ID   GPDA_RABIT              Reviewed;         349 AA.
AC   P08507;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 115.
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   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   SECONDARY STRUCTURE PREDICTION.
RX   PubMed=6773774; DOI=10.1111/j.1432-1033.1980.tb04798.x;
RA   Otto J., Argos P., Rossmann M.G.;
RT   "Prediction of secondary structural elements in glycerol-3-phosphate
RT   dehydrogenase by comparison with other dehydrogenases.";
RL   Eur. J. Biochem. 109:325-330(1980).
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.
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   PIR; A32512; A32512.
DR   AlphaFoldDB; P08507; -.
DR   SMR; P08507; -.
DR   InParanoid; P08507; -.
DR   BRENDA; 1.1.1.8; 1749.
DR   SABIO-RK; P08507; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] 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; IEA:InterPro.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR   Gene3D; 1.10.1040.10; -; 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   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; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR03376; glycerol3P_DH; 1.
DR   PROSITE; PS00957; NAD_G3PDH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..349
FT                   /note="Glycerol-3-phosphate dehydrogenase [NAD(+)],
FT                   cytoplasmic"
FT                   /id="PRO_0000138081"
FT   ACT_SITE        204
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         10..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         120
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
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;  37610 MW;  A11FE0E1F4ADD807 CRC64;
     MAGKKVCIVG SGDWGSAIAK IVGGNAAQLA QFDPRVTMWV FEEDIGGKKL TEIINTHQEN
     VKYLPGHKLP PNVVAVPDVV KAAADADILI FVVPHQFIGK ICDEIKGHLK ANAIGISLIK
     GVNEGPKGLK LISEVIGEHL GIPMSVLMGA NIASEVADEK FCETTIGCKD QAQGQLLKQL
     MQTPNFRIVV TQEVNTVEIC GALKDLVAVG AGFCDGIGFG DNTKAAVIRL GLMEMIAFAK
     LFCSGPVSPA TFLESCGVAD LITTCYGGRN RKVAEAFART GKSIEQLEKE MLNGQKLQGP
     ETARELHSIL QHKGLVDWFP LFMAVYKVCY QGQPVGEFIR CLQNHPEHM