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}.
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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
//
