ID   A8W1U0_PICKU            Unreviewed;       388 AA.
AC   A8W1U0;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   18-JUN-2025, entry version 80.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243};
DE            EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243};
GN   Name=GPD {ECO:0000313|EMBL:ABW38024.1};
OS   Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC   Pichiales; Pichiaceae; Pichia.
OX   NCBI_TaxID=4909 {ECO:0000313|EMBL:ABW38024.1};
RN   [1] {ECO:0000313|EMBL:ABW38024.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18452539; DOI=10.1111/j.1567-1364.2008.00382.x;
RA   Chen X., Fang H., Rao Z., Shen W., Zhuge B., Wang Z., Zhuge J.;
RT   "Cloning and characterization of a NAD+-dependent glycerol-3-phosphate
RT   dehydrogenase gene from Candida glycerinogenes, an industrial glycerol
RT   producer.";
RL   FEMS Yeast Res. 8:725-734(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=sn-glycerol 3-phosphate + NAD(+) = dihydroxyacetone phosphate
CC         + NADH + H(+); 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         Evidence={ECO:0000256|ARBA:ARBA00048683,
CC         ECO:0000256|RuleBase:RU361243};
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009,
CC       ECO:0000256|RuleBase:RU000437}.
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DR   EMBL; EU186536; ABW38024.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8W1U0; -.
DR   VEuPathDB; FungiDB:C5L36_0E02100; -.
DR   BRENDA; 1.1.1.8; 1107.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0141152; F:glycerol-3-phosphate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR   FunFam; 1.10.1040.10:FF:000004; Glycerol-3-phosphate dehydrogenase [NAD(+)]; 1.
DR   FunFam; 3.40.50.720:FF:000294; Glycerol-3-phosphate dehydrogenase [NAD(+)]; 1.
DR   Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
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   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000114-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000437}.
FT   DOMAIN          36..201
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01210"
FT   DOMAIN          234..379
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07479"
FT   ACT_SITE        245
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-1"
FT   BINDING         41..46
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT   BINDING         129
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT   BINDING         185
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT   BINDING         310..311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT   BINDING         310
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT   BINDING         339
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
SQ   SEQUENCE   388 AA;  42762 MW;  8A8770A660E845A9 CRC64;
     MVSPAERLST IASTIKPNRK DSTSLQPEDY PEHPFKVTVV GSGNWGCTIA KVIAENTVER
     PRQFQRDVNM WVYEELIEGE KLTEIINTRH ENVKYLPGIK LPVNVVAVPD IVEACAGSDL
     IVFNIPHQFL PRILSQLKGK VNPKARAISC LKGLDVNPNG CKLLFTVITE ELGIYCGALS
     GANLAPEVAQ CKWSETTVAY TIPDDFRGKG KDIDHQILKS LFHRPYFRVR VISDVAGISI
     AGALKNVVAM AAGFVEGLGW GDNAKAAVMR IGLVETIQFA KTFFDGCHAA TFTHESAGVA
     DLITTCAGGR NVRVGRYMAQ HSVSATEAEE KLLNGQSCQG IHTTREVYEF LSNMGRTDEF
     PLFTTTYRII YENFPIEKLP ECLEPVED
//