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    gluQ glutamyl-Q tRNA(Asp) synthetase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 944846, updated on 17-Dec-2024

    Summary

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    Official Symbol
    gluQ
    Official Full Name
    glutamyl-Q tRNA(Asp) synthetase
    Primary source
    ECOCYC:EG11362
    Locus tag
    b0144
    See related
    ASAP:ABE-0000497
    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
    ECK0143; yadB
    Summary
    A downstream start site at M10 is also possible; both starts have been used to overproduce active protein (Dubois, 2004; Campanacci, 2004). [More information is available at EcoGene: EG11362]. Glutamyl-Q tRNA(Asp) synthetase (Glu-Q-RS) catalyzes the addition of a glutamate residue to the queosine-modified wobble base of tRNA(Asp). [More information is available at EcoCyc: EG11362].
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    Genomic context

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    Sequence:
    NC_000913.3 (159186..160112, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative fimbrial protein YadN Neighboring gene 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase Neighboring gene poly(A) polymerase I Neighboring gene RNA polymerase-binding transcription factor DksA Neighboring gene sugar fermentation stimulation protein A

    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. Critical role of zinc ion on E. coli glutamyl-queuosine-tRNA(Asp) synthetase (Glu-Q-RS) structure and function. Ray S, et al. Protein J, 2014 Apr. PMID 24505021
    2. Fusion with anticodon binding domain of GluRS is not sufficient to alter the substrate specificity of a chimeric Glu-Q-RS. Ray S, et al. Protein J, 2014 Feb. PMID 24374508
    3. Crystal structure of glutamyl-queuosine tRNAAsp synthetase complexed with L-glutamate: structural elements mediating tRNA-independent activation of glutamate and glutamylation of tRNAAsp anticodon. Blaise M, et al. J Mol Biol, 2008 Sep 19. PMID 18602926
    4. Turning tRNA upside down: When aminoacylation is not a prerequisite to protein synthesis. Ibba M, et al. Proc Natl Acad Sci U S A, 2004 May 18. PMID 15138304, Free PMC Article
    5. The Escherichia coli YadB gene product reveals a novel aminoacyl-tRNA synthetase like activity. Campanacci V, et al. J Mol Biol, 2004 Mar 19. PMID 15003446

    See all (14) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The chimeric Glu-Q-RS is still able to aminoacylate tRNA(Asp) but has also the capacity to bind tRNA(Glu).
      Title: Fusion with anticodon binding domain of GluRS is not sufficient to alter the substrate specificity of a chimeric Glu-Q-RS.
    Submit: New GeneRIF Correction

    General gene information

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    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 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 metal ion 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
    		  
    enables zinc ion binding ISS
    Inferred from Sequence or Structural Similarity
    more info
    		 PubMed 
    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
    		  
    involved_in tRNA modification IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tRNA wobble base modification IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    glutamyl-Q tRNA(Asp) synthetase

    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
      159186..160112 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_414686.3 glutamyl-Q tRNA(Asp) synthetase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_414686.3

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A066Q893, A0A0E0Y597, A0A2I6LMI9, A0A376U2V8, A0A7U9J0U7, A0A8E0FKH7, A0AA35F450, A0AAD2V788, A0AAD2VG64, A0AAN1S1P3, A0AAP9MNM3, B7LGK6, E0IYN7
      Conserved Domains (1) summary
      PRK05710
      Location:11 → 303
      PRK05710; tRNA glutamyl-Q(34) synthetase GluQRS
    Nucleotide Protein
    Heading Accession and Version

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