ID G3P_METFE Reviewed; 337 AA. AC P10618; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 27-MAR-2024, entry version 149. 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; OS Methanothermus fervidus. OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria; OC Methanobacteriales; Methanothermaceae; Methanothermus. OX NCBI_TaxID=2180; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2841192; DOI=10.1016/0378-1119(88)90334-4; RA Fabry S., Hensel R.; RT "Primary structure of glyceraldehyde-3-phosphate dehydrogenase deduced from RT the nucleotide sequence of the thermophilic archaebacterium Methanothermus RT fervidus."; RL Gene 64:189-197(1988). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NADP, AND SUBUNIT. RX PubMed=10715215; DOI=10.1006/jmbi.2000.3565; RA Charron C., Talfournier F., Isupov M.N., Littlechild J.A., Branlant G., RA Vitoux B., Aubry A.; RT "The crystal structure of D-glyceraldehyde-3-phosphate dehydrogenase from RT the hyperthermophilic archaeon Methanothermus fervidus in the presence of RT NADP(+) at 2.1 A resolution."; RL J. Mol. Biol. 297:481-500(2000). CC -!- FUNCTION: Exhibits a dual-cofactor specificity, with a marked CC preference for NADP(+) over NAD(+). CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3- CC phospho-glyceroyl phosphate + H(+) + NADPH; Xref=Rhea:RHEA:10296, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57604, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.59; 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=1.2.1.59; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10715215}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M19980; AAA88227.1; -; Genomic_DNA. DR PIR; JT0286; JT0286. DR RefSeq; WP_013413357.1; NC_014658.1. DR PDB; 1CF2; X-ray; 2.10 A; O/P/Q/R=1-337. DR PDBsum; 1CF2; -. DR AlphaFoldDB; P10618; -. DR SMR; P10618; -. DR GeneID; 9961991; -. DR OMA; YIQAVHQ; -. DR SABIO-RK; P10618; -. DR UniPathway; UPA00109; UER00184. DR EvolutionaryTrace; P10618; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:InterPro. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-UniRule. DR GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IMP:CACAO. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_00559; G3P_dehdrog_arch; 1. DR InterPro; IPR000846; DapB_N. 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; IPR006436; Glyceraldehyde-3-P_DH_2_arc. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR01546; GAPDH-II_archae; 1. DR Pfam; PF01113; DapB_N; 1. DR Pfam; PF02800; Gp_dh_C; 1. DR PIRSF; PIRSF000149; GAP_DH; 1. DR SMART; SM00846; Gp_dh_N; 1. DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00071; GAPDH; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Glycolysis; NAD; NADP; Oxidoreductase. FT CHAIN 1..337 FT /note="Glyceraldehyde-3-phosphate dehydrogenase" FT /id="PRO_0000145722" FT ACT_SITE 140 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT BINDING 11..12 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:10715215" FT BINDING 34..35 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:10715215" FT BINDING 110 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:10715215" FT BINDING 139..141 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 171 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:10715215" FT BINDING 194..195 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 300 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT STRAND 2..7 FT /evidence="ECO:0007829|PDB:1CF2" FT HELIX 13..21 FT /evidence="ECO:0007829|PDB:1CF2" FT STRAND 23..35 FT /evidence="ECO:0007829|PDB:1CF2" FT HELIX 38..45 FT /evidence="ECO:0007829|PDB:1CF2" FT STRAND 50..54 FT /evidence="ECO:0007829|PDB:1CF2" FT HELIX 55..57 FT /evidence="ECO:0007829|PDB:1CF2" FT HELIX 58..63 FT /evidence="ECO:0007829|PDB:1CF2" FT HELIX 72..77 FT /evidence="ECO:0007829|PDB:1CF2" FT STRAND 80..84 FT /evidence="ECO:0007829|PDB:1CF2" FT HELIX 90..101 FT /evidence="ECO:0007829|PDB:1CF2" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:1CF2" FT HELIX 113..116 FT /evidence="ECO:0007829|PDB:1CF2" FT HELIX 122..125 FT /evidence="ECO:0007829|PDB:1CF2" FT HELIX 126..129 FT /evidence="ECO:0007829|PDB:1CF2" FT STRAND 133..137 FT /evidence="ECO:0007829|PDB:1CF2" FT HELIX 140..156 FT /evidence="ECO:0007829|PDB:1CF2" FT STRAND 158..170 FT /evidence="ECO:0007829|PDB:1CF2" FT STRAND 184..191 FT /evidence="ECO:0007829|PDB:1CF2" FT HELIX 194..199 FT /evidence="ECO:0007829|PDB:1CF2" FT STRAND 206..214 FT /evidence="ECO:0007829|PDB:1CF2" FT STRAND 219..229 FT /evidence="ECO:0007829|PDB:1CF2" FT HELIX 233..242 FT /evidence="ECO:0007829|PDB:1CF2" FT STRAND 246..249 FT /evidence="ECO:0007829|PDB:1CF2" FT TURN 251..254 FT /evidence="ECO:0007829|PDB:1CF2" FT HELIX 258..268 FT /evidence="ECO:0007829|PDB:1CF2" FT HELIX 271..273 FT /evidence="ECO:0007829|PDB:1CF2" FT STRAND 277..281 FT /evidence="ECO:0007829|PDB:1CF2" FT HELIX 282..284 FT /evidence="ECO:0007829|PDB:1CF2" FT STRAND 286..288 FT /evidence="ECO:0007829|PDB:1CF2" FT STRAND 291..298 FT /evidence="ECO:0007829|PDB:1CF2" FT TURN 300..303 FT /evidence="ECO:0007829|PDB:1CF2" FT HELIX 304..315 FT /evidence="ECO:0007829|PDB:1CF2" FT HELIX 322..333 FT /evidence="ECO:0007829|PDB:1CF2" SQ SEQUENCE 337 AA; 37408 MW; D83CBA88AAE5B0B8 CRC64; MKAVAINGYG TVGKRVADAI AQQDDMKVIG VSKTRPDFEA RMALKKGYDL YVAIPERVKL FEKAGIEVAG TVDDMLDEAD IVIDCTPEGI GAKNLKMYKE KGIKAIFQGG EKHEDIGLSF NSLSNYEESY GKDYTRVVSC NTTGLCRTLK PLHDSFGIKK VRAVIVRRGA DPAQVSKGPI NAIIPNPPKL PSHHGPDVKT VLDINIDTMA VIVPTTLMHQ HNVMVEVEET PTVDDIIDVF EDTPRVILIS AEDGLTSTAE IMEYAKELGR SRNDLFEIPV WRESITVVDN EIYYMQAVHQ ESDIVPENVD AVRAILEMEE DKYKSINKTN KAMNILQ //