A2BIS1 · A2BIS1_HYPBU

Function

function

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.

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 binding site.

TypeIDPosition(s)Description
Binding site173L-aspartate (UniProtKB | ChEBI)
Binding site217L-aspartate (UniProtKB | ChEBI)
Binding site217-219ATP (UniProtKB | ChEBI)
Binding site225-227ATP (UniProtKB | ChEBI)
Binding site365ATP (UniProtKB | ChEBI)
Binding site365Mg2+ 2 (UniProtKB | ChEBI)
Binding site365Mg2+ 3 (UniProtKB | ChEBI)
Binding site368L-aspartate (UniProtKB | ChEBI)
Binding site368Mg2+ 2 (UniProtKB | ChEBI)
Binding site372L-aspartate (UniProtKB | ChEBI)
Binding site413-416ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentaminoacyl-tRNA synthetase multienzyme complex
Cellular Componentcytosol
Molecular Functionaspartate-tRNA 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 ligase
  • EC number
  • Alternative names
    • Aspartyl-tRNA synthetase
      (AspRS
      )

Gene names

    • Name
      aspS
    • Ordered locus names
      Hbut_0034

Organism names

Accessions

  • Primary accession
    A2BIS1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain140-442Aminoacyl-transfer RNA synthetases class-II family profile
Region195-198Aspartate

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    442
  • Mass (Da)
    50,581
  • Last updated
    2007-02-20 v1
  • Checksum
    422ABDB8AD05AA4A
MPLKLRERVYIRDLLEKGVIGNEYTVAGWVDTVRVHGGLVFVVVRDRTGKMQLVVKRNISREAWEHARKLAPESVVAARGRLVESKAALGGRELQVYELEVLNKADPLPIDIYAPDKTTLAKRLDWRFLDLRNPRNQLIMRIAAEVARAAREWFVENGFIEIFTPKIVGAATEGGAEVFSIVYFDKPAFLAQSPQLYKQMGVIAGLEKVFEIGPAFRAEPHHTTRHLTEYTSIDLEMGFIDSYEDVMDIVEAVIRHVISSVLSRYRSEIKEYFPNAITEPPKEIPRITIREAYKLLEAAGTPVEWGEDLSSEAERKLGEIVEREYGSYLVFVTEYPWAVRPFYTMRKSDEPDWTYSFDLLMRGLEIATGGQREHRYDVLVKQLEEKGLNPRNFEWYLAMFRYGAPPHGGAGIGLERVVMQLLGLGNIREARMLPRDPERLVP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000493
EMBL· GenBank· DDBJ
ABM79912.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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