ID   Q9AAR8_CAUVC            Unreviewed;       352 AA.
AC   Q9AAR8;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Dihydroorotate dehydrogenase (quinone) {ECO:0000256|ARBA:ARBA00018366};
DE            EC=1.3.5.2 {ECO:0000256|ARBA:ARBA00012791};
DE   AltName: Full=DHOdehase {ECO:0000256|ARBA:ARBA00032000};
DE   AltName: Full=Dihydroorotate oxidase {ECO:0000256|ARBA:ARBA00031623};
GN   OrderedLocusNames=CC_0528 {ECO:0000313|EMBL:AAK22515.1};
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650 {ECO:0000313|EMBL:AAK22515.1, ECO:0000313|Proteomes:UP000001816};
RN   [1] {ECO:0000313|EMBL:AAK22515.1, ECO:0000313|Proteomes:UP000001816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15 {ECO:0000313|Proteomes:UP000001816};
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R., Ohta N., Maddock J.R., Potocka I.,
RA   Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B., DeBoy R.T.,
RA   Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Smit J.,
RA   Craven M.B., Khouri H., Shetty J., Berry K., Utterback T., Tran K.,
RA   Wolf A., Vamathevan J., Ermolaeva M., White O., Salzberg S.L., Venter J.C.,
RA   Shapiro L., Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
CC   -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with
CC       quinone as electron acceptor. {ECO:0000256|ARBA:ARBA00003125}.
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};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}.
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 2
CC       subfamily. {ECO:0000256|ARBA:ARBA00005359}.
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; AE005673; AAK22515.1; -; Genomic_DNA.
DR   PIR; G87314; G87314.
DR   RefSeq; NP_419347.1; NC_002696.2.
DR   RefSeq; WP_010918416.1; NC_002696.2.
DR   AlphaFoldDB; Q9AAR8; -.
DR   SMR; Q9AAR8; -.
DR   STRING; 190650.CC_0528; -.
DR   EnsemblBacteria; AAK22515; AAK22515; CC_0528.
DR   KEGG; ccr:CC_0528; -.
DR   PATRIC; fig|190650.5.peg.538; -.
DR   eggNOG; COG0167; Bacteria.
DR   HOGENOM; CLU_013640_2_1_5; -.
DR   BioCyc; CAULO:CC0528-MONOMER; -.
DR   UniPathway; UPA00070; UER00946.
DR   Proteomes; UP000001816; 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   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012135; Dihydroorotate_DH_1_2.
DR   InterPro; IPR005719; Dihydroorotate_DH_2.
DR   InterPro; IPR005720; Dihydroorotate_DH_cat.
DR   InterPro; IPR001295; Dihydroorotate_DH_CS.
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   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001816}.
FT   DOMAIN          43..337
FT                   /note="Dihydroorotate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01180"
SQ   SEQUENCE   352 AA;  36320 MW;  A53E5216089C2FF9 CRC64;
     MSLHDIAARA LHAFDPEDAH GWAIRGLKWG LGPRDAQPDD PILAVKIAGL ELPNCVGLAA
     GFDKNAEVPD AMLAAGFGFV EAGTVTPLAQ AGNPRPRLFR LTEDQAVINR MGFNNGGLEP
     FAQRLAARQG RGGVVGANIG ANKDATDRIQ DYVTGLTRLW GLSDYFTANI SSPNTPGLRA
     LQTKAALEEL LGRLAETRAA LKVASGADYP IFLKVAPDLE DGEVEAIVET VVGAGLDAII
     VSNTTIARPE TLKSRFAGES GGLSGAPLLE ASTAVLARFH AAAAGRVALI GAGGVADGAG
     AYAKIRAGAR AVQLYSALVY GGPGLVTRIK RDLAARLRAD GFAAVEDAIG AA
//