(data stored in ACNUC7421 zone)

SWISSPROT: PYRD_RHOOB

ID   PYRD_RHOOB              Reviewed;         356 AA.
AC   C1ASU1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 53.
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=ROP_06260;
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate
CC       with quinone as electron acceptor. {ECO:0000255|HAMAP-
CC       Rule:MF_00225}.
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + a quinone = orotate + a
CC       quinol. {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
CC       pathway; orotate from (S)-dihydroorotate (quinone route): step
CC       1/1. {ECO:0000255|HAMAP-Rule:MF_00225}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00225}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00225}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00225}.
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.
CC       Type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00225}.
DR   EMBL; AP011115; BAH48873.1; -; Genomic_DNA.
DR   RefSeq; WP_012687878.1; NC_012522.1.
DR   SMR; C1ASU1; -.
DR   STRING; 632772.ROP_06260; -.
DR   EnsemblBacteria; BAH48873; BAH48873; ROP_06260.
DR   KEGG; rop:ROP_06260; -.
DR   PATRIC; fig|632772.20.peg.686; -.
DR   eggNOG; ENOG4107QYT; Bacteria.
DR   eggNOG; COG0167; LUCA.
DR   HOGENOM; HOG000225103; -.
DR   KO; K00254; -.
DR   OMA; LQNAMGF; -.
DR   OrthoDB; POG091H018H; -.
DR   UniPathway; UPA00070; UER00946.
DR   Proteomes; UP000002212; 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-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; -; 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;
DR   PRODOM; C1ASU1.
DR   SWISS-2DPAGE; C1ASU1.
KW   Cell membrane; Complete proteome; Flavoprotein; FMN; Membrane;
KW   Oxidoreductase; Pyrimidine biosynthesis.
FT   CHAIN         1    356       Dihydroorotate dehydrogenase (quinone).
FT                                /FTId=PRO_1000195088.
FT   NP_BIND      66     70       FMN. {ECO:0000255|HAMAP-Rule:MF_00225}.
FT   NP_BIND     316    317       FMN. {ECO:0000255|HAMAP-Rule:MF_00225}.
FT   REGION      115    119       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00225}.
FT   REGION      241    242       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00225}.
FT   ACT_SITE    179    179       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00225}.
FT   BINDING      70     70       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00225}.
FT   BINDING      90     90       FMN; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00225}.
FT   BINDING     143    143       FMN. {ECO:0000255|HAMAP-Rule:MF_00225}.
FT   BINDING     176    176       FMN. {ECO:0000255|HAMAP-Rule:MF_00225}.
FT   BINDING     176    176       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00225}.
FT   BINDING     181    181       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00225}.
FT   BINDING     212    212       FMN. {ECO:0000255|HAMAP-Rule:MF_00225}.
FT   BINDING     240    240       FMN; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00225}.
FT   BINDING     266    266       FMN; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00225}.
FT   BINDING     295    295       FMN; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00225}.
SQ   SEQUENCE   356 AA;  37728 MW;  F930961BEF2F8709 CRC64;
     MYHLLLRVMF RLPPERIHHL AFAAMRLVTR FSPLRQLVGR VLVVDDPVLR NTVFGLDFPA
     PLGLAAGFDK DATGVDAWGP LGFGFAEVGT VTAQAQPGNP APRLFRLPAD RALINRMGFN
     NHGAGNAANH LRQRRAGVPI GANIGKTKIV DAADAPADYT ASAHLLGPLA DFMVVNVSSP
     NTPGLRDLQA VESLRPLLRA VLDSVTVPVL VKIAPDLSDD DVDAVADLAL ELGLAGIVAT
     NTTIRRDGLN TPDDEVTAIG AGGLSGPPVA ERSLEVLRRL HARVGDRLVL ISVGGIETVD
     QAWERILAGA SLVQGYTGFI YGGPFWARRI HKGLARKVRE AGYSSVADAV GAGAVR
//

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