(data stored in ACNUC7421 zone)

SWISSPROT: PYRR_PSEAB

ID   PYRR_PSEAB              Reviewed;         170 AA.
AC   Q02U09;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   07-JUN-2017, entry version 64.
DE   RecName: Full=Bifunctional protein PyrR {ECO:0000255|HAMAP-Rule:MF_01219};
DE   Includes:
DE     RecName: Full=Pyrimidine operon regulatory protein {ECO:0000255|HAMAP-Rule:MF_01219};
DE   Includes:
DE     RecName: Full=Uracil phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01219};
DE              Short=UPRTase {ECO:0000255|HAMAP-Rule:MF_01219};
DE              EC=2.4.2.9 {ECO:0000255|HAMAP-Rule:MF_01219};
GN   Name=pyrR {ECO:0000255|HAMAP-Rule:MF_01219};
GN   OrderedLocusNames=PA14_05270;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Regulates the transcription of the pyrimidine nucleotide
CC       (pyr) operon in response to exogenous pyrimidines.
CC       {ECO:0000255|HAMAP-Rule:MF_01219}.
CC   -!- FUNCTION: Also displays a weak uracil phosphoribosyltransferase
CC       activity which is not physiologically significant.
CC       {ECO:0000255|HAMAP-Rule:MF_01219}.
CC   -!- CATALYTIC ACTIVITY: UMP + diphosphate = uracil + 5-phospho-alpha-
CC       D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_01219}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. PyrR subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01219}.
DR   EMBL; CP000438; ABJ15370.1; -; Genomic_DNA.
DR   RefSeq; WP_003084574.1; NC_008463.1.
DR   ProteinModelPortal; Q02U09; -.
DR   SMR; Q02U09; -.
DR   EnsemblBacteria; ABJ15370; ABJ15370; PA14_05270.
DR   KEGG; pau:PA14_05270; -.
DR   HOGENOM; HOG000245771; -.
DR   KO; K02825; -.
DR   OMA; RISHEIL; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   HAMAP; MF_01219; PyrR; 1.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR023050; PyrR.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q02U09.
DR   SWISS-2DPAGE; Q02U09.
KW   Complete proteome; Glycosyltransferase; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    170       Bifunctional protein PyrR.
FT                                /FTId=PRO_1000053856.
FT   MOTIF        90    102       PRPP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01219}.
SQ   SEQUENCE   170 AA;  18676 MW;  E418A0F708A6D201 CRC64;
     MSLPNPAELL PRMASDLRAH LAERGIERPR FVGIHTGGIW VAEALLRELG NQEPLGTLDV
     SFYRDDFTQN GLHPQVRPSA LPFEIDGQHL VLVDDVLMSG RTIRAALNEL FDYGRPASVT
     LVCLLDLNAR ELPIRPDVVG QTLSLGRDER VKLVGPAPLA LERKVLSSAS
//

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