A0A8J4WMH2 · A0A8J4WMH2_9BACT
- ProteinAspartate--tRNA(Asp/Asn) ligase
- GeneaspS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids590 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
- tRNA(Asx) + L-aspartate + ATP = L-aspartyl-tRNA(Asx) + AMP + diphosphate
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 31 | Important for tRNA non-discrimination | |||
Site | 83 | Important for tRNA non-discrimination | |||
Binding site | 174 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 220 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 220-222 | ATP (UniProtKB | ChEBI) | |||
Binding site | 229 | ATP (UniProtKB | ChEBI) | |||
Binding site | 448 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 483 | ATP (UniProtKB | ChEBI) | |||
Binding site | 490 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 535-538 | 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 | |
Biological Process | aspartyl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAspartate--tRNA(Asp/Asn) ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Verrucomicrobiota > Spartobacteria > Chthoniobacterales > Chthoniobacteraceae > Candidatus Udaeobacter
Accessions
- Primary accessionA0A8J4WMH2
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 149-556 | Aminoacyl-transfer RNA synthetases class-II family profile | |||
Region | 198-201 | Aspartate | |||
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length590
- Mass (Da)66,955
- Last updated2022-05-25 v1
- Checksum4394BEEA47918F8C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAALOD010000051 EMBL· GenBank· DDBJ | KAF5407826.1 EMBL· GenBank· DDBJ | Genomic DNA |