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    glnS glutamine--tRNA ligase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945310, updated on 17-Dec-2024

    Summary

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    Official Symbol
    glnS
    Official Full Name
    glutamine--tRNA ligase
    Primary source
    ECOCYC:EG10390
    Locus tag
    b0680
    See related
    ASAP:ABE-0002317
    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
    ECK0668
    Summary
    Glutaminyl-tRNA synthetase (GlnRS) 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: EG10390].
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    Genomic context

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    Sequence:
    NC_000913.3 (706093..707757)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene glucosamine-6-phosphate deaminase Neighboring gene N-acetylglucosamine-specific PTS enzyme IIABC component Neighboring gene ncRNA Neighboring gene chitooligosaccharide outer membrane channel

    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. Association of tRNA(Gln) acceptor identity with phosphate-sugar backbone interactions observed in the crystal structure of the Escherichia coli glutaminyl-tRNA synthetase-tRNA(Gln) complex. McClain WH, et al. Biochimie, 1993. PMID 8199248
    2. Structural basis of tRNA discrimination as derived from the high resolution crystal structure of glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP. Steitz TA, et al. Mol Biol Rep, 1990. PMID 2194108
    3. Glutaminyl-tRNA synthetase. Freist W, et al. Biol Chem, 1997 Oct. PMID 9372179
    4. Characterization of an 'orthogonal' suppressor tRNA derived from E. coli tRNA2(Gln). Liu DR, et al. Chem Biol, 1997 Sep. PMID 9331409
    5. Escherichia coli glutaminyl-tRNA synthetase: a single amino acid replacement relaxes rRNA specificity. Uemura H, et al. Protein Seq Data Anal, 1988. PMID 2464170

    See all (81) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The designed double mutant (K236E/E328A) of glutamyl-tRNA synthetase has been successfully crystallized.
      Title: Preliminary X-ray crystallographic analysis of an engineered glutamyl-tRNA synthetase from Escherichia coli.
    2. E. coli glutamyl-tRNA synthetase is inhibited by anticodon stem-loop domains and a minihelix
      Title: E. coli glutamyl-tRNA synthetase is inhibited by anticodon stem-loop domains and a minihelix.
    3. N-terminus verified by Edman degradation on mature peptide
      Title: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
    4. the sequence difference in the variable loop of glutaminyl-tRNA synthetase causes the difference in the internal mobility of the tertiary core region tRNAs and leads to the difference in the affinity to aminoacyl-tRNA synthetases through the entropy term
      Title: Mechanism of the difference in the binding affinity of E. coli tRNAGln to glutaminyl-tRNA synthetase caused by noninterface nucleotides in variable loop.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables aminoacyl-tRNA ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables glutamine-tRNA ligase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables glutamine-tRNA ligase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables glutamine-tRNA ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in glutaminyl-tRNA aminoacylation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within glutaminyl-tRNA aminoacylation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in glutaminyl-tRNA aminoacylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in glutamyl-tRNA aminoacylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tRNA aminoacylation for protein translation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in translation IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    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
    glutamine--tRNA ligase
    NP_415206.1

    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
      706093..707757
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415206.1 glutamine--tRNA ligase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415206.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8S7JXG0, A0A8S7R4V6, A0A8S7TQQ7
      Conserved Domains (1) summary
      PRK05347
      Location:1 → 552
      PRK05347; glutaminyl-tRNA synthetase; Provisional
    Nucleotide Protein
    Heading Accession and Version

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