Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bifunctional protein PyrR

Gene

pyrR

Organism
Leifsonia xyli subsp. xyli (strain CTCB07)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Regulates the transcription of the pyrimidine nucleotide (pyr) operon in response to exogenous pyrimidines.UniRule annotation
Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant.UniRule annotation

Catalytic activityi

UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosyltransferase, Transferase
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

BioCyciLXYL281090:G1G06-1137-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional protein PyrRUniRule annotation
Including the following 2 domains:
Pyrimidine operon regulatory proteinUniRule annotation
Uracil phosphoribosyltransferaseUniRule annotation (EC:2.4.2.9UniRule annotation)
Short name:
UPRTaseUniRule annotation
Gene namesi
Name:pyrRUniRule annotation
Ordered Locus Names:Lxx11050
OrganismiLeifsonia xyli subsp. xyli (strain CTCB07)
Taxonomic identifieri281090 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrobacteriaceaeLeifsonia
Proteomesi
  • UP000001306 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001392001 – 183Bifunctional protein PyrRAdd BLAST183

Proteomic databases

PRIDEiQ6AF89

Interactioni

Protein-protein interaction databases

STRINGi281090.Lxx11050

Structurei

3D structure databases

ProteinModelPortaliQ6AF89
SMRiQ6AF89
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi102 – 114PRPP-bindingUniRule annotationAdd BLAST13

Sequence similaritiesi

Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrR subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108UK1 Bacteria
COG2065 LUCA
HOGENOMiHOG000245770
KOiK02825
OMAiRISHEIL
OrthoDBiPOG091H02JM

Family and domain databases

CDDicd06223 PRTases_typeI, 1 hit
HAMAPiMF_01219 PyrR, 1 hit
InterProiView protein in InterPro
IPR000836 PRibTrfase_dom
IPR029057 PRTase-like
IPR023050 PyrR
PfamiView protein in Pfam
PF00156 Pribosyltran, 1 hit
SUPFAMiSSF53271 SSF53271, 1 hit

Sequencei

Sequence statusi: Complete.

Q6AF89-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTRVVLQQA DISRALTRIS HEILESNRGI DGLAILGIPT RGVVLARRIA
60 70 80 90 100
ESIQRIEQEA VGASADIVGA LDVTMYRDDL ARNPTRAPQP TSLPGPIDGK
110 120 130 140 150
TVVLVDDVLF SGRTIRAALD ALSDLGRPRA VRLAVLVDRG HRELPIRADF
160 170 180
VGKNLPSAAS ERIFVRFAEV DGQDAVTIEE GGA
Length:183
Mass (Da):19,664
Last modified:September 13, 2004 - v1
Checksum:iBE3AEF9128507E58
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016822 Genomic DNA Translation: AAT88956.1
RefSeqiWP_011185952.1, NC_006087.1

Genome annotation databases

EnsemblBacteriaiAAT88956; AAT88956; Lxx11050
KEGGilxx:Lxx11050

Similar proteinsi

Entry informationi

Entry nameiPYRR_LEIXX
AccessioniPrimary (citable) accession number: Q6AF89
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 13, 2004
Last modified: May 23, 2018
This is version 91 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health