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thrS threonine--tRNA ligase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 946222, updated on 2-May-2024

Summary

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Gene symbol
thrS
Gene description
threonine--tRNA ligase
Primary source
ASAP:ABE-0005736
Locus tag
b1719
See related
ECOCYC:EG11001
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK1717
Summary
Threonyl-tRNA synthetase (ThrRS) is a member of the family of aminoacyl-tRNA synthetases, which interpret the genetic code by covalently linking amino acids to their specific tRNA molecules. [More information is available at EcoCyc: EG11001].
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Genomic context

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Sequence:
NC_000913.3 (1800642..1802570, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene 50S ribosomal subunit protein L35 Neighboring gene translation initiation factor IF-3 Neighboring gene pseudo Neighboring gene uncharacterized protein YniD

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase. Minajigi A, et al. J Biol Chem, 2010 Jul 30. PMID 20504770, Free PMC Article
  2. RNA-assisted catalysis in a protein enzyme: The 2'-hydroxyl of tRNA(Thr) A76 promotes aminoacylation by threonyl-tRNA synthetase. Minajigi A, et al. Proc Natl Acad Sci U S A, 2008 Nov 18. PMID 18997014, Free PMC Article
  3. Mutations in residues involved in zinc binding in the catalytic site of Escherichia coli threonyl-tRNA synthetase confer a dominant lethal phenotype. Caillet J, et al. J Bacteriol, 2007 Oct. PMID 17644600, Free PMC Article
  4. Achieving error-free translation; the mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution. Dock-Bregeon AC, et al. Mol Cell, 2004 Nov 5. PMID 15525511
  5. Induced fit and kinetic mechanism of adenylation catalyzed by Escherichia coli threonyl-tRNA synthetase. Bovee ML, et al. Biochemistry, 2003 Dec 30. PMID 14690420

See all (76) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. the relative contributions of pre- and post-transfer editing in ThrRS are subject to modulation by the rate of aminoacyl transfer
    Title: Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase.
  2. Mutations in any of the three amino acids forming the zinc-binding site inactivate the enzyme and have a dominant negative effect on growth.
    Title: Mutations in residues involved in zinc binding in the catalytic site of Escherichia coli threonyl-tRNA synthetase confer a dominant lethal phenotype.
Submit: New GeneRIF Correction

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables ATP binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables RNA binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables aminoacyl-tRNA editing activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables aminoacyl-tRNA ligase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables aminoacyl-tRNA ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables mRNA 5'-UTR binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables mRNA regulatory element binding translation repressor activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein homodimerization activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables tRNA binding IEA
Inferred from Electronic Annotation
more info
  
enables threonine-tRNA ligase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables threonine-tRNA ligase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables threonine-tRNA ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables zinc ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables zinc ion binding IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Process Evidence Code Pubs
involved_in aminoacyl-tRNA metabolism involved in translational fidelity IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within negative regulation of translational initiation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within regulation of translation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in regulation of translation IEA
Inferred from Electronic Annotation
more info
  
involved_in response to antibiotic IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within tRNA aminoacylation IDA
Inferred from Direct Assay
more info
 PubMed 
acts_upstream_of_or_within tRNA aminoacylation for protein translation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in threonyl-tRNA aminoacylation IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within threonyl-tRNA aminoacylation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in threonyl-tRNA aminoacylation IEA
Inferred from Electronic Annotation
more info
  
involved_in translation IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
threonine--tRNA ligase
NP_416234.1

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    1800642..1802570 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_416234.1 threonine--tRNA ligase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_416234.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A0B5HQT2
    Conserved Domains (1) summary
    PRK00413
    Location:1 → 638
    thrS; threonyl-tRNA synthetase; Reviewed
Nucleotide Protein
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Gene LinkOut

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Other Literature Sources
Molecular Biology Databases
Research Materials