PYRR_GEOTN
ID PYRR_GEOTN Reviewed; 179 AA.
AC A4IM28;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=GTNG_1004;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
CC -!- FUNCTION: Regulates transcriptional attenuation of the pyrimidine
CC nucleotide (pyr) operon by binding in a uridine-dependent manner to
CC specific sites on pyr mRNA. This disrupts an antiterminator hairpin in
CC the RNA and favors formation of a downstream transcription terminator,
CC leading to a reduced expression of downstream genes.
CC {ECO:0000255|HAMAP-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 -!- SUBUNIT: Homodimer and homohexamer; in equilibrium. {ECO:0000255|HAMAP-
CC 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; CP000557; ABO66382.1; -; Genomic_DNA.
DR RefSeq; WP_008878661.1; NC_009328.1.
DR AlphaFoldDB; A4IM28; -.
DR SMR; A4IM28; -.
DR STRING; 420246.GTNG_1004; -.
DR EnsemblBacteria; ABO66382; ABO66382; GTNG_1004.
DR KEGG; gtn:GTNG_1004; -.
DR eggNOG; COG2065; Bacteria.
DR HOGENOM; CLU_094234_2_1_9; -.
DR OMA; PIQPDFC; -.
DR OrthoDB; 1725260at2; -.
DR Proteomes; UP000001578; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006353; P:DNA-templated transcription, termination; 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; RNA-binding; Transcription; Transcription regulation;
KW Transcription termination; Transferase.
FT CHAIN 1..179
FT /note="Bifunctional protein PyrR"
FT /id="PRO_1000053836"
FT MOTIF 100..112
FT /note="PRPP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01219"
SQ SEQUENCE 179 AA; 19857 MW; 61A34584941EA600 CRC64;
MQKAVVMDEQ AIRRALTRIA HEIIERNKGI DGCVLVGIKT RGIYLARRLA ERIEQIEGTS
VPVGELDITL YRDDLTMKTE DHEPLVKGTN VPFPVSEQKV ILVDDVLFTG RTVRAAMDAV
MDLGRPARIQ LAVLVDRGHR ELPIRADFVG KNVPTSSAEV IVVELAEVDG VDQVSIHEK
