ID   GPD2_ZYGRO              Reviewed;         389 AA.
AC   Q9HGY1;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] 2;
DE            EC=1.1.1.8;
DE   AltName: Full=ZrGPD2;
GN   Name=GPD2;
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 [MRNA].
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB047395; BAB11958.1; -; mRNA.
DR   AlphaFoldDB; Q9HGY1; -.
DR   SMR; Q9HGY1; -.
DR   STRING; 4956.XP_002494605.1; -.
DR   eggNOG; KOG2711; Eukaryota.
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   2: Evidence at transcript level;
KW   Cytoplasm; NAD; Oxidoreductase.
FT   CHAIN           1..389
FT                   /note="Glycerol-3-phosphate dehydrogenase [NAD(+)] 2"
FT                   /id="PRO_0000138102"
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   389 AA;  42511 MW;  70BBA9C2AAB463D0 CRC64;
     MAATDRLNQT SDILSHSMKK TDTSMSIVTA ENPYKVAVVG SGNWGTTIAK VVAENTKEKP
     ELFQGRVDMW VFEEQIDGTP LTQIINTKHQ NVKYLPNIDL PGNLVANPDL ISTTKDADVI
     VFNVPHQFLG RIVSQMKGQI KPDARAISCL KGFEVGPKGV QLLSDYVTQE LGIQCGALSG
     ANLAPEVAKE HWSETTVAYQ VPDDFKGEGK DIDHRVLKQL FHRPYFHVNV IDDVAGISIA
     GALKNVVALG CGFVTGLGWG NNAAAAIQRV GLGEIIKFGR MFFPESKVET YYQESAGVAD
     LITTCSGGRN VRVATEMAKT GKSGEQVEKD ILNGQSAQGL ITAKEVHQWL ESSGHTEEYP
     LFEAVYQITY ENVPMKELPS MIEELDIVE