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Database: UniProt
Entry: A0A0T0MEC1_9CELL
LinkDB: A0A0T0MEC1_9CELL
Original site: A0A0T0MEC1_9CELL 
ID   A0A0T0MEC1_9CELL        Unreviewed;       195 AA.
AC   A0A0T0MEC1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Bifunctional protein PyrR {ECO:0000256|HAMAP-Rule:MF_01219};
DE   Includes:
DE     RecName: Full=Pyrimidine operon regulatory protein {ECO:0000256|HAMAP-Rule:MF_01219};
DE   Includes:
DE     RecName: Full=Uracil phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01219};
DE              Short=UPRTase {ECO:0000256|HAMAP-Rule:MF_01219};
DE              EC=2.4.2.9 {ECO:0000256|HAMAP-Rule:MF_01219};
GN   Name=pyrR {ECO:0000256|HAMAP-Rule:MF_01219};
GN   ORFNames=ASG23_16770 {ECO:0000313|EMBL:KQS97217.1};
OS   Cellulomonas sp. Leaf395.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1736362 {ECO:0000313|EMBL:KQS97217.1, ECO:0000313|Proteomes:UP000051971};
RN   [1] {ECO:0000313|EMBL:KQS97217.1, ECO:0000313|Proteomes:UP000051971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf395 {ECO:0000313|EMBL:KQS97217.1,
RC   ECO:0000313|Proteomes:UP000051971};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS97217.1, ECO:0000313|Proteomes:UP000051971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf395 {ECO:0000313|EMBL:KQS97217.1,
RC   ECO:0000313|Proteomes:UP000051971};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Also displays a weak uracil phosphoribosyltransferase
CC       activity which is not physiologically significant. {ECO:0000256|HAMAP-
CC       Rule:MF_01219}.
CC   -!- FUNCTION: Regulates the transcription of the pyrimidine nucleotide
CC       (pyr) operon in response to exogenous pyrimidines. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01219};
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. PyrR subfamily. {ECO:0000256|ARBA:ARBA00005565,
CC       ECO:0000256|HAMAP-Rule:MF_01219}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQS97217.1}.
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DR   EMBL; LMQI01000005; KQS97217.1; -; Genomic_DNA.
DR   RefSeq; WP_056027434.1; NZ_LMQI01000005.1.
DR   AlphaFoldDB; A0A0T0MEC1; -.
DR   STRING; 1736362.ASG23_16770; -.
DR   OrthoDB; 9802227at2; -.
DR   Proteomes; UP000051971; Unassembled WGS sequence.
DR   GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; 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   PANTHER; PTHR11608; BIFUNCTIONAL PROTEIN PYRR; 1.
DR   PANTHER; PTHR11608:SF0; BIFUNCTIONAL PROTEIN PYRR; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01219,
KW   ECO:0000313|EMBL:KQS97217.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051971};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_01219};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_01219};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01219, ECO:0000313|EMBL:KQS97217.1}.
FT   DOMAIN          22..166
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
FT   MOTIF           114..126
FT                   /note="PRPP-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01219"
SQ   SEQUENCE   195 AA;  20805 MW;  DEC7E39FFAFE3CAD CRC64;
     MSTGTPTPET RVDDDANVVL GAPEINRALT RIAHEILERN KGGSDVVLLG IPTRGLPLAR
     RLAERLIAVE PGLDPALLVG SLDVTMYRDD LAHQPTRTIG ATDIPGGGLD GKVVVLVDDV
     LYSGRTIRAA LDAISDLGRP RAVQLAALVD RGHRELPIRA DYVGKNLPTS TSERVRVLLE
     ESDGRDAVLI DGGTR
//
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