A0A102U6Z1 · A0A102U6Z1_BURCE

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

Features

Showing features for site, binding site.

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Type
IDPosition(s)Description
Site32Important for tRNA non-discrimination
Site83Important for tRNA non-discrimination
Binding site174L-aspartate (UniProtKB | ChEBI)
Binding site220L-aspartate (UniProtKB | ChEBI)
Binding site220-222ATP (UniProtKB | ChEBI)
Binding site229ATP (UniProtKB | ChEBI)
Binding site457L-aspartate (UniProtKB | ChEBI)
Binding site491ATP (UniProtKB | ChEBI)
Binding site498L-aspartate (UniProtKB | ChEBI)
Binding site543-546ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionaspartate-tRNA ligase activity
Molecular Functionaspartate-tRNA(Asn) ligase activity
Molecular FunctionATP binding
Molecular Functionnucleic acid 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
    • ORF names
      DPR02_04255
      , E3D37_19890
      , JAO13_16505
      , NCTC10661_04018
      , WS90_14905
      , WT26_18060

Organism names

  • Taxonomic identifier
  • Strains
    • 871
    • MSMB1302
    • MSMB1184WGS
    • PT02
    • NCTC10661
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Burkholderia > Burkholderia cepacia complex

Accessions

  • Primary accession
    A0A102U6Z1
  • Secondary accessions
    • A0A1I0LCD3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain141-564Aminoacyl-transfer RNA synthetases class-II family profile
Region198-201Aspartate

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    600
  • Mass (Da)
    67,727
  • Last updated
    2016-04-13 v1
  • Checksum
    177BBA564629909A
MSMRTEYCGLVTEHLLGQTVSLCGWVQRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFATAEGVRNEFCVQIKGLVRNRPDGTVNAGLKSGKIEVLCHELNVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTIDVELDAKFPVMPYSEAMARFGSDKPDLRVQLEFTELTDAMKDVDFKVFSTPANAKDGRVAALRVPKGGELSRGDIDGYTEFVRIYGAKGLAWIKVNEKAKGRDGLQSPIVKNLHDASIAAILERTGAEDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVQAGWKPLWVVDFPMFEYDDEDARYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDMVLNGWEIGGGSVRIYQEEVQSKVFRALKIGAEEAQLKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQDLLTQAPSPVDERQLRELHIRLRQPEQPKA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP013443
EMBL· GenBank· DDBJ
AOK17728.1
EMBL· GenBank· DDBJ
Genomic DNA
LOYH01000049
EMBL· GenBank· DDBJ
KVK82724.1
EMBL· GenBank· DDBJ
Genomic DNA
JAEDXG010000014
EMBL· GenBank· DDBJ
MBH9698039.1
EMBL· GenBank· DDBJ
Genomic DNA
QLUZ01000002
EMBL· GenBank· DDBJ
RAQ15219.1
EMBL· GenBank· DDBJ
Genomic DNA
UARD01000023
EMBL· GenBank· DDBJ
SPV20652.1
EMBL· GenBank· DDBJ
Genomic DNA
SNSQ01000022
EMBL· GenBank· DDBJ
TEU45194.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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