ala Val Val Trp Val Gly Gln Leu Ala Thr Glu Tyr 750 755 760 cgt cgt cgc ttc ggc aag gac gtc ttc atc gac ctc gtt tgc tac cgc 2776 Arg Arg Arg Phe Gly Lys Asp Val Phe Ile Asp Leu Val Cys Tyr Arg 765 770 775 ctc cgc ggc cac aac gaa gct gat gat cct tcc atg acc cag cca aag 2824 Leu Arg Gly His Asn Glu Ala Asp Asp Pro Ser Met Thr Gln Pro Lys 780 785 790 atg tat gag ctc atc acc ggc cgc gag acc gtt cgt gct cag tac acc 2872 Met Tyr Glu Leu Ile Thr Gly Arg Glu Thr Val Arg Ala Gln Tyr Thr 795 800 805 810 gaa gac ctg ctc gga cgt gga gac ctc tcc aac gaa gat gca gaa gca 2920 Glu Asp Leu Leu Gly Arg Gly Asp Leu Ser Asn Glu Asp Ala Glu Ala 815 820 825 gtc gtc cgc gac ttc cac gac cag atg gaa tct gtg ttc aac gaa gtc 2968 Val Val Arg Asp Phe His Asp Gln Met Glu Ser Val Phe Asn Glu Val 830 835 840 aag gaa ggc ggc aag aag cag gct gag gca cag acc ggc atc acc ggc 3016 Lys Glu Gly Gly Lys Lys Gln Ala Glu Ala Gln Thr Gly Ile Thr Gly 845 850 855 tcc cag aag ctt cca cac ggc ctt gag acc aac atc tcc cgt gaa gag 3064 Ser Gln Lys Leu Pro His Gly Leu Glu Thr Asn Ile Ser Arg Glu Glu 860 865 870 ctc ctg gaa ctg gga cag gct ttc gcc aac acc cca gaa ggc ttc aac 3112 Leu Leu Glu Leu Gly Gln Ala Phe Ala Asn Thr Pro Glu Gly Phe Asn 875 880 885 890 tac cac cca cgt gtg gct cca gtt gct aag aag cgc gtc tcc tct gtc 3160 Tyr His Pro Arg Val Ala Pro Val Ala Lys Lys Arg Val Ser Ser Val 895 900 905 acc gaa ggt ggc atc gac tgg gca tgg ggc gag ctc ctc gcc ttc ggt 3208 Thr Glu Gly Gly Ile Asp Trp Ala Trp Gly Glu Leu Leu Ala Phe Gly 910 915 920 tcc ctg gct aac tcc ggc cgc ttg gtt cgc ctt gca ggt gaa gat tcc 3256 Ser Leu Ala Asn Ser Gly Arg Leu Val Arg Leu Ala Gly Glu Asp Ser 925 930 935 cgc cgc ggt acc ttc acc cag cgc cac gca gtt gcc atc gac cca gcg 3304 Arg Arg Gly Thr Phe Thr Gln Arg His Ala Val Ala Ile Asp Pro Ala 940 945 950 acc gct gaa gag ttc aac cca ctc cac gag ctt gca cag tcc aag ggc 3352 Thr Ala Glu Glu Phe Asn Pro Leu His Glu Leu Ala Gln Ser Lys Gly 955 960 965 970 aac aac ggt aag ttc ctg gtc tac aac tcc gca ctg acc gag tac gca 3400 Asn Asn Gly Lys Phe Leu Val Tyr Asn Ser Ala Leu Thr Glu Tyr Ala 975 980 985 ggc atg ggc ttc gag tac ggc tac tcc gta gga aac gaa gac tcc gtc 3448 Gly Met Gly Phe Glu Tyr Gly Tyr Ser Val Gly Asn Glu Asp Ser Val 990 995 1000 gtt gca tgg gaa gca cag ttc ggc gac ttc gcc aac ggc gct cag 3493 Val Ala Trp Glu Ala Gln Phe Gly Asp Phe Ala Asn Gly Ala Gln 1005 1010 1015 acc atc atc gat gag tac gtc tcc tca ggc gaa gct aag tgg ggc 3538 Thr Ile Ile Asp Glu Tyr Val Ser Ser Gly Glu Ala Lys Trp Gly 1020 1025 1030 cag acc tcc aag ctg atc ctt ctg ctg cct cac ggc tac gaa ggc 3583 Gln Thr Ser Lys Leu Ile Leu Leu Leu Pro His Gly Tyr Glu Gly 1035 1040 1045 cag ggc cca gac cac tct tcc gca cgt atc gag cgc ttc ctg cag 3628 Gln Gly Pro Asp His Ser Ser Ala Arg Ile Glu Arg Phe Leu Gln 1050 1055 1060 ctg tgc gct gag ggt tcc atg act gtt gct cag cca tcc acc cca 3673 Leu Cys Ala Glu Gly Ser Met Thr Val Ala Gln Pro Ser Thr Pro 1065 1070 1075 gca aac cac ttc cac ctg ctg cgt cgt cac gct ctg tcc gac ctg 3718 Ala Asn His Phe His Leu Leu Arg Arg His Ala Leu Ser Asp Leu 1080 1085 1090 aag cgt cca ctg gtt atc ttc acc ccg aag tcc atg ctg cgt aac 3763 Lys Arg Pro Leu Val Ile Phe Thr Pro Lys Ser Met Leu Arg Asn 1095 1100 1105 aag gct gct gcc tcc gca cca gaa gac ttc act gag gtc acc aag 3808 Lys Ala Ala Ala Ser Ala Pro Glu Asp Phe Thr Glu Val Thr Lys 1110 1115 1120 ttc caa tcc gtg atc gac gat cca aac gtt gca gat gca gcc aag 3853 Phe Gln Ser Val Ile Asp Asp Pro Asn Val Ala Asp Ala Ala Lys 1125 1130 1135 gtg aag aag gtc atg ctg gtc tcc ggc aag ctg tac tac gaa ttg 3898 Val Lys Lys Val Met Leu Val Ser Gly Lys Leu Tyr Tyr Glu Leu 1140 1145 1150 gca aag cgc aag gag aag gac gga cgc gac gac atc gcg atc gtt 3943 Ala Lys Arg Lys Glu Lys Asp Gly Arg Asp Asp Ile Ala Ile Val 1155 1160 1165 cgt atc gaa atg ctc cac cca att ccg ttc aac cgc atc tcc gag 3988 Arg Ile Glu Met Leu His Pro Ile Pro Phe Asn Arg Ile Ser Glu 1170 1175 1180 gct ctt gcc ggc tac cct aac gct gag gaa gtc ctc ttc gtt cag 4033 Ala Leu Ala Gly Tyr Pro Asn Ala Glu Glu Val Leu Phe Val Gln 1185 1190 1195 gat gag cca gca aac cag ggc cca tgg ccg ttc tac cag gag cac 4078 Asp Glu Pro Ala Asn Gln Gly Pro Trp Pro Phe Tyr Gln Glu His 1200 1205 1210 ctc cca gag ctg atc ccg aac atg cca aag atg cgc cgc gtt tcc 4123 Leu Pro Glu Leu Ile Pro Asn Met Pro Lys Met Arg Arg Val Ser 1215 1220 1225 cgc cgc gct cag tcc tcc acc gca act ggt gtt gct aag gtg cac 4168 Arg Arg Ala Gln Ser Ser Thr Ala Thr Gly Val Ala Lys Val His 1230 1235 1240 cag ctg gag gag aag cag ctt atc gac gag gct ttc gag gct 4210 Gln Leu Glu Glu Lys Gln Leu Ile Asp Glu Ala Phe Glu Ala 1245 1250 1255 taagtcttta tagtcctgca ctagcctaga gggccttatg cagtgtgaat cacacagcat 4270 aaggcccttt ttgctgccgt ggttgcctaa ggtggaaggc atgaaacgaa tctgtgcggt 4330 cacgatctct tcagtacttt tgctaagtgg ctgctcctcc acttccacca cgcagctcga 4390 g 4391 45 1256 PRT Corynebacterium glutamicum 45 Met Leu Gln Leu Gly Leu Arg His Asn Gln Pro Thr Thr Asn Val Thr 1 5 10 15 Val Asp Lys Ile Lys Leu Asn Lys Pro Ser Arg Ser Lys Glu Lys Arg 20 25 30 Arg Val Pro Ala Val Ser Ser Ala Ser Thr Phe Gly Gln Asn Ala Trp 35 40 45 Leu Val Asp Glu Met Phe Gln Gln Phe Gln Lys Asp Pro Lys Ser Val 50 55 60 Asp Lys Glu Trp Arg Glu Leu Phe Glu Ala Gln Gly Gly Pro Asn Ala 65 70 75 80 Thr Pro Ala Thr Thr Glu Ala Gln Pro Ser Ala Pro Lys Glu Ser Ala 85 90 95 Lys Pro Ala Pro Lys Ala Ala Pro Ala Ala Lys Ala Ala Pro Arg Val 100 105 110 Glu Thr Lys Pro Ala Ala Lys Thr Ala Pro Lys Ala Lys Glu Ser Ser 115 120 125 Val Pro Gln Gln Pro Lys Leu Pro Glu Pro Gly Gln Thr Pro Ile Arg 130 135 140 Gly Ile Phe Lys Ser Ile Ala Lys Asn Met Asp Ile Ser Leu Glu Ile 145 150 155 160 Pro Thr Ala Thr Ser Val Arg Asp Met Pro Ala Arg Leu Met Phe Glu 165 170 175 Asn Arg Ala Met Val Asn Asp Gln Leu Lys Arg Thr Arg Gly Gly Lys 180 185 190 Ile Ser Phe Thr His Ile Ile Gly Tyr Ala Met Val Lys Ala Val Met 195 200 205 Ala His Pro Asp Met Asn Asn Ser Tyr Asp Val Ile Asp Gly Lys Pro 210 215 220 Thr Leu Ile Val Pro Glu His Ile Asn Leu Gly Leu Ala Ile Asp Leu 225 230 235 240 Pro Gln Lys Asp Gly Ser Arg Ala Leu Val Val Ala Ala Ile Lys Glu 245 250 255 Thr Glu Lys Met Asn Phe Ser Glu Phe Leu Ala Ala Tyr Glu Asp Ile 260 265 270 Val Thr Arg Ser Arg Lys Gly Lys Leu Thr Met Asp Asp Tyr Gln Gly 275 280 285 Val Thr Val Ser Leu Thr Asn Pro Gly Gly Ile Gly Thr Arg His Ser 290 295 300 Val Pro Arg Leu Thr Lys Gly Gln Gly Thr Ile Ile Gly Val Gly Ser 305 310 315 320 Met Asp Tyr Pro Ala Glu Phe Gln Gly Ala Ser Glu Asp Arg Leu Ala 325 330 335 Glu Leu Gly Val Gly Lys Leu Val Thr Ile Thr Ser Thr Tyr Asp His 340 345 350 Arg Val Ile Gln Gly Ala Val Ser Gly Glu Phe Leu Arg Thr Met Ser 355 360 365 Arg Leu Leu Thr Asp Asp Ser Phe Trp Asp Glu Ile Phe Asp Ala Met 370 375 380 Asn Val Pro Tyr Thr Pro Met Arg Trp Ala Gln Asp Val Pro Asn Thr 385 390 395 400 Gly Val Asp Lys Asn Thr Arg Val Met Gln Leu Ile Glu Ala Tyr Arg 405 410 415 Ser Arg Gly His Leu Ile Ala Asp Thr Asn Pro Leu Ser Trp Val Gln 420 425 430 Pro Gly Met Pro Val Pro Asp His Arg Asp Leu Asp Ile Glu Thr His 435 440 445 Ser Leu Thr Ile Trp Asp Leu Asp Arg Thr Phe Ser Val Gly Gly Phe 450 455 460 Gly Gly Lys Glu Thr Met Thr Leu Arg Glu Val Leu Ser Arg Leu Arg 465 470 475 480 Ala Ala Tyr Thr Leu Lys Val Gly Ser Glu Tyr Thr His Ile Leu Asp 485 490 495 Arg Asp Glu Arg Thr Trp Leu Gln Asp Arg Leu Glu Ala Gly Met Pro 500 505 510 Lys Pro Thr Gln Ala Glu Gln Lys Tyr Ile Leu Gln Lys Leu Asn Ala 515 520 525 Ala Glu Ala

Phe Glu Asn Phe Leu Gln Thr Lys Tyr Val Gly Gln Lys 530 535 540 Arg Phe Ser Leu Glu Gly Ala Glu Ala Leu Ile Pro Leu Met Asp Ser 545 550 555 560 Ala Ile Asp Thr Ala Ala Gly Gln Gly Leu Asp Glu Val Val Ile Gly 565 570 575 Met Pro His Arg Gly Arg Leu Asn Val Leu Phe Asn Ile Val Gly Lys 580 585 590 Pro Leu Ala Ser Ile Phe Asn Glu Phe Glu Gly Gln Met Glu Gln Gly 595 600 605 Gln Ile Gly Gly Ser Gly Asp Val Lys Tyr His Leu Gly Ser Glu Gly 610 615 620 Gln His Leu Gln Met Phe Gly Asp Gly Glu Ile Lys Val Ser Leu Thr 625 630 635 640 Ala Asn Pro Ser His Leu Glu Ala Val Asn Pro Val Met Glu Gly Ile 645 650 655 Val Arg Ala Lys Gln Asp Tyr Leu Asp Lys Gly Val Asp Gly Lys Thr 660 665 670 Val Val Pro Leu Leu Leu His Gly Asp Ala Ala Phe Ala Gly Leu Gly 675 680 685 Ile Val Pro Glu Thr Ile Asn Leu Ala Lys Leu Arg Leu Asp Val Gly 690 695 700 Gly Thr Ile His Ile Val Val Asn Asn Gln Ile Gly Phe Thr Thr Thr 705 710 715 720 Pro Asp Ser Ser Arg Ser Met His Tyr Ala Thr Asp Tyr Ala Lys Ala 725 730 735 Phe Gly Cys Pro Val Phe His Val Asn Gly Asp Asp Pro Glu Ala Val 740 745 750 Val Trp Val Gly Gln Leu Ala Thr Glu Tyr Arg Arg Arg Phe Gly Lys 755 760 765 Asp Val Phe Ile Asp Leu Val Cys Tyr Arg Leu Arg Gly His Asn Glu 770 775 780 Ala Asp Asp Pro Ser Met Thr Gln Pro Lys Met Tyr Glu Leu Ile Thr 785 790 795 800 Gly Arg Glu Thr Val Arg Ala Gln Tyr Thr Glu Asp Leu Leu Gly Arg 805 810 815 Gly Asp Leu Ser Asn Glu Asp Ala Glu Ala Val Val Arg Asp Phe His 820 825 830 Asp Gln Met Glu Ser Val Phe Asn Glu Val Lys Glu Gly Gly Lys Lys 835 840 845 Gln Ala Glu Ala Gln Thr Gly Ile Thr Gly Ser Gln Lys Leu Pro His 850 855 860 Gly Leu Glu Thr Asn Ile Ser Arg Glu Glu Leu Leu Glu Leu Gly Gln 865 870 875 880 Ala Phe Ala Asn Thr Pro Glu Gly Phe Asn Tyr His Pro Arg Val Ala 885 890 895 Pro Val Ala Lys Lys Arg Val Ser Ser Val Thr Glu Gly Gly Ile Asp 900 905 910 Trp Ala Trp Gly Glu Leu Leu Ala Phe Gly Ser Leu Ala Asn Ser Gly 915 920 925 Arg Leu Val Arg Leu Ala Gly Glu Asp Ser Arg Arg Gly Thr Phe Thr 930 935 940 Gln Arg His Ala Val Ala Ile Asp Pro Ala Thr Ala Glu Glu Phe Asn 945 950 955 960 Pro Leu His Glu Leu Ala Gln Ser Lys Gly Asn Asn Gly Lys Phe Leu 965 970 975 Val Tyr Asn Ser Ala Leu Thr Glu Tyr Ala Gly Met Gly Phe Glu Tyr 980 985 990 Gly Tyr Ser Val Gly Asn Glu Asp Ser Val Val Ala Trp Glu Ala Gln 995 1000 1005 Phe Gly Asp Phe Ala Asn Gly Ala Gln Thr Ile Ile Asp Glu Tyr 1010 1015 1020 Val Ser Ser Gly Glu Ala Lys Trp Gly Gln Thr Ser Lys Leu Ile 1025 1030 1035 Leu Leu Leu Pro His Gly Tyr Glu Gly Gln Gly Pro Asp His Ser 1040 1045 1050 Ser Ala Arg Ile Glu Arg Phe Leu Gln Leu Cys Ala Glu Gly Ser 1055 1060 1065 Met Thr Val Ala Gln Pro Ser Thr Pro Ala Asn His Phe His Leu 1070 1075 1080 Leu Arg Arg His Ala Leu Ser Asp Leu Lys Arg Pro Leu Val Ile 1085 1090 1095 Phe Thr Pro Lys Ser Met Leu Arg Asn Lys Ala Ala Ala Ser Ala 1100 1105 1110 Pro Glu Asp Phe Thr Glu Val Thr Lys Phe Gln Ser Val Ile Asp 1115 1120 1125 Asp Pro Asn Val Ala Asp Ala Ala Lys Val Lys Lys Val Met Leu 1130 1135 1140 Val Ser Gly Lys Leu Tyr Tyr Glu Leu Ala Lys Arg Lys Glu Lys 1145 1150 1155 Asp Gly Arg Asp Asp Ile Ala Ile Val Arg Ile Glu Met Leu His 1160 1165 1170 Pro Ile Pro Phe Asn Arg Ile Ser Glu Ala Leu Ala Gly Tyr Pro 1175 1180 1185 Asn Ala Glu Glu Val Leu Phe Val Gln Asp Glu Pro Ala Asn Gln 1190 1195 1200 Gly Pro Trp Pro Phe Tyr Gln Glu His Leu Pro Glu Leu Ile Pro 1205 1210 1215 Asn Met Pro Lys Met Arg Arg Val Ser Arg Arg Ala Gln Ser Ser 1220 1225 1230 Thr Ala Thr Gly Val Ala Lys Val His Gln Leu Glu Glu Lys Gln 1235 1240 1245 Leu Ile Asp Glu Ala Phe Glu Ala 1250 1255 46 4391 DNA Corynebacterium glutamicum CDS (443)..(4210) sucA805 46 gtcgacaagc aaaatcgaag cggcagcacg ccgcgtcgga gccttaaacg ccatcgccgc 60 catccctgat ggtttcaatc atcaagtcgg tgaacgcggg cgcaacctgt catccggaca 120 gcgccaactg atcgcgctgg cgcgcgccga actcatcgag ccttccatca tgcttctcga 180 cgaagccacc tccaccctcg accccgccac cgaagccgtt atcctcaacg cctccgatcg 240 agtcactaag ggacgcacca gcatcatcgt cgcgcaccgc ttggcaaccg ctaaaagggc 300 cgaccgtatt cttgttgttg aacaaggacg tatcattgag gacggatctc acgacgcgtt 360 gttgtctgct aacggcacct acgcccgcat gtggcattta atggcctgac acgttatttt 420 taggagaact gtcaacaaat ta atg cta caa ctg ggg ctt agg cat aat cag 472 Met Leu Gln Leu Gly Leu Arg His Asn Gln 1 5 10 cca acg acc aac gtt aca gtg gat aaa ata aag ctc aat aaa ccc tca 520 Pro Thr Thr Asn Val Thr Val Asp Lys Ile Lys Leu Asn Lys Pro Ser 15 20 25 aga agc aag gaa aag agg cga gta cct gcc gtg agc agc gct agt act 568 Arg Ser Lys Glu Lys Arg Arg Val Pro Ala Val Ser Ser Ala Ser Thr 30 35 40 ttc ggc cag aat gcg tgg ctg gta gac gag atg ttc cag cag ttc cag 616 Phe Gly Gln Asn Ala Trp Leu Val Asp Glu Met Phe Gln Gln Phe Gln 45 50 55 aag gac ccc aag tcc gtg gac aag gaa tgg aga gaa ctc ttt gag gcg 664 Lys Asp Pro Lys Ser Val Asp Lys Glu Trp Arg Glu Leu Phe Glu Ala 60 65 70 cag ggg gga cca aat gct acc ccc gct aca aca gaa gca cag cct tca 712 Gln Gly Gly Pro Asn Ala Thr Pro Ala Thr Thr Glu Ala Gln Pro Ser 75 80 85 90 gcg ccc aag gag tct gcg aaa cca gca cca aag gct gcc cct gca gcc 760 Ala Pro Lys Glu Ser Ala Lys Pro Ala Pro Lys Ala Ala Pro Ala Ala 95 100 105 aag gca gca ccg cgc gta gaa acc aag ccg gcc gcc aag acc gcc cct 808 Lys Ala Ala Pro Arg Val Glu Thr Lys Pro Ala Ala Lys Thr Ala Pro 110 115 120 aag gcc aag gag tcc tca gtg cca cag caa cct aag ctt ccg gag cca 856 Lys Ala Lys Glu Ser Ser Val Pro Gln Gln Pro Lys Leu Pro Glu Pro 125 130 135 gga caa acc cca atc agg ggt att ttc aag tcc atc gcg aag aac atg 904 Gly Gln Thr Pro Ile Arg Gly Ile Phe Lys Ser Ile Ala Lys Asn Met 140 145 150 gat atc tcc ctg gaa atc cca acc gca acc tcg gtt cgc gat atg cca 952 Asp Ile Ser Leu Glu Ile Pro Thr Ala Thr Ser Val Arg Asp Met Pro 155 160 165 170 gct cgc ctc atg ttc gaa aac cgc gcg atg gtc aac gat cag ctc aag 1000 Ala Arg Leu Met Phe Glu Asn Arg Ala Met Val Asn Asp Gln Leu Lys 175 180 185 cgc acc cgc ggt ggc aag atc tcc ttc acc cac atc att ggc tac gcc 1048 Arg Thr Arg Gly Gly Lys Ile Ser Phe Thr His Ile Ile Gly Tyr Ala 190 195 200 atg gtg aag gca gtc atg gct cac ccg gac atg aac aac tcc tac gac 1096 Met Val Lys Ala Val Met Ala His Pro Asp Met Asn Asn Ser Tyr Asp 205 210 215 gtc atc gac ggc aag cca acc ctg atc gtg cct gag cac atc aac ctg 1144 Val Ile Asp Gly Lys Pro Thr Leu Ile Val Pro Glu His Ile Asn Leu 220 225 230 ggc ctt gcc atc gac ctt cct cag aag gac ggc tcc cgc gca ctt gtc 1192 Gly Leu Ala Ile Asp Leu Pro Gln Lys Asp Gly Ser Arg Ala Leu Val 235 240 245 250 gta gca gcc atc aag gaa acc gag aag atg aac ttc tcc gag ttc ctc 1240 Val Ala Ala Ile Lys Glu Thr Glu Lys Met Asn Phe Ser Glu Phe Leu 255 260 265 gca gca tac gaa gac atc gtg aca cgc tcc cgc aag ggc aag ctc acc 1288 Ala Ala Tyr Glu Asp Ile Val Thr Arg Ser Arg Lys Gly Lys Leu Thr 270 275 280 atg gat gac tac cag ggc gtt acc gtt tcc ttg acc aac cca ggt ggc 1336 Met Asp Asp Tyr Gln Gly Val Thr Val Ser Leu Thr Asn Pro Gly Gly 285 290 295 atc ggt acc cgc cac tct gtc cca cgt ctg acc aag ggc cag ggc acc 1384 Ile Gly Thr Arg His Ser Val Pro Arg Leu Thr Lys Gly Gln Gly Thr 300 305 310 atc atc ggt gtc ggt tcc atg gat tac cca gca gag ttc cag ggc gct 1432 Ile Ile Gly Val Gly Ser Met Asp Tyr Pro Ala Glu Phe Gln Gly Ala 315 320 325 330 tcc gaa gac cgc ctt gca gag ctc ggc gtt gga aag ctt gtc acc atc 1480 Ser Glu Asp Arg Leu Ala Glu Leu Gly Val Gly Lys Leu Val Thr Ile 335 340 345 acc tcc acc tac gat cac cgc gtg atc cag ggt gct gtg tcc ggt gaa 1528 Thr Ser Thr Tyr Asp His Arg Val Ile Gln Gly Ala Val Ser Gly Glu 350 355 360 ttc ctg cgt acc atg tct cgc ctg ctc acc gat gat tcc ttc tgg gat 1576 Phe Leu Arg Thr Met Ser Arg Leu Leu Thr Asp Asp Ser Phe Trp Asp 365 370 375 gag atc ttc gac gca atg aac gtt cct tac acc cca atg cgt tgg gca 1624 Glu Ile Phe Asp Ala Met Asn Val Pro Tyr Thr Pro Met Arg Trp Ala 380 385 390 cag gac gtt cca aac acc ggt gtt gat aag aac acc cgc gtc atg cag 1672 Gln Asp Val Pro Asn Thr Gly Val Asp Lys Asn Thr Arg Val Met Gln 395 400 405 410 ctc att gag gca tac cgc tcc cgt gga cac ctc atc gct gac acc aac 1720 Leu Ile Glu Ala Tyr Arg Ser Arg Gly His Leu Ile Ala Asp Thr Asn 415 420 425 cca ctt tca tgg gtt cag cct ggc atg cca gtt cca gac cac cgc gac 1768 Pro Leu Ser Trp Val Gln Pro Gly Met Pro Val Pro Asp His Arg Asp 430 435 440 ctc gac atc gag acc cac agc ctg acc atc tgg gat ctg gac cgt acc 1816 Leu Asp Ile Glu Thr His Ser Leu Thr Ile Trp Asp Leu Asp Arg Thr 445 450 455 ttc agc gtc ggt ggc ttc ggc ggc aag gag acc atg acc ctg cgc gag 1864 Phe Ser Val Gly Gly Phe Gly Gly Lys Glu Thr Met Thr Leu Arg Glu 460 465 470 gta ctg tcc cgc ctg cgc gct gcc tac acc ttg aag gtc ggc tcc gaa 1912 Val Leu Ser Arg Leu Arg Ala Ala Tyr Thr Leu Lys Val Gly Ser Glu 475 480 485 490 tac acc cac atc ctg gac cgc gac gag cgc acc tgg ctg cag gac cgc 1960 Tyr Thr His Ile Leu Asp Arg Asp Glu Arg Thr Trp Leu Gln Asp Arg 495 500 505 ctc gaa gcc gga atg cca aag cca acc cag gca gag cag aag tac atc 2008 Leu Glu Ala Gly Met Pro Lys Pro Thr Gln Ala Glu Gln Lys Tyr Ile 510 515 520 ctg cag aag ctg aac gcc gca gag gct ttc gag aac ttc ctg cag acc 2056 Leu Gln Lys Leu Asn Ala Ala Glu Ala Phe Glu Asn Phe Leu Gln Thr 525 530 535 aag tac gtc ggc cag aag cgc ttc tcc ctc gaa ggt gca gaa gct ctc 2104 Lys Tyr Val Gly Gln Lys Arg Phe Ser Leu Glu Gly Ala Glu Ala Leu 540 545 550 atc cca ctg atg gac tcc gcc atc gac acc gcc gca ggc cag ggc ctc 2152 Ile Pro Leu Met Asp Ser Ala Ile Asp Thr Ala Ala Gly Gln Gly Leu 555 560 565 570 gac gaa gtt gtc atc ggt atg cca cac cgt ggt cgc ctc aac gtg ctg 2200 Asp Glu Val Val Ile Gly Met Pro His Arg Gly Arg Leu Asn Val Leu 575 580 585 ttc aac atc gtg ggc aag cca ctg gca tcc atc ttc aac gag ttt gaa 2248 Phe Asn Ile Val Gly Lys Pro Leu Ala Ser Ile Phe Asn Glu Phe Glu 590 595 600 ggc caa atg gag cag ggc cag atc ggt ggc tcc ggt gac gtg aag tac 2296 Gly Gln Met Glu Gln Gly Gln Ile Gly Gly Ser Gly Asp Val Lys Tyr 605 610 615 cac ctc ggt tcc gaa ggc cag cac ctg cag atg ttc ggc gac ggc gag 2344 His Leu Gly Ser Glu Gly Gln His Leu Gln Met Phe Gly Asp Gly Glu 620 625 630 atc aag gtc tcc ctg act gct aac ccg tcc cac ctg gaa gct gtt aac 2392 Ile Lys Val Ser Leu Thr Ala Asn Pro Ser His Leu Glu Ala Val Asn 635 640 645 650 cca gtg atg gaa ggt atc gtc cgc gca aag cag gac tac ctg gac aag 2440 Pro Val Met Glu Gly Ile Val Arg Ala Lys Gln Asp Tyr Leu Asp Lys 655 660 665 ggc gta gac ggc aag act gtt gtg cca ctg ctg ctc cac ggt gac gct 2488 Gly Val Asp Gly Lys Thr Val Val Pro Leu Leu Leu His Gly Asp Ala 670 675 680 gca ttc gca ggc ctg ggc atc gtg cca gaa acc atc aac ctg gct aaa 2536 Ala Phe Ala Gly Leu Gly Ile Val Pro Glu Thr Ile Asn Leu Ala Lys 685 690 695 agc tgc gtc gac gtc gga ggc acc atc cac atc gtg gtg aac aac cag 2584 Ser Cys Val Asp Val Gly Gly Thr Ile His Ile Val Val Asn Asn Gln 700 705 710 atc ggc ttc acc acc acc cca gac tcc agc cgc tcc atg cac tac gca 2632 Ile Gly Phe Thr Thr Thr Pro Asp Ser Ser Arg Ser Met His Tyr Ala 715 720 725 730 acc gac tac gcc aag gca ttc ggc tgc cca gtc ttc cac gtc aat ggt 2680 Thr Asp Tyr Ala Lys Ala Phe Gly Cys Pro Val Phe His Val Asn Gly 735 740 745 gat gac cca gag gca gtt gtc tgg gtt ggc cag ctg gca acc gag tac 2728 Asp Asp Pro Glu Ala Val Val Trp Val Gly Gln Leu Ala Thr Glu Tyr 750 755 760 cgt cgt cgc ttc ggc aag gac gtc ttc atc gac ctc gtt tgc tac cgc 2776 Arg Arg Arg Phe Gly Lys Asp Val Phe Ile Asp Leu Val Cys Tyr Arg 765 770 775 ctc cgc ggc cac aac gaa gct gat gat cct tcc atg acc cag cca aag 2824 Leu Arg Gly His Asn Glu Ala Asp Asp Pro Ser Met Thr Gln Pro Lys 780 785 790 atg tat gag ctc atc acc ggc cgc gag acc gtt cgt gct cag tac acc 2872 Met Tyr Glu Leu Ile Thr Gly Arg Glu Thr Val Arg Ala Gln Tyr Thr 795 800 805 810 gaa gac ctg ctc gga cgt gga gac ctc tcc aac gaa gat gca gaa gca 2920 Glu Asp Leu Leu Gly Arg Gly Asp Leu Ser Asn Glu Asp Ala Glu Ala 815 820 825 gtc gtc cgc gac ttc cac gac cag atg gaa tct gtg ttc aac gaa gtc 2968 Val Val Arg Asp Phe His Asp Gln Met Glu Ser Val Phe Asn Glu Val 830 835 840 aag gaa ggc ggc aag aag cag gct gag gca cag acc ggc atc acc ggc 3016 Lys Glu Gly Gly Lys Lys Gln Ala Glu Ala Gln Thr Gly Ile Thr Gly 845 850 855 tcc cag aag ctt cca cac ggc ctt gag acc aac atc tcc cgt gaa gag 3064 Ser Gln Lys Leu Pro His Gly Leu Glu Thr Asn Ile Ser Arg Glu Glu 860 865 870 ctc ctg gaa ctg gga cag gct ttc gcc aac acc cca gaa ggc ttc aac 3112 Leu Leu Glu Leu Gly Gln Ala Phe Ala Asn Thr Pro Glu Gly Phe Asn 875 880 885 890 tac cac cca cgt gtg gct cca gtt gct aag aag cgc gtc tcc tct gtc 3160 Tyr His Pro Arg Val Ala Pro Val Ala Lys Lys Arg Val Ser Ser Val 895 900 905 acc gaa ggt ggc atc gac tgg gca tgg ggc gag ctc ctc gcc ttc ggt 3208 Thr Glu Gly Gly Ile Asp Trp Ala Trp Gly Glu Leu Leu Ala Phe Gly 910 915 920 tcc ctg gct aac tcc ggc cgc ttg gtt cgc ctt gca ggt gaa gat tcc 3256 Ser Leu Ala Asn Ser Gly Arg Leu Val Arg Leu Ala Gly Glu Asp Ser 925 930 935 cgc cgc ggt acc ttc acc cag cgc cac gca gtt gcc atc gac cca gcg 3304 Arg Arg Gly Thr Phe Thr Gln Arg His Ala Val Ala Ile Asp Pro Ala 940 945 950 acc gct gaa gag ttc aac cca ctc cac gag ctt gca cag tcc aag ggc 3352 Thr Ala Glu Glu Phe Asn Pro Leu His Glu Leu Ala Gln Ser Lys Gly 955 960 965 970 aac aac ggt aag ttc ctg gtc tac aac tcc gca ctg acc gag tac gca 3400 Asn Asn Gly Lys Phe Leu Val Tyr Asn Ser Ala Leu Thr Glu Tyr Ala 975 980 985 ggc atg ggc ttc gag tac ggc tac tcc gta gga aac gaa gac tcc gtc 3448 Gly Met Gly Phe Glu Tyr Gly Tyr Ser Val Gly Asn Glu Asp Ser Val 990 995 1000 gtt gca tgg gaa gca cag ttc ggc gac ttc gcc aac ggc gct cag 3493 Val Ala Trp Glu Ala Gln Phe Gly Asp Phe

Ala Asn Gly Ala Gln 1005 1010 1015 acc atc atc gat gag tac gtc tcc tca ggc gaa gct aag tgg ggc 3538 Thr Ile Ile Asp Glu Tyr Val Ser Ser Gly Glu Ala Lys Trp Gly 1020 1025 1030 cag acc tcc aag ctg atc ctt ctg ctg cct cac ggc tac gaa ggc 3583 Gln Thr Ser Lys Leu Ile Leu Leu Leu Pro His Gly Tyr Glu Gly 1035 1040 1045 cag ggc cca gac cac tct tcc gca cgt atc gag cgc ttc ctg cag 3628 Gln Gly Pro Asp His Ser Ser Ala Arg Ile Glu Arg Phe Leu Gln 1050 1055 1060 ctg tgc gct gag ggt tcc atg act gtt gct cag cca tcc acc cca 3673 Leu Cys Ala Glu Gly Ser Met Thr Val Ala Gln Pro Ser Thr Pro 1065 1070 1075 gca aac cac ttc cac ctg ctg cgt cgt cac gct ctg tcc gac ctg 3718 Ala Asn His Phe His Leu Leu Arg Arg His Ala Leu Ser Asp Leu 1080 1085 1090 aag cgt cca ctg gtt atc ttc acc ccg aag tcc atg ctg cgt aac 3763 Lys Arg Pro Leu Val Ile Phe Thr Pro Lys Ser Met Leu Arg Asn 1095 1100 1105 aag gct gct gcc tcc gca cca gaa gac ttc act gag gtc acc aag 3808 Lys Ala Ala Ala Ser Ala Pro Glu Asp Phe Thr Glu Val Thr Lys 1110 1115 1120 ttc caa tcc gtg atc gac gat cca aac gtt gca gat gca gcc aag 3853 Phe Gln Ser Val Ile Asp Asp Pro Asn Val Ala Asp Ala Ala Lys 1125 1130 1135 gtg aag aag gtc atg ctg gtc tcc ggc aag ctg tac tac gaa ttg 3898 Val Lys Lys Val Met Leu Val Ser Gly Lys Leu Tyr Tyr Glu Leu 1140 1145 1150 gca aag cgc aag gag aag gac gga cgc gac gac atc gcg atc gtt 3943 Ala Lys Arg Lys Glu Lys Asp Gly Arg Asp Asp Ile Ala Ile Val 1155 1160 1165 cgt atc gaa atg ctc cac cca att ccg ttc aac cgc atc tcc gag 3988 Arg Ile Glu Met Leu His Pro Ile Pro Phe Asn Arg Ile Ser Glu 1170 1175 1180 gct ctt gcc ggc tac cct aac gct gag gaa gtc ctc ttc gtt cag 4033 Ala Leu Ala Gly Tyr Pro Asn Ala Glu Glu Val Leu Phe Val Gln 1185 1190 1195 gat gag cca gca aac cag ggc cca tgg ccg ttc tac cag gag cac 4078 Asp Glu Pro Ala Asn Gln Gly Pro Trp Pro Phe Tyr Gln Glu His 1200 1205 1210 ctc cca gag ctg atc ccg aac atg cca aag atg cgc cgc gtt tcc 4123 Leu Pro Glu Leu Ile Pro Asn Met Pro Lys Met Arg Arg Val Ser 1215 1220 1225 cgc cgc gct cag tcc tcc acc gca act ggt gtt gct aag gtg cac 4168 Arg Arg Ala Gln Ser Ser Thr Ala Thr Gly Val Ala Lys Val His 1230 1235 1240 cag ctg gag gag aag cag ctt atc gac gag gct ttc gag gct 4210 Gln Leu Glu Glu Lys Gln Leu Ile Asp Glu Ala Phe Glu Ala 1245 1250 1255 taagtcttta tagtcctgca ctagcctaga gggccttatg cagtgtgaat cacacagcat 4270 aaggcccttt ttgctgccgt ggttgcctaa ggtggaaggc atgaaacgaa tctgtgcggt 4330 cacgatctct tcagtacttt tgctaagtgg ctgctcctcc acttccacca cgcagctcga 4390 g 4391 47 1256 PRT Corynebacterium glutamicum 47 Met Leu Gln Leu Gly Leu Arg His Asn Gln Pro Thr Thr Asn Val Thr 1 5 10 15 Val Asp Lys Ile Lys Leu Asn Lys Pro Ser Arg Ser Lys Glu Lys Arg 20 25 30 Arg Val Pro Ala Val Ser Ser Ala Ser Thr Phe Gly Gln Asn Ala Trp 35 40 45 Leu Val Asp Glu Met Phe Gln Gln Phe Gln Lys Asp Pro Lys Ser Val 50 55 60 Asp Lys Glu Trp Arg Glu Leu Phe Glu Ala Gln Gly Gly Pro Asn Ala 65 70 75 80 Thr Pro Ala Thr Thr Glu Ala Gln Pro Ser Ala Pro Lys Glu Ser Ala 85 90 95 Lys Pro Ala Pro Lys Ala Ala Pro Ala Ala Lys Ala Ala Pro Arg Val 100 105 110 Glu Thr Lys Pro Ala Ala Lys Thr Ala Pro Lys Ala Lys Glu Ser Ser 115 120 125 Val Pro Gln Gln Pro Lys Leu Pro Glu Pro Gly Gln Thr Pro Ile Arg 130 135 140 Gly Ile Phe Lys Ser Ile Ala Lys Asn Met Asp Ile Ser Leu Glu Ile 145 150 155 160 Pro Thr Ala Thr Ser Val Arg Asp Met Pro Ala Arg Leu Met Phe Glu 165 170 175 Asn Arg Ala Met Val Asn Asp Gln Leu Lys Arg Thr Arg Gly Gly Lys 180 185 190 Ile Ser Phe Thr His Ile Ile Gly Tyr Ala Met Val Lys Ala Val Met 195 200 205 Ala His Pro Asp Met Asn Asn Ser Tyr Asp Val Ile Asp Gly Lys Pro 210 215 220 Thr Leu Ile Val Pro Glu His Ile Asn Leu Gly Leu Ala Ile Asp Leu 225 230 235 240 Pro Gln Lys Asp Gly Ser Arg Ala Leu Val Val Ala Ala Ile Lys Glu 245 250 255 Thr Glu Lys Met Asn Phe Ser Glu Phe Leu Ala Ala Tyr Glu Asp Ile 260 265 270 Val Thr Arg Ser Arg Lys Gly Lys Leu Thr Met Asp Asp Tyr Gln Gly 275 280 285 Val Thr Val Ser Leu Thr Asn Pro Gly Gly Ile Gly Thr Arg His Ser 290 295 300 Val Pro Arg Leu Thr Lys Gly Gln Gly Thr Ile Ile Gly Val Gly Ser 305 310 315 320 Met Asp Tyr Pro Ala Glu Phe Gln Gly Ala Ser Glu Asp Arg Leu Ala 325 330 335 Glu Leu Gly Val Gly Lys Leu Val Thr Ile Thr Ser Thr Tyr Asp His 340 345 350 Arg Val Ile Gln Gly Ala Val Ser Gly Glu Phe Leu Arg Thr Met Ser 355 360 365 Arg Leu Leu Thr Asp Asp Ser Phe Trp Asp Glu Ile Phe Asp Ala Met 370 375 380 Asn Val Pro Tyr Thr Pro Met Arg Trp Ala Gln Asp Val Pro Asn Thr 385 390 395 400 Gly Val Asp Lys Asn Thr Arg Val Met Gln Leu Ile Glu Ala Tyr Arg 405 410 415 Ser Arg Gly His Leu Ile Ala Asp Thr Asn Pro Leu Ser Trp Val Gln 420 425 430 Pro Gly Met Pro Val Pro Asp His Arg Asp Leu Asp Ile Glu Thr His 435 440 445 Ser Leu Thr Ile Trp Asp Leu Asp Arg Thr Phe Ser Val Gly Gly Phe 450 455 460 Gly Gly Lys Glu Thr Met Thr Leu Arg Glu Val Leu Ser Arg Leu Arg 465 470 475 480 Ala Ala Tyr Thr Leu Lys Val Gly Ser Glu Tyr Thr His Ile Leu Asp 485 490 495 Arg Asp Glu Arg Thr Trp Leu Gln Asp Arg Leu Glu Ala Gly Met Pro 500 505 510 Lys Pro Thr Gln Ala Glu Gln Lys Tyr Ile Leu Gln Lys Leu Asn Ala 515 520 525 Ala Glu Ala Phe Glu Asn Phe Leu Gln Thr Lys Tyr Val Gly Gln Lys 530 535 540 Arg Phe Ser Leu Glu Gly Ala Glu Ala Leu Ile Pro Leu Met Asp Ser 545 550 555 560 Ala Ile Asp Thr Ala Ala Gly Gln Gly Leu Asp Glu Val Val Ile Gly 565 570 575 Met Pro His Arg Gly Arg Leu Asn Val Leu Phe Asn Ile Val Gly Lys 580 585 590 Pro Leu Ala Ser Ile Phe Asn Glu Phe Glu Gly Gln Met Glu Gln Gly 595 600 605 Gln Ile Gly Gly Ser Gly Asp Val Lys Tyr His Leu Gly Ser Glu Gly 610 615 620 Gln His Leu Gln Met Phe Gly Asp Gly Glu Ile Lys Val Ser Leu Thr 625 630 635 640 Ala Asn Pro Ser His Leu Glu Ala Val Asn Pro Val Met Glu Gly Ile 645 650 655 Val Arg Ala Lys Gln Asp Tyr Leu Asp Lys Gly Val Asp Gly Lys Thr 660 665 670 Val Val Pro Leu Leu Leu His Gly Asp Ala Ala Phe Ala Gly Leu Gly 675 680 685 Ile Val Pro Glu Thr Ile Asn Leu Ala Lys Ser Cys Val Asp Val Gly 690 695 700 Gly Thr Ile His Ile Val Val Asn Asn Gln Ile Gly Phe Thr Thr Thr 705 710 715 720 Pro Asp Ser Ser Arg Ser Met His Tyr Ala Thr Asp Tyr Ala Lys Ala 725 730 735 Phe Gly Cys Pro Val Phe His Val Asn Gly Asp Asp Pro Glu Ala Val 740 745 750 Val Trp Val Gly Gln Leu Ala Thr Glu Tyr Arg Arg Arg Phe Gly Lys 755 760 765 Asp Val Phe Ile Asp Leu Val Cys Tyr Arg Leu Arg Gly His Asn Glu 770 775 780 Ala Asp Asp Pro Ser Met Thr Gln Pro Lys Met Tyr Glu Leu Ile Thr 785 790 795 800 Gly Arg Glu Thr Val Arg Ala Gln Tyr Thr Glu Asp Leu Leu Gly Arg 805 810 815 Gly Asp Leu Ser Asn Glu Asp Ala Glu Ala Val Val Arg Asp Phe His 820 825 830 Asp Gln Met Glu Ser Val Phe Asn Glu Val Lys Glu Gly Gly Lys Lys 835 840 845 Gln Ala Glu Ala Gln Thr Gly Ile Thr Gly Ser Gln Lys Leu Pro His 850 855 860 Gly Leu Glu Thr Asn Ile Ser Arg Glu Glu Leu Leu Glu Leu Gly Gln 865 870 875 880 Ala Phe Ala Asn Thr Pro Glu Gly Phe Asn Tyr His Pro Arg Val Ala 885 890 895 Pro Val Ala Lys Lys Arg Val Ser Ser Val Thr Glu Gly Gly Ile Asp 900 905 910 Trp Ala Trp Gly Glu Leu Leu Ala Phe Gly Ser Leu Ala Asn Ser Gly 915 920 925 Arg Leu Val Arg Leu Ala Gly Glu Asp Ser Arg Arg Gly Thr Phe Thr 930 935 940 Gln Arg His Ala Val Ala Ile Asp Pro Ala Thr Ala Glu Glu Phe Asn 945 950 955 960 Pro Leu His Glu Leu Ala Gln Ser Lys Gly Asn Asn Gly Lys Phe Leu 965 970 975 Val Tyr Asn Ser Ala Leu Thr Glu Tyr Ala Gly Met Gly Phe Glu Tyr 980 985 990 Gly Tyr Ser Val Gly Asn Glu Asp Ser Val Val Ala Trp Glu Ala Gln 995 1000 1005 Phe Gly Asp Phe Ala Asn Gly Ala Gln Thr Ile Ile Asp Glu Tyr 1010 1015 1020 Val Ser Ser Gly Glu Ala Lys Trp Gly Gln Thr Ser Lys Leu Ile 1025 1030 1035 Leu Leu Leu Pro His Gly Tyr Glu Gly Gln Gly Pro Asp His Ser 1040 1045 1050 Ser Ala Arg Ile Glu Arg Phe Leu Gln Leu Cys Ala Glu Gly Ser 1055 1060 1065 Met Thr Val Ala Gln Pro Ser Thr Pro Ala Asn His Phe His Leu 1070 1075 1080 Leu Arg Arg His Ala Leu Ser Asp Leu Lys Arg Pro Leu Val Ile 1085 1090 1095 Phe Thr Pro Lys Ser Met Leu Arg Asn Lys Ala Ala Ala Ser Ala 1100 1105 1110 Pro Glu Asp Phe Thr Glu Val Thr Lys Phe Gln Ser Val Ile Asp 1115 1120 1125 Asp Pro Asn Val Ala Asp Ala Ala Lys Val Lys Lys Val Met Leu 1130 1135 1140 Val Ser Gly Lys Leu Tyr Tyr Glu Leu Ala Lys Arg Lys Glu Lys 1145 1150 1155 Asp Gly Arg Asp Asp Ile Ala Ile Val Arg Ile Glu Met Leu His 1160 1165 1170 Pro Ile Pro Phe Asn Arg Ile Ser Glu Ala Leu Ala Gly Tyr Pro 1175 1180 1185 Asn Ala Glu Glu Val Leu Phe Val Gln Asp Glu Pro Ala Asn Gln 1190 1195 1200 Gly Pro Trp Pro Phe Tyr Gln Glu His Leu Pro Glu Leu Ile Pro 1205 1210 1215 Asn Met Pro Lys Met Arg Arg Val Ser Arg Arg Ala Gln Ser Ser 1220 1225 1230 Thr Ala Thr Gly Val Ala Lys Val His Gln Leu Glu Glu Lys Gln 1235 1240 1245 Leu Ile Asp Glu Ala Phe Glu Ala 1250 1255 48 4391 DNA Corynebacterium glutamicum CDS (443)..(4210) 48 gtcgacaagc aaaatcgaag cggcagcacg ccgcgtcgga gccttaaacg ccatcgccgc 60 catccctgat ggtttcaatc atcaagtcgg tgaacgcggg cgcaacctgt catccggaca 120 gcgccaactg atcgcgctgg cgcgcgccga actcatcgag ccttccatca tgcttctcga 180 cgaagccacc tccaccctcg accccgccac cgaagccgtt atcctcaacg cctccgatcg 240 agtcactaag ggacgcacca gcatcatcgt cgcgcaccgc ttggcaaccg ctaaaagggc 300 cgaccgtatt cttgttgttg aacaaggacg tatcattgag gacggatctc acgacgcgtt 360 gttgtctgct aacggcacct acgcccgcat gtggcattta atggcctgac acgttatttt 420 taggagaact gtcaacaaat ta atg cta caa ctg ggg ctt agg cat aat cag 472 Met Leu Gln Leu Gly Leu Arg His Asn Gln 1 5 10 cca acg acc aac gtt aca gtg gat aaa ata aag ctc aat aaa ccc tca 520 Pro Thr Thr Asn Val Thr Val Asp Lys Ile Lys Leu Asn Lys Pro Ser 15 20 25 aga agc aag gaa aag agg cga gta cct gcc gtg agc agc gct agt act 568 Arg Ser Lys Glu Lys Arg Arg Val Pro Ala Val Ser Ser Ala Ser Thr 30 35 40 ttc ggc cag aat gcg tgg ctg gta gac gag atg ttc cag cag ttc cag 616 Phe Gly Gln Asn Ala Trp Leu Val Asp Glu Met Phe Gln Gln Phe Gln 45 50 55 aag gac ccc aag tcc gtg gac aag gaa tgg aga gaa ctc ttt gag gcg 664 Lys Asp Pro Lys Ser Val Asp Lys Glu Trp Arg Glu Leu Phe Glu Ala 60 65 70 cag ggg gga cca aat gct acc ccc gct aca aca gaa gca cag cct tca 712 Gln Gly Gly Pro Asn Ala Thr Pro Ala Thr Thr Glu Ala Gln Pro Ser 75 80 85 90 gcg ccc aag gag tct gcg aaa cca gca cca aag gct gcc cct gca gcc 760 Ala Pro Lys Glu Ser Ala Lys Pro Ala Pro Lys Ala Ala Pro Ala Ala 95 100 105 aag gca gca ccg cgc gta gaa acc aag ccg gcc gcc aag acc gcc cct 808 Lys Ala Ala Pro Arg Val Glu Thr Lys Pro Ala Ala Lys Thr Ala Pro 110 115 120 aag gcc aag gag tcc tca gtg cca cag caa cct aag ctt ccg gag cca 856 Lys Ala Lys Glu Ser Ser Val Pro Gln Gln Pro Lys Leu Pro Glu Pro 125 130 135 gga caa acc cca atc agg ggt att ttc aag tcc atc gcg aag aac atg 904 Gly Gln Thr Pro Ile Arg Gly Ile Phe Lys Ser Ile Ala Lys Asn Met 140 145 150 gat atc tcc ctg gaa atc cca acc gca acc tcg gtt cgc gat atg cca 952 Asp Ile Ser Leu Glu Ile Pro Thr Ala Thr Ser Val Arg Asp Met Pro 155 160 165 170 gct cgc ctc atg ttc gaa aac cgc gcg atg gtc aac gat cag ctc aag 1000 Ala Arg Leu Met Phe Glu Asn Arg Ala Met Val Asn Asp Gln Leu Lys 175 180 185 cgc acc cgc ggt ggc aag atc tcc ttc acc cac atc att ggc tac gcc 1048 Arg Thr Arg Gly Gly Lys Ile Ser Phe Thr His Ile Ile Gly Tyr Ala 190 195 200 atg gtg aag gca gtc atg gct cac ccg gac atg aac aac tcc tac gac 1096 Met Val Lys Ala Val Met Ala His Pro Asp Met Asn Asn Ser Tyr Asp 205 210 215 gtc atc gac ggc aag cca acc ctg atc gtg cct gag cac atc aac ctg 1144 Val Ile Asp Gly Lys Pro Thr Leu Ile Val Pro Glu His Ile Asn Leu 220 225 230 ggc ctt gcc atc gac ctt cct cag aag gac ggc tcc cgc gca ctt gtc 1192 Gly Leu Ala Ile Asp Leu Pro Gln Lys Asp Gly Ser Arg Ala Leu Val 235 240 245 250 gta gca gcc atc aag gaa acc gag aag atg aac ttc tcc gag ttc ctc 1240 Val Ala Ala Ile Lys Glu Thr Glu Lys Met Asn Phe Ser Glu Phe Leu 255 260 265 gca gca tac gaa gac atc gtg aca cgc tcc cgc aag ggc aag ctc acc 1288 Ala Ala Tyr Glu Asp Ile Val Thr Arg Ser Arg Lys Gly Lys Leu Thr 270 275 280 atg gat gac tac cag ggc gtt acc gtt tcc ttg acc aac cca ggt ggc 1336 Met Asp Asp Tyr Gln Gly Val Thr Val Ser Leu Thr Asn Pro Gly Gly 285 290 295 atc ggt acc cgc cac tct gtc cca cgt ctg acc aag ggc cag ggc acc 1384 Ile Gly Thr Arg His Ser Val Pro Arg Leu Thr Lys Gly Gln Gly Thr 300 305 310 atc atc ggt gtc ggt tcc atg gat tac cca gca gag ttc cag ggc gct 1432 Ile Ile Gly Val Gly Ser Met Asp Tyr Pro Ala Glu Phe Gln Gly Ala 315 320 325 330 tcc gaa gac cgc ctt gca gag ctc ggc gtt gga aag ctt gtc acc atc 1480 Ser Glu Asp Arg Leu Ala Glu Leu Gly Val Gly Lys Leu Val Thr Ile 335 340 345 acc tcc acc tac gat cac cgc gtg atc cag ggt gct gtg tcc ggt gaa 1528 Thr Ser Thr Tyr Asp His Arg Val Ile Gln Gly Ala Val Ser Gly Glu 350 355 360 ttc ctg cgt acc atg tct cgc ctg ctc acc gat gat tcc ttc tgg gat 1576 Phe Leu Arg Thr Met Ser Arg Leu Leu Thr Asp Asp Ser Phe Trp Asp 365 370 375 gag atc ttc gac gca atg aac gtt cct tac acc cca atg cgt tgg gca 1624 Glu Ile Phe Asp Ala Met Asn Val Pro Tyr Thr Pro Met Arg Trp Ala 380 385 390 cag gac gtt cca aac

acc ggt gtt gat aag aac acc cgc gtc atg cag 1672 Gln Asp Val Pro Asn Thr Gly Val Asp Lys Asn Thr Arg Val Met Gln 395 400 405 410 ctc att gag gca tac cgc tcc cgt gga cac ctc atc gct gac acc aac 1720 Leu Ile Glu Ala Tyr Arg Ser Arg Gly His Leu Ile Ala Asp Thr Asn 415 420 425 cca ctt tca tgg gtt cag cct ggc atg cca gtt cca gac cac cgc gac 1768 Pro Leu Ser Trp Val Gln Pro Gly Met Pro Val Pro Asp His Arg Asp 430 435 440 ctc gac atc gag acc cac agc ctg acc atc tgg gat ctg gac cgt acc 1816 Leu Asp Ile Glu Thr His Ser Leu Thr Ile Trp Asp Leu Asp Arg Thr 445 450 455 ttc agc gtc ggt ggc ttc ggc ggc aag gag acc atg acc ctg cgc gag 1864 Phe Ser Val Gly Gly Phe Gly Gly Lys Glu Thr Met Thr Leu Arg Glu 460 465 470 gta ctg tcc cgc ctg cgc gct gcc tac acc ttg aag gtc ggc tcc gaa 1912 Val Leu Ser Arg Leu Arg Ala Ala Tyr Thr Leu Lys Val Gly Ser Glu 475 480 485 490 tac acc cac atc ctg gac cgc gac gag cgc acc tgg ctg cag gac cgc 1960 Tyr Thr His Ile Leu Asp Arg Asp Glu Arg Thr Trp Leu Gln Asp Arg 495 500 505 ctc gaa gcc gga atg cca aag cca acc cag gca gag cag aag tac atc 2008 Leu Glu Ala Gly Met Pro Lys Pro Thr Gln Ala Glu Gln Lys Tyr Ile 510 515 520 ctg cag aag ctg aac gcc gca gag gct ttc gag aac ttc ctg cag acc 2056 Leu Gln Lys Leu Asn Ala Ala Glu Ala Phe Glu Asn Phe Leu Gln Thr 525 530 535 aag tac gtc ggc cag aag cgc ttc tcc ctc gaa ggt gca gaa gct ctc 2104 Lys Tyr Val Gly Gln Lys Arg Phe Ser Leu Glu Gly Ala Glu Ala Leu 540 545 550 atc cca ctg atg gac tcc gcc atc gac acc gcc gca ggc cag ggc ctc 2152 Ile Pro Leu Met Asp Ser Ala Ile Asp Thr Ala Ala Gly Gln Gly Leu 555 560 565 570 gac gaa gtt gtc atc ggt atg cca cac cgt ggt cgc ctc aac gtg ctg 2200 Asp Glu Val Val Ile Gly Met Pro His Arg Gly Arg Leu Asn Val Leu 575 580 585 ttc aac atc gtg ggc aag cca ctg gca tcc atc ttc aac gag ttt gaa 2248 Phe Asn Ile Val Gly Lys Pro Leu Ala Ser Ile Phe Asn Glu Phe Glu 590 595 600 ggc caa atg gag cag ggc cag atc ggt ggc tcc ggt gac gtg aag tac 2296 Gly Gln Met Glu Gln Gly Gln Ile Gly Gly Ser Gly Asp Val Lys Tyr 605 610 615 cac ctc ggt tcc gaa ggc cag cac ctg cag atg ttc ggc gac ggc gag 2344 His Leu Gly Ser Glu Gly Gln His Leu Gln Met Phe Gly Asp Gly Glu 620 625 630 atc aag gtc tcc ctg act gct aac ccg tcc cac ctg gaa gct gtt aac 2392 Ile Lys Val Ser Leu Thr Ala Asn Pro Ser His Leu Glu Ala Val Asn 635 640 645 650 cca gtg atg gaa ggt atc gtc cgc gca aag cag gac tac ctg gac aag 2440 Pro Val Met Glu Gly Ile Val Arg Ala Lys Gln Asp Tyr Leu Asp Lys 655 660 665 ggc gta gac ggc aag act gtt gtg cca ctg ctg ctc cac ggt gac gct 2488 Gly Val Asp Gly Lys Thr Val Val Pro Leu Leu Leu His Gly Asp Ala 670 675 680 gca ttc gca ggc ctg ggc atc gtg cca gaa acc atc aac ctg gct ata 2536 Ala Phe Ala Gly Leu Gly Ile Val Pro Glu Thr Ile Asn Leu Ala Ile 685 690 695 agc tgc gtc gac gtc gga ggc acc atc cac atc gtg gtg aac aac cag 2584 Ser Cys Val Asp Val Gly Gly Thr Ile His Ile Val Val Asn Asn Gln 700 705 710 atc ggc ttc acc acc acc cca gac tcc agc cgc tcc atg cac tac gca 2632 Ile Gly Phe Thr Thr Thr Pro Asp Ser Ser Arg Ser Met His Tyr Ala 715 720 725 730 acc gac tac gcc aag gca ttc ggc tgc cca gtc ttc cac gtc aat ggt 2680 Thr Asp Tyr Ala Lys Ala Phe Gly Cys Pro Val Phe His Val Asn Gly 735 740 745 gat gac cca gag gca gtt gtc tgg gtt ggc cag ctg gca acc gag tac 2728 Asp Asp Pro Glu Ala Val Val Trp Val Gly Gln Leu Ala Thr Glu Tyr 750 755 760 cgt cgt cgc ttc ggc aag gac gtc ttc atc gac ctc gtt tgc tac cgc 2776 Arg Arg Arg Phe Gly Lys Asp Val Phe Ile Asp Leu Val Cys Tyr Arg 765 770 775 ctc cgc ggc cac aac gaa gct gat gat cct tcc atg acc cag cca aag 2824 Leu Arg Gly His Asn Glu Ala Asp Asp Pro Ser Met Thr Gln Pro Lys 780 785 790 atg tat gag ctc atc acc ggc cgc gag acc gtt cgt gct cag tac acc 2872 Met Tyr Glu Leu Ile Thr Gly Arg Glu Thr Val Arg Ala Gln Tyr Thr 795 800 805 810 gaa gac ctg ctc gga cgt gga gac ctc tcc aac gaa gat gca gaa gca 2920 Glu Asp Leu Leu Gly Arg Gly Asp Leu Ser Asn Glu Asp Ala Glu Ala 815 820 825 gtc gtc cgc gac ttc cac gac cag atg gaa tct gtg ttc aac gaa gtc 2968 Val Val Arg Asp Phe His Asp Gln Met Glu Ser Val Phe Asn Glu Val 830 835 840 aag gaa ggc ggc aag aag cag gct gag gca cag acc ggc atc acc ggc 3016 Lys Glu Gly Gly Lys Lys Gln Ala Glu Ala Gln Thr Gly Ile Thr Gly 845 850 855 tcc cag aag ctt cca cac ggc ctt gag acc aac atc tcc cgt gaa gag 3064 Ser Gln Lys Leu Pro His Gly Leu Glu Thr Asn Ile Ser Arg Glu Glu 860 865 870 ctc ctg gaa ctg gga cag gct ttc gcc aac acc cca gaa ggc ttc aac 3112 Leu Leu Glu Leu Gly Gln Ala Phe Ala Asn Thr Pro Glu Gly Phe Asn 875 880 885 890 tac cac cca cgt gtg gct cca gtt gct aag aag cgc gtc tcc tct gtc 3160 Tyr His Pro Arg Val Ala Pro Val Ala Lys Lys Arg Val Ser Ser Val 895 900 905 acc gaa ggt ggc atc gac tgg gca tgg ggc gag ctc ctc gcc ttc ggt 3208 Thr Glu Gly Gly Ile Asp Trp Ala Trp Gly Glu Leu Leu Ala Phe Gly 910 915 920 tcc ctg gct aac tcc ggc cgc ttg gtt cgc ctt gca ggt gaa gat tcc 3256 Ser Leu Ala Asn Ser Gly Arg Leu Val Arg Leu Ala Gly Glu Asp Ser 925 930 935 cgc cgc ggt acc ttc acc cag cgc cac gca gtt gcc atc gac cca gcg 3304 Arg Arg Gly Thr Phe Thr Gln Arg His Ala Val Ala Ile Asp Pro Ala 940 945 950 acc gct gaa gag ttc aac cca ctc cac gag ctt gca cag tcc aag ggc 3352 Thr Ala Glu Glu Phe Asn Pro Leu His Glu Leu Ala Gln Ser Lys Gly 955 960 965 970 aac aac ggt aag ttc ctg gtc tac aac tcc gca ctg acc gag tac gca 3400 Asn Asn Gly Lys Phe Leu Val Tyr Asn Ser Ala Leu Thr Glu Tyr Ala 975 980 985 ggc atg ggc ttc gag tac ggc tac tcc gta gga aac gaa gac tcc gtc 3448 Gly Met Gly Phe Glu Tyr Gly Tyr Ser Val Gly Asn Glu Asp Ser Val 990 995 1000 gtt gca tgg gaa gca cag ttc ggc gac ttc gcc aac ggc gct cag 3493 Val Ala Trp Glu Ala Gln Phe Gly Asp Phe Ala Asn Gly Ala Gln 1005 1010 1015 acc atc atc gat gag tac gtc tcc tca ggc gaa gct aag tgg ggc 3538 Thr Ile Ile Asp Glu Tyr Val Ser Ser Gly Glu Ala Lys Trp Gly 1020 1025 1030 cag acc tcc aag ctg atc ctt ctg ctg cct cac ggc tac gaa ggc 3583 Gln Thr Ser Lys Leu Ile Leu Leu Leu Pro His Gly Tyr Glu Gly 1035 1040 1045 cag ggc cca gac cac tct tcc gca cgt atc gag cgc ttc ctg cag 3628 Gln Gly Pro Asp His Ser Ser Ala Arg Ile Glu Arg Phe Leu Gln 1050 1055 1060 ctg tgc gct gag ggt tcc atg act gtt gct cag cca tcc acc cca 3673 Leu Cys Ala Glu Gly Ser Met Thr Val Ala Gln Pro Ser Thr Pro 1065 1070 1075 gca aac cac ttc cac ctg ctg cgt cgt cac gct ctg tcc gac ctg 3718 Ala Asn His Phe His Leu Leu Arg Arg His Ala Leu Ser Asp Leu 1080 1085 1090 aag cgt cca ctg gtt atc ttc acc ccg aag tcc atg ctg cgt aac 3763 Lys Arg Pro Leu Val Ile Phe Thr Pro Lys Ser Met Leu Arg Asn 1095 1100 1105 aag gct gct gcc tcc gca cca gaa gac ttc act gag gtc acc aag 3808 Lys Ala Ala Ala Ser Ala Pro Glu Asp Phe Thr Glu Val Thr Lys 1110 1115 1120 ttc caa tcc gtg atc gac gat cca aac gtt gca gat gca gcc aag 3853 Phe Gln Ser Val Ile Asp Asp Pro Asn Val Ala Asp Ala Ala Lys 1125 1130 1135 gtg aag aag gtc atg ctg gtc tcc ggc aag ctg tac tac gaa ttg 3898 Val Lys Lys Val Met Leu Val Ser Gly Lys Leu Tyr Tyr Glu Leu 1140 1145 1150 gca aag cgc aag gag aag gac gga cgc gac gac atc gcg atc gtt 3943 Ala Lys Arg Lys Glu Lys Asp Gly Arg Asp Asp Ile Ala Ile Val 1155 1160 1165 cgt atc gaa atg ctc cac cca att ccg ttc aac cgc atc tcc gag 3988 Arg Ile Glu Met Leu His Pro Ile Pro Phe Asn Arg Ile Ser Glu 1170 1175 1180 gct ctt gcc ggc tac cct aac gct gag gaa gtc ctc ttc gtt cag 4033 Ala Leu Ala Gly Tyr Pro Asn Ala Glu Glu Val Leu Phe Val Gln 1185 1190 1195 gat gag cca gca aac cag ggc cca tgg ccg ttc tac cag gag cac 4078 Asp Glu Pro Ala Asn Gln Gly Pro Trp Pro Phe Tyr Gln Glu His 1200 1205 1210 ctc cca gag ctg atc ccg aac atg cca aag atg cgc cgc gtt tcc 4123 Leu Pro Glu Leu Ile Pro Asn Met Pro Lys Met Arg Arg Val Ser 1215 1220 1225 cgc cgc gct cag tcc tcc acc gca act ggt gtt gct aag gtg cac 4168 Arg Arg Ala Gln Ser Ser Thr Ala Thr Gly Val Ala Lys Val His 1230 1235 1240 cag ctg gag gag aag cag ctt atc gac gag gct ttc gag gct 4210 Gln Leu Glu Glu Lys Gln Leu Ile Asp Glu Ala Phe Glu Ala 1245 1250 1255 taagtcttta tagtcctgca ctagcctaga gggccttatg cagtgtgaat cacacagcat 4270 aaggcccttt ttgctgccgt ggttgcctaa ggtggaaggc atgaaacgaa tctgtgcggt 4330 cacgatctct tcagtacttt tgctaagtgg ctgctcctcc acttccacca cgcagctcga 4390 g 4391 49 1256 PRT Corynebacterium glutamicum 49 Met Leu Gln Leu Gly Leu Arg His Asn Gln Pro Thr Thr Asn Val Thr 1 5 10 15 Val Asp Lys Ile Lys Leu Asn Lys Pro Ser Arg Ser Lys Glu Lys Arg 20 25 30 Arg Val Pro Ala Val Ser Ser Ala Ser Thr Phe Gly Gln Asn Ala Trp 35 40 45 Leu Val Asp Glu Met Phe Gln Gln Phe Gln Lys Asp Pro Lys Ser Val 50 55 60 Asp Lys Glu Trp Arg Glu Leu Phe Glu Ala Gln Gly Gly Pro Asn Ala 65 70 75 80 Thr Pro Ala Thr Thr Glu Ala Gln Pro Ser Ala Pro Lys Glu Ser Ala 85 90 95 Lys Pro Ala Pro Lys Ala Ala Pro Ala Ala Lys Ala Ala Pro Arg Val 100 105 110 Glu Thr Lys Pro Ala Ala Lys Thr Ala Pro Lys Ala Lys Glu Ser Ser 115 120 125 Val Pro Gln Gln Pro Lys Leu Pro Glu Pro Gly Gln Thr Pro Ile Arg 130 135 140 Gly Ile Phe Lys Ser Ile Ala Lys Asn Met Asp Ile Ser Leu Glu Ile 145 150 155 160 Pro Thr Ala Thr Ser Val Arg Asp Met Pro Ala Arg Leu Met Phe Glu 165 170 175 Asn Arg Ala Met Val Asn Asp Gln Leu Lys Arg Thr Arg Gly Gly Lys 180 185 190 Ile Ser Phe Thr His Ile Ile Gly Tyr Ala Met Val Lys Ala Val Met 195 200 205 Ala His Pro Asp Met Asn Asn Ser Tyr Asp Val Ile Asp Gly Lys Pro 210 215 220 Thr Leu Ile Val Pro Glu His Ile Asn Leu Gly Leu Ala Ile Asp Leu 225 230 235 240 Pro Gln Lys Asp Gly Ser Arg Ala Leu Val Val Ala Ala Ile Lys Glu 245 250 255 Thr Glu Lys Met Asn Phe Ser Glu Phe Leu Ala Ala Tyr Glu Asp Ile 260 265 270 Val Thr Arg Ser Arg Lys Gly Lys Leu Thr Met Asp Asp Tyr Gln Gly 275 280 285 Val Thr Val Ser Leu Thr Asn Pro Gly Gly Ile Gly Thr Arg His Ser 290 295 300 Val Pro Arg Leu Thr Lys Gly Gln Gly Thr Ile Ile Gly Val Gly Ser 305 310 315 320 Met Asp Tyr Pro Ala Glu Phe Gln Gly Ala Ser Glu Asp Arg Leu Ala 325 330 335 Glu Leu Gly Val Gly Lys Leu Val Thr Ile Thr Ser Thr Tyr Asp His 340 345 350 Arg Val Ile Gln Gly Ala Val Ser Gly Glu Phe Leu Arg Thr Met Ser 355 360 365 Arg Leu Leu Thr Asp Asp Ser Phe Trp Asp Glu Ile Phe Asp Ala Met 370 375 380 Asn Val Pro Tyr Thr Pro Met Arg Trp Ala Gln Asp Val Pro Asn Thr 385 390 395 400 Gly Val Asp Lys Asn Thr Arg Val Met Gln Leu Ile Glu Ala Tyr Arg 405 410 415 Ser Arg Gly His Leu Ile Ala Asp Thr Asn Pro Leu Ser Trp Val Gln 420 425 430 Pro Gly Met Pro Val Pro Asp His Arg Asp Leu Asp Ile Glu Thr His 435 440 445 Ser Leu Thr Ile Trp Asp Leu Asp Arg Thr Phe Ser Val Gly Gly Phe 450 455 460 Gly Gly Lys Glu Thr Met Thr Leu Arg Glu Val Leu Ser Arg Leu Arg 465 470 475 480 Ala Ala Tyr Thr Leu Lys Val Gly Ser Glu Tyr Thr His Ile Leu Asp 485 490 495 Arg Asp Glu Arg Thr Trp Leu Gln Asp Arg Leu Glu Ala Gly Met Pro 500 505 510 Lys Pro Thr Gln Ala Glu Gln Lys Tyr Ile Leu Gln Lys Leu Asn Ala 515 520 525 Ala Glu Ala Phe Glu Asn Phe Leu Gln Thr Lys Tyr Val Gly Gln Lys 530 535 540 Arg Phe Ser Leu Glu Gly Ala Glu Ala Leu Ile Pro Leu Met Asp Ser 545 550 555 560 Ala Ile Asp Thr Ala Ala Gly Gln Gly Leu Asp Glu Val Val Ile Gly 565 570 575 Met Pro His Arg Gly Arg Leu Asn Val Leu Phe Asn Ile Val Gly Lys 580 585 590 Pro Leu Ala Ser Ile Phe Asn Glu Phe Glu Gly Gln Met Glu Gln Gly 595 600 605 Gln Ile Gly Gly Ser Gly Asp Val Lys Tyr His Leu Gly Ser Glu Gly 610 615 620 Gln His Leu Gln Met Phe Gly Asp Gly Glu Ile Lys Val Ser Leu Thr 625 630 635 640 Ala Asn Pro Ser His Leu Glu Ala Val Asn Pro Val Met Glu Gly Ile 645 650 655 Val Arg Ala Lys Gln Asp Tyr Leu Asp Lys Gly Val Asp Gly Lys Thr 660 665 670 Val Val Pro Leu Leu Leu His Gly Asp Ala Ala Phe Ala Gly Leu Gly 675 680 685 Ile Val Pro Glu Thr Ile Asn Leu Ala Ile Ser Cys Val Asp Val Gly 690 695 700 Gly Thr Ile His Ile Val Val Asn Asn Gln Ile Gly Phe Thr Thr Thr 705 710 715 720 Pro Asp Ser Ser Arg Ser Met His Tyr Ala Thr Asp Tyr Ala Lys Ala 725 730 735 Phe Gly Cys Pro Val Phe His Val Asn Gly Asp Asp Pro Glu Ala Val 740 745 750 Val Trp Val Gly Gln Leu Ala Thr Glu Tyr Arg Arg Arg Phe Gly Lys 755 760 765 Asp Val Phe Ile Asp Leu Val Cys Tyr Arg Leu Arg Gly His Asn Glu 770 775 780 Ala Asp Asp Pro Ser Met Thr Gln Pro Lys Met Tyr Glu Leu Ile Thr 785 790 795 800 Gly Arg Glu Thr Val Arg Ala Gln Tyr Thr Glu Asp Leu Leu Gly Arg 805 810 815 Gly Asp Leu Ser Asn Glu Asp Ala Glu Ala Val Val Arg Asp Phe His 820 825 830 Asp Gln Met Glu Ser Val Phe Asn Glu Val Lys Glu Gly Gly Lys Lys 835 840 845 Gln Ala Glu Ala Gln Thr Gly Ile Thr Gly Ser Gln Lys Leu Pro His 850 855 860 Gly Leu Glu Thr Asn Ile Ser Arg Glu Glu Leu Leu Glu Leu Gly Gln 865 870 875 880 Ala Phe Ala Asn Thr Pro Glu Gly Phe Asn Tyr His Pro Arg Val Ala 885 890 895 Pro Val Ala Lys Lys Arg Val Ser Ser Val Thr Glu Gly Gly Ile Asp 900 905 910 Trp Ala Trp Gly Glu Leu Leu Ala Phe Gly Ser Leu Ala Asn Ser Gly 915 920 925 Arg Leu Val Arg Leu Ala Gly Glu Asp Ser Arg Arg Gly Thr Phe Thr 930 935 940 Gln Arg His Ala Val Ala Ile Asp Pro Ala Thr Ala Glu Glu Phe Asn 945 950 955 960 Pro Leu His Glu Leu Ala Gln Ser Lys Gly Asn Asn Gly Lys Phe Leu 965 970 975 Val Tyr Asn Ser Ala Leu Thr Glu Tyr Ala Gly Met Gly Phe Glu Tyr 980 985 990

Gly Tyr Ser Val Gly Asn Glu Asp Ser Val Val Ala Trp Glu Ala Gln 995 1000 1005 Phe Gly Asp Phe Ala Asn Gly Ala Gln Thr Ile Ile Asp Glu Tyr 1010 1015 1020 Val Ser Ser Gly Glu Ala Lys Trp Gly Gln Thr Ser Lys Leu Ile 1025 1030 1035 Leu Leu Leu Pro His Gly Tyr Glu Gly Gln Gly Pro Asp His Ser 1040 1045 1050 Ser Ala Arg Ile Glu Arg Phe Leu Gln Leu Cys Ala Glu Gly Ser 1055 1060 1065 Met Thr Val Ala Gln Pro Ser Thr Pro Ala Asn His Phe His Leu 1070 1075 1080 Leu Arg Arg His Ala Leu Ser Asp Leu Lys Arg Pro Leu Val Ile 1085 1090 1095 Phe Thr Pro Lys Ser Met Leu Arg Asn Lys Ala Ala Ala Ser Ala 1100 1105 1110 Pro Glu Asp Phe Thr Glu Val Thr Lys Phe Gln Ser Val Ile Asp 1115 1120 1125 Asp Pro Asn Val Ala Asp Ala Ala Lys Val Lys Lys Val Met Leu 1130 1135 1140 Val Ser Gly Lys Leu Tyr Tyr Glu Leu Ala Lys Arg Lys Glu Lys 1145 1150 1155 Asp Gly Arg Asp Asp Ile Ala Ile Val Arg Ile Glu Met Leu His 1160 1165 1170 Pro Ile Pro Phe Asn Arg Ile Ser Glu Ala Leu Ala Gly Tyr Pro 1175 1180 1185 Asn Ala Glu Glu Val Leu Phe Val Gln Asp Glu Pro Ala Asn Gln 1190 1195 1200 Gly Pro Trp Pro Phe Tyr Gln Glu His Leu Pro Glu Leu Ile Pro 1205 1210 1215 Asn Met Pro Lys Met Arg Arg Val Ser Arg Arg Ala Gln Ser Ser 1220 1225 1230 Thr Ala Thr Gly Val Ala Lys Val His Gln Leu Glu Glu Lys Gln 1235 1240 1245 Leu Ile Asp Glu Ala Phe Glu Ala 1250 1255 50 3774 DNA Corynebacterium glutamicum CDS (1)..(3774) 50 atg cta caa ctg ggg ctt agg cat aat cag cca acg acc aac gtt aca 48 Met Leu Gln Leu Gly Leu Arg His Asn Gln Pro Thr Thr Asn Val Thr 1 5 10 15 gtg gat aaa aca aag ctc aat aaa ccc tca aga agc aag gaa aag agg 96 Val Asp Lys Thr Lys Leu Asn Lys Pro Ser Arg Ser Lys Glu Lys Arg 20 25 30 cga gta cct gcc gtg agc agc gct agt act ttc ggc cag aat gcg tgg 144 Arg Val Pro Ala Val Ser Ser Ala Ser Thr Phe Gly Gln Asn Ala Trp 35 40 45 ctg gta gac gag atg ttc cag cag ttc cag aag gac ccc aag tcc gtg 192 Leu Val Asp Glu Met Phe Gln Gln Phe Gln Lys Asp Pro Lys Ser Val 50 55 60 gac aag gaa tgg aga gaa ctc ttt gag gcg cag ggg gga cca aat act 240 Asp Lys Glu Trp Arg Glu Leu Phe Glu Ala Gln Gly Gly Pro Asn Thr 65 70 75 80 acc ccc gct aca aca gaa gca cag cct tca gcg ccc aag gag tct gcg 288 Thr Pro Ala Thr Thr Glu Ala Gln Pro Ser Ala Pro Lys Glu Ser Ala 85 90 95 aaa cca gca cca aag gct gcc cct gca gcc aag gca gca ccg cgc gta 336 Lys Pro Ala Pro Lys Ala Ala Pro Ala Ala Lys Ala Ala Pro Arg Val 100 105 110 gaa acc aag ccg gcc gac aag acc gcc cct aag gcc aag gag tcc tca 384 Glu Thr Lys Pro Ala Asp Lys Thr Ala Pro Lys Ala Lys Glu Ser Ser 115 120 125 gtg cca cag caa cct aag ctt ccg gag cca gga caa acc cca atc agg 432 Val Pro Gln Gln Pro Lys Leu Pro Glu Pro Gly Gln Thr Pro Ile Arg 130 135 140 ggt att ttc aag tcc atc gcg aag aac atg gat atc tcc ctg gaa atc 480 Gly Ile Phe Lys Ser Ile Ala Lys Asn Met Asp Ile Ser Leu Glu Ile 145 150 155 160 cca acc gca acc tcg gtt cgc gat atg cca gct cgc ctc atg ttc gaa 528 Pro Thr Ala Thr Ser Val Arg Asp Met Pro Ala Arg Leu Met Phe Glu 165 170 175 aac cgc gcg atg gtc aac gat cag ctc aag cgc acc cgc ggt ggc aag 576 Asn Arg Ala Met Val Asn Asp Gln Leu Lys Arg Thr Arg Gly Gly Lys 180 185 190 atc tcc ttc acc cac atc att ggc tac gcc atg gtg aag gca gtc atg 624 Ile Ser Phe Thr His Ile Ile Gly Tyr Ala Met Val Lys Ala Val Met 195 200 205 gct cac ccg gac atg aac aac tcc tac gac gtc atc gac ggc aag cca 672 Ala His Pro Asp Met Asn Asn Ser Tyr Asp Val Ile Asp Gly Lys Pro 210 215 220 acc ctg atc gtg cct gag cac atc aac ctg ggc ctt gct atc gac ctt 720 Thr Leu Ile Val Pro Glu His Ile Asn Leu Gly Leu Ala Ile Asp Leu 225 230 235 240 cct cag aag gac ggc tcc cgc gca ctt gtc gta gca gcc atc aag gaa 768 Pro Gln Lys Asp Gly Ser Arg Ala Leu Val Val Ala Ala Ile Lys Glu 245 250 255 acc gag aag atg aac ttc tcc gag ttc ctc gca gcc tac gaa gac atc 816 Thr Glu Lys Met Asn Phe Ser Glu Phe Leu Ala Ala Tyr Glu Asp Ile 260 265 270 gtg gca cgc tcc cgc aag ggc aag ctc acc atg gat gac tac cag ggc 864 Val Ala Arg Ser Arg Lys Gly Lys Leu Thr Met Asp Asp Tyr Gln Gly 275 280 285 gtt acc gtt tcc ttg acc aac cca ggt ggc atc ggt acc cgc cac tct 912 Val Thr Val Ser Leu Thr Asn Pro Gly Gly Ile Gly Thr Arg His Ser 290 295 300 gtt cca cgt cta acc aag ggc cag ggc acc atc atc ggt gtc ggt tcc 960 Val Pro Arg Leu Thr Lys Gly Gln Gly Thr Ile Ile Gly Val Gly Ser 305 310 315 320 atg gat tac cca gca gag ttc cag ggc gct tca gaa gac cgc ctt gca 1008 Met Asp Tyr Pro Ala Glu Phe Gln Gly Ala Ser Glu Asp Arg Leu Ala 325 330 335 gag ctc ggc gtt ggc aaa ctt gtc acc atc acc tcc acc tac gat cac 1056 Glu Leu Gly Val Gly Lys Leu Val Thr Ile Thr Ser Thr Tyr Asp His 340 345 350 cgc gtg atc cag ggt gct gtg tcc ggt gaa ttc ctg cgc acc atg tct 1104 Arg Val Ile Gln Gly Ala Val Ser Gly Glu Phe Leu Arg Thr Met Ser 355 360 365 cgc ctg ctc acc gat gat tcc ttc tgg gat gag atc ttc gac gca atg 1152 Arg Leu Leu Thr Asp Asp Ser Phe Trp Asp Glu Ile Phe Asp Ala Met 370 375 380 aac gtt cct tac acc cca atg cgt tgg gca cag gac gtt cca aac acc 1200 Asn Val Pro Tyr Thr Pro Met Arg Trp Ala Gln Asp Val Pro Asn Thr 385 390 395 400 ggt gtt gat aag aac acc cgc gtc atg cag ctc att gag gca tac cgc 1248 Gly Val Asp Lys Asn Thr Arg Val Met Gln Leu Ile Glu Ala Tyr Arg 405 410 415 tcc cgt gga cac ctc atc gct gac acc aac cca ctt tca tgg gtt cag 1296 Ser Arg Gly His Leu Ile Ala Asp Thr Asn Pro Leu Ser Trp Val Gln 420 425 430 cct ggc atg cca gtt cca gac cac cgc gac ctc gac atc gag acc cac 1344 Pro Gly Met Pro Val Pro Asp His Arg Asp Leu Asp Ile Glu Thr His 435 440 445 aac ctg acc atc tgg gat ctg gac cgt acc ttc aac gtc ggt ggc ttc 1392 Asn Leu Thr Ile Trp Asp Leu Asp Arg Thr Phe Asn Val Gly Gly Phe 450 455 460 ggc ggc aag gag acc atg acc ctg cgc gag gta ctg tcc cgc ctc cgc 1440 Gly Gly Lys Glu Thr Met Thr Leu Arg Glu Val Leu Ser Arg Leu Arg 465 470 475 480 gct gcg tac acc ctc aag gtc ggc tcc gaa tac acc cac atc ctg gac 1488 Ala Ala Tyr Thr Leu Lys Val Gly Ser Glu Tyr Thr His Ile Leu Asp 485 490 495 cgc gac gag cgc acc tgg ctg cag gac cgc ctc gag gcc gga atg cca 1536 Arg Asp Glu Arg Thr Trp Leu Gln Asp Arg Leu Glu Ala Gly Met Pro 500 505 510 aag cca acc cag gca gag cag aag tac atc ctg cag aag ctg aac gcc 1584 Lys Pro Thr Gln Ala Glu Gln Lys Tyr Ile Leu Gln Lys Leu Asn Ala 515 520 525 gcg gag gct ttc gag aac ttc ctg cag acc aag tac gtc ggc cag aag 1632 Ala Glu Ala Phe Glu Asn Phe Leu Gln Thr Lys Tyr Val Gly Gln Lys 530 535 540 cgc ttc tcc ctc gaa ggt gca gaa gca ctt atc cca ctg atg gac tcc 1680 Arg Phe Ser Leu Glu Gly Ala Glu Ala Leu Ile Pro Leu Met Asp Ser 545 550 555 560 gcc atc gac acc gcc gca ggc caa ggc ctc gac gaa gtt gtc atc ggt 1728 Ala Ile Asp Thr Ala Ala Gly Gln Gly Leu Asp Glu Val Val Ile Gly 565 570 575 atg cca cac cgt ggt cgc ctc aac gtg ctg ttc aac atc gtg ggc aag 1776 Met Pro His Arg Gly Arg Leu Asn Val Leu Phe Asn Ile Val Gly Lys 580 585 590 cca ctg gca tcc atc ttc aac gag ttt gaa ggc caa atg gag cag ggc 1824 Pro Leu Ala Ser Ile Phe Asn Glu Phe Glu Gly Gln Met Glu Gln Gly 595 600 605 cag atc ggt ggc tcc ggt gac gtg aag tac cac ctc ggt tcc gaa ggc 1872 Gln Ile Gly Gly Ser Gly Asp Val Lys Tyr His Leu Gly Ser Glu Gly 610 615 620 cag cac ctg cag atg ttc ggc gac ggc gag atc aag gtc tcc ctg act 1920 Gln His Leu Gln Met Phe Gly Asp Gly Glu Ile Lys Val Ser Leu Thr 625 630 635 640 gct aac ccg tcc cac ctg gaa gct gtt aac cca gtg atg gaa ggt atc 1968 Ala Asn Pro Ser His Leu Glu Ala Val Asn Pro Val Met Glu Gly Ile 645 650 655 gtc cgc gca aag cag gac tac ctg gac aag ggc gta gac ggc aag act 2016 Val Arg Ala Lys Gln Asp Tyr Leu Asp Lys Gly Val Asp Gly Lys Thr 660 665 670 gtt gtg cca ctg ctg ctc cac ggt gac gct gca ttc gca ggc ctg ggc 2064 Val Val Pro Leu Leu Leu His Gly Asp Ala Ala Phe Ala Gly Leu Gly 675 680 685 atc gtg cca gaa acc atc aac ctg gct aag ctg cgt ggc tac gac gtc 2112 Ile Val Pro Glu Thr Ile Asn Leu Ala Lys Leu Arg Gly Tyr Asp Val 690 695 700 ggc ggc acc atc cac atc gtg gtg aac aac cag atc ggc ttc acc acc 2160 Gly Gly Thr Ile His Ile Val Val Asn Asn Gln Ile Gly Phe Thr Thr 705 710 715 720 acc cca gac tcc agc cgc tcc atg cac tac gca acc gac tac gcc aag 2208 Thr Pro Asp Ser Ser Arg Ser Met His Tyr Ala Thr Asp Tyr Ala Lys 725 730 735 gca ttc ggc tgc cca gtc ttc cac gtc aac ggc gac gac cca gag gca 2256 Ala Phe Gly Cys Pro Val Phe His Val Asn Gly Asp Asp Pro Glu Ala 740 745 750 gtt gtc tgg gtt ggc cag ctg gcc acc gag tac cgt cgt cgc ttc ggc 2304 Val Val Trp Val Gly Gln Leu Ala Thr Glu Tyr Arg Arg Arg Phe Gly 755 760 765 aag gac gtc ttc atc gac ctc gtc tgc tac cgc ctc cgc ggc cac aac 2352 Lys Asp Val Phe Ile Asp Leu Val Cys Tyr Arg Leu Arg Gly His Asn 770 775 780 gaa gct gat gat cct tcc atg acc cag cca aag atg tat gag ctc atc 2400 Glu Ala Asp Asp Pro Ser Met Thr Gln Pro Lys Met Tyr Glu Leu Ile 785 790 795 800 acc ggc cgc gag acc gtt cgt gct cag tac acc gaa gac ctg ctc gga 2448 Thr Gly Arg Glu Thr Val Arg Ala Gln Tyr Thr Glu Asp Leu Leu Gly 805 810 815 cgt gga gac ctc tcc aac gaa gat gca gaa gca gtc gtc cgc gac ttc 2496 Arg Gly Asp Leu Ser Asn Glu Asp Ala Glu Ala Val Val Arg Asp Phe 820 825 830 cac gac cag atg gaa tct gtg ttc aac gaa gtc aag gaa ggc ggc aag 2544 His Asp Gln Met Glu Ser Val Phe Asn Glu Val Lys Glu Gly Gly Lys 835 840 845 aag cag gct gag gca cag acc ggc atc acc ggc tcc cag aag ctt cca 2592 Lys Gln Ala Glu Ala Gln Thr Gly Ile Thr Gly Ser Gln Lys Leu Pro 850 855 860 cac ggc ctt gag acc aac atc tcc cgt gaa gag ctc ctg gaa ctg gga 2640 His Gly Leu Glu Thr Asn Ile Ser Arg Glu Glu Leu Leu Glu Leu Gly 865 870 875 880 cag gct ttc gcc aac acc cca gaa ggc ttc aac tac cac cca cgt gtg 2688 Gln Ala Phe Ala Asn Thr Pro Glu Gly Phe Asn Tyr His Pro Arg Val 885 890 895 gct ccc gtt gct aag aag cgc gtc tcc tct gtc acc gaa ggt ggc atc 2736 Ala Pro Val Ala Lys Lys Arg Val Ser Ser Val Thr Glu Gly Gly Ile 900 905 910 gac tgg gca tgg ggc gag ctc ctc gcc ttc ggt tcc ctg gct aac tcc 2784 Asp Trp Ala Trp Gly Glu Leu Leu Ala Phe Gly Ser Leu Ala Asn Ser 915 920 925 ggc cgc ttg gtt cgc ctt gca ggt gaa gat tcc cgc cgc ggt acc ttc 2832 Gly Arg Leu Val Arg Leu Ala Gly Glu Asp Ser Arg Arg Gly Thr Phe 930 935 940 acc cag cgc cac gca gtt gcc atc gac cca gcg acc gct gaa gag ttc 2880 Thr Gln Arg His Ala Val Ala Ile Asp Pro Ala Thr Ala Glu Glu Phe 945 950 955 960 aac cca ctc cac gag ctt gca cag tcc aag ggc aac aac ggt aag ttc 2928 Asn Pro Leu His Glu Leu Ala Gln Ser Lys Gly Asn Asn Gly Lys Phe 965 970 975 ctg gtc tac aac tcc gca ctg acc gag tac gca ggc atg ggc ttc gag 2976 Leu Val Tyr Asn Ser Ala Leu Thr Glu Tyr Ala Gly Met Gly Phe Glu 980 985 990 tac ggc tac tcc gta gga aac gaa gac tcc atc gtt gca tgg gaa gca 3024 Tyr Gly Tyr Ser Val Gly Asn Glu Asp Ser Ile Val Ala Trp Glu Ala 995 1000 1005 cag ttc ggc gac ttc gcc aac ggc gct cag acc atc atc gat gag 3069 Gln Phe Gly Asp Phe Ala Asn Gly Ala Gln Thr Ile Ile Asp Glu 1010 1015 1020 tac gtc tcc tca ggc gaa gct aag tgg ggc cag acc tcc aag ctg 3114 Tyr Val Ser Ser Gly Glu Ala Lys Trp Gly Gln Thr Ser Lys Leu 1025 1030 1035 atc ctt ctg ctg cct cac ggc tac gaa ggc cag ggc cca gac cac 3159 Ile Leu Leu Leu Pro His Gly Tyr Glu Gly Gln Gly Pro Asp His 1040 1045 1050 tct tcc gca cgt atc gag cgc ttc ctg cag ctg tgc gct gag ggt 3204 Ser Ser Ala Arg Ile Glu Arg Phe Leu Gln Leu Cys Ala Glu Gly 1055 1060 1065 tcc atg act gtt gct cag cca tcc acc cca gca aac cac ttc cac 3249 Ser Met Thr Val Ala Gln Pro Ser Thr Pro Ala Asn His Phe His 1070 1075 1080 cta ctg cgt cgt cac gct ctg tcc gac ctg aag cgt cca ctg gtt 3294 Leu Leu Arg Arg His Ala Leu Ser Asp Leu Lys Arg Pro Leu Val 1085 1090 1095 atc ttc acc ccg aag tcc atg ctg cgt aac aag gct gct gcc tcc 3339 Ile Phe Thr Pro Lys Ser Met Leu Arg Asn Lys Ala Ala Ala Ser 1100 1105 1110 gca cca gaa gac ttc act gag gtc acc aag ttc cag tcc gtg atc 3384 Ala Pro Glu Asp Phe Thr Glu Val Thr Lys Phe Gln Ser Val Ile 1115 1120 1125 aac gat cca aac gtt gca gat gca gcc aag gtg aag aag gtc atg 3429 Asn Asp Pro Asn Val Ala Asp Ala Ala Lys Val Lys Lys Val Met 1130 1135 1140 ctg gtc tcc ggc aag ctg tac tac gaa ttg gca aag cgc aag gag 3474 Leu Val Ser Gly Lys Leu Tyr Tyr Glu Leu Ala Lys Arg Lys Glu 1145 1150 1155 aag gac gga cgc gac gac atc gcg atc gtt cgt atc gaa atg ctc 3519 Lys Asp Gly Arg Asp Asp Ile Ala Ile Val Arg Ile Glu Met Leu 1160 1165 1170 cac cca att ccg ttc aac cgc atc tcc gag gct ctt gcc ggc tac 3564 His Pro Ile Pro Phe Asn Arg Ile Ser Glu Ala Leu Ala Gly Tyr 1175 1180 1185 cct aac gct gag gaa gtc ctc ttc gtt cag gat gag cca gca aac 3609 Pro Asn Ala Glu Glu Val Leu Phe Val Gln Asp Glu Pro Ala Asn 1190 1195 1200 cag ggc cca tgg ccg ttc tac cag gag cac ctc cca gag ctg atc 3654 Gln Gly Pro Trp Pro Phe Tyr Gln Glu His Leu Pro Glu Leu Ile 1205 1210 1215 ccg aac atg cca aag atg cgc cgc gtt tcc cgc cgc gct cag tcc 3699 Pro Asn Met Pro Lys Met Arg Arg Val Ser Arg Arg Ala Gln Ser 1220 1225 1230 tcc acc gca act ggt gtt gcc aag gtg cac cag ctg gag gag aag 3744 Ser Thr Ala Thr Gly Val Ala Lys Val His Gln Leu Glu Glu Lys 1235 1240 1245 cag ctt atc gac gag gct ttc gag gct taa 3774 Gln Leu Ile Asp Glu Ala Phe Glu Ala 1250 1255 51 1257 PRT Corynebacterium glutamicum 51 Met Leu Gln Leu Gly Leu Arg His Asn Gln Pro Thr Thr Asn Val Thr 1 5 10 15 Val Asp Lys Thr Lys Leu Asn Lys Pro Ser Arg Ser Lys Glu Lys Arg 20 25 30 Arg Val Pro Ala Val Ser Ser Ala Ser Thr Phe Gly Gln Asn Ala Trp 35 40 45 Leu Val Asp Glu Met Phe Gln Gln Phe Gln Lys Asp Pro Lys Ser Val 50 55 60 Asp Lys Glu Trp Arg Glu Leu Phe Glu Ala Gln Gly Gly Pro Asn Thr 65 70 75 80 Thr Pro Ala Thr Thr Glu Ala Gln Pro Ser Ala Pro Lys Glu Ser Ala 85 90 95 Lys Pro Ala Pro Lys Ala Ala Pro Ala Ala Lys Ala Ala Pro Arg Val 100 105 110 Glu Thr Lys Pro Ala Asp Lys Thr Ala Pro Lys Ala Lys Glu

Ser Ser 115 120 125 Val Pro Gln Gln Pro Lys Leu Pro Glu Pro Gly Gln Thr Pro Ile Arg 130 135 140 Gly Ile Phe Lys Ser Ile Ala Lys Asn Met Asp Ile Ser Leu Glu Ile 145 150 155 160 Pro Thr Ala Thr Ser Val Arg Asp Met Pro Ala Arg Leu Met Phe Glu 165 170 175 Asn Arg Ala Met Val Asn Asp Gln Leu Lys Arg Thr Arg Gly Gly Lys 180 185 190 Ile Ser Phe Thr His Ile Ile Gly Tyr Ala Met Val Lys Ala Val Met 195 200 205 Ala His Pro Asp Met Asn Asn Ser Tyr Asp Val Ile Asp Gly Lys Pro 210 215 220 Thr Leu Ile Val Pro Glu His Ile Asn Leu Gly Leu Ala Ile Asp Leu 225 230 235 240 Pro Gln Lys Asp Gly Ser Arg Ala Leu Val Val Ala Ala Ile Lys Glu 245 250 255 Thr Glu Lys Met Asn Phe Ser Glu Phe Leu Ala Ala Tyr Glu Asp Ile 260 265 270 Val Ala Arg Ser Arg Lys Gly Lys Leu Thr Met Asp Asp Tyr Gln Gly 275 280 285 Val Thr Val Ser Leu Thr Asn Pro Gly Gly Ile Gly Thr Arg His Ser 290 295 300 Val Pro Arg Leu Thr Lys Gly Gln Gly Thr Ile Ile Gly Val Gly Ser 305 310 315 320 Met Asp Tyr Pro Ala Glu Phe Gln Gly Ala Ser Glu Asp Arg Leu Ala 325 330 335 Glu Leu Gly Val Gly Lys Leu Val Thr Ile Thr Ser Thr Tyr Asp His 340 345 350 Arg Val Ile Gln Gly Ala Val Ser Gly Glu Phe Leu Arg Thr Met Ser 355 360 365 Arg Leu Leu Thr Asp Asp Ser Phe Trp Asp Glu Ile Phe Asp Ala Met 370 375 380 Asn Val Pro Tyr Thr Pro Met Arg Trp Ala Gln Asp Val Pro Asn Thr 385 390 395 400 Gly Val Asp Lys Asn Thr Arg Val Met Gln Leu Ile Glu Ala Tyr Arg 405 410 415 Ser Arg Gly His Leu Ile Ala Asp Thr Asn Pro Leu Ser Trp Val Gln 420 425 430 Pro Gly Met Pro Val Pro Asp His Arg Asp Leu Asp Ile Glu Thr His 435 440 445 Asn Leu Thr Ile Trp Asp Leu Asp Arg Thr Phe Asn Val Gly Gly Phe 450 455 460 Gly Gly Lys Glu Thr Met Thr Leu Arg Glu Val Leu Ser Arg Leu Arg 465 470 475 480 Ala Ala Tyr Thr Leu Lys Val Gly Ser Glu Tyr Thr His Ile Leu Asp 485 490 495 Arg Asp Glu Arg Thr Trp Leu Gln Asp Arg Leu Glu Ala Gly Met Pro 500 505 510 Lys Pro Thr Gln Ala Glu Gln Lys Tyr Ile Leu Gln Lys Leu Asn Ala 515 520 525 Ala Glu Ala Phe Glu Asn Phe Leu Gln Thr Lys Tyr Val Gly Gln Lys 530 535 540 Arg Phe Ser Leu Glu Gly Ala Glu Ala Leu Ile Pro Leu Met Asp Ser 545 550 555 560 Ala Ile Asp Thr Ala Ala Gly Gln Gly Leu Asp Glu Val Val Ile Gly 565 570 575 Met Pro His Arg Gly Arg Leu Asn Val Leu Phe Asn Ile Val Gly Lys 580 585 590 Pro Leu Ala Ser Ile Phe Asn Glu Phe Glu Gly Gln Met Glu Gln Gly 595 600 605 Gln Ile Gly Gly Ser Gly Asp Val Lys Tyr His Leu Gly Ser Glu Gly 610 615 620 Gln His Leu Gln Met Phe Gly Asp Gly Glu Ile Lys Val Ser Leu Thr 625 630 635 640 Ala Asn Pro Ser His Leu Glu Ala Val Asn Pro Val Met Glu Gly Ile 645 650 655 Val Arg Ala Lys Gln Asp Tyr Leu Asp Lys Gly Val Asp Gly Lys Thr 660 665 670 Val Val Pro Leu Leu Leu His Gly Asp Ala Ala Phe Ala Gly Leu Gly 675 680 685 Ile Val Pro Glu Thr Ile Asn Leu Ala Lys Leu Arg Gly Tyr Asp Val 690 695 700 Gly Gly Thr Ile His Ile Val Val Asn Asn Gln Ile Gly Phe Thr Thr 705 710 715 720 Thr Pro Asp Ser Ser Arg Ser Met His Tyr Ala Thr Asp Tyr Ala Lys 725 730 735 Ala Phe Gly Cys Pro Val Phe His Val Asn Gly Asp Asp Pro Glu Ala 740 745 750 Val Val Trp Val Gly Gln Leu Ala Thr Glu Tyr Arg Arg Arg Phe Gly 755 760 765 Lys Asp Val Phe Ile Asp Leu Val Cys Tyr Arg Leu Arg Gly His Asn 770 775 780 Glu Ala Asp Asp Pro Ser Met Thr Gln Pro Lys Met Tyr Glu Leu Ile 785 790 795 800 Thr Gly Arg Glu Thr Val Arg Ala Gln Tyr Thr Glu Asp Leu Leu Gly 805 810 815 Arg Gly Asp Leu Ser Asn Glu Asp Ala Glu Ala Val Val Arg Asp Phe 820 825 830 His Asp Gln Met Glu Ser Val Phe Asn Glu Val Lys Glu Gly Gly Lys 835 840 845 Lys Gln Ala Glu Ala Gln Thr Gly Ile Thr Gly Ser Gln Lys Leu Pro 850 855 860 His Gly Leu Glu Thr Asn Ile Ser Arg Glu Glu Leu Leu Glu Leu Gly 865 870 875 880 Gln Ala Phe Ala Asn Thr Pro Glu Gly Phe Asn Tyr His Pro Arg Val 885 890 895 Ala Pro Val Ala Lys Lys Arg Val Ser Ser Val Thr Glu Gly Gly Ile 900 905 910 Asp Trp Ala Trp Gly Glu Leu Leu Ala Phe Gly Ser Leu Ala Asn Ser 915 920 925 Gly Arg Leu Val Arg Leu Ala Gly Glu Asp Ser Arg Arg Gly Thr Phe 930 935 940 Thr Gln Arg His Ala Val Ala Ile Asp Pro Ala Thr Ala Glu Glu Phe 945 950 955 960 Asn Pro Leu His Glu Leu Ala Gln Ser Lys Gly Asn Asn Gly Lys Phe 965 970 975 Leu Val Tyr Asn Ser Ala Leu Thr Glu Tyr Ala Gly Met Gly Phe Glu 980 985 990 Tyr Gly Tyr Ser Val Gly Asn Glu Asp Ser Ile Val Ala Trp Glu Ala 995 1000 1005 Gln Phe Gly Asp Phe Ala Asn Gly Ala Gln Thr Ile Ile Asp Glu 1010 1015 1020 Tyr Val Ser Ser Gly Glu Ala Lys Trp Gly Gln Thr Ser Lys Leu 1025 1030 1035 Ile Leu Leu Leu Pro His Gly Tyr Glu Gly Gln Gly Pro Asp His 1040 1045 1050 Ser Ser Ala Arg Ile Glu Arg Phe Leu Gln Leu Cys Ala Glu Gly 1055 1060 1065 Ser Met Thr Val Ala Gln Pro Ser Thr Pro Ala Asn His Phe His 1070 1075 1080 Leu Leu Arg Arg His Ala Leu Ser Asp Leu Lys Arg Pro Leu Val 1085 1090 1095 Ile Phe Thr Pro Lys Ser Met Leu Arg Asn Lys Ala Ala Ala Ser 1100 1105 1110 Ala Pro Glu Asp Phe Thr Glu Val Thr Lys Phe Gln Ser Val Ile 1115 1120 1125 Asn Asp Pro Asn Val Ala Asp Ala Ala Lys Val Lys Lys Val Met 1130 1135 1140 Leu Val Ser Gly Lys Leu Tyr Tyr Glu Leu Ala Lys Arg Lys Glu 1145 1150 1155 Lys Asp Gly Arg Asp Asp Ile Ala Ile Val Arg Ile Glu Met Leu 1160 1165 1170 His Pro Ile Pro Phe Asn Arg Ile Ser Glu Ala Leu Ala Gly Tyr 1175 1180 1185 Pro Asn Ala Glu Glu Val Leu Phe Val Gln Asp Glu Pro Ala Asn 1190 1195 1200 Gln Gly Pro Trp Pro Phe Tyr Gln Glu His Leu Pro Glu Leu Ile 1205 1210 1215 Pro Asn Met Pro Lys Met Arg Arg Val Ser Arg Arg Ala Gln Ser 1220 1225 1230 Ser Thr Ala Thr Gly Val Ala Lys Val His Gln Leu Glu Glu Lys 1235 1240 1245 Gln Leu Ile Asp Glu Ala Phe Glu Ala 1250 1255

Claims

1. A method for producing L-glutamic acid comprising: a) culturing an L-glutamic acid-producing coryneform bacterium in a culture medium, and b) collecting L-glutamic acid from the culture medium and/or the bacterium, wherein said bacterium comprises a) intracellular .alpha.-ketoglutarate dehydrogenase activity which is less than half that of a non-mutated or wild-type strain, and b) a mutation in a coding region or an expression control region of a chromosomal odhA gene encoding the E1o subunit of the .alpha.-ketoglutarate dehydrogenase complex, and wherein said bacterium grows at a rate which is at least 80% as compared to the growth rate of a non-mutated or wild-type strain.

2. The method according to claim 1, wherein said odhA gene encodes a protein selected from the group consisting of: (A) a protein comprising an amino acid sequence of SEQ ID NO: 10, (B) a protein comprising an amino acid sequence of SEQ ID NO: 10, wherein 1 to 20 amino acids in said protein are substituted, deleted, inserted, or added, and wherein said protein has an activity of the E1o subunit of the .alpha.-ketoglutarate dehydrogenase complex, (C) a protein comprising amino acids 37 to 1257 of SEQ ID NO: 10, and (D) a protein comprising amino acids 37 to 1257 of SEQ ID NO: 10, wherein 1 to 20 amino acids in said protein are substituted, deleted, inserted, or added, and wherein said protein has an activity of the E1o subunit of the .alpha.-ketoglutarate dehydrogenase complex.

3. The method according to claim 1, wherein said odhA gene is selected from the group consisting of: (a) a gene comprising nucleotides 443 to 4213 of SEQ ID NO: 9, (b) a gene that is able to hybridize under stringent conditions to a polynucleotide comprising nucleotides 443 to 4213 of SEQ ID NO: 9, and wherein said gene encodes a protein which has the activity of the E1o subunit of the .alpha.-ketoglutarate dehydrogenase complex, (c) a gene comprising nucleotides 551 to 4213 of SEQ ID NO: 9, and (d) a gene that is able to hybridize under stringent conditions to a polynucleotide comprising nucleotides 551 to 4213 of SEQ ID NO: 9, and wherein said gene encodes a protein which has the activity of the E1o subunit of the .alpha.-ketoglutarate dehydrogenase complex and wherein said stringent conditions comprise washing in 1.times.SSC and 0.1% SDS at 60.degree. C.

4. The method according to claim 1, wherein said mutation is introduced into a region which encodes a thiamine pyrophosphate binding region.

5. The method according to claim 1, wherein said mutation is introduced into the region comprising nucleotides 2534 to 2548 of SEQ ID NO: 9.

6. The method according to claim 1, wherein said mutation comprises deletion of one or more amino acids in the region comprising amino acids 698 to 702 of SEQ ID NO: 10.

7. The method according to claim 1, wherein said mutation comprises replacement of an amino acid selected from the group consisting of Lys at position 698, Leu at position 699, Arg at position 700, Tyr at position 702, and combinations thereof in the amino acid sequence shown in SEQ ID NO: 10.

8. The method according to claim 1, wherein said mutation is introduced into the region comprising nucleotides 1094 to 1114 of SEQ ID NO: 9.