A0A102U6Z1 · A0A102U6Z1_BURCE
- ProteinAspartate--tRNA(Asp/Asn) ligase
- GeneaspS
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids600 (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
- tRNA(Asx) + L-aspartate + ATP = L-aspartyl-tRNA(Asx) + AMP + diphosphate
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 32 | Important for tRNA non-discrimination | |||
Site | 83 | Important for tRNA non-discrimination | |||
Binding site | 174 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 220 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 220-222 | ATP (UniProtKB | ChEBI) | |||
Binding site | 229 | ATP (UniProtKB | ChEBI) | |||
Binding site | 457 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 491 | ATP (UniProtKB | ChEBI) | |||
Binding site | 498 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 543-546 | ATP (UniProtKB | ChEBI) | |||
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
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Burkholderia > Burkholderia cepacia complex
Accessions
- Primary accessionA0A102U6Z1
- Secondary accessions
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 141-564 | Aminoacyl-transfer RNA synthetases class-II family profile | |||
Region | 198-201 | Aspartate | |||
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length600
- Mass (Da)67,727
- Last updated2016-04-13 v1
- Checksum177BBA564629909A
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP013443 EMBL· GenBank· DDBJ | AOK17728.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LOYH01000049 EMBL· GenBank· DDBJ | KVK82724.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JAEDXG010000014 EMBL· GenBank· DDBJ | MBH9698039.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
QLUZ01000002 EMBL· GenBank· DDBJ | RAQ15219.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
UARD01000023 EMBL· GenBank· DDBJ | SPV20652.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
SNSQ01000022 EMBL· GenBank· DDBJ | TEU45194.1 EMBL· GenBank· DDBJ | Genomic DNA |