ID B8GGC7_METPE Unreviewed; 340 AA. AC B8GGC7; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 96. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388}; DE Short=GAPDH {ECO:0000256|HAMAP-Rule:MF_00559}; DE EC=1.2.1.59 {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388}; DE AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00559}; GN Name=gap {ECO:0000256|HAMAP-Rule:MF_00559}; GN OrderedLocusNames=Mpal_2790 {ECO:0000313|EMBL:ACL18045.1}; OS Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c). OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanomicrobiales; Methanoregulaceae; Methanosphaerula. OX NCBI_TaxID=521011 {ECO:0000313|EMBL:ACL18045.1, ECO:0000313|Proteomes:UP000002457}; RN [1] {ECO:0000313|EMBL:ACL18045.1, ECO:0000313|Proteomes:UP000002457} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c RC {ECO:0000313|Proteomes:UP000002457}; RX PubMed=26543115; DOI=10.1128/genomea.01280-15; RA Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C., RA Yavitt J.B., Zinder S.H.; RT "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a RT Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland."; RL Genome Announc. 3:e01280-15(2015). 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 Evidence={ECO:0000256|ARBA:ARBA00001820, ECO:0000256|HAMAP- CC Rule:MF_00559, ECO:0000256|RuleBase:RU003388}; 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 Evidence={ECO:0000256|ARBA:ARBA00001295, ECO:0000256|HAMAP- CC Rule:MF_00559, ECO:0000256|RuleBase:RU003388}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869, CC ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881, CC ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00559, CC ECO:0000256|RuleBase:RU003388}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase CC family. {ECO:0000256|HAMAP-Rule:MF_00559, CC ECO:0000256|RuleBase:RU003388}. 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; CP001338; ACL18045.1; -; Genomic_DNA. DR RefSeq; WP_012619364.1; NC_011832.1. DR AlphaFoldDB; B8GGC7; -. DR STRING; 521011.Mpal_2790; -. DR GeneID; 7271376; -. DR KEGG; mpl:Mpal_2790; -. DR eggNOG; arCOG00493; Archaea. DR HOGENOM; CLU_069533_0_0_2; -. DR OrthoDB; 295712at2157; -. DR UniPathway; UPA00109; UER00184. DR Proteomes; UP000002457; Chromosome. 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; IEA:RHEA. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. 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 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_00559, KW ECO:0000256|RuleBase:RU003388}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00559}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00559}; Reference proteome {ECO:0000313|Proteomes:UP000002457}. FT DOMAIN 2..140 FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P) FT binding" FT /evidence="ECO:0000259|SMART:SM00846" FT ACT_SITE 140 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559, FT ECO:0000256|PIRSR:PIRSR000149-1" FT BINDING 11..12 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559" FT BINDING 110 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559" FT BINDING 139..141 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559" FT BINDING 168 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559" FT BINDING 194..195 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559" FT BINDING 302 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559" SQ SEQUENCE 340 AA; 36659 MW; 791C9B85CB444A52 CRC64; MIKVAINGYG TIGKRVADAV AAQPDMEIIG VSKTSPSAEA FVAQSRGYPL YIADIGRKPD FEKAGIRVAG SVEEMLTRAD VVVDATPGGV GAKNKPLYEK LGVRVIYQGG EKHLLAGFSF NSSCNYAKAI GRQFVRVVSC NTTGLCRIIH LVDTAYGVKK VRATMIRRAS DPGEIKRGPV DAIVLDPVTV PSHHGPDVQS VLPTIPITTA ALIVPTTFMH MHVVMIETEK EADREEIIQL IESHPRLGLV RPATGITSTA QLKEYMQDLG RSRADLWENG IFQDSVSVVD GHEVCLYQAI HQEADVVVEN VDAIRAMIGE VTDAETSIAI TNKALGFTAI //