O29313 · GLNA_ARCFU

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

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 2 Mg2+ ions per subunit.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.56 mMATP
3 mMalpha-glutamate

Temperature Dependence

Optimum temperature is 83 degrees Celsius.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site143Mg2+ 1 (UniProtKB | ChEBI)
Binding site145Mg2+ 2 (UniProtKB | ChEBI)
Binding site225ATP (UniProtKB | ChEBI)
Binding site230Mg2+ 2 (UniProtKB | ChEBI)
Binding site238Mg2+ 2 (UniProtKB | ChEBI)
Binding site282-283L-glutamate (UniProtKB | ChEBI)
Binding site283L-glutamate (UniProtKB | ChEBI)
Binding site287Mg2+ 1 (UniProtKB | ChEBI)
Binding site289-291ATP (UniProtKB | ChEBI)
Binding site291ATP (UniProtKB | ChEBI)
Binding site344L-glutamate (UniProtKB | ChEBI)
Binding site350L-glutamate (UniProtKB | ChEBI)
Binding site362ATP (UniProtKB | ChEBI)
Binding site362L-glutamate (UniProtKB | ChEBI)
Binding site367ATP (UniProtKB | ChEBI)
Binding site381Mg2+ 1 (UniProtKB | ChEBI)
Binding site383L-glutamate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentmembrane
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
      AF_0949

Organism names

Accessions

  • Primary accession
    O29313

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001532011-491Glutamine synthetase

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.

TypeIDPosition(s)Description
Domain23-111GS beta-grasp
Domain119-491GS catalytic

Sequence similarities

Belongs to the glutamine synthetase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    491
  • Mass (Da)
    55,723
  • Last updated
    1998-01-01 v1
  • Checksum
    5AADF719AF23F25D
MVRRLRGDCMEEVERAKAVLKENNVRQVLCAFADVRGYLQMFSIPAREFVDGSAFENGIGFDGSSVRGFRTIEKSDMVWMPDASSLKIIPWIDDPIQKSAIMFGNVYEAWGTEIADCDPRGYVAKRYEDMLKSEGMSAIFGPEIEFFLFEGVDFTRLSWDMWVSPNGGAGDSWGPPRIMPISSELESGYMIRPKEGYFRPPPEDTTVEYRNELVYYLEQLGIDIEYHHHEVATAGQVELDFKPKQLVDVGDAFYLYKFAAKNIAAMHGLYATFMPKPLYLDNASGMHTHQSLWKGEPFSGEAVFADPDDEYMLSQKARYYIGGLLEHAKALTALCAPTVNSYKRLVPGFEAPIYICWSPRNRSALVRVPMYVKKPSAIRVEYRGVDPSCNPYLAITAQLAAGLDGIKKKIDPGDPLLEDVYELTPAQKRELGVGELPTTLRDAIDHLASDELMQEVLGSHIFDAFMELKIDEWNQYCLYITPWEFMKYFDI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE000782
EMBL· GenBank· DDBJ
AAB90294.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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