ID F5XWJ7_RAMTT Unreviewed; 354 AA. AC F5XWJ7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 24-JAN-2024, entry version 65. 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; Pseudomonadota; 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 AlphaFoldDB; F5XWJ7; -. DR STRING; 365046.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; 9802377at2; -. 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:0106430; F:dihydroorotate dehydrogenase (quinone) activity; IEA:UniProtKB-EC. 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; Aldolase class I; 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 InterPro; IPR005720; Dihydroorotate_DH_dom. DR NCBIfam; TIGR01036; pyrD_sub2; 1. DR PANTHER; PTHR48109:SF4; DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL; 1. DR PANTHER; PTHR48109; DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL-RELATED; 1. DR Pfam; PF01180; DHO_dh; 1. DR PIRSF; PIRSF000164; DHO_oxidase; 1. DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 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 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..340 FT /note="Dihydroorotate dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF01180" FT ACT_SITE 186 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 65..69 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 69 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 89 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 114..118 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 150 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 183 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 183 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 188 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 228 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 256 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 257..258 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 279 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 308 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00225" FT BINDING 329..330 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" 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 //