A0A926NWX1 · A0A926NWX1_9HYPH
- ProteinGlutamate--tRNA ligase
- GenegltX
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids474 (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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Stappiaceae > Roseibium
Accessions
- Primary accessionA0A926NWX1
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain, motif, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-307 | Glutamyl/glutaminyl-tRNA synthetase class Ib catalytic | ||||
Sequence: VVTRFAPSPTGYLHIGGARTALFNWLFSRHHGGKMLLRIEDTDRARSTQEAVDAILDGLTWLGLDWDGEPISQASRVDRHKEVVEQMLAQGKAYRCYATQEDLAAMREKARAEGRPPRYDGTWRDRDPSEAPEGVAPAIRLKAPLEGETVVDDLVQGRVTFPNKDLDDLVLMRSDGTPTYMLAVVVDDHDMGITHIIRGDDHLTNAARQTLIFQAMGWDVPVMAHIPLIHGPDGAKLSKRHGALGAEAYRAMGYLPEAMRNYLARLGWSHGDEEIMSTDDMIKWFGMEAVGKSPARFDFKKLE | ||||||
Motif | 11-21 | 'HIGH' region | ||||
Sequence: PSPTGYLHIGG | ||||||
Compositional bias | 113-135 | Basic and acidic residues | ||||
Sequence: KARAEGRPPRYDGTWRDRDPSEA | ||||||
Region | 113-137 | Disordered | ||||
Sequence: KARAEGRPPRYDGTWRDRDPSEAPE | ||||||
Motif | 240-244 | 'KMSKS' region | ||||
Sequence: KLSKR | ||||||
Domain | 342-471 | Aminoacyl-tRNA synthetase class I anticodon-binding | ||||
Sequence: WLAEADHEATALAALPGLKERAKTLVELTESASYLWRQRPLDCDEKAANILNDEARALLSGLHETLSAVPTWEAEALEVSVKAFAEEKELKLGKVAQPLRAALTGRGTSPGIYDVLVALGREESLNRIRD |
Sequence similarities
Family and domain databases
Sequence
- Sequence statusComplete
- Length474
- Mass (Da)52,581
- Last updated2023-02-22 v1
- Checksum65D0469459CD0374
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 113-135 | Basic and acidic residues | ||||
Sequence: KARAEGRPPRYDGTWRDRDPSEA |