ID PYRD_CYCAE Reviewed; 328 AA. AC P28294; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 04-NOV-2026, entry version 113. DE RecName: Full=Dihydroorotate dehydrogenase (quinone), mitochondrial; DE Short=DHOD; DE Short=DHODase; DE Short=DHOdehase; DE EC=1.3.5.2; DE AltName: Full=Dihydroorotate oxidase; DE Flags: Precursor; GN Name=URA1; OS Cyclocybe aegerita (Black poplar mushroom) (Agrocybe aegerita). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Agaricomycetidae; Agaricales; Agaricineae; Hemipholiotaceae; Cyclocybe. OX NCBI_TaxID=1973307; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=WT-2 / G30; RX PubMed=1452035; DOI=10.1016/0378-1119(92)90057-v; RA Noel T., Labarere J.; RT "Sequence of the URA1 gene encoding dihydroorotate dehydrogenase from the RT basidiomycete fungus Agrocybe aegerita."; RL Gene 122:233-234(1992). CC -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with CC quinone as electron acceptor. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-dihydroorotate + a quinone = orotate + a quinol; CC Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, CC ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; CC Note=Binds 1 FMN per subunit. {ECO:0000250}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC orotate from (S)-dihydroorotate (quinone route): step 1/1. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}; CC Single-pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 2 CC subfamily. {ECO:0000305}. 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; M90295; AAA32636.1; -; Genomic_DNA. DR PIR; JN0453; JN0453. DR SMR; P28294; -. DR UniPathway; UPA00070; UER00946. DR CDD; cd04738; DHOD_2_like; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR050074; DHO_dehydrogenase. DR InterPro; IPR012135; Dihydroorotate_DH_1_2. DR InterPro; IPR005719; Dihydroorotate_DH_2. DR InterPro; IPR005720; Dihydroorotate_DH_cat. DR InterPro; IPR001295; Dihydroorotate_DH_CS. 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 PIRSF; PIRSF000164; DHO_oxidase; 1. DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1. DR NCBIfam; NF003645; PRK05286.1-2; 1. DR NCBIfam; NF003652; PRK05286.2-5; 1. DR NCBIfam; TIGR01036; pyrD_sub2; 1. DR PROSITE; PS00911; DHODEHASE_1; 1. DR PROSITE; PS00912; DHODEHASE_2; 1. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. 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 AlphaFoldDB; P28294; -. PE 3: Inferred from homology; KW Flavoprotein; FMN; Membrane; Mitochondrion; Mitochondrion inner membrane; KW Oxidoreductase; Pyrimidine biosynthesis; Transit peptide; Transmembrane; KW Transmembrane helix. FT TRANSIT 1..? FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN ?..328 FT /note="Dihydroorotate dehydrogenase (quinone), FT mitochondrial" FT /id="PRO_0000148499" FT TRANSMEM 21..38 FT /note="Helical" FT /evidence="ECO:0000255" FT ACT_SITE 173 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT BINDING 61..65 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250" FT BINDING 65 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 85 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250" FT BINDING 110..114 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 139 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250" FT BINDING 170..175 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 170 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250" FT BINDING 215 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250" FT BINDING 243 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250" FT BINDING 244..245 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 266 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250" FT BINDING 295 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250" SQ SEQUENCE 328 AA; 35085 MW; 71FA3D2A4D57EF75 CRC64; MSGLFETLGR RALFAFDAEQ AHGLSIAGLK TGLVTGSAPN DLALSVKVAG LQFPNPLGMA AGYDKNAEVP DALLKLGFGF TEIGTITPRP QSGNPRPRIF RLVDDKAVIN RLGFNNEGHD AAFKRLSQRA GKSGIVGVNI GANKDAEDRI ADYVAGIRRF YQLARYFTVN ISSPNTPGLR NLQARDSLRE LLSRVLEARN EEGKMCTLKR PVFLKIAPDL ANEELDDIAA EATEQKLDGI IISNTTLSRA GLKSAGGRDE TGGLSGAPLF DRSTIVLARM RERVGPDMPL IGVGGVDSAE TALTKVKAGA RSRPALYGPD LSRPEPAY //