ID G3P_METHJ Reviewed; 339 AA. AC Q2FNA2; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 04-NOV-2026, entry version 108. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00559}; DE Short=GAPDH {ECO:0000255|HAMAP-Rule:MF_00559}; DE EC=1.2.1.59 {ECO:0000255|HAMAP-Rule:MF_00559}; DE AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00559}; GN Name=gap {ECO:0000255|HAMAP-Rule:MF_00559}; GN OrderedLocusNames=Mhun_2462; OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / OS JF-1). OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group; OC Methanomicrobia; Methanomicrobiales; Methanospirillaceae; Methanospirillum. OX NCBI_TaxID=323259; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1; RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8; RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H., RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M., RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.; RT "Complete genome sequence of Methanospirillum hungatei type strain JF1."; RL Stand. Genomic Sci. 11:2-2(2016). CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glyceraldehyde 3-phosphate + phosphate + NADP(+) = (2R)-3- CC phospho-glyceroyl phosphate + NADPH + H(+); 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 Evidence={ECO:0000255|HAMAP-Rule:MF_00559}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = (2R)-3- CC phospho-glyceroyl phosphate + NADH + H(+); 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 Evidence={ECO:0000255|HAMAP-Rule:MF_00559}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000255|HAMAP- CC Rule:MF_00559}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00559}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00559}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase CC family. {ECO:0000255|HAMAP-Rule:MF_00559}. 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; CP000254; ABD42162.1; -; Genomic_DNA. DR RefSeq; WP_011449420.1; NC_007796.1. DR AlphaFoldDB; Q2FNA2; -. DR SMR; Q2FNA2; -. DR FunCoup; Q2FNA2; 152. DR STRING; 323259.Mhun_2462; -. DR EnsemblBacteria; ABD42162; ABD42162; Mhun_2462. DR GeneID; 3923967; -. DR KEGG; mhu:Mhun_2462; -. DR eggNOG; arCOG00493; Archaea. DR HOGENOM; CLU_069533_0_0_2; -. DR InParanoid; Q2FNA2; -. DR OMA; AACNYKE; -. DR OrthoDB; 295712at2157; -. DR UniPathway; UPA00109; UER00184. DR Proteomes; UP000001941; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase activity; 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; IEA:RHEA. 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:0009085; P:L-lysine biosynthetic process; IEA:InterPro. DR CDD; cd18127; GAPDH_II_C; 1. DR CDD; cd02278; GAPDH_II_N; 1. DR Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1. 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 NCBIfam; NF003251; PRK04207.1; 1. DR PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR10836:SF76; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED; 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 3: Inferred from homology; KW Cytoplasm; Glycolysis; NAD; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1..339 FT /note="Glyceraldehyde-3-phosphate dehydrogenase" FT /id="PRO_0000300974" FT ACT_SITE 140 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00559" FT BINDING 11..12 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00559" FT BINDING 110 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00559" FT BINDING 139..141 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00559" FT BINDING 168 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00559" FT BINDING 194..195 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00559" FT BINDING 301 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00559" SQ SEQUENCE 339 AA; 36818 MW; 3C149595098A350B CRC64; MIKVAINGYG TIGKRVADAV SAQKDMEIIG VSKTKPSAEA LIAVQRGYPI YIADMSKKDA FAKAGIPVAG SVEDMLKKAD IVVDGTPGGV GESNKALYEK AGVKAIWQGG EDHEVAGFSF NAHANYKDAI GRQFVRVVSC NTTGLCRVIK AVDDAFGVVK VRAVMVRRGA DPHVVKKGPI DAVVLDPPTI PSHHGPDVNT VLPHIDIVTM AMIVPTTQMH MHAITIELKK EVSRDDVLAV MRSHNRIGLV QPKTAIKSTA ELKEYVMDMG RPRSDLWENG IFEASVNMVG KELFFFQAIH QEADVVIENV DAIRAMMGEV RDPETSIRMT NEAMQFTAL //