ID A0A432GQJ8_9DELT Unreviewed; 336 AA. AC A0A432GQJ8; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 27-MAR-2024, entry version 15. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160}; DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160}; GN Name=gap {ECO:0000313|EMBL:RTZ85826.1}; GN ORFNames=DSY93_05285 {ECO:0000313|EMBL:RTZ90114.1}, DSY96_03995 GN {ECO:0000313|EMBL:RTZ85826.1}, DSY98_01625 GN {ECO:0000313|EMBL:RTZ82057.1}; OS SAR324 cluster bacterium. OC Bacteria; Deltaproteobacteria; SAR324 cluster. OX NCBI_TaxID=2024889 {ECO:0000313|EMBL:RTZ85826.1, ECO:0000313|Proteomes:UP000287917}; RN [1] {ECO:0000313|Proteomes:UP000286732, ECO:0000313|Proteomes:UP000287917} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MAG 151 {ECO:0000313|EMBL:RTZ90114.1}, MAG 58 RC {ECO:0000313|EMBL:RTZ85826.1}, and MAG 63_2 RC {ECO:0000313|EMBL:RTZ82057.1}; RA Trembath-Reichert E., Huber J.A.; RT "Combined omics and stable isotope probing to characterize newly discovered RT Mariana Back-Arc vent microbial communities."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3- CC phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor CC NAD. The first reaction step involves the formation of a hemiacetal CC intermediate between G3P and a cysteine residue, and this hemiacetal CC intermediate is then oxidized to a thioester, with concomitant CC reduction of NAD to NADH. The reduced NADH is then exchanged with the CC second NAD, and the thioester is attacked by a nucleophilic inorganic CC phosphate to produce BPG. {ECO:0000256|ARBA:ARBA00003501}. 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=1.2.1.12; CC Evidence={ECO:0000256|ARBA:ARBA00001810}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase CC family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RTZ85826.1}. 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; QNZM01000062; RTZ82057.1; -; Genomic_DNA. DR EMBL; QNZK01000140; RTZ85826.1; -; Genomic_DNA. DR EMBL; QNZH01000148; RTZ90114.1; -; Genomic_DNA. DR AlphaFoldDB; A0A432GQJ8; -. DR Proteomes; UP000286732; Unassembled WGS sequence. DR Proteomes; UP000287917; Unassembled WGS sequence. DR Proteomes; UP000288322; Unassembled WGS sequence. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. 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; IPR006424; Glyceraldehyde-3-P_DH_1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR01534; GAPDH-I; 1. DR PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR10836:SF76; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED; 1. DR Pfam; PF02800; Gp_dh_C; 1. DR Pfam; PF00044; Gp_dh_N; 1. DR PIRSF; PIRSF000149; GAP_DH; 1. DR PRINTS; PR00078; G3PDHDRGNASE. 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 NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000149-3}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU361160}. FT DOMAIN 3..153 FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P) FT binding" FT /evidence="ECO:0000259|SMART:SM00846" FT ACT_SITE 153 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1" FT BINDING 12..13 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT BINDING 34 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT BINDING 78 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT BINDING 120 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT BINDING 152..154 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT BINDING 183 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT BINDING 212..213 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT BINDING 235 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2" FT BINDING 317 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3" FT SITE 180 FT /note="Activates thiol group during catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4" SQ SEQUENCE 336 AA; 36093 MW; C1FA54E2ED5990A1 CRC64; MTIRIAINGF GRIGRMVVRA ANKNQNVEIV AINDLVPSEN LAYLLKYDST HGRFDGDVQA GQDCLVVDGK TIECLSERNP GDLPWNKMNI DYVIESTGLF TTSEKAEEHL KAGAKKVVIS APAKSAEIKT LVMGVNNETY DPGTDNIVSN ASCTTNCLAP IVKVVLDNYG IEEGLMTTVH SVTAAQPTVD GPSKKDWRGG RGGPQNIIPA STGAAKAVAL CIPEIAGKLT GMSFRVPTPN VSVVDLTVKL SKSTSYEEIN SSMKAASEGK LKGILGFTDE DVVSSDFIGS TYSSIYDAGA GIGLNDRFFK LVSWYDNEMG YSTRLIDLIE YMEGQN //