ID   PYRR_PSEU2              Reviewed;         170 AA.
AC   Q4ZZ69;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
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}; OrderedLocusNames=Psyr_0483;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- FUNCTION: Regulates the transcription of the pyrimidine nucleotide
CC       (pyr) operon in response to exogenous pyrimidines. {ECO:0000255|HAMAP-
CC       Rule:MF_01219}.
CC   -!- FUNCTION: Also displays a weak uracil phosphoribosyltransferase
CC       activity which is not physiologically significant. {ECO:0000255|HAMAP-
CC       Rule:MF_01219}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC         uracil; Xref=Rhea:RHEA:13017, ChEBI:CHEBI:17568, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57865, ChEBI:CHEBI:58017; EC=2.4.2.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01219};
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. PyrR subfamily. {ECO:0000255|HAMAP-Rule:MF_01219}.
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DR   EMBL; CP000075; AAY35553.1; -; Genomic_DNA.
DR   RefSeq; WP_011266430.1; NC_007005.1.
DR   RefSeq; YP_233591.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZZ69; -.
DR   SMR; Q4ZZ69; -.
DR   STRING; 205918.Psyr_0483; -.
DR   EnsemblBacteria; AAY35553; AAY35553; Psyr_0483.
DR   KEGG; psb:Psyr_0483; -.
DR   PATRIC; fig|205918.7.peg.502; -.
DR   eggNOG; COG2065; Bacteria.
DR   HOGENOM; CLU_094234_1_1_6; -.
DR   OMA; PIQPDFC; -.
DR   Proteomes; UP000000426; Chromosome.
DR   GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 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;
KW   Glycosyltransferase; Transcription; Transcription regulation; Transferase.
FT   CHAIN           1..170
FT                   /note="Bifunctional protein PyrR"
FT                   /id="PRO_1000053859"
FT   MOTIF           90..102
FT                   /note="PRPP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01219"
SQ   SEQUENCE   170 AA;  18428 MW;  DD5EDE3BDD9D503C CRC64;
     MSLPDPAELI RQMATDLNAH LSKRGISDPR FIGIRTGGVW VAQALLKALN NPAPLGTLDV
     SFYRDDFSQN GLHPQVRPSE LPFEIEGQHL VLIDDVLMSG RTVRAALNEL FDYGRPASVT
     LVCLLDLDAG ELPVRPNVVG ATLSLAPDER IKLSGPEPLA LELQDLSTAL