A0A7C6HLN5 · A0A7C6HLN5_9FIRM
- ProteinAspartate--tRNA ligase
- GeneaspS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids705 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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).
Catalytic activity
- ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H+ + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate
- ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H+ + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 180 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 226 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 226-228 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RDE | ||||||
Binding site | 235 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 454 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 488 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 495 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 540-543 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GLDR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | aspartate-tRNA ligase activity | |
Molecular Function | ATP binding | |
Molecular Function | nucleic acid binding | |
Molecular Function | transferase activity | |
Biological Process | aspartyl-tRNA aminoacylation | |
Biological Process | regulation of translational fidelity |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAspartate--tRNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Oscillospiraceae > Fastidiosipila
Accessions
- Primary accessionA0A7C6HLN5
Proteomes
Subcellular Location
Interaction
Subunit
Heterotrimer of A, B and C subunits.
Homodimer.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 157-561 | Aminoacyl-transfer RNA synthetases class-II family profile | ||||
Sequence: IHSFMDSQGFVEVETPVLGKSTPEGARDYLVPSRVHPGSFYALPQSPQIYKQLLMVSGLDRYYQIARCFRDEDLRADRQPEFTQLDLEMSFVEMGDVLELLEALMKHLAWELKGVKIEGAFPRMSWQEAVDKYGSDKPDLRFDLPIVDISDIAAKSDFSIFRQALKSGGVVRAITVPGKADFPRSTIDDLTDFAIAQGAKGMAWIAWRESGEVYSILDKYFSEELMQDLLERVNAQPGDFILFSADQLNTVRRVSGAIRLHLAELLGLCNPEELNFSFIVDFPMFEYSEEEKRYVAQHHPFTMPKVEDLQYLETEPERMNSQAYDLVLNGTELGSGSIRIHDRELQAQVFRQLGLSDEEVQLRFGFLLDAFRFGTPPHGGFALGLDRLVMLLAKAPSLREVIAFP | ||||||
Region | 204-207 | Aspartate | ||||
Sequence: QIYK |
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 statusComplete
- Length705
- Mass (Da)79,234
- Last updated2020-12-02 v1
- Checksum227BB4FC22B84004