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
