ID   GPD1_ZYGRO              Reviewed;         401 AA.
AC   Q9HGY2;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] 1;
DE            EC=1.1.1.8;
DE   AltName: Full=ZrGPD1;
GN   Name=GPD1;
OS   Zygosaccharomyces rouxii (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=4956;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 42981 / IAM 12879 / JCM 22060 / S-96;
RX   PubMed=11378901; DOI=10.1002/yea.722;
RA   Iwaki T., Kurono S., Yokose Y., Kubota K., Tamai Y., Watanabe Y.;
RT   "Cloning of glycerol-3-phosphate dehydrogenase genes (ZrGPD1 and ZrGPD2)
RT   and glycerol dehydrogenase genes (ZrGCY1 and ZrGCY2) from the salt-tolerant
RT   yeast Zygosaccharomyces rouxii.";
RL   Yeast 18:737-744(2001).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; AB047394; BAB11957.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HGY2; -.
DR   SMR; Q9HGY2; -.
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.
FT   CHAIN           1..401
FT                   /note="Glycerol-3-phosphate dehydrogenase [NAD(+)] 1"
FT                   /id="PRO_0000138101"
FT   ACT_SITE        244
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         40..45
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         309..310
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         338
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   401 AA;  43791 MW;  E698797A2AA20A16 CRC64;
     MAATDRLNQT SDILSQSMKK TDSSMSVVTA ENPYKVSVVG SGNWGTTIAK VVAENTKEKP
     ELFQERVDMW VFEEQIDGTP LAQIINTKHQ NVKYLPNIDL PDNLVANPDL IATTKDADVI
     VFNVPHQFLG RIVAQMKGQI KPTARAVSCL KGFEVGPKGV QLLSDYVTQE LGIECGALSG
     ANLAPEVAKE HWSETTVAYH IPDDFKGDGK DIDHRVLKQL FHRPYFHVNV IDDVAGISIA
     GALKNVVALG CGFVTGLGWG NNAAAAIQRV GLGEIIKFGR MFFPESKVET YYQESAGVAD
     LITTCSGGRN VRVATEMAKT GKSGEQVEKD ILNGQSAQGL VTCKEVHQWL ESSGNTEDFP
     LFEAVYQITY ENVPMKELPS MIEELDIDST SKCVLSYKMG L