Q9HH09 · GLNA_SULAC

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

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

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 mMADP
0.24 mMmanganese
1.3 mML-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.

TypeIDPosition(s)Description
Binding site133Mg2+ 1 (UniProtKB | ChEBI)
Binding site135Mg2+ 2 (UniProtKB | ChEBI)
Binding site207ATP (UniProtKB | ChEBI)
Binding site212Mg2+ 2 (UniProtKB | ChEBI)
Binding site220Mg2+ 2 (UniProtKB | ChEBI)
Binding site264-265L-glutamate (UniProtKB | ChEBI)
Binding site265L-glutamate (UniProtKB | ChEBI)
Binding site269Mg2+ 1 (UniProtKB | ChEBI)
Binding site271-273ATP (UniProtKB | ChEBI)
Binding site273ATP (UniProtKB | ChEBI)
Binding site324L-glutamate (UniProtKB | ChEBI)
Binding site330L-glutamate (UniProtKB | ChEBI)
Binding site342ATP (UniProtKB | ChEBI)
Binding site342L-glutamate (UniProtKB | ChEBI)
Binding site347ATP (UniProtKB | ChEBI)
Binding site357ATP (UniProtKB | ChEBI)
Binding site362Mg2+ 1 (UniProtKB | ChEBI)
Binding site364L-glutamate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionglutamine synthetase activity
Molecular Functionmetal ion binding
Biological Processglutamine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glutamine synthetase
  • EC number
  • Short names
    GS
  • Alternative names
    • Glutamate--ammonia ligase
    • Glutamine synthetase I alpha
      (GSI alpha
      )

Gene names

    • Name
      glnA
    • Ordered locus names
      Saci_1483

Organism names

Accessions

  • Primary accession
    Q9HH09
  • Secondary accessions
    • Q4J8S1

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for initiator methionine, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00001532132-473Glutamine synthetase

Keywords

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.

TypeIDPosition(s)Description
Domain18-102GS beta-grasp
Domain110-473GS catalytic

Sequence similarities

Belongs to the glutamine synthetase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    473
  • Mass (Da)
    53,586
  • Last updated
    2005-08-30 v2
  • Checksum
    F8EA4FD71B1CDD5D
MPGLPKNEHEALEFLKSNNIKWVDLQFTDLLGKLQHITIPSNEFDESSFKVGFGKLDGSSIKGFTSIYESDMVLLPIPQTMTLIPWMQGVARVLTKVFWGGGKGRFERDPRGIAEEAEKYQSEQGYVSYFGPELEFFVFDKVEVDASLPQSGTGYKIHSREAPWSKNGGYVIRYKEGYYPASPVDQLMDIRLEIISTLVDYFGFTIEAAHHEVATAGQGEIDFRFSTLADTADKVQVLKYVTKNIASKRGMIATFMPKPFFGDNGSGMHTHFSLWTKDGKNLMYDPNDEYAELSQIGRYIIGGLLEHGRALSAIVAPTTNSYRRLVPGYEAPVYLVWSKSNRSAAIRIPAYYKGMEKAKRLEYRPPDPSSNPYLVFSAILMAGLDGIRRKLDPGDPVDENIYHMSEEKKRSLKIRELPGSLDEALNELESDNEFLKPVFNSSILQAYLDLKKEEAKMMQLYPHPMEIYQYLDS

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict185in Ref. 1; CAC20905
Sequence conflict204-207in Ref. 1; CAC20905
Sequence conflict209in Ref. 1; CAC20905
Sequence conflict211-259in Ref. 1; CAC20905
Sequence conflict261-299in Ref. 1; CAC20905
Sequence conflict301-303in Ref. 1; CAC20905
Sequence conflict305-314in Ref. 1; CAC20905
Sequence conflict317in Ref. 1; CAC20905

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ224678
EMBL· GenBank· DDBJ
CAC20905.1
EMBL· GenBank· DDBJ
Genomic DNA
CP000077
EMBL· GenBank· DDBJ
AAY80804.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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