ID   PYRD_BURTA              Reviewed;         345 AA.
AC   Q2SVL9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   04-NOV-2026, entry version 110.
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};
GN   OrderedLocusNames=BTH_I2511;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS   CIP 106301 / E264).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CCUG 48851 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
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 = orotate + a quinol;
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; Evidence={ECO:0000255|HAMAP-
CC         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}.
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DR   EMBL; CP000086; ABC37940.1; -; Genomic_DNA.
DR   RefSeq; WP_009891396.1; NC_007651.1.
DR   AlphaFoldDB; Q2SVL9; -.
DR   SMR; Q2SVL9; -.
DR   GeneID; 45122221; -.
DR   KEGG; bte:BTH_I2511; -.
DR   HOGENOM; CLU_013640_2_0_4; -.
DR   OMA; AAACIDH; -.
DR   UniPathway; UPA00070; UER00946.
DR   Proteomes; UP000001930; Chromosome I.
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-UniRule.
DR   CDD; cd04738; DHOD_2_like; 1.
DR   FunFam; 3.20.20.70:FF:000028; Dihydroorotate dehydrogenase (quinone); 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; IPR050074; DHO_dehydrogenase.
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; NF003645; PRK05286.1-2; 1.
DR   NCBIfam; NF003646; PRK05286.1-4; 1.
DR   NCBIfam; NF003652; PRK05286.2-5; 1.
DR   NCBIfam; NF003644; pyrD; 1.
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; Flavoprotein; FMN; Membrane; Oxidoreductase;
KW   Pyrimidine biosynthesis; Reference proteome.
FT   CHAIN           1..345
FT                   /note="Dihydroorotate dehydrogenase (quinone)"
FT                   /id="PRO_1000024164"
FT   ACT_SITE        178
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         142
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         175
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         220
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         248
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         249..250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         271
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         300
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         321..322
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
SQ   SEQUENCE   345 AA;  36632 MW;  13D4A3AE13783409 CRC64;
     MFSSLYPLAR ASLFKMDAED AHHLTLRMLG AAGRTGLARA LSSRVPDAPR TVMGLTFRNP
     VGLAAGLDKD GAAIDGFAAL GFGFIEVGTV TPRAQPGNPR PRMFRLPEAG AIINRMGFNN
     SGVDQFVKNV QAARYRGVLG LNIGKNADTP IERAADDYLY CLERVYPFAS YVTINISSPN
     TKNLRQLQGA GELDALLAAL KNKQQRLADL HGKLVPLALK IAPDLDDEQV KDIAATLLRH
     NIEGVIATNT TLSRDAVKGL PHADEAGGLS GRPVFDASNA VIRKLHAELG DAVPIIGVGG
     IFSGDDARAK LAAGASLVQL YTGFIYRGPA LVAECVKAIA RGQTR
//