Q9HH09 · GLNA_SULAC
- ProteinGlutamine synthetase
- GeneglnA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids473 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Probably involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.
Miscellaneous
GlnA of S.acidocaldarius is unique among the archeal glutamine synthetase since the regulatory properties suggest a position within the GS I-alpha subgroup. However, the sequence shows more pronounced similarities to the GS I-beta subgroup.
Catalytic activity
- ATP + L-glutamate + NH4+ = ADP + H+ + L-glutamine + phosphate
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 2 Mg2+ or Mn2+ ions per subunit.
Activity regulation
Strongly inhibited by glycine and L-alanine. AMP at 10 mM displays a very weak inhibitory effect. The activity of this enzyme is not controlled by adenylation.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.15 mM | ADP | |||||
0.24 mM | manganese | |||||
1.3 mM | L-glutamine |
pH Dependence
Optimum pH is between 7 and 7.5.
Temperature Dependence
Optimum temperature is 90 degrees Celsius. In the absence of magnesium or manganese ions about 50% of the activity is lost within 100 minutes at 78 degrees Celsius, whereas more than 95% of the activity is retained in presence of 4 mM manganese ions. Magnesium ions are a less effective.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 133 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 135 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 207 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 212 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 220 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 264-265 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: NG | ||||||
Binding site | 265 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 269 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 271-273 | ATP (UniProtKB | ChEBI) | ||||
Sequence: HFS | ||||||
Binding site | 273 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 324 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 330 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 342 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 342 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 347 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 357 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 362 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 364 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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 > Thermoproteota > Thermoprotei > Sulfolobales > Sulfolobaceae > Sulfolobus
Accessions
- Primary accessionQ9HH09
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000153213 | 2-473 | Glutamine synthetase | |||
Sequence: PGLPKNEHEALEFLKSNNIKWVDLQFTDLLGKLQHITIPSNEFDESSFKVGFGKLDGSSIKGFTSIYESDMVLLPIPQTMTLIPWMQGVARVLTKVFWGGGKGRFERDPRGIAEEAEKYQSEQGYVSYFGPELEFFVFDKVEVDASLPQSGTGYKIHSREAPWSKNGGYVIRYKEGYYPASPVDQLMDIRLEIISTLVDYFGFTIEAAHHEVATAGQGEIDFRFSTLADTADKVQVLKYVTKNIASKRGMIATFMPKPFFGDNGSGMHTHFSLWTKDGKNLMYDPNDEYAELSQIGRYIIGGLLEHGRALSAIVAPTTNSYRRLVPGYEAPVYLVWSKSNRSAAIRIPAYYKGMEKAKRLEYRPPDPSSNPYLVFSAILMAGLDGIRRKLDPGDPVDENIYHMSEEKKRSLKIRELPGSLDEALNELESDNEFLKPVFNSSILQAYLDLKKEEAKMMQLYPHPMEIYQYLDS |
Keywords
- PTM
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 | 18-102 | GS beta-grasp | ||||
Sequence: NNIKWVDLQFTDLLGKLQHITIPSNEFDESSFKVGFGKLDGSSIKGFTSIYESDMVLLPIPQTMTLIPWMQGVARVLTKVFWGGG | ||||||
Domain | 110-473 | GS catalytic | ||||
Sequence: PRGIAEEAEKYQSEQGYVSYFGPELEFFVFDKVEVDASLPQSGTGYKIHSREAPWSKNGGYVIRYKEGYYPASPVDQLMDIRLEIISTLVDYFGFTIEAAHHEVATAGQGEIDFRFSTLADTADKVQVLKYVTKNIASKRGMIATFMPKPFFGDNGSGMHTHFSLWTKDGKNLMYDPNDEYAELSQIGRYIIGGLLEHGRALSAIVAPTTNSYRRLVPGYEAPVYLVWSKSNRSAAIRIPAYYKGMEKAKRLEYRPPDPSSNPYLVFSAILMAGLDGIRRKLDPGDPVDENIYHMSEEKKRSLKIRELPGSLDEALNELESDNEFLKPVFNSSILQAYLDLKKEEAKMMQLYPHPMEIYQYLDS |
Sequence similarities
Belongs to the glutamine synthetase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length473
- Mass (Da)53,586
- Last updated2005-08-30 v2
- ChecksumF8EA4FD71B1CDD5D
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 185 | in Ref. 1; CAC20905 | ||||
Sequence: D → V | ||||||
Sequence conflict | 204-207 | in Ref. 1; CAC20905 | ||||
Sequence: FTIE → TIEA | ||||||
Sequence conflict | 209 | in Ref. 1; CAC20905 | ||||
Sequence: A → H | ||||||
Sequence conflict | 211-259 | in Ref. 1; CAC20905 | ||||
Sequence: HEVATAGQGEIDFRFSTLADTADKVQVLKYVTKNIASKRGMIATFMPKP → EVATAGQGDIDFRFSTLADTADKVQVLKYVTKNIASKRGMIATFMPKPF | ||||||
Sequence conflict | 261-299 | in Ref. 1; CAC20905 | ||||
Sequence: FGDNGSGMHTHFSLWTKDGKNLMYDPNDEYAELSQIGRY → GDNGSGMHTHFSLWTKDGKNLMYDPNDEYAELSQIGRYI | ||||||
Sequence conflict | 301-303 | in Ref. 1; CAC20905 | ||||
Sequence: IGG → GPL | ||||||
Sequence conflict | 305-314 | in Ref. 1; CAC20905 | ||||
Sequence: LEHGRALSAI → EHGRALSAIV | ||||||
Sequence conflict | 317 | in Ref. 1; CAC20905 | ||||
Sequence: P → G |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ224678 EMBL· GenBank· DDBJ | CAC20905.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP000077 EMBL· GenBank· DDBJ | AAY80804.1 EMBL· GenBank· DDBJ | Genomic DNA |