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Database: UniProt
Entry: Q7WGE4
LinkDB: Q7WGE4
Original site: Q7WGE4 
ID   PYRD_BORBR              Reviewed;         349 AA.
AC   Q7WGE4;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   14-MAY-2014, entry version 77.
DE   RecName: Full=Dihydroorotate dehydrogenase (quinone);
DE            EC=1.3.5.2;
DE   AltName: Full=DHOdehase;
DE            Short=DHOD;
DE            Short=DHODase;
DE   AltName: Full=Dihydroorotate oxidase;
GN   Name=pyrD; OrderedLocusNames=BB3975;
OS   Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS   (Alcaligenes bronchisepticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate
CC       with quinone as electron acceptor (By similarity).
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + a quinone = orotate + a
CC       quinol.
CC   -!- COFACTOR: Binds 1 FMN per subunit (By similarity).
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; orotate from (S)-dihydroorotate (quinone route): step
CC       1/1.
CC   -!- SUBUNIT: Monomer (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; BX640449; CAE34338.1; -; Genomic_DNA.
DR   RefSeq; NP_890509.1; NC_002927.3.
DR   ProteinModelPortal; Q7WGE4; -.
DR   SMR; Q7WGE4; 8-344.
DR   STRING; 257310.BB3975; -.
DR   EnsemblBacteria; CAE34338; CAE34338; BB3975.
DR   GeneID; 2662207; -.
DR   KEGG; bbr:BB3975; -.
DR   PATRIC; 21141365; VBIBorBro124907_4037.
DR   eggNOG; COG0167; -.
DR   HOGENOM; HOG000225103; -.
DR   KO; K00254; -.
DR   OMA; DARDEMQ; -.
DR   OrthoDB; EOG65BDN8; -.
DR   BioCyc; BBRO257310:BB3975-MONOMER; -.
DR   UniPathway; UPA00070; UER00946.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004158; F:dihydroorotate oxidase activity; IEA:InterPro.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00225; DHO_dh_type2; 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   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    349       Dihydroorotate dehydrogenase (quinone).
FT                                /FTId=PRO_0000148423.
FT   NP_BIND      67     71       FMN (By similarity).
FT   NP_BIND     326    327       FMN (By similarity).
FT   REGION      116    120       Substrate binding (By similarity).
FT   REGION      254    255       Substrate binding (By similarity).
FT   ACT_SITE    183    183       Nucleophile (By similarity).
FT   BINDING      71     71       Substrate (By similarity).
FT   BINDING      91     91       FMN; via amide nitrogen (By similarity).
FT   BINDING     147    147       FMN (By similarity).
FT   BINDING     180    180       FMN (By similarity).
FT   BINDING     180    180       Substrate (By similarity).
FT   BINDING     185    185       Substrate (By similarity).
FT   BINDING     225    225       FMN (By similarity).
FT   BINDING     253    253       FMN; via carbonyl oxygen (By similarity).
FT   BINDING     276    276       FMN; via amide nitrogen (By similarity).
FT   BINDING     305    305       FMN; via amide nitrogen (By similarity).
SQ   SEQUENCE   349 AA;  37017 MW;  BE6C5634D87A135A CRC64;
     MSILFHAYPL ARPALFAMDA ETAHEVTLAQ LQRAYDCGLT RKLLHAQPEA PATLMGLSLR
     NPVGLAAGLD KNGAHIDALG NLGFGFVEVG TVTPRAQPGN PKPRMFRLPR ANALINRLGF
     NNQGLDAFIA NVQRSQWRSQ GGILGLNIGK NADTPIERAA EDYLIGLAGV YPHADYVTVN
     ISSPNTKNLR ALQGGDELSA LLGQLQERRL ALADQHQRHV PLAVKIAPDL SDDQIDAIAE
     ILPRHGIDGV IATNTTLARD AVQGLPHAEE AGGVSGAPVH ELSLRVIERL RSRLGDAVAI
     IGVGGILSGR QASEKMAAGA QAVQLYTGLI YRGPALVGEC VRALAQGSR
//
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