ID G4VFD7_SCHMA Unreviewed; 379 AA. AC G4VFD7; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAR-2024, entry version 74. DE RecName: Full=Dihydroorotate dehydrogenase (quinone), mitochondrial {ECO:0000256|ARBA:ARBA00017599}; DE EC=1.3.5.2 {ECO:0000256|ARBA:ARBA00012791}; 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_078730.1}; 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_078730.1} RP IDENTIFICATION. RC STRAIN=Puerto Rican {ECO:0000313|WBParaSite:Smp_078730.1}; RG WormBaseParasite; RL Submitted (DEC-2018) to UniProtKB. RN [3] {ECO:0007829|PDB:6UY4} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH FMN. RX PubMed=32428996; DOI=10.1111/febs.15367; RA de Mori R.M., Aleixo M.A.A., Zapata L.C.C., Calil F.A., Emery F.S., RA Nonato M.C.; RT "Structural basis for the function and inhibition of dihydroorotate RT dehydrogenase from Schistosomamansoni."; RL FEBS J. 288:930-944(2021). CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; CC Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, CC ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; CC Evidence={ECO:0000256|ARBA:ARBA00001532}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|ARBA:ARBA00001917}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC orotate from (S)-dihydroorotate (quinone route): step 1/1. CC {ECO:0000256|ARBA:ARBA00005161}. CC -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 2 CC subfamily. {ECO:0000256|ARBA:ARBA00005359}. 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_018651255.1; XM_018799469.1. DR PDB; 6UY4; X-ray; 2.80 A; A=1-379. DR AlphaFoldDB; G4VFD7; -. DR SMR; G4VFD7; -. DR STRING; 6183.G4VFD7; -. DR BindingDB; G4VFD7; -. DR ChEMBL; CHEMBL4523950; -. DR EnsemblMetazoa; Smp_078730.1; Smp_078730.1; Smp_078730. DR GeneID; 8355274; -. DR KEGG; smm:Smp_078730; -. DR WBParaSite; Smp_078730.1; Smp_078730.1; Smp_078730. DR CTD; 8355274; -. DR eggNOG; KOG1436; Eukaryota. DR HOGENOM; CLU_013640_0_0_1; -. DR InParanoid; G4VFD7; -. DR OMA; ERIKMGA; -. DR OrthoDB; 313431at2759; -. DR PhylomeDB; G4VFD7; -. DR UniPathway; UPA00070; UER00946. DR Proteomes; UP000008854; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0106430; F:dihydroorotate dehydrogenase (quinone) activity; IEA:UniProtKB-EC. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd04738; DHOD_2_like; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005719; Dihydroorotate_DH_2. DR InterPro; IPR005720; Dihydroorotate_DH_cat. DR InterPro; IPR001295; Dihydroorotate_DH_CS. DR NCBIfam; TIGR01036; pyrD_sub2; 1. DR PANTHER; PTHR48109:SF4; DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL; 1. DR PANTHER; PTHR48109; DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL-RELATED; 1. DR Pfam; PF01180; DHO_dh; 1. DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1. DR PROSITE; PS00911; DHODEHASE_1; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:6UY4}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0007829|PDB:6UY4}; KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0007829|PDB:6UY4}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Nucleotide-binding {ECO:0007829|PDB:6UY4}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000008854}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..22 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 23..379 FT /note="Dihydroorotate dehydrogenase (quinone), FT mitochondrial" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5030171989" FT DOMAIN 73..374 FT /note="Dihydroorotate dehydrogenase catalytic" FT /evidence="ECO:0000259|Pfam:PF01180" FT BINDING 90 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:6UY4" FT BINDING 94 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:6UY4" FT BINDING 114 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:6UY4" FT BINDING 200 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:6UY4" FT BINDING 241 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:6UY4" FT BINDING 271 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:6UY4" FT BINDING 304 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:6UY4" FT BINDING 333 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:6UY4" FT BINDING 355 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0007829|PDB:6UY4" SQ SEQUENCE 379 AA; 41289 MW; ECFD1BFB9BD01E4D CRC64; MSRIRTSLEV LSLGFGLFTA EALYSGNEHF YKDWFLPTAR LLVRDGETAH NLSVYLASYG FIPHKQRNSF PQLKCKVFGL EFDHPIGLAA GFDKDGKAFM GLLNAGFSHI EVGTVTPNPQ LGNARPRIFR WTEKEAVVNR CGFNSDGHDA VYERLKDRPW EGRGVIGVNL GCNKTSADPT ADYVAGVRKF GEVADYLVIN VSSPNTPGLR SLQTKEKLRD LLSKVLAARN QLSKKTPILL KISPDENDQN LKDIVEVALD SKTRIDGMII SNTTLTTYEE AVACGAAPIP GNNKQNVVYG GLSGRPLFEK STDCLRKVSA LTKGAIPLIG VGGISCGEDA LSKLNAGASL VQLYTSFVYQ GPPVAHKVAR EINKLKMTS //