O29313 · GLNA_ARCFU
- ProteinGlutamine synthetase
- GeneglnA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids491 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Probably involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Beta-glutamate is a much poorer substrate than alpha-glutamate.
Catalytic activity
- L-glutamate + NH4+ + ATP = L-glutamine + ADP + phosphate + H+
Cofactor
Note: Binds 2 Mg2+ ions per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.56 mM | ATP | |||||
3 mM | alpha-glutamate |
Temperature Dependence
Optimum temperature is 83 degrees Celsius.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 143 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 145 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 225 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 230 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 238 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 282-283 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: NA | ||||||
Binding site | 283 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 287 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 289-291 | ATP (UniProtKB | ChEBI) | ||||
Sequence: HQS | ||||||
Binding site | 291 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 344 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 350 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 362 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 362 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 367 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 381 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 383 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | membrane | |
Molecular Function | ATP binding | |
Molecular Function | glutamine synthetase activity | |
Molecular Function | metal ion binding | |
Biological Process | glutamine biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlutamine synthetase
- EC number
- Short namesGS
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Archaeoglobi > Archaeoglobales > Archaeoglobaceae > Archaeoglobus
Accessions
- Primary accessionO29313
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000153201 | 1-491 | Glutamine synthetase | |||
Sequence: MVRRLRGDCMEEVERAKAVLKENNVRQVLCAFADVRGYLQMFSIPAREFVDGSAFENGIGFDGSSVRGFRTIEKSDMVWMPDASSLKIIPWIDDPIQKSAIMFGNVYEAWGTEIADCDPRGYVAKRYEDMLKSEGMSAIFGPEIEFFLFEGVDFTRLSWDMWVSPNGGAGDSWGPPRIMPISSELESGYMIRPKEGYFRPPPEDTTVEYRNELVYYLEQLGIDIEYHHHEVATAGQVELDFKPKQLVDVGDAFYLYKFAAKNIAAMHGLYATFMPKPLYLDNASGMHTHQSLWKGEPFSGEAVFADPDDEYMLSQKARYYIGGLLEHAKALTALCAPTVNSYKRLVPGFEAPIYICWSPRNRSALVRVPMYVKKPSAIRVEYRGVDPSCNPYLAITAQLAAGLDGIKKKIDPGDPLLEDVYELTPAQKRELGVGELPTTLRDAIDHLASDELMQEVLGSHIFDAFMELKIDEWNQYCLYITPWEFMKYFDI |
Proteomic databases
Interaction
Subunit
Oligomer of 12 subunits arranged in the form of two hexagons.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 23-111 | GS beta-grasp | ||||
Sequence: NNVRQVLCAFADVRGYLQMFSIPAREFVDGSAFENGIGFDGSSVRGFRTIEKSDMVWMPDASSLKIIPWIDDPIQKSAIMFGNVYEAWG | ||||||
Domain | 119-491 | GS catalytic | ||||
Sequence: PRGYVAKRYEDMLKSEGMSAIFGPEIEFFLFEGVDFTRLSWDMWVSPNGGAGDSWGPPRIMPISSELESGYMIRPKEGYFRPPPEDTTVEYRNELVYYLEQLGIDIEYHHHEVATAGQVELDFKPKQLVDVGDAFYLYKFAAKNIAAMHGLYATFMPKPLYLDNASGMHTHQSLWKGEPFSGEAVFADPDDEYMLSQKARYYIGGLLEHAKALTALCAPTVNSYKRLVPGFEAPIYICWSPRNRSALVRVPMYVKKPSAIRVEYRGVDPSCNPYLAITAQLAAGLDGIKKKIDPGDPLLEDVYELTPAQKRELGVGELPTTLRDAIDHLASDELMQEVLGSHIFDAFMELKIDEWNQYCLYITPWEFMKYFDI |
Sequence similarities
Belongs to the glutamine synthetase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length491
- Mass (Da)55,723
- Last updated1998-01-01 v1
- Checksum5AADF719AF23F25D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE000782 EMBL· GenBank· DDBJ | AAB90294.1 EMBL· GenBank· DDBJ | Genomic DNA |