ID G3P_HALS3 Reviewed; 335 AA. AC B0R2M2; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 02-SEP-2026, entry version 102. 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=OE_1154F; OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1). OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group; OC Halobacteria; Halobacteriales; Halobacteriaceae; Halobacterium; OC Halobacterium salinarum NRC-34001. OX NCBI_TaxID=478009; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29341 / DSM 671 / R1; RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001; RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K., RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.; RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain RT R1 compared to that of strain NRC-1."; RL Genomics 91:335-346(2008). 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; AM774415; CAP12976.1; -; Genomic_DNA. DR RefSeq; WP_010902020.1; NC_010364.1. DR AlphaFoldDB; B0R2M2; -. DR SMR; B0R2M2; -. DR EnsemblBacteria; CAP12976; CAP12976; OE_1154F. DR GeneID; 68693074; -. DR KEGG; hsl:OE_1154F; -. DR HOGENOM; CLU_069533_0_0_2; -. DR PhylomeDB; B0R2M2; -. DR UniPathway; UPA00109; UER00184. 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 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 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. FT CHAIN 1..335 FT /note="Glyceraldehyde-3-phosphate dehydrogenase" FT /id="PRO_1000129245" 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 335 AA; 35683 MW; CA10FD928E368CB1 CRC64; MIRVGINGYG TIGKRVADAV AAQPDMTVAG VAKTSPNFEA TQARKRGFDL YTAVEDRADQ FPAAGIETAG PVDDLIADSD VVVDATPSGV GAENRSRYAA HDTPAIYQGG EDASVADVSF NARANFEAAA DADHVRVVSC NTTGLSRLLA PLREQYGIEK VRATLVRRGG DPGQTDRGPI NDILPDPITI PSHHGPDVNT IFPDLDIDTL GMKVPATLMH MHSINVTLER DPDAADVRDV LAGQSRIMLL DDDLGIDGTG PLKEYAQDMG RPRGDLWENC LWGESVTMDG RDFYCFQAIH QESDVVPENV DAVRAIAGDA DAAESIATTN DALGI //