A0A369L999 · A0A369L999_9ACTN
- ProteinAlanine--tRNA ligase
- GenealaS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids877 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catalytic activity
- tRNA(Ala) + L-alanine + ATP = L-alanyl-tRNA(Ala) + AMP + diphosphate
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 566 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 570 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 668 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 672 | Zn2+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | alanine-tRNA ligase activity | |
Molecular Function | aminoacyl-tRNA editing activity | |
Molecular Function | ATP binding | |
Molecular Function | tRNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | alanyl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAlanine--tRNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Coriobacteriia > Coriobacteriales > Coriobacteriaceae > Senegalimassilia
Accessions
- Primary accessionA0A369L999
Proteomes
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 4-711 | Alanyl-transfer RNA synthetases family profile | |||
Domain
Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length877
- Mass (Da)95,298
- Last updated2018-11-07 v1
- MD5 Checksum4F50E5DF2ECDC88CEB858189B2EFCB33
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
PPTP01000003 EMBL· GenBank· DDBJ | RDB56231.1 EMBL· GenBank· DDBJ | Genomic DNA |