B2UKT4 · SYA_AKKM8
- ProteinAlanine--tRNA ligase
- GenealaS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids942 (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 | 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 > Verrucomicrobiota > Verrucomicrobiia > Verrucomicrobiales > Akkermansiaceae > Akkermansia
Accessions
- Primary accessionB2UKT4
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000347482 | 1-942 | Alanine--tRNA ligase | |||
Sequence: MMTATEIRQSFLDFFREKQHTVVPSASLMPQSPGLLFTNAGMNQFVPYFLGVWTPPWTPARATDTQKCIRAGGKHNDLEDVGYDSYHHTFFEMLGNWSFGDYFKREAIRWAWELVVERWGFPAERLYATVYAPDKSKGDPGEFDREAWDFWAELFRSRGLDPDVHIVHGNVKDNFWMMGETGPCGPCSELHVDLTPEGNTKGSLVNKDSDQCIEIWNLVFIQYNAESDGSMRNLPACHVDTGMGFERACSIMQCTNGFKDFSRKPSNYATDVFRPLFDRLEVLSGRKYADVYPAPGSKRVDAEDGTLQEAIAFRVIADHLRTLSFSIADGILPGNNGRNYVLRRILRRAVRYGRRLGFTQPFLAELVDTLVESFGQVFPELAARATTVKEVLNREEASFNETLDRGLELFDAETASAGKVSGEFAFKLYDTYGFPIDLTALLAEERGLDIDMERFNRLMEEQRERARAARKSEVVRALDLKTDAVTEFTGYDVDECAATVLEVSRQGDSLFIITDKTPFYAEMGGQVSDAGLIEIGGESYHVMAVQQIGNARAHVVEARPGLEVKPGDRVHLSIDAERRRRIEAHHTATHLLHCALHQVVSPDAAQQGSFVSEDRLRFDFNSSAVSPDQLRLIEEKVNGWIEESLPVHCTERAYADVKGNAAIAQFFGDKYGDVVRVVQVGGCRDGLDGVSMEFCGGTHIANTKNIGLFKIKSEGAIASGVRRIEAMTGDAALEMIRQHVVAKSLEIAKAVEKIKEVNYELADMGLEQVPVPTIEGKPGLTALGASDIRTVNDSLARFDASVEHFKQTALDAEKKLKKARAGQSAAKADALLNEWLSDAPSSLIQVAEGAGELLQELLNGLKKRQYAGAAFLLCVDSSSLLLGAYCGKDAIADGLSAGDMIREVAALAGGKGGGRADQARGSAPQDADPQALAAAARNIING |
Proteomic databases
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
- Length942
- Mass (Da)103,645
- Last updated2008-07-01 v1
- ChecksumED53F46EB999D0D9
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001071 EMBL· GenBank· DDBJ | ACD05207.1 EMBL· GenBank· DDBJ | Genomic DNA |