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 01-MAY-2013, entry version 73.
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; K00226; -.
DR OMA; ALNRMGF; -.
DR ProtClustDB; PRK05286; -.
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
//
