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PYRD_DEIDV
ID   PYRD_DEIDV              Reviewed;         360 AA.
AC   C1CX89;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=Deide_18190;
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
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; CP001114; ACO46806.1; -; Genomic_DNA.
DR   RefSeq; WP_012693928.1; NC_012526.1.
DR   AlphaFoldDB; C1CX89; -.
DR   SMR; C1CX89; -.
DR   STRING; 546414.Deide_18190; -.
DR   PaxDb; C1CX89; -.
DR   EnsemblBacteria; ACO46806; ACO46806; Deide_18190.
DR   KEGG; ddr:Deide_18190; -.
DR   eggNOG; COG0167; Bacteria.
DR   HOGENOM; CLU_013640_2_0_0; -.
DR   OMA; ERIKMGA; -.
DR   OrthoDB; 1109542at2; -.
DR   UniPathway; UPA00070; UER00946.
DR   Proteomes; UP000002208; 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..360
FT                   /note="Dihydroorotate dehydrogenase (quinone)"
FT                   /id="PRO_1000204313"
FT   ACT_SITE        179
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         67..71
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         91
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         116..120
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         176
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         222
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         250
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         251..252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         272
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         301
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT   BINDING         322..323
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
SQ   SEQUENCE   360 AA;  38239 MW;  B4FC0441DAB4C40E CRC64;
     MYRRVIKPAL FRLDAEDAHH LTVNALALMS RLPGWPAAAR RLSAPADSRL MQTLWGHTYA
     SPVGLAAGLD KNGVAVPAFS ALGFGFVEVG TVTPQPQPGN DRPRLFRLPP DEALINRMGF
     NNAGAAALRG QLSRLGRRTV PVWVNIGKNK LTEEAAQDYV ACVQELYDVA DAFVVNVSSP
     NTPGLRALQA SAELEALLRA VLNETEAQRL RTARRAPPVL VKLAPDLHPA DFEASVQGAL
     NAGVQGLIVS NTTLSRDGLT HAHREQAGGL SGRPLTGRST ALVQDAYRLT RGAVPVVGVG
     GIFSADDAYA KIRAGASLVE VYSSLIYEGP GLPARIHRGL GQLLERDGIS HVRDAVGADA
 
 
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