ID   PYRD_BARHE              Reviewed;         362 AA.
AC   Q6G4F7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 43.
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=BH03870;
OS   Bartonella henselae (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=38323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897699; CAF27197.1; -; Genomic_DNA.
DR   RefSeq; YP_033228.1; -.
DR   GeneID; 2864782; -.
DR   GenomeReviews; BX897699_GR; BH03870.
DR   KEGG; bhe:BH03870; -.
DR   NMPDR; fig|283166.1.peg.356; -.
DR   HOGENOM; Q6G4F7; -.
DR   OMA; Q6G4F7; NASTELI.
DR   BioCyc; BHEN283166:BH03870-MON; -.
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    362       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_0000336454.
FT   ACT_SITE    171    171       Nucleophile (By similarity).
SQ   SEQUENCE   362 AA;  40555 MW;  52B31703E536D0B4 CRC64;
     MSFFRCIGRS ALFMLDPEHA HRLAIMGLKS GLNSYQKVVD NRLCVTIAGL KFENFIGLAA
     GFDKNAEVVN DVFHLGFGFT EIGTVTPRPQ VGNPKPRLFR LRKDEAIINR MGFNNDGRQI
     VYGRLHGYKR LGIVGINIGA NKDTVDKIDD YITSIAYFYD VADYFTVNIS SPNTPGLRDL
     QVRDSLHLLM NAISQARNEQ KKKHGFFVPI FLKIAPDLSE KELDDVAEEM KLSDFDGLIV
     SNTTLSRQGL RECTLRNEEG GLSGRPLFER STIVLAKMRQ KLGKKIAIIG VGGIRDAKTA
     LEKVKAGADL VQLYSGMVYE GPDLAITILK EILQFMQKDG VESIKAYRDQ RVEYWAKHML
     SS
//