A2BIS1 · A2BIS1_HYPBU
- ProteinAspartate--tRNA ligase
- GeneaspS
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids442 (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
- ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)
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 binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 173 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 217 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 217-219 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RAE | ||||||
Binding site | 225-227 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RHL | ||||||
Binding site | 365 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 365 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 365 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 368 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 368 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 372 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 413-416 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GLER |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | aminoacyl-tRNA synthetase multienzyme complex | |
Cellular Component | cytosol | |
Molecular Function | aspartate-tRNA 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 ligase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Desulfurococcales > Pyrodictiaceae > Hyperthermus
Accessions
- Primary accessionA2BIS1
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 140-442 | Aminoacyl-transfer RNA synthetases class-II family profile | ||||
Sequence: MRIAAEVARAAREWFVENGFIEIFTPKIVGAATEGGAEVFSIVYFDKPAFLAQSPQLYKQMGVIAGLEKVFEIGPAFRAEPHHTTRHLTEYTSIDLEMGFIDSYEDVMDIVEAVIRHVISSVLSRYRSEIKEYFPNAITEPPKEIPRITIREAYKLLEAAGTPVEWGEDLSSEAERKLGEIVEREYGSYLVFVTEYPWAVRPFYTMRKSDEPDWTYSFDLLMRGLEIATGGQREHRYDVLVKQLEEKGLNPRNFEWYLAMFRYGAPPHGGAGIGLERVVMQLLGLGNIREARMLPRDPERLVP | ||||||
Region | 195-198 | Aspartate | ||||
Sequence: QLYK |
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length442
- Mass (Da)50,581
- Last updated2007-02-20 v1
- Checksum422ABDB8AD05AA4A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000493 EMBL· GenBank· DDBJ | ABM79912.1 EMBL· GenBank· DDBJ | Genomic DNA |