A5EML9 · SYA_BRASB
- ProteinAlanine--tRNA ligase
- GenealaS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids896 (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
- ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | alanine-tRNA ligase 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 > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Nitrobacteraceae > Bradyrhizobium
Accessions
- Primary accessionA5EML9
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000347512 | 1-896 | Alanine--tRNA ligase | |||
Sequence: MSGVNEIRSTFLNFFAANGHEIVPSSPLVPRNDPTLMFTNAGMVQFKNVFTGVEKRPYHRATTSQKCVRAGGKHNDLDNVGYTARHHTFFEMLGNFSFGDYFKENAIELAWKLVTKEFGLPKDKLTATVYIDDDEAFGLWKKIAGLPESRIIRIAGSDNFWQMGDTGPCGPCSEIFYDHGDKVWGGPPGSPEADGDRFIEIWNLVFMQYEQLEGGVRNPLPKPSIDTGAGLERVAAVLQGKHDNYDIDLFVALIRAIADLTNADPQGPQKASLRVIADHLRASSFLISDGVLPSNEGRGYVLRRIMRRAMRHAQLLGAREPLMHKLVGALTREMGQAYPELIRAEALIKETLRLEETRFRKTLERGLAILDEKSSTLKKGDMFDGDVAFTLYDTYGFPLDLTQDALKSRGISVDQASFTDAMERQRAKARAAWAGSGEAATENVWFPLREKLGATEFLGYETETAEGAVTALVKDGAEVEGLKAGESGAIVLNQTPFYGESGGQVGDTGVMSGDGVRVRITDTQKKAGDLFVHIGTVEQGTLKLGAALQLEVDHGRRSAIRANHSATHILHEALRQVLGDHIAQRGSLVSPDRLRFDFAHPKPISAEELARVEDIANDVVLENAEVTTRLMALDDAREAGARALFGEKYGDEVRVVSMGNAARDQASNAQASNAMGWSVELCGGTHVKRTGDIGLIAVTSESAVSSGVRRIEALTARGARAHANHNLSLAKAAAAELRTTVDEVPARIAALMEERKKLERELSDARKKLAMGGGAAAGGSASGIREVAGVKLMARAVEGVEMKDLKSLVDEAKKQLGSGVVAIVGRAEDGKAGVVVGVTADLTARFNAVELVRAASEALGGKGGGGRPDMAQAGGPDGSKAEAALAAIESAISRAG |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 859-878 | Disordered | ||||
Sequence: LGGKGGGGRPDMAQAGGPDG |
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
- Length896
- Mass (Da)96,149
- Last updated2007-06-12 v1
- Checksum6194E916C462EE8C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000494 EMBL· GenBank· DDBJ | ABQ37413.1 EMBL· GenBank· DDBJ | Genomic DNA |