A0A4U7J9J7 · A0A4U7J9J7_9FIRM

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

Features

Showing features for binding site.

159350100150200250300350400450500550
TypeIDPosition(s)Description
Binding site181L-aspartate (UniProtKB | ChEBI)
Binding site227L-aspartate (UniProtKB | ChEBI)
Binding site227-229ATP (UniProtKB | ChEBI)
Binding site236ATP (UniProtKB | ChEBI)
Binding site455L-aspartate (UniProtKB | ChEBI)
Binding site489ATP (UniProtKB | ChEBI)
Binding site496L-aspartate (UniProtKB | ChEBI)
Binding site541-544ATP (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

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
      EHE19_011605

Organism names

Accessions

  • Primary accession
    A0A4U7J9J7

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain148-562Aminoacyl-transfer RNA synthetases class-II family profile
Region205-208Aspartate

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
    593
  • Mass (Da)
    67,257
  • Last updated
    2019-07-31 v1
  • MD5 Checksum
    33816DEC40D8D138735A8748DE1FA042
MGESIYGLKRSHKCTELGVENIGETVTVMGWVQKQRDLGSLVFVDLRDISGILQIVFTDKDGEMFERAKTIRSEFVLAVVGTVSARAPEAVNKKMATGAIEITAKELRILSTAETPPIYIEENLDANEMTRLKYRYLDLRRPDMQRNFILRHRVAKVARDYYDENGFLEVETPILIKSTPEGARDYLVPSRVHQGKFFALPQSPQLYKQLLMVSGFDRYFQIAKCFRDEDLRADRQPEFTQIDIEMSFVNVDDVITCNEGFIKRAFKEALGVELETPFIRMPYAEAMERFGSDKPDIRFGMELVNMSDLVANCGFKVFTDAIASGGSVRAINAKGCSKFSRKEIDALVEVVKTYKAKGMAWVSISADNEIKSSFAKFMTEEEMKALLERADAQPGDLICFVADKNDIVFDALGQLRLEVARRLNILNPDEFKFLWVTEFPLFEYDEEEKRYVAKHHPFTCPMDEDLELLDTDPGKVRAKAYDIVLNGVELGGGSIRIHIQDLQAKMLEMLGFTEEDANRKFGFLLNAFKYGTPPHGGMAFGLDRMIMLMAKTDSIRDVIAFPKVQNSSSPMDNAPDIVDEGQLEELHIRITKD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP061336
EMBL· GenBank· DDBJ
QNU65572.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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