ID   PYRD_AGRAE              Reviewed;         328 AA.
AC   P28294;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 102.
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   Agrocybe aegerita (Black poplar mushroom) (Agaricus aegerita).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Bolbitiaceae; 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 = 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   -!- 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}.
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DR   EMBL; M90295; AAA32636.1; -; Genomic_DNA.
DR   PIR; JN0453; JN0453.
DR   AlphaFoldDB; P28294; -.
DR   SMR; P28294; -.
DR   UniPathway; UPA00070; UER00946.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004152; F:dihydroorotate dehydrogenase 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; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005720; Dihydroorotate_DH.
DR   InterPro; IPR012135; Dihydroorotate_DH_1_2.
DR   InterPro; IPR005719; Dihydroorotate_DH_2.
DR   InterPro; IPR001295; Dihydroorotate_DH_CS.
DR   Pfam; PF01180; DHO_dh; 1.
DR   PIRSF; PIRSF000164; DHO_oxidase; 1.
DR   TIGRFAMs; TIGR01036; pyrD_sub2; 1.
DR   PROSITE; PS00911; DHODEHASE_1; 1.
DR   PROSITE; PS00912; DHODEHASE_2; 1.
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