Q5FQ60 · SYDND_GLUOX
- ProteinAspartate--tRNA(Asp/Asn) ligase
- GeneaspS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids598 (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 | 33 | Important for tRNA non-discrimination | ||||
Sequence: H | ||||||
Binding site | 175 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 221 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 221-223 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RDE | ||||||
Binding site | 452 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 486 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 493 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 538-541 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GVDR |
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Acetobacteraceae > Gluconobacter
Accessions
- Primary accessionQ5FQ60
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000110878 | 1-598 | Aspartate--tRNA(Asp/Asn) ligase | |||
Sequence: MHPYRTHDCSALREENAGQVVRLSGWVHSKRDHGGLLFIDLRDHYGVTQIVIPAGTDLLEKAERLRVESVITVTGKVVVRHGSQRNPNLPTGDVEVLADALEVRSSAEVLPFQVAGNENYPEDLRLKYRYIDLRRDKMHQNIMLRSKVITSLRQRMIEQGFTEFQTPILTASSPEGARDFLVPARLHPGKFYALPQAPQQFKQLAMVAGFDRYFQIAPCFRDEASRADRSPGEFYQLDFEMSFVTQEDVFTVLEPVLAGVFNEFTPEGWKITDGAFPRIPYADAMRDYGSDKPDLRNPLIIKDVTDAFRDSGFGLFAKIAASGGQIRAIPAPGAGDRPRGFFDKLNSWARENGAGGLGYIIFGEEGGKGPIVKNLEADRVESIREICGLKAGDAVFFAAGKGDEVAKFSGVVRTKVATELDLIEKNAFRFCWVVDFPMYELNEETGKVDFSHNPFSMPQGGLEALNTQDPLTINAYQYDIVCNGVELSSGAIRNHLPDVMLRAFEIAGYGPEVVEERFGGMLNAFRYGAPPHGGAAPGVDRIVMLLADEPNIREVILFPLNQSGEDLMMEAPAPVEPARLKELHLALDLPKPKPTASK |
Interaction
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 199-202 | Aspartate | ||||
Sequence: QQFK |
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length598
- Mass (Da)66,287
- Last updated2005-03-01 v1
- ChecksumD6FBBA26A23AF058
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000009 EMBL· GenBank· DDBJ | AAW61486.1 EMBL· GenBank· DDBJ | Genomic DNA |