PYRD_RHOPA
ID PYRD_RHOPA Reviewed; 364 AA.
AC Q6NBN1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=RPA0797;
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
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}.
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DR EMBL; BX572595; CAE26241.1; -; Genomic_DNA.
DR RefSeq; WP_011156364.1; NC_005296.1.
DR AlphaFoldDB; Q6NBN1; -.
DR SMR; Q6NBN1; -.
DR STRING; 258594.RPA0797; -.
DR PRIDE; Q6NBN1; -.
DR EnsemblBacteria; CAE26241; CAE26241; RPA0797.
DR GeneID; 66891813; -.
DR KEGG; rpa:RPA0797; -.
DR eggNOG; COG0167; Bacteria.
DR HOGENOM; CLU_013640_2_1_5; -.
DR OMA; ERIKMGA; -.
DR PhylomeDB; Q6NBN1; -.
DR BioCyc; RPAL258594:TX73_RS04110-MON; -.
DR UniPathway; UPA00070; UER00946.
DR Proteomes; UP000001426; 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; IPR005719; Dihydroorotate_DH_2.
DR InterPro; IPR001295; Dihydroorotate_DH_CS.
DR Pfam; PF01180; DHO_dh; 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..364
FT /note="Dihydroorotate dehydrogenase (quinone)"
FT /id="PRO_1000100279"
FT ACT_SITE 173
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 61..65
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 85
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 110..114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 139
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 170
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 214
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 242
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 243..244
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 266
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 295
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 316..317
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
SQ SEQUENCE 364 AA; 39178 MW; 9C1C4EE6853918A0 CRC64;
MIRAFDAVSL PLLRWLDPED AHRLAIQGLK LWPPVKPRPD DSKLAVRAFG LNFSNPVGIA
AGFDKNAEAP DALLRLGFGF VEVGTVTPKP QAGNPRPRLF RLERDEAVIN RMGFNNEGAE
VVLRRLAARA QYGGIVGVNV GANKDSDDRV ADYVKLIETF APLASYFTVN VSSPNTPGLR
NLQQAAALDD LLARVIDARE RVRAAAGDTP VLLKIAPDLS LGELDDVVHI ARSRRVDGMI
VANTTLSRSP TLRERTKMNE QGGLSGRPLF RLSTRMVAET FVRAEGAFPL IGVGGIDSGG
AALTKIRAGA TLVQLYSALV YKGLGLVESI KADLASTLLR TDRDSLAEIV GADAPMITAE
EWPV
