A0A1G7EQS4 · A0A1G7EQS4_9DEIN
- ProteinGlutamate--tRNA ligase
- GenegltX
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids468 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic activity
- tRNA(Glu) + L-glutamate + ATP = L-glutamyl-tRNA(Glu) + AMP + diphosphate
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | glutamate-tRNA ligase activity | |
Molecular Function | tRNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | glutamyl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlutamate--tRNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Deinococcota > Deinococci > Thermales > Thermaceae > Thermus
Accessions
- Primary accessionA0A1G7EQS4
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for domain, motif, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-312 | Glutamyl/glutaminyl-tRNA synthetase class Ib catalytic | ||||
Sequence: VVTRIAPSPTGDPHVGTAYIALFNYAWARKNGGRFIVRIEDTDRTRYVPGAEERILAALRWLGLTYDEGPDVGGPHGPYRQSERLPLYKGHAEELLKRGWAYRAFETPEELEQIRKEKGGYDGRARNIPPEEAEERARRGEPHVIRLKVPRPGTTEVKDELRGVVVYDNQEIPDVVLLKSDGYPTYHLANVVDDHLMGVTDVIRAEEWLVSTPIHVLLYRAFGWEAPRFYHMPLLRNPDKTKISKRKSHTSLDWYKAEGFLPEALRNYLGLMGFSMPDGREIFTLEEFIQAFTWERVSLGGPVFDLEKLRW | ||||||
Motif | 8-18 | 'HIGH' region | ||||
Sequence: PSPTGDPHVGT | ||||||
Region | 121-140 | Disordered | ||||
Sequence: GYDGRARNIPPEEAEERARR | ||||||
Motif | 243-247 | 'KMSKS' region | ||||
Sequence: KISKR | ||||||
Domain | 326-466 | Aminoacyl-tRNA synthetase class I anticodon-binding | ||||
Sequence: EVAERVKPFLREAGLSWESEAYLRRAVELMRPRFDTLKEFPEKARYLFTEDYPVSEKAKRALEEGLPLLRELYPRLEAQEEWSEAALEALLRGFAAEKGVKLGQVAQPLRAALTGSLETPGLFEILALLGKGRALSRLARV |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length468
- Mass (Da)53,585
- Last updated2017-11-22 v1
- Checksum9EFD3BFA8860A457