A0A4U7J9J7 · A0A4U7J9J7_9FIRM
- ProteinAspartate--tRNA ligase
- GeneaspS
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids593 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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).
Catalytic activity
- tRNA(Asp) + L-aspartate + ATP = L-aspartyl-tRNA(Asp) + AMP + diphosphate
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 181 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 227 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 227-229 | ATP (UniProtKB | ChEBI) | |||
Binding site | 236 | ATP (UniProtKB | ChEBI) | |||
Binding site | 455 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 489 | ATP (UniProtKB | ChEBI) | |||
Binding site | 496 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 541-544 | ATP (UniProtKB | ChEBI) | |||
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 |
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
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Oscillospiraceae > Ruminiclostridium
Accessions
- Primary accessionA0A4U7J9J7
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 148-562 | Aminoacyl-transfer RNA synthetases class-II family profile | |||
Region | 205-208 | Aspartate | |||
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length593
- Mass (Da)67,257
- Last updated2019-07-31 v1
- MD5 Checksum33816DEC40D8D138735A8748DE1FA042
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP061336 EMBL· GenBank· DDBJ | QNU65572.1 EMBL· GenBank· DDBJ | Genomic DNA |