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aspS aspartate--tRNA ligase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 946385, updated on 2-May-2024

Summary

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Gene symbol
aspS
Gene description
aspartate--tRNA ligase
Primary source
ASAP:ABE-0006226
Locus tag
b1866
See related
ECOCYC:EG10097
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
ECK1867; tls
Summary
Aspartyl-tRNA synthetase (AspRS) 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: EG10097].
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Genomic context

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Sequence:
NC_000913.3 (1948750..1950522, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative transcriptional regulator YebC Neighboring gene dihydroneopterin triphosphate diphosphatase Neighboring gene isochorismatase family protein YecD Neighboring gene DUF72 domain-containing protein YecE Neighboring gene MAPEG family inner membrane protein YecN

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. Probing electrostatic interactions and ligand binding in aspartyl-tRNA synthetase through site-directed mutagenesis and computer simulations. Thompson D, et al. Proteins, 2008 May 15. PMID 18076053
  2. Ammonium scanning in an enzyme active site. The chiral specificity of aspartyl-tRNA synthetase. Thompson D, et al. J Biol Chem, 2007 Oct 19. PMID 17690095
  3. Molecular dynamics simulations show that bound Mg2+ contributes to amino acid and aminoacyl adenylate binding specificity in aspartyl-tRNA synthetase through long range electrostatic interactions. Thompson D, et al. J Biol Chem, 2006 Aug 18. PMID 16774919
  4. Aspartyl-tRNA synthetase is the target of peptide nucleotide antibiotic Microcin C. Metlitskaya A, et al. J Biol Chem, 2006 Jun 30. PMID 16574659
  5. Free-energy simulations and experiments reveal long-range electrostatic interactions and substrate-assisted specificity in an aminoacyl-tRNA synthetase. Thompson D, et al. Chembiochem, 2006 Feb. PMID 16408313

See all (39) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. A comparison of biophysical properties of human mitochondrial aspartyl-tRNA synthetase, HsaDRS2, with them to those of a E. coli homolog, EcoDRS.
    Title: Thermodynamic properties distinguish human mitochondrial aspartyl-tRNA synthetase from bacterial homolog with same 3D architecture.
  2. N-terminus verified by Edman degradation on complete protein
    Title: Aspartyl-tRNA synthetase from Escherichia coli: cloning and characterisation of the gene, homologies of its translated amino acid sequence with asparaginyl- and lysyl-tRNA synthetases.
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 IEA
Inferred from Electronic Annotation
more info
  
enables aminoacyl-tRNA ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables aspartate-tRNA ligase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables aspartate-tRNA ligase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables aspartate-tRNA ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables nucleic acid binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in aspartyl-tRNA aminoacylation IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within aspartyl-tRNA aminoacylation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in aspartyl-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
  
located_in cytosol HDA PubMed 
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
aspartate--tRNA ligase
NP_416380.1

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
    1948750..1950522 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_416380.1 aspartate--tRNA ligase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_416380.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A7A6ZS97
    Conserved Domains (1) summary
    PRK00476
    Location:1 → 587
    aspS; aspartyl-tRNA synthetase; Validated
Nucleotide Protein
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Gene LinkOut

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Other Literature Sources
Molecular Biology Databases
Research Materials