ID G3P1_SHIFL Reviewed; 331 AA. AC P0A9B5; P06977; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 25-NOV-2008, entry version 31. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase A; DE Short=GAPDH-A; DE EC=1.2.1.12; GN Name=gapA; OrderedLocusNames=SF1444, S1559; OS Shigella flexneri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 / Serotype 2a; RX MEDLINE=22272406; PubMed=12384590; DOI=10.1093/nar/gkf566; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., RA Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., RA Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., RA Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., RA Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; RX MEDLINE=22590274; PubMed=12704152; RX DOI=10.1128/IAI.71.5.2775-2786.2003; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., RA Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., RA Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., RA Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella RT flexneri serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE005674; AAN43042.1; ALT_INIT; Genomic_DNA. DR EMBL; AE014073; AAP16937.1; -; Genomic_DNA. DR RefSeq; NP_707335.2; -. DR RefSeq; NP_837130.1; -. DR SMR; P0A9B5; 2-331. DR GeneID; 1024650; -. DR GeneID; 1077928; -. DR GenomeReviews; AE014073_GR; S1559. DR GenomeReviews; AE005674_GR; SF1444. DR KEGG; sfl:SF1444; -. DR KEGG; sfx:S1559; -. DR HOGENOM; P0A9B5; -. DR BioCyc; SFLE198214:AAN43042.1-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:InterPro. DR GO; GO:0051287; F:NAD 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_DHase. DR InterPro; IPR006424; Glyceraldehyde-3-P_DHase_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_0000145678. 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 //