U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from Protein

    • Showing Current items.

    gltX glutamate--tRNA ligase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946906, updated on 3-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    gltX
    Official Full Name
    glutamate--tRNA ligase
    Primary source
    ECOCYC:EG10407
    Locus tag
    b2400
    See related
    ASAP:ABE-0007911
    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
    ECK2394; gltM; gluRS
    Summary
    The zinc binding motif Cys98-x-Cys100-x(24)-Cys125-x-H127 of GltX categorizes this as a SWIM domain (standard C-x-C-x(n)-C-x-H with n=6-25). [More information is available at EcoGene: EG10407].
    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 (2519257..2520672, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene DNA-binding transcriptional dual regulator YfeC Neighboring gene putative DNA-binding transcriptional regulator YfeD Neighboring gene tRNA-Val Neighboring gene tRNA-Val

    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. Glutamyl transfer ribonucleic acid synthetase of Escherichia coli. 3. Influence of the 46K protein on the affinity of the 56K glutamyl transfer ribonucleic acid synthetase for its substrates. Lapointe J, et al. J Biol Chem, 1972 Aug 25. PMID 4560497
    2. Isolation of temperature-sensitive aminoacyl-tRNA synthetase mutants from an Escherichia coli strain harboring the pemK plasmid. Masuda Y, et al. Mol Gen Genet, 1993 Apr. PMID 8479423
    3. A 2-thiouridine derivative in tRNAGlu is a positive determinant for aminoacylation by Escherichia coli glutamyl-tRNA synthetase. Sylvers LA, et al. Biochemistry, 1993 Apr 20. PMID 8385989
    4. The glutamyl-tRNA synthetase of Escherichia coli contains one atom of zinc essential for its native conformation and its catalytic activity. Liu J, et al. Biochemistry, 1993 Oct 26. PMID 8218204
    5. The zinc-binding site of Escherichia coli glutamyl-tRNA synthetase is located in the acceptor-binding domain. Studies by extended x-ray absorption fine structure, molecular modeling, and site-directed mutagenesis. Liu J, et al. J Biol Chem, 1995 Jun 23. PMID 7797500

    See all (63) citations in PubMed

    GeneRIFs: Gene References Into Functions

    General gene information

    Go to the top of the page Help

    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 glutamate-tRNA ligase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables glutamate-tRNA ligase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables glutamate-tRNA ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables tRNA binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables zinc ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables zinc ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in glutamyl-tRNA aminoacylation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in glutamyl-tRNA aminoacylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within glutamyl-tRNA aminoacylation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    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

    Go to the top of the page Help
    Preferred Names
    glutamate--tRNA ligase
    NP_416899.1

    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
      2519257..2520672 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_416899.1 glutamate--tRNA ligase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_416899.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A0B5HLG4, A0A376FYL4, A0A8S7HVE6
      Conserved Domains (1) summary
      PRK01406
      Location:1 → 461
      gltX; glutamyl-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.