ID   PYRD_BURXL              Reviewed;         340 AA.
AC   Q13ZM3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   25-NOV-2008, entry version 23.
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=Bxeno_A1928; ORFNames=Bxe_A2507;
OS   Burkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(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; CP000270; ABE30466.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_558518.1; -.
DR   GeneID; 4004345; -.
DR   GenomeReviews; CP000270_GR; Bxeno_A1928.
DR   KEGG; bxe:Bxe_A2507; -.
DR   HOGENOM; Q13ZM3; -.
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    340       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_0000336461.
FT   ACT_SITE    178    178       Nucleophile (By similarity).
SQ   SEQUENCE   340 AA;  36285 MW;  2B2D9D2478FBADBF CRC64;
     MFSSLYPLVR AQLFRMDAED AHHLTLRILG AAGRTGLAGA LAPRVPDAPR TVMGLTFRNP
     VGLAAGLDKD GACIDGLAAL GFGFIEVGTV TPRAQPGNPR PRMFRLPQAN AVINRMGFNN
     AGVDQFVKNV QAARYRGILG LNIGKNADTP IERAAEDYLY CLDRVYPFAS YVTVNISSPN
     TKNLRQLQGA GELDALLAAL KDKQQRLADM HGKLVPLALK IAPDLDDEQI KSIADTLLRH
     RFEGVIATNT TLSRTAVAGM QYGDEAGGLS GKPVFDASNA VIRKLRAEVG ETVPIIGVGG
     IFSGEDARAK MAAGASLVQL YTGFIYRGPA LVAECVQALR
//