ID   PYRD_BAUCH              Reviewed;         336 AA.
AC   Q1LT62;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=BCI_0409;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(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; CP000238; ABF14134.1; -; Genomic_DNA.
DR   RefSeq; YP_588852.1; -.
DR   SMR; Q1LT62; 1-336.
DR   GeneID; 4056320; -.
DR   GenomeReviews; CP000238_GR; BCI_0409.
DR   KEGG; bci:BCI_0409; -.
DR   HOGENOM; Q1LT62; -.
DR   OMA; Q1LT62; NAEQQGG.
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    336       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_1000024153.
FT   ACT_SITE    175    175       Nucleophile (By similarity).
SQ   SEQUENCE   336 AA;  36873 MW;  B00B0E763B82D580 CRC64;
     MLYPLIRQFL FQLDPEKAHE LTIQQLKRIA GTPLEYLVRQ SVPTKAVTCM GIAFKNPLGL
     AAGLDKNGEC IDALGAMGFG FIEVGTVTPH AQIGNEKPRL FRLTKAYGLI NRMGFNNKGV
     DNLVNNIQKS HFGGVLGINI GKNKDTPIEQ GKDDYLICME KVYPYANYIA VNISSPNTPQ
     LTTLQSGEIL DDLLRAIKDK QAKLQEYHHK YVPIAVKITP DMTESELIQM ADLLVQHKID
     GIIATNTTTS RELVHGLDHS SQSGGLSGRP LQLMSTEVIR ILSSKLQGKL PIIGVGGIDS
     LISAREKMAA GATLIQIYSS FIFHGPRLIK DIISDL
//