ID C7Z6K6_FUSV7 Unreviewed; 417 AA. AC C7Z6K6; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 24-JAN-2024, entry version 78. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243}; DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243}; GN ORFNames=NECHADRAFT_76134 {ECO:0000313|EMBL:EEU40148.1}; OS Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL OS 45880 / 77-13-4) (Fusarium solani subsp. pisi). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium; OC Fusarium solani species complex; Fusarium vanettenii. OX NCBI_TaxID=660122 {ECO:0000313|EMBL:EEU40148.1, ECO:0000313|Proteomes:UP000005206}; RN [1] {ECO:0000313|EMBL:EEU40148.1, ECO:0000313|Proteomes:UP000005206} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4 RC {ECO:0000313|Proteomes:UP000005206}; RX PubMed=19714214; DOI=10.1371/journal.pgen.1000618; RA Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C., RA Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C., RA Freitag M., Ma L.J., Danchin E.G., Henrissat B., Coutinho P.M., RA Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M., RA Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L., RA Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E., RA Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E., RA Vanetten H.D.; RT "The genome of Nectria haematococca: contribution of supernumerary RT chromosomes to gene expansion."; RL PLoS Genet. 5:E1000618-E1000618(2009). 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 --------------------------------------------------------------------------- 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; GG698910; EEU40148.1; -; Genomic_DNA. DR RefSeq; XP_003045861.1; XM_003045815.1. DR AlphaFoldDB; C7Z6K6; -. DR STRING; 660122.C7Z6K6; -. DR EnsemblFungi; NechaT76134; NechaP76134; NechaG76134. DR GeneID; 9668695; -. DR KEGG; nhe:NECHADRAFT_76134; -. DR VEuPathDB; FungiDB:NECHADRAFT_76134; -. DR eggNOG; KOG2711; Eukaryota. DR HOGENOM; CLU_033449_2_3_1; -. DR InParanoid; C7Z6K6; -. DR OMA; NRMFGNM; -. DR OrthoDB; 3675564at2759; -. DR Proteomes; UP000005206; 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: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; 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 PIRSF; PIRSF000114; Glycerol-3-P_dh; 2. 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:UP000005206}. FT DOMAIN 12..193 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 264..410 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF07479" FT REGION 191..216 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 275 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1" FT BINDING 17..22 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 120 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 143 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 176 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 341..342 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 341 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 368 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 370 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" SQ SEQUENCE 417 AA; 45442 MW; 6D7C65BF6C50E804 CRC64; MTNLGGHSKK HKVTIVGSGN WGSTIAKIVA ENTRANKDVF EEEVQMWVYE EDVTISKDSK YYDETIGDKP QKLTEVINKH HENVKYLPGI ALPPNIVANP DIRAAVKDST ILVFNLPHQF IANVCKQING HILPFARGIS CIKGVNVTDD GVSLFSEWIG DGLGIYCGAL SGANLAREIA EEKWSETTIA YDPPALDNSR APSPRDGSPN PTIGELPEIR HKDVRGRTSK TKLTAMPADY PPLDQDCFRT LFHRHYFHVQ MVSDVAGVSL SGALKNVVAL AAGFVDGRGW GDNAKAAIMR VGLMEMVKFG KEFFGETVHT ATFTESSAGV ADLITSCSGG RNFRCAKKSV EKGISVQEVE QQELNGQKIQ GTTTAEEVNS FLKARGLESE YPLFTAVHAI LNGQAKVDDI PNLVQDS //