ID   PYRD_CUPMC              Reviewed;         344 AA.
AC   Q1LP27;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Dihydroorotate dehydrogenase (quinone) {ECO:0000255|HAMAP-Rule:MF_00225};
DE            EC=1.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00225};
DE   AltName: Full=DHOdehase {ECO:0000255|HAMAP-Rule:MF_00225};
DE            Short=DHOD {ECO:0000255|HAMAP-Rule:MF_00225};
DE            Short=DHODase {ECO:0000255|HAMAP-Rule:MF_00225};
DE   AltName: Full=Dihydroorotate oxidase {ECO:0000255|HAMAP-Rule:MF_00225};
GN   Name=pyrD {ECO:0000255|HAMAP-Rule:MF_00225}; OrderedLocusNames=Rmet_1213;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
CC   -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with
CC       quinone as electron acceptor. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00225};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00225};
CC       Note=Binds 1 FMN per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00225}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00225}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00225};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00225}.
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00225}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABF08099.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000352; ABF08099.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_017514992.1; NC_007973.1.
DR   AlphaFoldDB; Q1LP27; -.
DR   SMR; Q1LP27; -.
DR   STRING; 266264.Rmet_1213; -.
DR   EnsemblBacteria; ABF08099; ABF08099; Rmet_1213.
DR   KEGG; rme:Rmet_1213; -.
DR   eggNOG; COG0167; Bacteria.
DR   HOGENOM; CLU_013640_2_0_4; -.
DR   OrthoDB; 1109542at2; -.
DR   UniPathway; UPA00070; UER00946.
DR   Proteomes; UP000002429; 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; Flavoprotein; FMN; Membrane; Oxidoreductase;
KW   Pyrimidine biosynthesis; Reference proteome.
FT   CHAIN           1..344
FT                   /note="Dihydroorotate dehydrogenase (quinone)"
FT                   /id="PRO_0000336483"
FT   ACT_SITE        181
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         65..69
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         89
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         114..118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         145
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         178
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         223
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         251
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         252..253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         274
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         303
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         324..325
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
SQ   SEQUENCE   344 AA;  36977 MW;  C3E49ACB89F75F11 CRC64;
     MLNALYPLLR PALFSMDAED AHHFTLNNLM RAKRMGLAGC IGNSIADDPR TVMGVRFPNP
     VGLAAGLDKD GAYIDGLAAF GFGFIEVGTV TPRAQPGNPR PRMFRLPQAD ALINRMGFNN
     GGVDAFIRNV QASRWKAEGG VLGLNIGKNA DTPIERAADD YLYCLERVYP HASYVTVNIS
     SPNTKNLRQL QGASELDSLL STLKAAQQRL ADQHKRYVPV ALKIAPDLDD DQVRNIGDAL
     VRHKIDGVIA TNTTISRDAV KGLPHAEEAG GLSGRPVFEA STRVVRALRE VIGDALPIIG
     VGGIFSGADA RAKIDAGAQL VQVYSGLIYR GPTLVRECAS ALRR