SubtiBank SubtiBank
gltA
You are currently viewing an outdated version of SubtiWiki. Please use the newest version!

gltA

large subunit of glutamate synthase
Locus
BSU_18450
Isoelectric point
5.47
Molecular weight
168.61 kDa
Protein length
1520 aa Sequence Blast
Gene length
4563 bp Sequence Blast
Function
glutamate biosynthesis
Product
glutamate synthase (large subunit)
Essential
no
E.C.
1.4.1.13
Synonyms
Outlinks
KEGGBsubCycSubtiListUniProtExpression Browser

Genomic Context

      
Loading

Categories containing this gene/protein

  • Metabolism → Amino acid/ nitrogen metabolism → Biosynthesis/ acquisition of amino acids → Biosynthesis/ acquisition of glutamate/ glutamine/ ammonium assimilation
  • Groups of genes → Efp-dependent proteins
  • Groups of genes → Phosphoproteins → Phosphorylation on an Arg residue

    • Gene

    Coordinates
    2,010,070 2,014,632

    Phenotypes of a mutant

  • auxotrophic for glutamate

    • The protein

    Catalyzed reaction/ biological activity

  • 2 L-glutamate + NADP+ --> 2-oxoglutarate + H+ + L-glutamine + NADPH (according to UniProt)

    • Protein family

  • glutamate synthase family (with YerD and GltB, according to UniProt)

    • Paralogous protein(s)

  • YerD

    • Domains

  • Glutamine amidotransferase type-2 domain (aa 22-415) (according to UniProt)
  • Nucleotide binding domain (1060-1112)

    • Modification

  • phosphorylated on Arg-904 AND/OR Arg-914 PubMed

    • Cofactors

  • Fe-S cluster PubMed
  • FAD (according to UniProt)

    • Structure

  • 2VDC (the GltA-GltB complex of Azospirillum brasiliense) PubMed

    • Localization

  • membrane associated PubMed, cytoplasm (according to UniProt)

    • Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed
  • translation is likely to require Efp due to the presence of several consecutive proline residues PubMed

    • Expression and Regulation

    Operons

    Genes
    gltA-gltB
    Description
    PubMed

    Sigma factors

  • SigA: sigma factor, PubMed, in SigA regulon

    • Regulatory mechanism

  • TnrA: repression, PubMed, in TnrA regulon
  • GltC: activation, PubMed, in GltC regulon
  • Fur: indirect effect, in Fur regulon

    • Regulation

  • expressed in the presence of ammonium PubMed
    • view in new tab

    Other regulations

  • FsrA: translation inhibition, PubMed

    • Biological materials

    Mutant

  • BP123 (ΔgltA-gltB::ermC) , available in Fabian Commichau's lab
  • GP807 (ΔgltA-gltB::tet) , available in Jörg Stülke's lab
  • GP222 (gltA under the control of p-xyl), available in Jörg Stülke's lab
  • 1A808 ( gltA::cat), PubMed, available at BGSC
  • 1A809 ( gltA::kan), PubMed, available at BGSC
  • BKE18450 (gltA::erm trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATAATTCCTCTCCCCCGAT, downstream forward: _UP4_GTACAGTAAGGAAGGGGAGA
  • BKK18450 (gltA::kan trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATAATTCCTCTCCCCCGAT, downstream forward: _UP4_GTACAGTAAGGAAGGGGAGA

    • LacZ fusion

  • pGP526 (in pAC7), available in Jörg Stülke's lab PubMed
  • pGP919 (in pAC5), available in Jörg Stülke's lab PubMed

    • Two-hybrid system

  • B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab

    • Labs working on this gene/protein

  • Linc Sonenshein, Tufts University, Boston, MA, USA Homepage
  • Jörg Stülke, University of Göttingen, Germany Homepage
  • Fabian Commichau Brandenburg Technical University Cottbus-Senftenberg, Germany Homepage

    • References

    Reviews

    Loading

    Original publications

    Loading