ID   GPD1_SACBA              Reviewed;         391 AA.
AC   Q6J5J3;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD+] 1;
DE            EC=1.1.1.8;
GN   Name=GPD1;
OS   Saccharomyces bayanus (Yeast) (Saccharomyces uvarum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YY;
RA   Ma X., Guo Y., Zhang F., Yu H., Kuang J., Yao J., Li Z., He G.;
RT   "Research on the mechanism of osmotolerance and thermotolerance of
RT   yeast.";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(+) = glycerone
CC       phosphate + NADH.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family.
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DR   EMBL; AY598967; AAT27377.1; -; Genomic_DNA.
DR   BRENDA; 1.1.1.8; 164752.
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   CHAIN         1    391       Glycerol-3-phosphate dehydrogenase [NAD+]
FT                                1.
FT                                /FTId=PRO_0000138099.
FT   NP_BIND      41     46       NAD (By similarity).
FT   REGION      310    311       Substrate binding (By similarity).
FT   ACT_SITE    245    245       Proton acceptor (By similarity).
FT   BINDING     129    129       NAD (By similarity).
FT   BINDING     152    152       NAD; via amide nitrogen (By similarity).
FT   BINDING     152    152       Substrate (By similarity).
FT   BINDING     185    185       NAD; via amide nitrogen (By similarity).
FT   BINDING     310    310       NAD (By similarity).
FT   BINDING     339    339       NAD (By similarity).
SQ   SEQUENCE   391 AA;  42869 MW;  F5F1F7F111F707D1 CRC64;
     MSAAADRLNL TSGHLNAGRK RSSSSVSLKA AEKPFKVTVI GSGNWGTTIA KVVAENCKGY
     PEVFAPIVQM WVFEEEINGE KLTEIINTRH QNVKYLPGIT LPDNLVANPD LIDSVKDVDI
     IVFNIPHQFL PRICSQLKGH VDSHVRAISC LKGFEVGAKG VQLLSSYITE ELGIQCGALS
     GANIATEVAQ EHWSETTVAY HIPKDFRGEG KDVDHKVLKA LFHRPYFHVS VIEDVAGISI
     CGALKNVVAL GCGFVEGLGW GNNASAAIQR VGLGEIIRFG QMFFPESREE TYYQESAGVA
     DLITTCAGGR NVKVARLMAT SGKDAWECEK ELLNGQSAQG LITCKEVHEW LETCGSVEDF
     PLFEAVYQIV YNNYPMKNLP DMIEELDLHE D
//