ID   PYRD_BORA1              Reviewed;         349 AA.
AC   Q2KW44;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=BAV2753;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.
CC       Type 2 subfamily.
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DR   EMBL; AM167904; CAJ50364.1; -; Genomic_DNA.
DR   RefSeq; YP_787251.1; -.
DR   GeneID; 6266676; -.
DR   GenomeReviews; AM167904_GR; BAV2753.
DR   KEGG; bav:BAV2753; -.
DR   NMPDR; fig|521.1.peg.356; -.
DR   HOGENOM; Q2KW44; -.
DR   OMA; Q2KW44; AALNRMG.
DR   GO; GO:0005886; C:plasma membrane; 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_00225; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012135; Dihydroorotate_DH_1_2.
DR   InterPro; IPR005719; Dihydroorotate_DH_2.
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; TIGR01036; pyrD_sub2; 1.
DR   PROSITE; PS00911; DHODEHASE_1; 1.
DR   PROSITE; PS00912; DHODEHASE_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Flavoprotein; FMN; Membrane;
KW   Oxidoreductase; Pyrimidine biosynthesis.
FT   CHAIN         1    349       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_1000024154.
FT   ACT_SITE    183    183       Nucleophile (By similarity).
SQ   SEQUENCE   349 AA;  37027 MW;  2B79F6391D1BAF15 CRC64;
     MSILFNAYPL ARPALFAMDA ETAHEVTLAS LQRAYDCGTT RRWLHDQPQL PTTLMGMTLR
     NPVGLAAGLD KNGAFIDALG NLGFGFVEVG TVTPRAQSGN PKPRMFRLPK ANALINRLGF
     NNQGLDAFLA NVTRSRFRSQ GGILGLNIGK NADTPIERAA DDYLIGLAGV YPHADYVTVN
     ISSPNTKNLR ALQGGDELSQ LLAALRDKRA ELAQQHARQV PLVVKIAPDL SQEQIDIIAD
     TLLSNGVDGV IATNTTLSRE AVQGMPHAAE TGGLSGAPVH ELSLAVIERL RQRVGSALAI
     IGVGGILSGQ QAREKIAAGA DAVQLYTGLI YRGPALVGEC VGTLKNTAR
//