Difference between revisions of "GltB"

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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=GltB GltB]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=GltB GltB]
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/glutamate.html Ammonium/ glutamate]'''
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/subtipathways/search.php?enzyme=gltB gltB]'''
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 54.6 kDa, 7.69
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 54.6 kDa, 7.69

Revision as of 10:55, 7 January 2014

  • Description: small subunit of glutamate synthase

Gene name gltB
Synonyms
Essential no
Product glutamate synthase (small subunit)
Function glutamate biosynthesis
Gene expression levels in SubtiExpress: gltB
Interactions involving this protein in SubtInteract: GltB
Metabolic function and regulation of this protein in SubtiPathways:
gltB
MW, pI 54.6 kDa, 7.69
Gene length, protein length 1479 bp, 493 amino acids
Immediate neighbours yogA, gltA
Sequences Protein DNA DNA_with_flanks
Genetic context
GltB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
GltB expression.png
















Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, glutamate metabolism

This gene is a member of the following regulons

GltC regulon, FsrA regulon, TnrA regulon

The gene

Basic information

  • Locus tag: BSU18440

Phenotypes of a mutant

auxotrophic for glutamate

Database entries

  • DBTBS entry: [1]
  • SubtiList entry:[2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH (according to Swiss-Prot) 2 L-glutamate + NADP(+) <=> L-glutamine + 2-oxoglutarate + NADPH
  • Protein family: glutamate synthase family.
  • Paralogous protein(s): none

Extended information on the protein

  • Kinetic information:
  • Domains:
    • nucleotide binding domain (NADP) (299–313)
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation: see gltA
  • Additional information:

Biological materials

  • Mutant: GP807 (del gltAB::tet), GP517 (ermC), both available in Stülke lab
  • Expression vector:
    • pGP1119 (in pGP380, for SPINE, expression in B. subtilis), available in Stülke lab
  • lacZ fusion: see gltA
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • Antibody:

Labs working on this gene/protein

Linc Sonenshein, Tufts University, Boston, MA, USA Homepage

Jörg Stülke, University of Göttingen, Germany Homepage

Fabian Commichau University of Göttingen, Germany Homepage

Your additional remarks

References

Reviews

Katrin Gunka, Fabian M Commichau
Control of glutamate homeostasis in Bacillus subtilis: a complex interplay between ammonium assimilation, glutamate biosynthesis and degradation.
Mol Microbiol: 2012, 85(2);213-24
[PubMed:22625175] [WorldCat.org] [DOI] (I p)

Akira Suzuki, David B Knaff
Glutamate synthase: structural, mechanistic and regulatory properties, and role in the amino acid metabolism.
Photosynth Res: 2005, 83(2);191-217
[PubMed:16143852] [WorldCat.org] [DOI] (P p)

Frank M Raushel, James B Thoden, Hazel M Holden
Enzymes with molecular tunnels.
Acc Chem Res: 2003, 36(7);539-48
[PubMed:12859215] [WorldCat.org] [DOI] (P p)


Original publications