U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

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

    Gene ID: 946222, updated on 3-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    thrS
    Official Full Name
    threonine--tRNA ligase
    Primary source
    ECOCYC:EG11001
    Locus tag
    b1719
    See related
    ASAP:ABE-0005736
    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].
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    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

    Go to the top of the page Help
    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. Effect of the antibiotic Borrelidin on the regulation of threonine biosynthetic enzymes in E. coli. Nass G, et al. Biochem Biophys Res Commun, 1969 Jan 6. PMID 4883496
    2. Translational repression mechanisms in prokaryotes. Schlax PJ, et al. Mol Microbiol, 2003 Jun. PMID 12787346
    3. Bacterial translational control at atomic resolution. Romby P, et al. Trends Genet, 2003 Mar. PMID 12615010
    4. The modular structure of Escherichia coli threonyl-tRNA synthetase as both an enzyme and a regulator of gene expression. Caillet J, et al. Mol Microbiol, 2003 Feb. PMID 12581352
    5. Alteration of structure of level of threonyl-tRNA-synthetase in Borrelidin resistant mutants of E. coli. Nass G, et al. FEBS Lett, 1974 Feb 15. PMID 4368395

    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

    Go to the top of the page

    Interactions

    Go to the top of the page Help
    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Go to the top of the page Help

    Homology

    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 catalytic activity, acting on a tRNA 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 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

    Go to the top of the page Help
    Preferred Names
    threonine--tRNA ligase
    NP_416234.1

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    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

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.