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   16-JUN-2009, entry version 62.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic;
DE            Short=GPDH-C;
DE            Short=GPD-C;
DE            EC=1.1.1.8;
GN   Name=GPD1;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   SECONDARY STRUCTURE PREDICTION.
RX   MEDLINE=81003924; PubMed=6773774;
RX   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   -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(+) = glycerone
CC       phosphate + NADH.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family.
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DR   PIR; A32512; A32512.
DR   HSSP; P90551; 1EVY.
DR   HOVERGEN; P08507; -.
DR   BRENDA; 1.1.1.8; 255.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase (NAD+) a...; IEA:EC.
DR   GO; GO:0051287; F:NAD or NADH 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   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013328; DH_multihelical.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR006168; NAD-dep_Gly3P_DH.
DR   InterPro; IPR017751; NAD-dep_Gly3P_DH_euk.
DR   InterPro; IPR011128; NAD-dep_Gly3P_DH_N.
DR   InterPro; IPR006109; NAD_Gly3P_DH_C.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1.
DR   PANTHER; PTHR11728; NAD_Gly3P_DH; 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   ProDom; PD001278; NAD_Gly3P_C; 1.
DR   TIGRFAMs; TIGR03376; glycerol3P_DH; 1.
DR   PROSITE; PS00957; NAD_G3PDH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; Oxidoreductase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    349       Glycerol-3-phosphate dehydrogenase
FT                                [NAD+], cytoplasmic.
FT                                /FTId=PRO_0000138081.
FT   NP_BIND      10     15       NAD (By similarity).
FT   REGION      269    270       Substrate binding (By similarity).
FT   ACT_SITE    204    204       Proton acceptor (By similarity).
FT   BINDING      97     97       NAD (By similarity).
FT   BINDING     120    120       NAD; via amide nitrogen (By similarity).
FT   BINDING     120    120       Substrate (By similarity).
FT   BINDING     153    153       NAD; via amide nitrogen (By similarity).
FT   BINDING     269    269       NAD (By similarity).
FT   BINDING     298    298       NAD (By similarity).
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
//