ID A8Q3M8_MALGO Unreviewed; 347 AA. AC A8Q3M8; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 13-SEP-2023, entry version 88. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243}; DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243}; GN ORFNames=MGL_2451 {ECO:0000313|EMBL:EDP43441.1}; OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated OS fungus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina; OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia. OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP43441.1, ECO:0000313|Proteomes:UP000008837}; RN [1] {ECO:0000313|EMBL:EDP43441.1, ECO:0000313|Proteomes:UP000008837} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837}; RX PubMed=18000048; DOI=10.1073/pnas.0706756104; RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E., RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M., RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T., RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.; RT "Dandruff-associated Malassezia genomes reveal convergent and divergent RT virulence traits shared with plant and human fungal pathogens."; RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007). 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 Evidence={ECO:0000256|ARBA:ARBA00001662, 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}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EDP43441.1}. 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; AAYY01000008; EDP43441.1; -; Genomic_DNA. DR RefSeq; XP_001730655.1; XM_001730603.1. DR AlphaFoldDB; A8Q3M8; -. DR STRING; 425265.A8Q3M8; -. DR GeneID; 5854962; -. DR KEGG; mgl:MGL_2451; -. DR VEuPathDB; FungiDB:MGL_2451; -. DR InParanoid; A8Q3M8; -. DR OMA; NRMFGNM; -. DR OrthoDB; 3675564at2759; -. DR Proteomes; UP000008837; Unassembled WGS sequence. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule. DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] 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 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|PIRSR:PIRSR000114-3, ECO:0000256|RuleBase:RU000437}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU000437}; KW Reference proteome {ECO:0000313|Proteomes:UP000008837}. FT DOMAIN 7..175 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 198..343 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF07479" FT ACT_SITE 209 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1" FT BINDING 12..17 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 100 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 123 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 156 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 274..275 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 274 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 301 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 303 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" SQ SEQUENCE 347 AA; 37976 MW; ED90F5ADE4D493B8 CRC64; MVAHKQKVAI IGSGNWGSAI AKIAGFNTAR HSDVFEPIVH MYVYEEIVDG RKLTSIINED HVNTKYLPHA KLPENVVATP SPEEAARDAT LLVFVLPHQF ILNVCKSLKH ALAPDAHAIS MIKGVEVADK NISIFPDVIE KALGIPCAAL SGANIANEVA SGLFSETTVG YRPHQRALAE YYVKLFDTPK FRVGMIEDVA GVSLCGALKN IIAVGAGFVD GLGWGGNAKA AIMRIGLMEM RRFALEFFKD VRPETFTETS AGVADLITTC YGGRNRKCAE AFVKTGKPFN VLEAELLNGQ KLQGTETTRD VYEFLQSRGK IEEYPLFKTI YDISFNGLDP KLLTERL //