ID   PYRDA_STRA3             Reviewed;         310 AA.
AC   Q8E6L0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Putative dihydroorotate dehydrogenase A (fumarate);
DE            Short=DHOD A;
DE            Short=DHODase A;
DE            Short=DHOdehase A;
DE            EC=1.3.98.1;
GN   Name=pyrD; OrderedLocusNames=gbs0553;
OS   Streptococcus agalactiae serotype III (strain NEM316).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=211110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEM316;
RX   PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA   Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA   Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT   "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT   neonatal disease.";
RL   Mol. Microbiol. 45:1499-1513(2002).
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; AL766846; CAD46197.1; -; Genomic_DNA.
DR   RefSeq; WP_000254063.1; NC_004368.1.
DR   AlphaFoldDB; Q8E6L0; -.
DR   SMR; Q8E6L0; -.
DR   STRING; 211110.gbs0553; -.
DR   EnsemblBacteria; CAD46197; CAD46197; CAD46197.
DR   KEGG; san:gbs0553; -.
DR   eggNOG; COG0167; Bacteria.
DR   HOGENOM; CLU_042042_3_0_9; -.
DR   OMA; CPISFIT; -.
DR   UniPathway; UPA00070; -.
DR   Proteomes; UP000000823; Chromosome.
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; 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; 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; PS00912; DHODEHASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Flavoprotein; FMN; Oxidoreductase; Pyrimidine biosynthesis.
FT   CHAIN           1..310
FT                   /note="Putative dihydroorotate dehydrogenase A (fumarate)"
FT                   /id="PRO_1000100228"
FT   ACT_SITE        131
FT                   /note="Nucleophile"
FT   BINDING         45..46
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         69..73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         193
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         194..195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         248..249
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         270..271
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   310 AA;  34257 MW;  7BEBDD482D828ED9 CRC64;
     MVSLKTEIAG FSFDNCLMNA AGIYCMTKEE LLAIENSEAG SFVTKTGTLE AREGNPQPRY
     ADTDWGSINS MGLPNKGIDY YLDFVTELQD QDNSKNHVLS LVGLSPEETH IILKKVENSS
     YNGLIELNLS CPNVPGKPQI AYDFEMTDLI LSEIFSYYQK PLGIKLPPYF DIVHFDQAAT
     IFNKYPLAFI NCVNSIGNGL VIDDETVVIK PKNGFGGIGG DFIKPTALAN VHAFYKRLNP
     SIKIIGTGGV KNGRDAFEHI LCGASMVQIG TALQKEGPEI FQRVSRELKE IMADKGYQSL
     EDFRGQLNYL