ID   PYRR_MANSM              Reviewed;         179 AA.
AC   Q65UX5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 105.
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=MS0628;
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E;
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(2004).
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; AE016827; AAU37235.1; -; Genomic_DNA.
DR   RefSeq; WP_011199807.1; NC_006300.1.
DR   AlphaFoldDB; Q65UX5; -.
DR   SMR; Q65UX5; -.
DR   STRING; 221988.MS0628; -.
DR   EnsemblBacteria; AAU37235; AAU37235; MS0628.
DR   KEGG; msu:MS0628; -.
DR   eggNOG; COG2065; Bacteria.
DR   HOGENOM; CLU_094234_2_1_6; -.
DR   OMA; PIQPDFC; -.
DR   OrthoDB; 1725260at2; -.
DR   Proteomes; UP000000607; 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..179
FT                   /note="Bifunctional protein PyrR"
FT                   /id="PRO_1000053846"
FT   MOTIF           100..112
FT                   /note="PRPP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01219"
SQ   SEQUENCE   179 AA;  20252 MW;  A5B1C3AFE4CA13AF CRC64;
     MEKIIIDESQ FMRTISRISH EIIEKHQNLN DLVIVGIKRR GAEIADLIKR KINELSGQSL
     PSIDLDITFY RDDLEYVEPA SQSPVYSGAS EFISVQNKTV ILIDDVLFTG RTIRAALDAL
     VDFGRAAKVE LVIFVDRGHR ELPIRADYVG KNVPTSRSEK VQVRTMKFDG CYEVALISK