ID   PYRDA_LIMRD             Reviewed;         308 AA.
AC   A5VHS3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=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=Lreu_0125;
OS   Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=557436;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20016;
RX   PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA   Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA   Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA   Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA   Kyrpides N.C., Walter J.;
RT   "The evolution of host specialization in the vertebrate gut symbiont
RT   Lactobacillus reuteri.";
RL   PLoS Genet. 7:E1001314-E1001314(2011).
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; CP000705; ABQ82397.1; -; Genomic_DNA.
DR   RefSeq; WP_003669699.1; NZ_AZDD01000012.1.
DR   AlphaFoldDB; A5VHS3; -.
DR   SMR; A5VHS3; -.
DR   STRING; 557436.Lreu_0125; -.
DR   PRIDE; A5VHS3; -.
DR   EnsemblBacteria; ABQ82397; ABQ82397; Lreu_0125.
DR   GeneID; 66470206; -.
DR   KEGG; lre:Lreu_0125; -.
DR   PATRIC; fig|557436.17.peg.300; -.
DR   eggNOG; COG0167; Bacteria.
DR   HOGENOM; CLU_042042_0_0_9; -.
DR   OMA; SCPHAKG; -.
DR   UniPathway; UPA00070; -.
DR   Proteomes; UP000001991; 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; cd04740; DHOD_1B_like; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00224; DHO_dh_type1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR033888; DHOD_1B.
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;
KW   Reference proteome.
FT   CHAIN           1..308
FT                   /note="Dihydroorotate dehydrogenase A (fumarate)"
FT                   /id="PRO_0000336448"
FT   ACT_SITE        135
FT                   /note="Nucleophile"
FT   BINDING         24
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         48..49
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         72..76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         198..199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         249..250
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   308 AA;  32737 MW;  31F7EA849B3CA062 CRC64;
     MQETQRLAVE LPGLSLKNPI IAASGTCGYG QEAAKKYNLN HLGSLVLKST TLYPRQGNPR
     PRVCETSAGW LNANGLQNVG ITAATNEKIP WLRKNYPQLP IIASAAGFSE DEYVKVVSEF
     ANTAGVKAIE LNVSCPNVKH GGMAMGTDPE VLQRLVKQVV KAALGIPIYV KLTPNVTNIV
     PLAQAAEQGG ANGLTMINTL TGLSIDLKTR RPALANVTGG LSGPAIKPLA LRMIHQVRQV
     SSLPIIGVGG IESAEDVLEF MMAGANAVQI GAASFHDPLA CPKIAADLPI VMDRYGIKKL
     TDLWEVRF