A0A7C6HLN5 · A0A7C6HLN5_9FIRM

  • Protein
    Aspartate--tRNA ligase
  • Gene
    aspS
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site180L-aspartate (UniProtKB | ChEBI)
Binding site226L-aspartate (UniProtKB | ChEBI)
Binding site226-228ATP (UniProtKB | ChEBI)
Binding site235ATP (UniProtKB | ChEBI)
Binding site454L-aspartate (UniProtKB | ChEBI)
Binding site488ATP (UniProtKB | ChEBI)
Binding site495L-aspartate (UniProtKB | ChEBI)
Binding site540-543ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionaspartate-tRNA ligase activity
Molecular FunctionATP binding
Molecular Functionnucleic acid binding
Molecular Functiontransferase activity
Biological Processaspartyl-tRNA aminoacylation
Biological Processregulation of translational fidelity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Aspartate--tRNA ligase
  • EC number
  • Alternative names
    • Aspartyl-tRNA synthetase
      (AspRS
      )

Gene names

    • Name
      aspS
    • ORF names
      GXZ81_07465

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • AS08sgBPME_367
  • Taxonomic lineage
    Bacteria > Bacillota > Clostridia > Eubacteriales > Oscillospiraceae > Fastidiosipila

Accessions

  • Primary accession
    A0A7C6HLN5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Heterotrimer of A, B and C subunits.
Homodimer.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain157-561Aminoacyl-transfer RNA synthetases class-II family profile
Region204-207Aspartate

Sequence similarities

Belongs to the GatC family.
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    705
  • Mass (Da)
    79,234
  • Last updated
    2020-12-02 v1
  • Checksum
    227BB4FC22B84004
MDKQMKRTKYCGHFSERDVGQEAYAYGWVQSKRDMGGVIFIDLVDREGVLQIVFNPENTDAKTFALAERVRNQSVLEVKGQMHLRDPETVNPKIATGTVELRVKQATLLSAAETLPFVPEESAHVRDELRLRYRYLDLRRSDLRNNLLLRHRASSLIHSFMDSQGFVEVETPVLGKSTPEGARDYLVPSRVHPGSFYALPQSPQIYKQLLMVSGLDRYYQIARCFRDEDLRADRQPEFTQLDLEMSFVEMGDVLELLEALMKHLAWELKGVKIEGAFPRMSWQEAVDKYGSDKPDLRFDLPIVDISDIAAKSDFSIFRQALKSGGVVRAITVPGKADFPRSTIDDLTDFAIAQGAKGMAWIAWRESGEVYSILDKYFSEELMQDLLERVNAQPGDFILFSADQLNTVRRVSGAIRLHLAELLGLCNPEELNFSFIVDFPMFEYSEEEKRYVAQHHPFTMPKVEDLQYLETEPERMNSQAYDLVLNGTELGSGSIRIHDRELQAQVFRQLGLSDEEVQLRFGFLLDAFRFGTPPHGGFALGLDRLVMLLAKAPSLREVIAFPKLSNASDPLTAAPGPVNQAQLDDLHIALSGEVAAGLYASAGEAAAAARTFDLEHLEALSGLRLTPSETAVMQKEIGHLITFADKMKEHNTDDVEPTRSMIKEQRVFQGEIREPSLSQEEALANTALAEDGAFVVPVAVDVEQEL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DUQA01000141
EMBL· GenBank· DDBJ
HHU04824.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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