ID G2RD01_THETT Unreviewed; 404 AA. AC G2RD01; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 03-MAY-2023, entry version 57. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243}; DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243}; GN ORFNames=THITE_2122377 {ECO:0000313|EMBL:AEO70694.1}; OS Thermothielavioides terrestris (strain ATCC 38088 / NRRL 8126) (Thielavia OS terrestris). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides; OC Thermothielavioides terrestris. OX NCBI_TaxID=578455 {ECO:0000313|EMBL:AEO70694.1, ECO:0000313|Proteomes:UP000008181}; RN [1] {ECO:0000313|EMBL:AEO70694.1, ECO:0000313|Proteomes:UP000008181} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38088 / NRRL 8126 {ECO:0000313|Proteomes:UP000008181}; RX PubMed=21964414; DOI=10.1038/nbt.1976; RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I., RA Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M., RA Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P., RA Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P., RA Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J., RA Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S., RA Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W., RA Tsang A.; RT "Comparative genomic analysis of the thermophilic biomass-degrading fungi RT Myceliophthora thermophila and Thielavia terrestris."; RL Nat. Biotechnol. 29:922-927(2011). 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; CP003013; AEO70694.1; -; Genomic_DNA. DR RefSeq; XP_003657030.1; XM_003656982.1. DR AlphaFoldDB; G2RD01; -. DR STRING; 578455.G2RD01; -. DR GeneID; 11519295; -. DR KEGG; ttt:THITE_2122377; -. DR eggNOG; KOG2711; Eukaryota. DR HOGENOM; CLU_033449_2_3_1; -. DR OrthoDB; 3675564at2759; -. DR Proteomes; UP000008181; Chromosome 5. 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. 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:UP000008181}. FT DOMAIN 13..194 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 253..398 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF07479" FT ACT_SITE 264 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1" FT BINDING 18..23 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 121 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 144 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 177 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 329..330 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 329 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 356 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 358 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" SQ SEQUENCE 404 AA; 44768 MW; 822DC46E551D39E2 CRC64; MAGPSDSPRR KHKVTVVGSG NWGTTVAKLV AENTREHPDV FEEEVQMWVY EENVVVPSDS PHYDPAVGDA PQKLTSVINK YHENVKYLPK IKLPSNVIAN PSLVDAVKDS SILIFNLPHE FIGNVCKQIK GHILPFARGI SCIKGVTVTD DKVELICDYI GEILGIYCGA LSGANIANEI ANELWCETTI AYNTPPCDQR LTNGVNGAHG AGVPVRFPKT KLTPLPEDYP PLDHGEIHKL FDRPYFTVSM VSDVVGVSLA GALKNIVALA CGFIEGHGWN ATAKTAVMRR GMLETIRFAQ EFFPESIQEM TFWESAGWSD MIVSCTSARN WRYSKMAVER GVSLQEIERT ELNGQKLQGI STTKEVMSFL RARGREDHYP LFKAVEGIVD GTFEVKDIPM LFRK //