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

    Gene ID: 946222, updated on 23-Nov-2023

    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 RNA binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    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 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 nucleotide 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 
    involved_in tRNA aminoacylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within tRNA aminoacylation for protein translation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in tRNA aminoacylation for protein translation IEA
    Inferred from Electronic Annotation
    more info
    		  
    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
    Heading Accession and Version

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    Other Literature Sources
    Molecular Biology Databases
    Research Materials