ID   PYRD_BACFN              Reviewed;         303 AA.
AC   Q5LCI2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Dihydroorotate dehydrogenase;
DE            EC=1.3.3.1;
DE   AltName: Full=Dihydroorotate oxidase;
DE   AltName: Full=DHOdehase;
DE            Short=DHODase;
DE            Short=DHOD;
GN   Name=pyrD; OrderedLocusNames=BF2483;
OS   Bacteroides fragilis (strain ATCC 25285 / NCTC 9343).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G.,
RA   Abratt V., Lennard N., Poxton I., Duerden B., Harris B., Quail M.A.,
RA   Barron A., Clark L., Corton C., Doggett J., Holden M.T.G., Larke N.,
RA   Line A., Lord A., Norbertczak H., Ormond D., Price C.,
RA   Rabbinowitsch E., Woodward J., Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable
RT   gene expression.";
RL   Science 307:1463-1465(2005).
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + O(2) = orotate +
CC       H(2)O(2).
CC   -!- COFACTOR: Binds 1 FMN per subunit (By similarity).
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from HCO(3)(-): step 4/6.
CC   -!- SUBUNIT: Heterotetramer of 2 pyrK and 2 pyrD subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.
CC       Type 1 subfamily.
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DR   EMBL; CR626927; CAH08183.1; -; Genomic_DNA.
DR   RefSeq; YP_212107.1; -.
DR   GeneID; 3289320; -.
DR   GenomeReviews; CR626927_GR; BF2483.
DR   KEGG; bfs:BF2483; -.
DR   HOGENOM; Q5LCI2; -.
DR   OMA; Q5LCI2; NSIGLQN.
DR   BioCyc; BFRA272559:BF2483-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004158; F:dihydroorotate oxidase activity; IEA:HAMAP.
DR   GO; GO:0006207; P:'de novo' pyrimidine base biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006222; P:UMP biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00224; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012135; Dihydroorotate_DH_1_2.
DR   InterPro; IPR005720; Dihydroorotate_DH_1_core.
DR   InterPro; IPR001295; Dihydroorotate_DH_CS.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
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   Complete proteome; Cytoplasm; Flavoprotein; FMN; Oxidoreductase;
KW   Pyrimidine biosynthesis.
FT   CHAIN         1    303       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_1000024127.
FT   ACT_SITE    130    130       Nucleophile (By similarity).
SQ   SEQUENCE   303 AA;  32332 MW;  92360403BBB5F984 CRC64;
     MADLSVNIGK LQMKNPVMTA SGTFGYGEEF ADFIDITRIG GIIVKGTTLH KREGNPYPRM
     AETPSGMLNA VGLQNKGVEY FSNHIYPRIK DIQTHMIVNV SGSAIEDYVK TAEIINELDK
     IPAIELNISC PNVKQGGMAF GVTTKGVSEV VQAVRSAYKK TLIVKLSPNV TDIAEMARAA
     EANGADSVSL INTLLGMAID AERKRPILST VTGGMSGAAV KPIALRMVWQ VAKAVNIPVI
     GLGGIMNWKD AVEFMLAGAS AIQIGTANFI DPAITIKVID GINDYLERHG CKSVSEIIGA
     LEV
//