ID   PYRD_BRUAB              Reviewed;         364 AA.
AC   Q57F47;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   16-JUN-2009, entry version 38.
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=BruAb1_0337;
OS   Brucella abortus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941 / Biovar 1;
RX   PubMed=15805518; DOI=10.1128/JB.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L.,
RA   Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison
RT   to the highly similar genomes of Brucella melitensis and Brucella
RT   suis.";
RL   J. Bacteriol. 187:2715-2726(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: 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; AE017223; AAX73737.1; -; Genomic_DNA.
DR   RefSeq; YP_221098.1; -.
DR   GeneID; 3339285; -.
DR   GenomeReviews; AE017223_GR; BruAb1_0337.
DR   KEGG; bmb:BruAb1_0337; -.
DR   HOGENOM; Q57F47; -.
DR   OMA; Q57F47; AALNRMG.
DR   BioCyc; BABO262698:BRUAB1_0337-MON; -.
DR   BRENDA; 1.3.3.1; 575.
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    364       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_0000244528.
FT   ACT_SITE    173    173       Nucleophile (By similarity).
SQ   SEQUENCE   364 AA;  39257 MW;  909F4EAB00AF230E CRC64;
     MSGLFETLGR RALFTFDAEQ AHGLSITGLK TGIVTCRTPE DPALSVKVAG LKFPNPLGMA
     AGYDKNAEVP DALLKLGFGF AEVGTLTPRP QSGNPRPRIF RLVDDKAVIN RLGFNNEGHE
     AAFKRLSRRA GKSGIVGVNI GANKDAEDRI ADYVAGIRRF YLLARYFTVN ISSPNTPGLR
     NLQAREALHE LLSRVLEARD EEGNMCTLKR PVFLKIAPDL TDEELDDIAA EADAQKLDGI
     IVSNTTLSRS GLKNPENSNE TGGLSGAPLF ERSTVVLARM RERVGPDMPL IGVGGIDSAE
     TALAKIKAGA DLVQLYTGLI YRGPGLPGEI LRGLSTAIKH EGVSSIAELR DRDTKEWAAR
     KLIS
//