ID   PYRD_SACBA              Reviewed;         314 AA.
AC   Q7Z894;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Dihydroorotate dehydrogenase (fumarate);
DE            Short=DHOD;
DE            Short=DHODase;
DE            Short=DHOdehase;
DE            EC=1.3.98.1;
DE   AltName: Full=Dihydroorotate oxidase;
GN   Name=URA1;
OS   Saccharomyces bayanus (Yeast) (Saccharomyces uvarum x Saccharomyces
OS   eubayanus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CBS 424 / BCRC 21964 / CLIB 250 / NBRC 0254 / NRRL Y-12645;
RX   PubMed=15947202; DOI=10.1128/ec.4.6.1102-1115.2005;
RA   Hall C.R., Brachat S., Dietrich F.S.;
RT   "Contribution of horizontal gene transfer to the evolution of Saccharomyces
RT   cerevisiae.";
RL   Eukaryot. Cell 4:1102-1115(2005).
CC   -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with
CC       fumarate as the electron acceptor. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-dihydroorotate + fumarate = orotate + succinate;
CC         Xref=Rhea:RHEA:30059, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:30839, ChEBI:CHEBI:30864; EC=1.3.98.1;
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY323900; AAQ01777.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7Z894; -.
DR   SMR; Q7Z894; -.
DR   UniPathway; UPA00070; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:1990663; F:dihydroorotate dehydrogenase (fumarate) 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; cd04741; DHOD_1A_like; 1.
DR   Gene3D; 2.30.26.10; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00224; DHO_dh_type1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR033886; DHOD_1A.
DR   InterPro; IPR023359; Dihydro_DH_chainA_dom2.
DR   InterPro; IPR005720; Dihydroorotate_DH.
DR   InterPro; IPR024920; Dihydroorotate_DH_1.
DR   InterPro; IPR012135; Dihydroorotate_DH_1_2.
DR   InterPro; IPR001295; Dihydroorotate_DH_CS.
DR   Pfam; PF01180; DHO_dh; 1.
DR   PIRSF; PIRSF000164; DHO_oxidase; 1.
DR   TIGRFAMs; TIGR01037; pyrD_sub1_fam; 1.
DR   PROSITE; PS00911; DHODEHASE_1; 1.
DR   PROSITE; PS00912; DHODEHASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Flavoprotein; FMN; Oxidoreductase; Pyrimidine biosynthesis.
FT   CHAIN           1..314
FT                   /note="Dihydroorotate dehydrogenase (fumarate)"
FT                   /id="PRO_0000148501"
FT   ACT_SITE        132
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        133
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         46..47
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         70..74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         196..197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         252..253
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         274..275
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   314 AA;  34702 MW;  DB479332CDEA49E7 CRC64;
     MTASLTTKFL DNTYENPFMN ASGVHCMTTP ELDELANSKA GAFITKSATT LEREGNPKPR
     YISVPLGSIN SMGLPNEGVD YYLSHVLNRQ KKYPDAPAIF FSVAGMSIDE NLGLLKKIQE
     SEFNGITELN LSCPNVPGKP QVAYDFDLTK ETLEKVFAFF NKPLGIKLPP YFDFAHFDIM
     AKILNEFPLA YVNSINSVGN GLFIDVEKES VVVKPKNGFG GIGGEYVKPT ALANVRAFYT
     RLRPEIKIIG TGGIKSGKDA FEHLLCGASM LQIGTELQKE GVQIFERIER ELKDIMEAKG
     YTSIDEFRGK LNSL