ID G3P_NATPD Reviewed; 338 AA. AC Q3IUT3; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 16-JUN-2009, entry version 31. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase; DE Short=GAPDH; DE EC=1.2.1.59; DE AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase; GN Name=gap; OrderedLocusNames=NP0012A; OS Natronomonas pharaonis (strain DSM 2160 / ATCC 35678). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Natronomonas. OX NCBI_TaxID=348780; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16169924; DOI=10.1101/gr.3952905; RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J., RA Oesterhelt D.; RT "Living with two extremes: conclusions from the genome sequence of RT Natronomonas pharaonis."; RL Genome Res. 15:1336-1343(2005). CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + CC NAD(P)(+) = 3-phospho-D-glyceroyl phosphate + NAD(P)H. 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; CR936257; CAI48097.1; -; Genomic_DNA. DR RefSeq; YP_325669.1; -. DR GeneID; 3702737; -. DR GenomeReviews; CR936257_GR; NP0012A. DR KEGG; nph:NP0012A; -. DR NMPDR; fig|348780.3.peg.621; -. DR HOGENOM; Q3IUT3; -. DR OMA; Q3IUT3; AIFQGGE. DR BioCyc; NPHA348780:NP0012A-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043891; F:glyceraldehyde-3-phosphate dehydrogenase (N...; IEA:EC. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:HAMAP. DR GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro. DR GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro. DR GO; GO:0006096; P:glycolysis; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_00559; -; 1. DR InterPro; IPR000173; GlycerAld_3-P_DH. DR InterPro; IPR006436; Glyceraldehyde-3-P_DH_2_arc. DR Pfam; PF02800; Gp_dh_C; 1. DR Pfam; PF00044; Gp_dh_N; 1. DR PIRSF; PIRSF000149; GAP_DH; 1. DR ProDom; PD007761; GAPDH_like; 1. DR TIGRFAMs; TIGR01546; GAPDH-II_archae; 1. DR PROSITE; PS00071; GAPDH; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycolysis; NAD; NADP; Oxidoreductase. FT CHAIN 1 338 Glyceraldehyde-3-phosphate dehydrogenase. FT /FTId=PRO_0000232393. FT NP_BIND 12 13 NAD (By similarity). FT REGION 140 142 Glyceraldehyde 3-phosphate binding (By FT similarity). FT REGION 195 196 Glyceraldehyde 3-phosphate binding (By FT similarity). FT ACT_SITE 141 141 Nucleophile (By similarity). FT BINDING 111 111 NAD; via amide nitrogen (By similarity). FT BINDING 169 169 NAD (By similarity). FT BINDING 302 302 NAD; via carbonyl oxygen (By similarity). SQ SEQUENCE 338 AA; 36122 MW; 9B67D5F6B9C526E7 CRC64; MSIQVAVNGY GTIGKRVADA VTLQPDMELV GVAKTSPNHE AELAVENDYP LYAAIEDRID DFEAAGIDLA GTVDELVEAA DIVVDACPSG IGADNKSLYE AHDTPALYQG GESADLVDVS FNARSNFEAA ADADHVRVVS CNTTGLSRLL APLQEEYGVE KARVTLVRRG GDPGQTGRGP INDILPNPVS LPSHHGPDVN TIFPDLDIDT LGLKVPATLM HTHSVNVTLE STPDAEAVAD LLDEQDRTFL IPESYGIDGA GKLKEFAMDR GRPRADIWEN CIWAESVSME GSDLYLFQAI HQESDVVPEN IDAIRAVLGT ADADESRETT NETLGVGL //