Q12XU7 · SYDND_METBU

Function

function

Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 3 Mg2+ cations per subunit. The strongest magnesium site (Mg1) is bound to the beta- and gamma-phosphates of ATP and four water molecules complete its coordination sphere.

Features

Showing features for site, binding site.

Type
IDPosition(s)Description
Site90Important for tRNA non-discrimination
Binding site175L-aspartate (UniProtKB | ChEBI)
Binding site219L-aspartate (UniProtKB | ChEBI)
Binding site219-221ATP (UniProtKB | ChEBI)
Binding site227-229ATP (UniProtKB | ChEBI)
Binding site366ATP (UniProtKB | ChEBI)
Binding site366Mg2+ 2 (UniProtKB | ChEBI)
Binding site366Mg2+ 3 (UniProtKB | ChEBI)
Binding site369L-aspartate (UniProtKB | ChEBI)
Binding site369Mg2+ 2 (UniProtKB | ChEBI)
Binding site373L-aspartate (UniProtKB | ChEBI)
Binding site414-417ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentaminoacyl-tRNA synthetase multienzyme complex
Cellular Componentcytosol
Molecular Functionaspartate-tRNA ligase activity
Molecular Functionaspartate-tRNA(Asn) ligase activity
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular FunctionRNA binding
Biological Processaspartyl-tRNA aminoacylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Aspartate--tRNA(Asp/Asn) ligase
  • EC number
  • Alternative names
    • Aspartyl-tRNA synthetase
      (AspRS
      )
    • Non-discriminating aspartyl-tRNA synthetase
      (ND-AspRS
      )

Gene names

    • Name
      aspS
    • Ordered locus names
      Mbur_0772

Organism names

Accessions

  • Primary accession
    Q12XU7

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000067021-443Aspartate--tRNA(Asp/Asn) ligase

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region197-200Aspartate

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    443
  • Mass (Da)
    50,241
  • Last updated
    2006-08-22 v1
  • Checksum
    2B0476A927C48F28
MSLETPRTHYTSQIDIEQIGDDKVTVCGWVHEVRDLGGICFVVVRDREGRAQITLVKKKIDKEIFDAARKLVRESIVAVTGTAKAEGKAPNGYEIIPESIVVLNEAESPLPMDTTGKVDAELDTRLDSRFMDLRRERTTAIFKIRHEVLRAVRDFLSKDGYIETCSPKVVATATEGGTSLFPITYFDREAFLNQSPQLFKQILMSGGLDKVFEIGPIFRAEEHDTRRHLNEATSIDIEASFLDHFDVMEVLEDMVAYVYEQVIENEAASLKALDIELSVPKTPFMKVPYSQAIDIVNAESEETVEWGGDLGTVAEHTIGEHVFKETGESHYFITDWPTEIKPFYAMPYEDNPLISKSFDMMHRTMELSSGAQRIHIHDMLKARIESQGLDSDGFDFYLRAFKYGMPPHSGWGIGCERLVMTMLSVENIRDTVLFPRDRKRLSP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000300
EMBL· GenBank· DDBJ
ABE51729.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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