ID F5XWJ7_RAMTT Unreviewed; 354 AA. AC F5XWJ7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 25-MAY-2022, entry version 58. DE RecName: Full=Dihydroorotate dehydrogenase (quinone) {ECO:0000256|HAMAP-Rule:MF_00225}; DE EC=1.3.5.2 {ECO:0000256|HAMAP-Rule:MF_00225}; DE AltName: Full=DHOdehase {ECO:0000256|HAMAP-Rule:MF_00225}; DE Short=DHOD {ECO:0000256|HAMAP-Rule:MF_00225}; DE Short=DHODase {ECO:0000256|HAMAP-Rule:MF_00225}; DE AltName: Full=Dihydroorotate oxidase {ECO:0000256|HAMAP-Rule:MF_00225}; GN Name=pyrD {ECO:0000256|HAMAP-Rule:MF_00225, GN ECO:0000313|EMBL:AEG92951.1}; GN OrderedLocusNames=Rta_18600 {ECO:0000313|EMBL:AEG92951.1}; OS Ramlibacter tataouinensis (strain ATCC BAA-407 / DSM 14655 / LMG 21543 / OS TTB310). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Ramlibacter. OX NCBI_TaxID=365046 {ECO:0000313|EMBL:AEG92951.1, ECO:0000313|Proteomes:UP000008385}; RN [1] {ECO:0000313|Proteomes:UP000008385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310 RC {ECO:0000313|Proteomes:UP000008385}; RA Barakat M., Ortet P., De Luca G., Jourlin-Castelli C., Ansaldi M., Py B., RA Fichant G., Coutinho P., Voulhoux R., Bastien O., Roy S., Marechal E., RA Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V., DuBow M., RA Barras F., Heulin T.; RT "Genome of the cyst-dividing bacterium Ramlibacter tataouinensis."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AEG92951.1, ECO:0000313|Proteomes:UP000008385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310 RC {ECO:0000313|Proteomes:UP000008385}; RX PubMed=21912644; DOI=10.1371/journal.pone.0023784; RA De Luca G., Barakat M., Ortet P., Fochesato S., Jourlin-Castelli C., RA Ansaldi M., Py B., Fichant G., Coutinho P.M., Voulhoux R., Bastien O., RA Marechal E., Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V., RA Dubow M.S., Barras F., Barbe V., Weissenbach J., Mihalcescu I., RA Vermeglio A., Achouak W., Heulin T.; RT "The Cyst-Dividing Bacterium Ramlibacter tataouinensis TTB310 Genome RT Reveals a Well-Stocked Toolbox for Adaptation to a Desert Environment."; RL PLoS ONE 6:E23784-E23784(2011). CC -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with CC quinone as electron acceptor. {ECO:0000256|ARBA:ARBA00003125, CC ECO:0000256|HAMAP-Rule:MF_00225}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; CC Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, CC ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; CC Evidence={ECO:0000256|ARBA:ARBA00001532, ECO:0000256|HAMAP- CC Rule:MF_00225}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00225}; CC Note=Binds 1 FMN per subunit. {ECO:0000256|HAMAP-Rule:MF_00225}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC orotate from (S)-dihydroorotate (quinone route): step 1/1. CC {ECO:0000256|ARBA:ARBA00005161, ECO:0000256|HAMAP-Rule:MF_00225}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00225}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202, CC ECO:0000256|HAMAP-Rule:MF_00225}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004202, ECO:0000256|HAMAP-Rule:MF_00225}. CC -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 2 CC subfamily. {ECO:0000256|ARBA:ARBA00005359, ECO:0000256|HAMAP- CC Rule:MF_00225}. 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; WP_013901183.1; NC_015677.1. DR STRING; 365046.Rta_18600; -. DR EnsemblBacteria; AEG92951; AEG92951; Rta_18600. DR KEGG; rta:Rta_18600; -. DR PATRIC; fig|365046.3.peg.1896; -. DR eggNOG; COG0167; Bacteria. DR HOGENOM; CLU_013640_2_0_4; -. DR OMA; ERIKMGA; -. DR OrthoDB; 1109542at2; -. DR UniPathway; UPA00070; UER00946. DR Proteomes; UP000008385; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IEA:UniProtKB-UniRule. 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 CDD; cd04738; DHOD_2_like; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00225; DHO_dh_type2; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005720; Dihydroorotate_DH. 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 {ECO:0000256|HAMAP-Rule:MF_00225}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP- KW Rule:MF_00225}; KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_00225}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00225}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00225}; KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP- KW Rule:MF_00225}; Reference proteome {ECO:0000313|Proteomes:UP000008385}. FT DOMAIN 50..341 FT /note="DHO_dh" FT /evidence="ECO:0000259|Pfam:PF01180" FT NP_BIND 65..69 FT /note="FMN" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT NP_BIND 329..330 FT /note="FMN" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT REGION 114..118 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT REGION 257..258 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT COILED 198..218 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 186 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 69 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 89 FT /note="FMN; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 150 FT /note="FMN" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 183 FT /note="FMN" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 183 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 188 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 228 FT /note="FMN" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 256 FT /note="FMN; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 279 FT /note="FMN; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 308 FT /note="FMN; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" 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 //