ID C4Q5J8_SCHMA Unreviewed; 351 AA. AC C4Q5J8; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 24-JAN-2024, entry version 93. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243}; DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243}; OS Schistosoma mansoni (Blood fluke). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda; OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma. OX NCBI_TaxID=6183 {ECO:0000313|Proteomes:UP000008854, ECO:0000313|WBParaSite:Smp_030500.1}; RN [1] {ECO:0000313|Proteomes:UP000008854} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Puerto Rican {ECO:0000313|Proteomes:UP000008854}; RX PubMed=22253936; DOI=10.1371/journal.pntd.0001455; RA Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A., RA De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C., RA Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J., RA Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A., RA Zerlotini A., Dunne D.W., Berriman M.; RT "A systematically improved high quality genome and transcriptome of the RT human blood fluke Schistosoma mansoni."; RL PLoS Negl. Trop. Dis. 6:E1455-E1455(2012). RN [2] {ECO:0000313|WBParaSite:Smp_030500.1} RP IDENTIFICATION. RC STRAIN=Puerto Rican {ECO:0000313|WBParaSite:Smp_030500.1}; RG WormBaseParasite; RL Submitted (DEC-2018) to UniProtKB. 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 RefSeq; XP_018644200.1; XM_018792589.1. DR AlphaFoldDB; C4Q5J8; -. DR STRING; 6183.C4Q5J8; -. DR EnsemblMetazoa; Smp_030500.1; Smp_030500.1; Smp_030500. DR GeneID; 8349719; -. DR KEGG; smm:Smp_030500.1; -. DR WBParaSite; Smp_030500.1; Smp_030500.1; Smp_030500. DR CTD; 8349719; -. DR eggNOG; KOG2711; Eukaryota. DR HOGENOM; CLU_033449_2_2_1; -. DR InParanoid; C4Q5J8; -. DR OMA; NRMFGNM; -. DR OrthoDB; 3675564at2759; -. DR PhylomeDB; C4Q5J8; -. DR Proteomes; UP000008854; 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:UP000008854}. FT DOMAIN 6..173 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 194..341 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF07479" FT ACT_SITE 205 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1" FT BINDING 10..15 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 41 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 97 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 120 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 154 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 271..272 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 271 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 300 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" SQ SEQUENCE 351 AA; 38861 MW; 89E97E9CF48A253B CRC64; MSLRRVSVIG SGNWGSTIAK IVGNNIKKFP EYVPEVRMWV FEELVNGRKL TEIINTSHEN VKYLPNVKLP ENVVADPDVK SVARDADVLI IVMPHQFLNR TLAEMKPVVK PTSYAISLMK GLALSDDHGI KLLTDCIRDV LSIPCAVLMG ANLATEVSQE NYCEATIGID NPKMGSELKK LFQTDYFRIV VIKDEVATEL CGALKNIVAV AAGVIEGLGY GDNTKAAVIR LGFMEMKSFI YQFFADRHPQ EGTFLESCGV ADLITTCYGG RNKQMGIALA TTNEPLAQLE KERLHGQSAQ GPLTAAEVYA MLERKGLLEK YPIFTAVHKL CTRQFDPKNF ICCLANHPEH R //