ID GPDA_PONAB Reviewed; 349 AA. AC Q5RCE0; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 107. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic; DE Short=GPD-C; DE Short=GPDH-C; DE EC=1.1.1.8 {ECO:0000250|UniProtKB:P21695}; GN Name=GPD1; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pongo. OX NCBI_TaxID=9601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Has glycerol-3-phosphate dehydrogenase activity. CC {ECO:0000250|UniProtKB:P21695}. CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate CC + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, CC ChEBI:CHEBI:57945; EC=1.1.1.8; CC Evidence={ECO:0000250|UniProtKB:P21695}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11093; CC Evidence={ECO:0000250|UniProtKB:P21695}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P21695}. CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate CC dehydrogenase 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; CR858331; CAH90567.1; -; mRNA. DR RefSeq; NP_001125302.1; NM_001131830.1. DR AlphaFoldDB; Q5RCE0; -. DR SMR; Q5RCE0; -. DR STRING; 9601.ENSPPYP00000005145; -. DR Ensembl; ENSPPYT00000005346.2; ENSPPYP00000005145.1; ENSPPYG00000004507.2. DR GeneID; 100172201; -. DR KEGG; pon:100172201; -. DR CTD; 2819; -. DR eggNOG; KOG2711; Eukaryota. DR GeneTree; ENSGT00390000003114; -. DR HOGENOM; CLU_033449_2_2_1; -. DR InParanoid; Q5RCE0; -. DR OMA; NRMFGNM; -. DR OrthoDB; 3675564at2759; -. DR TreeFam; TF300836; -. DR Proteomes; UP000001595; Chromosome 12. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro. DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro. DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl. DR GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl. DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro. DR GO; GO:0006127; P:glycerophosphate shuttle; IEA:Ensembl. DR GO; GO:0045821; P:positive regulation of glycolytic process; IEA:Ensembl. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. DR InterPro; IPR013328; 6PGD_dom2. DR InterPro; IPR006168; G3P_DH_NAD-dep. DR InterPro; IPR006109; G3P_DH_NAD-dep_C. DR InterPro; IPR017751; G3P_DH_NAD-dep_euk. DR InterPro; IPR011128; G3P_DH_NAD-dep_N. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR03376; glycerol3P_DH; 1. DR PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR11728:SF32; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)], CYTOPLASMIC; 1. DR Pfam; PF07479; NAD_Gly3P_dh_C; 1. DR Pfam; PF01210; NAD_Gly3P_dh_N; 1. DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 1. DR PRINTS; PR00077; GPDHDRGNASE. DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00957; NAD_G3PDH; 1. PE 2: Evidence at transcript level; KW Cytoplasm; NAD; Oxidoreductase; Phosphoprotein; Reference proteome. FT CHAIN 1..349 FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)], FT cytoplasmic" FT /id="PRO_0000262290" FT ACT_SITE 204 FT /note="Proton acceptor" FT /evidence="ECO:0000255" FT BINDING 10..15 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P21695" FT BINDING 120 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 153 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P21695" FT BINDING 269..270 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 269 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P21695" FT BINDING 296 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P21695" FT BINDING 298 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P21695" FT MOD_RES 154 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P21695" FT MOD_RES 289 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P13707" FT MOD_RES 326 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:O35077" SQ SEQUENCE 349 AA; 37537 MW; B8FC0A005E326BAF CRC64; MASKKVCIVG SGNWGSAIAK IVGGNAAQLA QFDPRVTMWV FEEDIGGKKL TEIINTQHEN VKYLPGHKLP PNVVAVPDVV QAAADADILI FVVPHQFIGK ICDQLKGHLK ANATGISLIK GVDEGPNGLK LISEVIGEHL GIPMSVLMGA NIASEVADEK FCETTIGCKD PAQGQLLKEL MQTPNFRITV VQEVDTVEIC GALKNVVAVG AGFCDGLGFG DNTKAAVIRL GLMEMIAFAK LFRSGPVSSA TFLESCGVAD LITTCYGGRN RKVAEAFART GKSIEQLEKE LLNGQKLQGP ETARELHSIL QHKGLVDKFP LFMAVYKVCY EGQPVGEFIR CLQNHPEHM //