A0A015TVY8 · A0A015TVY8_BACFG
- ProteinGlutamate--tRNA ligase
- GenegltX
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids505 (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 | cytoplasm | |
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 > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Bacteroides
Accessions
- Primary accessionA0A015TVY8
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-343 | Glutamyl/glutaminyl-tRNA synthetase class Ib catalytic | ||||
Sequence: KVRVRFAPSPTGALHIGGVRTALYNYLFARQHGGDLIFRIEDTDSNRFVPGAEEYILESFKWLGIQFDEGVSFGGEYGPYRQSERREIYKKYVQVLLDNGKAYIAFDTPEELDAKRAEIANFQYDASTRVGMRNSLTLPKEEVEALIADGKQYVVRFKIEPNEDIHVNDLIRGEVVINSSILDDKVLYKSADELPTYHLANIVDDHLMEVSHVIRGEEWLPSAPLHVLLYRAFGWEDTMPAFAHLPLLLKPEGNGKLSKRDGDRLGFPVFPLEWHDPKSGEISSGYRESGYLPEAVINFLALLGWNPGNDQEVMSMDELIRLFDLHRCSKSGAKFDYKK | ||||||
Motif | 12-22 | 'HIGH' region | ||||
Sequence: PSPTGALHIGG | ||||||
Motif | 260-264 | 'KMSKS' region | ||||
Sequence: KLSKR | ||||||
Domain | 376-500 | Aminoacyl-tRNA synthetase class I anticodon-binding | ||||
Sequence: PFEKVVTVVGMMKDRVSFVKELWEVCSFFFVAPTEYDEKTVKKRWKEDSAKCITELAEVLAGIEDFSIEGQEKIVMDWIAEKGYHTGNIMNAFRLTLVGEGKGPHMFDISWVLGKEETLARMKRA |
Sequence similarities
Family and domain databases
Sequence
- Sequence statusComplete
- Length505
- Mass (Da)57,704
- Last updated2014-06-11 v1
- ChecksumCD00B7BFC31BFE0D
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JGDB01000278 EMBL· GenBank· DDBJ | EXY88564.1 EMBL· GenBank· DDBJ | Genomic DNA |