ID   PYRD_BART1              Reviewed;         360 AA.
AC   A9IQ81;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   16-JUN-2009, entry version 13.
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=BT_0576;
OS   Bartonella tribocorum (strain CIP 105476 / IBS 506).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=382640;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18037886; DOI=10.1038/ng.2007.38;
RA   Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G.,
RA   Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
RT   "Genomic analysis of Bartonella identifies type IV secretion systems
RT   as host adaptability factors.";
RL   Nat. Genet. 39:1469-1476(2007).
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; AM260525; CAK01023.1; -; Genomic_DNA.
DR   RefSeq; YP_001609018.1; -.
DR   GeneID; 5829298; -.
DR   GenomeReviews; AM260525_GR; BT_0576.
DR   OMA; A9IQ81; 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    360       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_0000336456.
FT   ACT_SITE    171    171       Nucleophile (By similarity).
SQ   SEQUENCE   360 AA;  39905 MW;  8A403EC0D4EF371F CRC64;
     MSFFRCIGRS ALFMLDPEHA HRLAIVGLKS GLNGCQKVVD KRLSVTIAGL KFKNFIGLAA
     GFDKNAEVVD EIFRLGFGFT EIGTVTPKPQ IGNPKPRLFR LKEDEAIINR MGFNNDGHQV
     VDDRLRICKK AGVVGVNIGA NKDTVDKIDD YTVGIAHFYD VADYFTVNIS SPNTPGLRDL
     QARDSLHLLL NAISKARKEQ EKKHGFSIPI FLKIAPDLSE KELDDIAEEI KLSDFDGLIV
     SNTTLSRQGL NNSHFSNEEG GLSGRPLFER STIVLAKMRQ KLGKEIAIIG VGGVKDAQTA
     LEKVKAGADL IQLYSGMVYE GPNLVITILK EILQMMQQDG VDNIKDYRDH NLEHWAKFPL
//