ID   PYRD_BURCH              Reviewed;         345 AA.
AC   A0K729;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   25-NOV-2008, entry version 20.
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=Bcen2424_1554;
OS   Burkholderia cenocepacia (strain HI2424).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=331272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F.,
RA   Konstantinidis K., Tiedje J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cenocepacia
RT   HI2424.";
RL   Submitted (AUG-2006) 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; CP000458; ABK08306.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_835199.1; -.
DR   GeneID; 4448955; -.
DR   GenomeReviews; CP000458_GR; Bcen2424_1554.
DR   KEGG; bch:Bcen2424_1554; -.
DR   HOGENOM; A0K729; -.
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   InterPro; IPR001295; Dihydroorotate_DHase_core.
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    345       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_0000336458.
FT   ACT_SITE    178    178       Nucleophile (By similarity).
SQ   SEQUENCE   345 AA;  36756 MW;  48BBC0EDFFFC0917 CRC64;
     MFSSLYPLAR ASLFKMDAED AHHLTLRALG AAGRTGLACA LSARVPDAPR TVMGLTFRNP
     VGLAAGLDKD GAAIDGLAAL GFGFIEVGTV TPRPQPGNPR PRMFRLPQAE ALINRMGFNN
     HGVDQFVKNV QAARYRGILG LNIGKNADTP IERAAEDYLY CLERVYPFAS YVTINISSPN
     TKNLRQLQGA GELDALLAAL KDKQQRLADL HGKLVPLALK IAPDLDDEQV KEIGDTLLRH
     KIEAVIATNT TLSRAAVQGL PHADEAGGLS GRPVFDASNE VIRKLHAEVG NDVPIIGVGG
     IFSGEDAHAK LAAGAALVQL YTGFIYRGPA LVSECVKAIA RERSA
//