A0A2M7B5H3 · A0A2M7B5H3_9BACT
- ProteinAspartate--tRNA(Asp/Asn) ligase
- GeneaspS
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids467 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Catalytic activity
- ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx)
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 28 | Important for tRNA non-discrimination | ||||
Sequence: H | ||||||
Site | 79 | Important for tRNA non-discrimination | ||||
Sequence: G | ||||||
Binding site | 172 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 218 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 218-220 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RDE | ||||||
Binding site | 227 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 324 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 362 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 369 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 414-417 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GLDR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | aspartate-tRNA ligase activity | |
Molecular Function | aspartate-tRNA(Asn) ligase activity | |
Molecular Function | ATP binding | |
Molecular Function | nucleic acid binding | |
Biological Process | aspartyl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAspartate--tRNA(Asp/Asn) ligase
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageBacteria > Candidatus Wolfebacteria
Accessions
- Primary accessionA0A2M7B5H3
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 142-435 | Aminoacyl-transfer RNA synthetases class-II family profile | ||||
Sequence: RAEIEKFIRDFLTGMDFTEIETPILSKSTPEGARDYLVPSRLHEGKFYALPQSPQQYKQLLMVAGLEKYFQIVRCFRDEDTRGDRQPEFTQLDIEMSFIEEEDVLNLIETLYTELVGKLYPDKKIQQTPFVRLSHKEAMEKYNSDKPDLRKDKDNPDELAFVFVVDFPMFEWKETEKRWDAVHHPFTLPKVKDKNDFLAQFKKEPAKIKAYQYDLVLNGYEIAGGSIRIHDSELLAAVFEVMGNEPEEVREKFGHMFEAFKYGVPPHGGIASGLDRFVAILQNEPNIREVIAFP | ||||||
Region | 196-199 | Aspartate | ||||
Sequence: QQYK |
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length467
- Mass (Da)54,397
- Last updated2018-04-25 v1
- Checksum9C4B654BB8DC31A7