ID   GPD1_YARLI              Reviewed;         398 AA.
AC   Q9UVF4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 136.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] 1;
DE            EC=1.1.1.8;
GN   Name=GPD1; OrderedLocusNames=YALI0B02948g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29;
RA   Nicaud J.-M., le Dall M.-T., Choquer M.;
RT   "Glycerol 3 phosphate dehydrogenase from Yarrowia lipolityca.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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   -!- CAUTION: It is uncertain whether Met-1 or Met-14 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; AJ250328; CAB58452.1; -; Genomic_DNA.
DR   EMBL; CR382128; CAG82664.1; -; Genomic_DNA.
DR   RefSeq; XP_500444.1; XM_500444.1.
DR   AlphaFoldDB; Q9UVF4; -.
DR   SMR; Q9UVF4; -.
DR   STRING; 284591.Q9UVF4; -.
DR   EnsemblFungi; CAG82664; CAG82664; YALI0_B02948g.
DR   GeneID; 2906777; -.
DR   KEGG; yli:YALI0B02948g; -.
DR   VEuPathDB; FungiDB:YALI0_B02948g; -.
DR   HOGENOM; CLU_033449_2_2_1; -.
DR   InParanoid; Q9UVF4; -.
DR   OMA; NRMFGNM; -.
DR   OrthoDB; 3675564at2759; -.
DR   Proteomes; UP000001300; Chromosome B.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006116; P:NADH oxidation; IBA:GO_Central.
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   Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..398
FT                   /note="Glycerol-3-phosphate dehydrogenase [NAD(+)] 1"
FT                   /id="PRO_0000138098"
FT   ACT_SITE        253
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         50..55
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         318..319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         318
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         350
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   398 AA;  43459 MW;  C576DA65AB076E1E CRC64;
     MSALLRSSLR FKHMSAVNRL TQQLRLLTAS APLSAANTAG KAPFKVAVVG SGNWGTTVAK
     IVAENCTAHP ELFEPEVRVW VREEKVNGKN LTDIFNAEHE NVRYLPKIKL PHNLIAEPDL
     LKAVEGANII VFNLPHQFLA GVCKQLKGHV NPKARAISCL KGLDVTPQGV YLLSDVIENE
     TGLHCGVLSG ANLATEIALE KYSETTVAYN RPKDFFGEGD VTNDVLKALF HRPYFHVRCV
     QDVAGVSIGG ALKNVVALCA GFVEGKNWGD NAKAAIMRRG MLEMINFSKR FFPETDINTL
     TVESAGVADL ITSCAGGRNF KVGRAFGKES GSGKTIQDVE KELLNGQSAQ GVITCNEVHE
     LLKNKNMQKD FPLFESTWGI IHGELKIDDL PEILYHAN
//