ID GPD_PYRO7 Reviewed; 433 AA. AC P0CT11; A4RGF7; G4NER8; Q5G5B9; DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot. DT 18-SEP-2013, sequence version 1. DT 24-JAN-2024, entry version 40. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)]; DE EC=1.1.1.8; GN ORFNames=MGG_00067; OS Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast OS fungus) (Magnaporthe oryzae). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia. OX NCBI_TaxID=242507; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958; RX PubMed=15846337; DOI=10.1038/nature03449; RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K., RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D., RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S., RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M., RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E., RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.; RT "The genome sequence of the rice blast fungus Magnaporthe grisea."; RL Nature 434:980-986(2005). 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 -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate CC dehydrogenase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=EHA49491.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; CM001235; EHA49491.1; ALT_INIT; Genomic_DNA. DR RefSeq; XP_003719075.1; XM_003719027.1. DR AlphaFoldDB; P0CT11; -. DR SMR; P0CT11; -. DR STRING; 242507.P0CT11; -. DR GeneID; 2675060; -. DR KEGG; mgr:MGG_00067; -. DR eggNOG; KOG2711; Eukaryota. DR InParanoid; P0CT11; -. DR OrthoDB; 3675564at2759; -. DR Proteomes; UP000009058; Chromosome 5. 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: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; IPR011128; G3P_DH_NAD-dep_N. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. 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 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..433 FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)]" FT /id="PRO_0000138091" FT REGION 187..246 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 201..225 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 226..240 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 283 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P21695" FT BINDING 17..22 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P21695" FT BINDING 49 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P21695" FT BINDING 117 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P21695" FT BINDING 140 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P21695" FT BINDING 173 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P21695" FT BINDING 349..350 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P21695" FT BINDING 349 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P21695" FT BINDING 378 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P21695" SQ SEQUENCE 433 AA; 46756 MW; AAFF086871BA1913 CRC64; MASLGSYAKK HKVTIIGSGN WGSTIAKIVA ESTREHKDVF EEDVQMWVFE EKVTIPKDSP YYESEEPQKL TEVINKHHEN VKYLPGIKLP SNIIANPSLT DAVRDSSVLV FNLPHEFLGK VCQQLNGHIV PFARGISCIK GVDVSGSGIN LFCEVIGEKL GIYCGALSGA NVASQIAAEE GVSETTIAYD PPPIDSSRAA TPRDRSPNYD STSANKLPDL TVTSADSNGK DDRGRRTKAK LTPVPESYPP LDHGTLQILF DRPYFSVSMV SDVAGVSLSG ALKNIVALAA GFVDGKGWGS NVQSAVIRVG LAEMLKFARE FFGESVDPFT ILLESAGVAD VITSCISGRN FRCASMAVKR GVSVAEIEEK ELNGQKLQGT STAKEVNSLL KARGREGDYP LFTTVNEILE GKARVDDLPK LVIRQKHTIE KSG //