F8IE36 · F8IE36_ALIAT
- ProteinGlutamate--tRNA ligase
- GenegltX
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids513 (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
- ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
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
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Alicyclobacillaceae > Alicyclobacillus
Accessions
- Primary accessionF8IE36
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-339 | Glutamyl/glutaminyl-tRNA synthetase class Ib catalytic | ||||
Sequence: EVRVRFAPSPTGALHIGGARTAYFNWLFARKHGGKFVLRIDDTDRARSTEASYQQILEGLRWLGILWDEGPDVGGPYGPYRQSERMHIYRRHLDRLLAEDKAYPCFCTPEELARDREAAQREGKPPRYVGRCRQLSPEERSRRIAAGEPHVYRIRSRVEGETVVHDLIRGDVAFANSEIDDFIIWKADDTPTYHFASCVDDVEMKISHVIRAEEHLSNTPRHIVLFEALGAEPPAFAHVPMILAPDRSKLSKRHGATSVSEYRDMGILPEALVNYLLLLGFSPGDDREIVDRETAIQLFDLEKVAKHAAIYDVKKLEW | ||||||
Motif | 29-39 | 'HIGH' region | ||||
Sequence: PSPTGALHIGG | ||||||
Motif | 270-274 | 'KMSKS' region | ||||
Sequence: KLSKR | ||||||
Domain | 379-500 | Aminoacyl-tRNA synthetase class I anticodon-binding | ||||
Sequence: WIRTVIAFVQTRSRNLQELVDGLQPYFEPVRAYDEKGVRKHFAHPETASRLRTVADRLTEVAPFLAPVVEREFRQWIEDMGVKSGELIHPVRLAITGLTVGPGLFDVIALIGRDEAVRRLRE |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length513
- Mass (Da)58,298
- Last updated2011-09-21 v1
- Checksum7FCD018D5698614F
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP002902 EMBL· GenBank· DDBJ | AEJ43878.1 EMBL· GenBank· DDBJ | Genomic DNA |