ID   G3P1_ECO57              Reviewed;         331 AA.
AC   P0A9B4; P06977;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 32.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase A;
DE            Short=GAPDH-A;
DE            EC=1.2.1.12;
GN   Name=gapA; OrderedLocusNames=Z2818, ECs2488;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   MEDLINE=21074935; PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   MEDLINE=21156231; PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
CC       NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family.
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DR   EMBL; AE005174; AAG56768.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35911.1; -; Genomic_DNA.
DR   PIR; D85788; D85788.
DR   PIR; H90939; H90939.
DR   RefSeq; NP_288215.1; -.
DR   RefSeq; NP_310515.1; -.
DR   SMR; P0A9B4; 2-331.
DR   GeneID; 913285; -.
DR   GeneID; 961753; -.
DR   GenomeReviews; AE005174_GR; Z2818.
DR   GenomeReviews; BA000007_GR; ECs2488.
DR   KEGG; ece:Z2818; -.
DR   KEGG; ecs:ECs2488; -.
DR   HOGENOM; P0A9B4; -.
DR   OMA; P0A9B4; KEICTEV.
DR   BioCyc; ECOL83334:ECS2488-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:EC.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000173; GlycerAld_3-P_DH.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   PANTHER; PTHR10836; GAP_DH; 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   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   Acetylation; Complete proteome; Cytoplasm; Glycolysis; NAD;
KW   Oxidoreductase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    331       Glyceraldehyde-3-phosphate dehydrogenase
FT                                A.
FT                                /FTId=PRO_0000145651.
FT   NP_BIND      12     13       NAD (By similarity).
FT   REGION      149    151       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      209    210       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    150    150       Nucleophile (By similarity).
FT   BINDING      34     34       NAD (By similarity).
FT   BINDING      78     78       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     180    180       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     232    232       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     314    314       NAD (By similarity).
FT   SITE        177    177       Activates thiol group during catalysis
FT                                (By similarity).
FT   MOD_RES     132    132       N6-acetyllysine (By similarity).
FT   MOD_RES     138    138       N6-acetyllysine (By similarity).
FT   MOD_RES     192    192       N6-acetyllysine (By similarity).
FT   MOD_RES     249    249       N6-acetyllysine (By similarity).
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
//