ID GPD1_CANGA Reviewed; 400 AA. AC Q6FN96; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 18-JUN-2025, entry version 125. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] 1; DE EC=1.1.1.8; GN Name=GPD1; OrderedLocusNames=CAGL0K01683g; OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces. OX NCBI_TaxID=284593; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS RC 138; 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=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 -!- 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; CR380957; CAG61259.1; -; Genomic_DNA. DR RefSeq; XP_448298.1; XM_448298.1. DR AlphaFoldDB; Q6FN96; -. DR SMR; Q6FN96; -. DR FunCoup; Q6FN96; 650. DR STRING; 284593.Q6FN96; -. DR EnsemblFungi; CAGL0K01683g-T; CAGL0K01683g-T-p1; CAGL0K01683g. DR GeneID; 2890024; -. DR KEGG; cgr:2890024; -. DR CGD; CAL0133949; GPD1. DR VEuPathDB; FungiDB:CAGL0K01683g; -. DR eggNOG; KOG2711; Eukaryota. DR HOGENOM; CLU_033449_2_4_1; -. DR InParanoid; Q6FN96; -. DR OMA; NRMFGNM; -. DR Proteomes; UP000002428; Chromosome K. 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-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 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; Oxidoreductase; Reference proteome. FT CHAIN 1..400 FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)] 1" FT /id="PRO_0000138086" FT ACT_SITE 254 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 319..320 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 319 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 348 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" SQ SEQUENCE 400 AA; 43988 MW; DE850B128571D8E5 CRC64; MSNSAAGRLN QTSHILNESI KNDDISLRRS QPSTTSLQAL EHPFKVTVIG SGNWGTTIAK VVAENTALNP HLFVSRVDMW VFEEKIDGKN LTEIINEQHE NVKYLPDIKL PENLVANPNL IDSVKGADIL IFNIPHQFLP RIVSNLKNHV GPHVRAISCL KGFEVGKKGV QLLSSYVTDE LGIQCGALSG ANLAPEVAKE HWSETTVAYH IPKDFRGEGK DVDHKLLKAL FHRPYFHVNV IEDVAGISIA GALKNVVALG CGFVEGLGWG NNAAAAIQRV GLGEIIKFGQ MFFPESRVQT YYQESAGVAD LITTCSGGRN VRVAKHMAKT GKSALDAEKE LLNGQSAQGI ITCKEVHEWL ETCEMTHEFP LFEAVYQIVY NNVPMKNLPD MIEELECIAD //