ID   PYRD_SACMI              Reviewed;         314 AA.
AC   Q7Z893;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 83.
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 mikatae (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=114525;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC MYA-4448 / CBS 8839 / NBRC 1815 / NCYC 2888;
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; AY323901; AAQ01778.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7Z893; -.
DR   SMR; Q7Z893; -.
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_0000148504"
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;  34812 MW;  DE661206FC2CB11E CRC64;
     MTASLTTKFL NNTYENPFMN ASGVHCMTTE ELDELADSKA GAFITKSATT LEREGNPKPR
     YISVPLGSIN SMGLPNEGID YYLSYVLNRQ KKYPDAPAIF FSVAGMSIDE NLNLLKKIQD
     SEFNGITELN LSCPNVPGKP QVAYDFELTK ETLEKVFVFF KKPLGIKLPP YFDFAHFDII
     AKILNEFPLA YVNSINSIGN GLFIDVEKES VVVKPKNGFG GIGGEYVKPT ALANVRAFYT
     RLRPDIKVIG TGGIKSGKDA FEHLLCGASM LQIGTELQKE GVKIFERIEK ELKDIMEAKG
     YTSIDQFRGK LNSL