Q8NQ22 · SYA_CORGL
- ProteinAlanine--tRNA ligase
- GenealaS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids888 (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.
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
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Corynebacteriaceae > Corynebacterium
Accessions
- Primary accessionQ8NQ22
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000075099 | 1-888 | Alanine--tRNA ligase | |||
Sequence: MQTHEIRERFTNHFVNAGHQAVPSASLILDDPNLLFVNAGMVPFKPYFLGQQTPPFENGTATSIQKCVRTLDIEEVGITTRHNTFFQMAGNFSFGQYFKEGAITHAWGLLTGSVADGGFGLDPERLWVTVYLDDDEAAEIWEKKIGVPSERIQRLGMADNYWSMGVPGPCGPCSEIYYDRGEKYGKEGGPVADDNRYMEIWNLVFMEKERGQGIGKDNFDILGDLPKKNIDTGMGVERVACILQDVENVYETDLLRPVIDVAETLTGTKYGSDNTSDIRFRVIADHSRTGMMLILDGVTPGNEGRGYILRRLLRRIIRSARLLGATGETMEQFMNTIMDTMTPSYPEIADNRERIMRVAVTEERAFLKTLVSGTHLFEEAATSIKAAGSTKVAGAQAFALHDTYGFPIDLTLEMAAEAGLEVDVEGFDSLMAEQRSRAKADSQAKKHGHTDLSIYREWVDNNPTVFTGFEELDSQSKVLGLLSDGAKISEATEGQEVEVILDQSPLYAESGGQLGDRGQILLGDTVLDVHDVQKIGKKLWVHKALVANGGLAVGDEVVASVDKQWRHAARQAHTATHLIHAALRQVLGPTALQAGSMNKPGYLRFDFNYTEQLTPAQVEQIQAITNEAVDTDWAVNTVETSLEEAKAMGAMALFGENYGSTVRVVEIGGPFSMELCGGTHVAHSSQIGPVALLGESSIGSGVRRIEAYSGLNSFNYLSKERALAEGLASSLKAPSEELPERVAQLVDKLKAAEKEIEALHRQQLMAQTADLLNNAQEIGGVTTLLLRVKDNTNAGDLRTIATTLKDKLGDREGVLVIASDNAGKVPFVVAATKAAVARGAHSGNLVKLVGSYIDGRGGGKADLAQGSGANIAGLESAFGAVRAEIEAL |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
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
- Length888
- Mass (Da)96,226
- Last updated2002-10-25 v1
- Checksum18AE4DC95F5DDD59
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BA000036 EMBL· GenBank· DDBJ | BAB99025.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX927152 EMBL· GenBank· DDBJ | CAF21641.1 EMBL· GenBank· DDBJ | Genomic DNA |