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 24-JAN-2024, entry version 94.
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}.
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DR EMBL; AB047395; BAB11958.1; -; mRNA.
DR AlphaFoldDB; Q9HGY1; -.
DR SMR; Q9HGY1; -.
DR eggNOG; KOG2711; Eukaryota.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR03376; glycerol3P_DH; 1.
DR PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11728:SF8; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)]-RELATED; 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 SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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
//
