ID   PYRD_BRUC2              Reviewed;         364 AA.
AC   A9M7Z9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-NOV-2008, entry version 10.
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=BCAN_A0319;
OS   Brucella canis (strain ATCC 23365 / NCTC 10854).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=483179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J.,
RA   Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S.,
RA   Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K.,
RA   Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W.,
RA   Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C.,
RA   Munk C., Brettin T.S.;
RT   "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000872; ABX61409.1; -; Genomic_DNA.
DR   RefSeq; YP_001592180.1; -.
DR   GeneID; 5785372; -.
DR   GenomeReviews; CP000872_GR; BCAN_A0319.
DR   KEGG; bcs:BCAN_A0319; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:HAMAP.
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; DHO_DHase_1_2.
DR   InterPro; IPR005719; DHO_DHase_2.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 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    364       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_1000078154.
FT   ACT_SITE    173    173       Nucleophile (By similarity).
SQ   SEQUENCE   364 AA;  39272 MW;  87BA9B721649C6D7 CRC64;
     MSGLFETLGR RALFTFDAEQ AHGLSITGLK TGIVTCRTPE DPALSVKVAG LKFPNPLGMA
     AGYDKNAEVP DALLKLGFGF AEVGTLTPRP QSGNPRPRIF RLVDDKAVIN RLGFNNEGHE
     AAFKRLSRRA GKSGIVGVNI GANKDAEDRI ADYVAGIRRF YQLARYFTVN ISSPNTPGLR
     NLQAREALHE LLSRVLEARD EEGNMCTLKR PVFLKIAPDL TDEELDDIAA EADAQKLDGI
     IVSNTTLSRS GLKNPENSNE TGGLSGAPLF ERSTVVLARM RERVGPDMPL IGVGGIDSAE
     TALAKIKAGA DLVQLYTGLI YRGPGLPGEI LRGLSTAIKH EGVSSIAELR DRDTKEWAAR
     KLIS
//