A0A6A7XZQ6 · A0A6A7XZQ6_9HYPH
- ProteinGlutamine synthetase
- GeneglnA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids469 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.
Catalytic activity
- ATP + L-glutamate + NH4+ = ADP + H+ + L-glutamine + phosphate
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 209 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 265-266 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: NG | ||||||
Binding site | 272-274 | ATP (UniProtKB | ChEBI) | ||||
Sequence: HQS | ||||||
Binding site | 322 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 328 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 340 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 340 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 353 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 360 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | glutamine synthetase activity | |
Biological Process | glutamine biosynthetic process | |
Biological Process | nitrogen fixation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlutamine synthetase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Segnochrobactraceae > Segnochrobactrum
Accessions
- Primary accessionA0A6A7XZQ6
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 398 | O-AMP-tyrosine | ||||
Sequence: Y |
Keywords
- PTM
Interaction
Subunit
Oligomer of 12 subunits arranged in the form of two hexagons.
Oligomer of 12 subunits arranged in the form of two hexameric ring.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-98 | GS beta-grasp | ||||
Sequence: QDIKFVDLRFTDPRGKMQHLTMDSREVNDDMFADGVAFDGSSIAGWKAINESDMTLILDAETAQIDPFFAQSTLAIFCDIVDPIS | ||||||
Domain | 106-469 | GS catalytic | ||||
Sequence: PRGTAKKAEAYVKASGVGDTVYFGPEPEFFVFDDVRFSATPFNTGYLVDSTELPSNTYTEYETGNLGHRTRTKGGYFPVPPVDSAQDLRSEMLSVLGEFGVTVEKHHHEVASAQHELGIKFAKLVKSADNVQLYKYVVHQVANAYGKTATFMPKPIFGDNGSGMHCHQSIWKDGKPVFAGNLYADLSETCLFYIGGILKHAKAINAFTNPTTNSYKRLVPGYEAPVLLAYSARNRSASCRIPFATSPKAKRMEIRFPDPLANPYLGFSAMLMAGLDGIKNKIHPGEPMDKNLYDLPPEELKQIPTVAGSLREALASLNADREFLKAGGVFDDDQIDAYIELKMEENMKYELTPHPVEYDMYYSS |
Sequence similarities
Belongs to the glutamine synthetase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length469
- Mass (Da)52,089
- Last updated2020-06-17 v1
- Checksum00590AD139CA9A4E
Keywords
- Technical term