ID F5XWJ7_9BURK Unreviewed; 354 AA. AC F5XWJ7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 21-SEP-2011, entry version 2. DE RecName: Full=Dihydroorotate dehydrogenase (quinone); DE EC=1.3.5.2; DE AltName: Full=DHOdehase; DE AltName: Full=Dihydroorotate oxidase; GN Name=pyrD; ORFNames=Rta_18600; OS Ramlibacter tataouinensis TTB310. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Ramlibacter. OX NCBI_TaxID=365046; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=TTB310; RA Barakat M., Ortet P., De Luca G., Jourlin-Castelli C., Ansaldi M., RA Py B., Fichant G., Coutinho P., Voulhoux R., Bastien O., Roy S., RA Marechal E., Henrissat B., Quentin Y., Noirot P., Filloux A., RA Mejean V., DuBow M., Barras F., Heulin T.; RT "Genome of the cyst-dividing bacterium Ramlibacter tataouinensis."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000245; AEG92951.1; -; Genomic_DNA. DR RefSeq; YP_004618970.1; NC_015677.1. DR GeneID; 10832465; -. 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 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; Flavoprotein; FMN; Membrane; Oxidoreductase; KW Pyrimidine biosynthesis. FT NP_BIND 65 69 FMN (By similarity). FT NP_BIND 329 330 FMN (By similarity). FT REGION 114 118 Substrate binding (By similarity). FT REGION 257 258 Substrate binding (By similarity). FT ACT_SITE 186 186 Nucleophile (By similarity). FT BINDING 69 69 Substrate (By similarity). FT BINDING 89 89 FMN; via amide nitrogen (By similarity). FT BINDING 150 150 FMN (By similarity). FT BINDING 183 183 FMN (By similarity). FT BINDING 183 183 Substrate (By similarity). FT BINDING 188 188 Substrate (By similarity). FT BINDING 228 228 FMN (By similarity). FT BINDING 256 256 FMN; via carbonyl oxygen (By similarity). FT BINDING 279 279 FMN; via amide nitrogen (By similarity). FT BINDING 308 308 FMN; via amide nitrogen (By similarity). SQ SEQUENCE 354 AA; 38074 MW; 0381C85A4F92EF2A CRC64; MPLLPYPLAR PFLFHLDAER AHDLTLASLA RLQGTPLQWA WRSRRVDDPV ELAGLRFPNR VGLAAGLDKN ARCIDAFAGM GFGFVEVGTV TPLAQPGNAK PRMFRLPQAQ ALVNRLGFNN EGLEAFVANV QRSAVRRRSL HDGGIVLGLN IGKNAATPIE DATRDYLTGL EGVYPHADYV TVNISSPNTQ NLRALQSDEA LDALLAALAR RRAELEQRHG RRVPLFVKIA PDLDEAQVRV IAATLQRHGM DGVIATNTTL SRDAVQGLPH AQEAGGLSGA PVLEASNRVI RQLRAALGPR FPIVGVGGVM SGPDAVSKIE AGADLVQVYT GLIYRGPALA GEAAYALRAH GRRR //