Q12XU7 · SYDND_METBU
- ProteinAspartate--tRNA(Asp/Asn) ligase
- GeneaspS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids443 (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
Cofactor
Note: Binds 3 Mg2+ cations per subunit. The strongest magnesium site (Mg1) is bound to the beta- and gamma-phosphates of ATP and four water molecules complete its coordination sphere.
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 90 | Important for tRNA non-discrimination | |||
Binding site | 175 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 219 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 219-221 | ATP (UniProtKB | ChEBI) | |||
Binding site | 227-229 | ATP (UniProtKB | ChEBI) | |||
Binding site | 366 | ATP (UniProtKB | ChEBI) | |||
Binding site | 366 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 366 | Mg2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 369 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 369 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 373 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 414-417 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | aminoacyl-tRNA synthetase multienzyme complex | |
Cellular Component | cytosol | |
Molecular Function | aspartate-tRNA ligase activity | |
Molecular Function | aspartate-tRNA(Asn) ligase activity | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | RNA 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
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Methanomicrobia > Methanosarcinales > Methanosarcinaceae > Methanococcoides
Accessions
- Primary accessionQ12XU7
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_1000006702 | 1-443 | Aspartate--tRNA(Asp/Asn) ligase | ||
Interaction
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 197-200 | Aspartate | |||
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length443
- Mass (Da)50,241
- Last updated2006-08-22 v1
- Checksum2B0476A927C48F28
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000300 EMBL· GenBank· DDBJ | ABE51729.1 EMBL· GenBank· DDBJ | Genomic DNA |