PYRR_THET8
ID PYRR_THET8 Reviewed; 181 AA.
AC Q5SK65; P83822;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Bifunctional protein PyrR;
DE Includes:
DE RecName: Full=Pyrimidine operon regulatory protein;
DE Includes:
DE RecName: Full=Uracil phosphoribosyltransferase;
DE Short=UPRTase;
DE EC=2.4.2.9;
GN Name=pyrR; OrderedLocusNames=TTHA0783;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RA Matsuura T., Sakai H., Terada T., Shirouzu M., Kuramitsu S., Yokoyama S.;
RL Submitted (JUN-2003) to the PDB data bank.
CC -!- FUNCTION: Probably regulates transcriptional attenuation of the
CC pyrimidine nucleotide (pyr) operon in response to exogenous
CC pyrimidines. In contrast to pyr attenuation in Bacillus, PyrR from
CC Thermus could act as a translational repressor: the binding of PyrR at
CC its proposed recognition site in the transcript would prevent
CC initiation of translation of the leader peptide, resulting in
CC terminator formation and reduced expression of downstream genes (By
CC similarity). Also displays uracil phosphoribosyltransferase activity
CC (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. PyrR subfamily. {ECO:0000305}.
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DR EMBL; AP008226; BAD70606.1; -; Genomic_DNA.
DR RefSeq; WP_011172875.1; NC_006461.1.
DR RefSeq; YP_144049.1; NC_006461.1.
DR PDB; 1UFR; X-ray; 2.60 A; A/B/C/D=1-181.
DR PDBsum; 1UFR; -.
DR AlphaFoldDB; Q5SK65; -.
DR SMR; Q5SK65; -.
DR STRING; 300852.55772165; -.
DR EnsemblBacteria; BAD70606; BAD70606; BAD70606.
DR GeneID; 3169141; -.
DR KEGG; ttj:TTHA0783; -.
DR PATRIC; fig|300852.9.peg.776; -.
DR eggNOG; COG2065; Bacteria.
DR HOGENOM; CLU_094234_2_1_0; -.
DR OMA; PIQPDFC; -.
DR PhylomeDB; Q5SK65; -.
DR EvolutionaryTrace; Q5SK65; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Reference proteome; Repressor;
KW RNA-binding; Transcription; Transcription regulation;
KW Transcription termination; Transferase.
FT CHAIN 1..181
FT /note="Bifunctional protein PyrR"
FT /id="PRO_0000294122"
FT MOTIF 99..111
FT /note="PRPP-binding"
FT /evidence="ECO:0000250"
FT BINDING 41..42
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 103..111
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:1UFR"
FT HELIX 10..28
FT /evidence="ECO:0007829|PDB:1UFR"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:1UFR"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1UFR"
FT HELIX 43..58
FT /evidence="ECO:0007829|PDB:1UFR"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:1UFR"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:1UFR"
FT STRAND 98..109
FT /evidence="ECO:0007829|PDB:1UFR"
FT HELIX 110..122
FT /evidence="ECO:0007829|PDB:1UFR"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:1UFR"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:1UFR"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:1UFR"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:1UFR"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:1UFR"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1UFR"
SQ SEQUENCE 181 AA; 20467 MW; 87FDF462E6E6D3C9 CRC64;
MRFKAELMNA PEMRRALYRI AHEIVEANKG TEGLALVGIH TRGIPLAHRI ARFIAEFEGK
EVPVGVLDIT LYRDDLTEIG YRPQVRETRI PFDLTGKAIV LVDDVLYTGR TARAALDALI
DLGRPRRIYL AVLVDRGHRE LPIRADFVGK NVPTSRSEVV KVKVEEVDGE DRVELWEREG
A
