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G3P1_ECOLI
ID   G3P1_ECOLI              Reviewed;         331 AA.
AC   P0A9B2; P06977;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase A {ECO:0000303|PubMed:2659073};
DE            Short=GAPDH-A {ECO:0000303|PubMed:2659073};
DE            EC=1.2.1.12 {ECO:0000269|PubMed:2659073};
DE   AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:2659073};
GN   Name=gapA {ECO:0000303|PubMed:2659073}; OrderedLocusNames=b1779, JW1768;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2990926; DOI=10.1111/j.1432-1033.1985.tb08988.x;
RA   Branlant G., Branlant C.;
RT   "Nucleotide sequence of the Escherichia coli gap gene. Different
RT   evolutionary behavior of the NAD+-binding domain and of the catalytic
RT   domain of D-glyceraldehyde-3-phosphate dehydrogenase.";
RL   Eur. J. Biochem. 150:61-66(1985).
RN   [2]
RP   SEQUENCE REVISION TO 295-300.
RA   Nelson K.;
RL   Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-13.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA   Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA   Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL   Submitted (SEP-1994) to UniProtKB.
RN   [7]
RP   PROTEIN SEQUENCE OF 2-13.
RC   STRAIN=K12 / EMG2;
RX   PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded in the
RT   genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-314.
RC   STRAIN=A8190, E2666-74, E3406, E830587, E851819, ECOR 14, ECOR 32, ECOR 40,
RC   ECOR 52, ECOR 58, ECOR 64, and ECOR 70;
RX   PubMed=1862091; DOI=10.1073/pnas.88.15.6667;
RA   Nelson K., Whittam T.S., Selander R.K.;
RT   "Nucleotide polymorphism and evolution in the glyceraldehyde-3-phosphate
RT   dehydrogenase gene (gapA) in natural populations of Salmonella and
RT   Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:6667-6671(1991).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-321.
RC   STRAIN=ECOR 10, ECOR 16, ECOR 38, ECOR 39, ECOR 4, ECOR 40, ECOR 49,
RC   ECOR 65, ECOR 68, ECOR 8, and O2:HN / ECOR 50 / P97 / UPEC;
RX   PubMed=7896119; DOI=10.1093/genetics/138.4.993;
RA   Guttman D.S., Dykhuizen D.E.;
RT   "Detecting selective sweeps in naturally occurring Escherichia coli.";
RL   Genetics 138:993-1003(1994).
RN   [10]
RP   GENE TRANSFER DISCUSSION.
RX   PubMed=2124629; DOI=10.1007/bf02106053;
RA   Doolittle R.F., Feng D.F., Anderson K.L., Alberro M.R.;
RT   "A naturally occurring horizontal gene transfer from a eukaryote to a
RT   prokaryote.";
RL   J. Mol. Evol. 31:383-388(1990).
RN   [11]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   MUTAGENESIS OF HIS-177.
RX   PubMed=2659073; DOI=10.1021/bi00432a036;
RA   Soukri A., Mougin A., Corbier C., Wonacott A., Branlant C., Branlant G.;
RT   "Role of the histidine 176 residue in glyceraldehyde-3-phosphate
RT   dehydrogenase as probed by site-directed mutagenesis.";
RL   Biochemistry 28:2586-2592(1989).
RN   [12]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132; LYS-138; LYS-192 AND
RP   LYS-249, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX   PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA   Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA   Grishin N.V., Zhao Y.;
RT   "Lysine acetylation is a highly abundant and evolutionarily conserved
RT   modification in Escherichia coli.";
RL   Mol. Cell. Proteomics 8:215-225(2009).
RN   [14]
RP   MALONYLATION AT LYS-331.
RC   STRAIN=K12;
RX   PubMed=21908771; DOI=10.1074/mcp.m111.012658;
RA   Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W.,
RA   Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J.,
RA   Verdin E., Ye Y., Zhao Y.;
RT   "The first identification of lysine malonylation substrates and its
RT   regulatory enzyme.";
RL   Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
RN   [15]
RP   SUCCINYLATION AT LYS-115; LYS-124; LYS-132; LYS-192; LYS-213; LYS-217;
RP   LYS-225; LYS-249; LYS-257; LYS-261 AND LYS-331.
RC   STRAIN=K12;
RX   PubMed=21151122; DOI=10.1038/nchembio.495;
RA   Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.;
RT   "Identification of lysine succinylation as a new post-translational
RT   modification.";
RL   Nat. Chem. Biol. 7:58-63(2011).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF WILD-TYPE AND THR-313 MUTANT IN
RP   COMPLEX WITH NAD, AND SUBUNIT.
RX   PubMed=8636984; DOI=10.1006/jmbi.1996.0204;
RA   Duee E., Olivier-Deyris L., Fanchon E., Corbier C., Branlant G.,
RA   Dideberg O.;
RT   "Comparison of the structures of wild-type and a N313T mutant of
RT   Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: implication for
RT   NAD binding and cooperativity.";
RL   J. Mol. Biol. 257:814-838(1996).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD AND
RP   GLYCERALDEHYDE 3-PHOSPHATE, AND SUBUNIT.
RX   PubMed=10978154; DOI=10.1021/bi9927080;
RA   Yun M., Park C.-G., Kim J.-Y., Park H.-W.;
RT   "Structural analysis of glyceraldehyde 3-phosphate dehydrogenase from
RT   Escherichia coli: direct evidence of substrate binding and cofactor-induced
RT   conformational changes.";
RL   Biochemistry 39:10702-10710(2000).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
RA   Shin D.H., Thor J., Yokota H., Kim R., Kim S.H.;
RT   "Crystal structure of MES buffer bound form of glyceraldehyde 3-phosphate
RT   dehydrogenase from Escherichia coli.";
RL   Submitted (JAN-2004) to the PDB data bank.
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE
RP   ANALOG, AND SUBUNIT.
RX   PubMed=19542219; DOI=10.1074/jbc.m109.004648;
RA   Frayne J., Taylor A., Cameron G., Hadfield A.T.;
RT   "Structure of insoluble rat sperm glyceraldehyde-3-phosphate dehydrogenase
RT   (GAPDH) via heterotetramer formation with Escherichia coli GAPDH reveals
RT   target for contraceptive design.";
RL   J. Biol. Chem. 284:22703-22712(2009).
CC   -!- FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-
CC       phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor
CC       NAD. The first reaction step involves the formation of a hemiacetal
CC       intermediate between G3P and a cysteine residue, and this hemiacetal
CC       intermediate is then oxidized to a thioester, with concomitant
CC       reduction of NAD to NADH. The reduced NADH is then exchanged with the
CC       second NAD, and the thioester is attacked by a nucleophilic inorganic
CC       phosphate to produce BPG. {ECO:0000269|PubMed:2659073}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC         phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC         Evidence={ECO:0000269|PubMed:2659073};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=15 uM for BPG {ECO:0000269|PubMed:2659073};
CC         KM=42 uM for NAD {ECO:0000269|PubMed:2659073};
CC         KM=1500 uM for G3P {ECO:0000269|PubMed:2659073};
CC         Note=kcat is 1056 sec(-1) for dehydrogenase activity.;
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10978154,
CC       ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984}.
CC   -!- INTERACTION:
CC       P0A9B2; P0A9H9: cheZ; NbExp=2; IntAct=EBI-368904, EBI-546726;
CC       P0A9B2; P0A9B2: gapA; NbExp=2; IntAct=EBI-368904, EBI-368904;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; X02662; CAA26498.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74849.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15576.1; -; Genomic_DNA.
DR   EMBL; M66870; AAA23838.1; -; Genomic_DNA.
DR   EMBL; M66871; AAA23839.1; -; Genomic_DNA.
DR   EMBL; M66872; AAA02930.1; -; Genomic_DNA.
DR   EMBL; M66873; AAA23840.1; -; Genomic_DNA.
DR   EMBL; M66874; AAA23841.1; -; Genomic_DNA.
DR   EMBL; M66875; AAA23842.1; -; Genomic_DNA.
DR   EMBL; M66876; AAA23843.1; -; Genomic_DNA.
DR   EMBL; M66877; AAA23844.1; -; Genomic_DNA.
DR   EMBL; M66878; AAA23845.1; -; Genomic_DNA.
DR   EMBL; M66879; AAA23846.1; -; Genomic_DNA.
DR   EMBL; M66880; AAA23847.1; -; Genomic_DNA.
DR   EMBL; M66881; AAA23848.1; -; Genomic_DNA.
DR   EMBL; M66882; AAA23849.1; -; Genomic_DNA.
DR   EMBL; U07750; AAC43271.1; -; Genomic_DNA.
DR   EMBL; U07751; AAC43272.1; -; Genomic_DNA.
DR   EMBL; U07752; AAC43273.1; -; Genomic_DNA.
DR   EMBL; U07754; AAC43274.1; -; Genomic_DNA.
DR   EMBL; U07765; AAC43284.1; -; Genomic_DNA.
DR   EMBL; U07768; AAC43285.1; -; Genomic_DNA.
DR   EMBL; U07769; AAC43286.1; -; Genomic_DNA.
DR   EMBL; U07770; AAC43287.1; -; Genomic_DNA.
DR   EMBL; U07771; AAC43288.1; -; Genomic_DNA.
DR   EMBL; U07772; AAC43289.1; -; Genomic_DNA.
DR   EMBL; U07773; AAC43290.1; -; Genomic_DNA.
DR   PIR; A25209; DEECG3.
DR   RefSeq; NP_416293.1; NC_000913.3.
DR   RefSeq; WP_000153502.1; NZ_STEB01000009.1.
DR   PDB; 1DC3; X-ray; 2.50 A; A/B=2-331.
DR   PDB; 1DC4; X-ray; 2.50 A; A/B=2-331.
DR   PDB; 1DC5; X-ray; 2.00 A; A/B=2-331.
DR   PDB; 1DC6; X-ray; 2.00 A; A/B=2-331.
DR   PDB; 1GAD; X-ray; 1.80 A; O/P=2-331.
DR   PDB; 1GAE; X-ray; 2.17 A; O/P=2-331.
DR   PDB; 1S7C; X-ray; 2.04 A; A=1-331.
DR   PDB; 2VYN; X-ray; 2.20 A; A/B/C=1-331.
DR   PDB; 2VYV; X-ray; 2.38 A; A/B/C=1-331.
DR   PDB; 5ZA0; X-ray; 2.00 A; A=1-331.
DR   PDB; 6IO4; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=3-331.
DR   PDB; 6IO6; X-ray; 2.64 A; A=3-331.
DR   PDB; 6IOJ; X-ray; 2.29 A; A=3-331.
DR   PDB; 6UTM; X-ray; 2.14 A; A/B=2-331.
DR   PDB; 6UTN; X-ray; 1.79 A; A/B=2-331.
DR   PDB; 6UTO; X-ray; 1.64 A; A/B=2-331.
DR   PDBsum; 1DC3; -.
DR   PDBsum; 1DC4; -.
DR   PDBsum; 1DC5; -.
DR   PDBsum; 1DC6; -.
DR   PDBsum; 1GAD; -.
DR   PDBsum; 1GAE; -.
DR   PDBsum; 1S7C; -.
DR   PDBsum; 2VYN; -.
DR   PDBsum; 2VYV; -.
DR   PDBsum; 5ZA0; -.
DR   PDBsum; 6IO4; -.
DR   PDBsum; 6IO6; -.
DR   PDBsum; 6IOJ; -.
DR   PDBsum; 6UTM; -.
DR   PDBsum; 6UTN; -.
DR   PDBsum; 6UTO; -.
DR   AlphaFoldDB; P0A9B2; -.
DR   SMR; P0A9B2; -.
DR   BioGRID; 4260308; 65.
DR   BioGRID; 851992; 1.
DR   DIP; DIP-31848N; -.
DR   IntAct; P0A9B2; 27.
DR   MINT; P0A9B2; -.
DR   STRING; 511145.b1779; -.
DR   DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR   DrugBank; DB02263; D-glyceraldehyde 3-phosphate.
DR   iPTMnet; P0A9B2; -.
DR   SWISS-2DPAGE; P0A9B2; -.
DR   jPOST; P0A9B2; -.
DR   PaxDb; P0A9B2; -.
DR   PRIDE; P0A9B2; -.
DR   EnsemblBacteria; AAC74849; AAC74849; b1779.
DR   EnsemblBacteria; BAA15576; BAA15576; BAA15576.
DR   GeneID; 67415525; -.
DR   GeneID; 947679; -.
DR   KEGG; ecj:JW1768; -.
DR   KEGG; eco:b1779; -.
DR   PATRIC; fig|1411691.4.peg.475; -.
DR   EchoBASE; EB0362; -.
DR   eggNOG; COG0057; Bacteria.
DR   HOGENOM; CLU_030140_0_3_6; -.
DR   InParanoid; P0A9B2; -.
DR   OMA; NCVAPMA; -.
DR   PhylomeDB; P0A9B2; -.
DR   BioCyc; EcoCyc:GAPDH-A-MON; -.
DR   BioCyc; MetaCyc:GAPDH-A-MON; -.
DR   BRENDA; 1.2.1.12; 2026.
DR   SABIO-RK; P0A9B2; -.
DR   UniPathway; UPA00109; UER00184.
DR   EvolutionaryTrace; P0A9B2; -.
DR   PRO; PR:P0A9B2; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IMP:EcoCyc.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10836; PTHR10836; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   SMART; SM00846; Gp_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Glycolysis; NAD; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9298646, ECO:0000269|Ref.6"
FT   CHAIN           2..331
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase A"
FT                   /id="PRO_0000145648"
FT   ACT_SITE        150
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305|PubMed:10978154"
FT   BINDING         12..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:10978154,
FT                   ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984,
FT                   ECO:0000269|Ref.18"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:10978154,
FT                   ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984"
FT   BINDING         78
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:10978154,
FT                   ECO:0000269|PubMed:19542219"
FT   BINDING         120
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:19542219"
FT   BINDING         149..151
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000269|PubMed:10978154"
FT   BINDING         180
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P00362"
FT   BINDING         209..210
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000269|PubMed:10978154"
FT   BINDING         232
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000269|PubMed:19542219, ECO:0000269|Ref.18,
FT                   ECO:0000305|PubMed:10978154"
FT   BINDING         314
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:10978154,
FT                   ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984"
FT   SITE            177
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000269|PubMed:2659073"
FT   MOD_RES         115
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000269|PubMed:21151122"
FT   MOD_RES         124
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000269|PubMed:21151122"
FT   MOD_RES         132
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:18723842"
FT   MOD_RES         132
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21151122"
FT   MOD_RES         138
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:18723842"
FT   MOD_RES         192
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:18723842"
FT   MOD_RES         192
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21151122"
FT   MOD_RES         213
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000269|PubMed:21151122"
FT   MOD_RES         217
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000269|PubMed:21151122"
FT   MOD_RES         225
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000269|PubMed:21151122"
FT   MOD_RES         249
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:18723842"
FT   MOD_RES         249
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000269|PubMed:21151122"
FT   MOD_RES         257
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000269|PubMed:21151122"
FT   MOD_RES         261
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000269|PubMed:21151122"
FT   MOD_RES         331
FT                   /note="N6-malonyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21908771"
FT   MOD_RES         331
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21151122"
FT   VARIANT         43
FT                   /note="Y -> I (in strain: ECOR 70)"
FT   VARIANT         266
FT                   /note="G -> D (in strain: E830587)"
FT   VARIANT         267
FT                   /note="E -> A (in strain: E2666-74)"
FT   MUTAGEN         177
FT                   /note="H->N: Reduces activity about 50-fold."
FT                   /evidence="ECO:0000269|PubMed:2659073"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   HELIX           12..22
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   STRAND          25..33
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   HELIX           38..46
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   TURN            49..51
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   STRAND          58..61
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   STRAND          64..67
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   STRAND          70..75
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   HELIX           80..82
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   HELIX           85..88
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   STRAND          92..95
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   HELIX           103..106
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   HELIX           108..111
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   STRAND          115..121
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   TURN            132..134
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   HELIX           136..138
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   STRAND          143..146
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   HELIX           150..166
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   STRAND          168..178
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   STRAND          183..187
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   HELIX           195..197
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   HELIX           200..202
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   STRAND          205..207
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   HELIX           211..218
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   HELIX           220..222
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   TURN            223..225
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   STRAND          226..234
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   STRAND          239..249
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   HELIX           253..265
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   TURN            266..271
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   STRAND          272..275
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   HELIX           281..284
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   STRAND          289..294
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   TURN            295..297
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   STRAND          299..302
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   STRAND          305..312
FT                   /evidence="ECO:0007829|PDB:6UTO"
FT   HELIX           316..330
FT                   /evidence="ECO:0007829|PDB:6UTO"
SQ   SEQUENCE   331 AA;  35532 MW;  B3A460AA6D59E46D CRC64;
     MTIKVGINGF GRIGRIVFRA AQKRSDIEIV AINDLLDADY MAYMLKYDST HGRFDGTVEV
     KDGHLIVNGK KIRVTAERDP ANLKWDEVGV DVVAEATGLF LTDETARKHI TAGAKKVVMT
     GPSKDNTPMF VKGANFDKYA GQDIVSNASC TTNCLAPLAK VINDNFGIIE GLMTTVHATT
     ATQKTVDGPS HKDWRGGRGA SQNIIPSSTG AAKAVGKVLP ELNGKLTGMA FRVPTPNVSV
     VDLTVRLEKA ATYEQIKAAV KAAAEGEMKG VLGYTEDDVV STDFNGEVCT SVFDAKAGIA
     LNDNFVKLVS WYDNETGYSN KVLDLIAHIS K
 
 
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