ID GPDA_BOVIN Reviewed; 349 AA. AC Q5EA88; Q2HJE6; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 08-NOV-2023, entry version 122. 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 Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=16305752; DOI=10.1186/1471-2164-6-166; RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; RT "Characterization of 954 bovine full-CDS cDNA sequences."; RL BMC Genomics 6:166-166(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-349. RC STRAIN=Hereford; TISSUE=Ascending colon; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (SEP-2005) 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; BT020681; AAX08698.1; -; mRNA. DR EMBL; BC105513; AAI05514.1; -; mRNA. DR RefSeq; NP_001030431.1; NM_001035354.1. DR AlphaFoldDB; Q5EA88; -. DR SMR; Q5EA88; -. DR STRING; 9913.ENSBTAP00000021683; -. DR PaxDb; 9913-ENSBTAP00000021683; -. DR PeptideAtlas; Q5EA88; -. DR GeneID; 525042; -. DR KEGG; bta:525042; -. DR CTD; 2819; -. DR eggNOG; KOG2711; Eukaryota. DR HOGENOM; CLU_033449_2_2_1; -. DR InParanoid; Q5EA88; -. DR OrthoDB; 3675564at2759; -. DR TreeFam; TF300836; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0005829; C:cytosol; ISS:AgBase. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro. DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; ISS:AgBase. 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:0005975; P:carbohydrate metabolic process; ISS:AgBase. DR GO; GO:0006094; P:gluconeogenesis; ISS:AgBase. DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; ISS:AgBase. DR GO; GO:0006116; P:NADH oxidation; IBA:GO_Central. 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_0000262289" 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 289 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P13707" FT MOD_RES 326 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:O35077" FT CONFLICT 122 FT /note="V -> L (in Ref. 1; AAX08698)" FT /evidence="ECO:0000305" FT CONFLICT 313 FT /note="K -> R (in Ref. 1; AAX08698)" FT /evidence="ECO:0000305" SQ SEQUENCE 349 AA; 37648 MW; 59E7DFADE8FC1A80 CRC64; MTGKKVCIVG SGNWGSAIAK IVGGNAAQLA HFDPRVTMWV FEEDIGGRKL TEIINTQHEN VKYLPGHKLP PNVVAVPDVV QAAADADILI FVVPHQFIGK ICDQLKGHLK ADTIGVSLIK GVDEGPKGLK LISEVIGERL GIPMSVLMGA NIANEVADEK FCETTIGSKN QAHGQLLKEL MQTPNFRITV VQEVDTVEIC GALKNIVAVG AGFCDGLGFG DNTKAAVIRL GLMEMIAFAK LFCSGSVSSA TFLESCGVAD LITTCYGGRN RKVAEAFART GKSIEQLEKE MLNGQKLQGP QTARELHSIL QHKGMVDKFP LFTAVYKVCY ENQPVGEFIH CLQNHPEHV //