ID A2EDY9_TRIV3 Unreviewed; 348 AA. AC A2EDY9; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 100. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243}; DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243}; GN ORFNames=TVAG_230610 {ECO:0000313|EMBL:EAY09101.1}; OS Trichomonas vaginalis (strain ATCC PRA-98 / G3). OC Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae; OC Trichomonas. OX NCBI_TaxID=412133 {ECO:0000313|EMBL:EAY09101.1, ECO:0000313|Proteomes:UP000001542}; RN [1] {ECO:0000313|EMBL:EAY09101.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=G3 {ECO:0000313|EMBL:EAY09101.1}; RA Amadeo P., Zhao Q., Wortman J., Fraser-Liggett C., Carlton J.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAY09101.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G3 {ECO:0000313|EMBL:EAY09101.1}; RX PubMed=17218520; DOI=10.1126/science.1132894; RA Carlton J.M., Hirt R.P., Silva J.C., Delcher A.L., Schatz M., Zhao Q., RA Wortman J.R., Bidwell S.L., Alsmark U.C.M., Besteiro S., RA Sicheritz-Ponten T., Noel C.J., Dacks J.B., Foster P.G., Simillion C., RA Van de Peer Y., Miranda-Saavedra D., Barton G.J., Westrop G.D., Mueller S., RA Dessi D., Fiori P.L., Ren Q., Paulsen I., Zhang H., Bastida-Corcuera F.D., RA Simoes-Barbosa A., Brown M.T., Hayes R.D., Mukherjee M., Okumura C.Y., RA Schneider R., Smith A.J., Vanacova S., Villalvazo M., Haas B.J., Pertea M., RA Feldblyum T.V., Utterback T.R., Shu C.L., Osoegawa K., de Jong P.J., RA Hrdy I., Horvathova L., Zubacova Z., Dolezal P., Malik S.B., RA Logsdon J.M. Jr., Henze K., Gupta A., Wang C.C., Dunne R.L., Upcroft J.A., RA Upcroft P., White O., Salzberg S.L., Tang P., Chiu C.-H., Lee Y.-S., RA Embley T.M., Coombs G.H., Mottram J.C., Tachezy J., Fraser-Liggett C.M., RA Johnson P.J.; RT "Draft genome sequence of the sexually transmitted pathogen Trichomonas RT vaginalis."; RL Science 315:207-212(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 --------------------------------------------------------------------------- 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; DS113364; EAY09101.1; -; Genomic_DNA. DR RefSeq; XP_001321324.1; XM_001321289.1. DR AlphaFoldDB; A2EDY9; -. DR STRING; 5722.A2EDY9; -. DR GeneID; 4767017; -. DR KEGG; tva:TVAG_2v0890200; -. DR VEuPathDB; TrichDB:TVAG_230610; -. DR VEuPathDB; TrichDB:TVAGG3_0890200; -. DR eggNOG; KOG2711; Eukaryota. DR InParanoid; A2EDY9; -. DR OMA; CVNETVG; -. DR Proteomes; UP000001542; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. 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 GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central. DR GO; GO:0006116; P:NADH oxidation; IBA:GO_Central. 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:UP000001542}. FT DOMAIN 5..168 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 191..338 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF07479" FT ACT_SITE 202 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1" FT BINDING 9..14 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 95 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 118 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 151 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 268..269 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 268 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 295 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 297 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" SQ SEQUENCE 348 AA; 38276 MW; D83554292105D2B7 CRC64; MPYKLSIIGS GNFGSCIARH CATNIKNVPE MDPHIKMWVL EEIVNGESLI HTINTTHENV KYLPGYNLGE NVEASGDVVE CCDADFFIFV VPHQFLPATL EKMKGHVKNT ATGCLLTKGI NFKDGKIQLL TDTVEEIIGI KCGSLMGANI ANEIARGDFC ESTLAFPDIP ERETWKQLFE SPKFKISCTN DIVTQQLSGT MKNIVALGGG IVDGLNMGQS TKAAILREGF VEIFDFAKMM FPERGVDILT MIESCGFGDI VASSYGGRNR KCAEYFVKSG KSFKECEAEL LNGQKLQGTL AAAEVYKILV ERKATEKFPL LTTIQLISER KVEPAEIINY RNHAAVTA //