Difference between revisions of "GltB"

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(Biological materials)
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=Biological materials =
 
=Biological materials =
  
* '''Mutant:''' GP807 (del ''gltAB''::''tet''), GP517 (ermC), both available in [[Stülke]] lab
+
* '''Mutant:'''
 +
** GP807 (del ''[[gltA]]-[[gltB]]''::''tet'') , available in [[Jörg Stülke]]'s lab
 +
** GP517 (ermC), available in [[Jörg Stülke]]'s lab
  
 
* '''Expression vector:'''  
 
* '''Expression vector:'''  
** pGP1119 (in [[pGP380]], for SPINE, expression in ''B. subtilis''), available in [[Stülke]] lab
+
** pGP1119 (in [[pGP380]], for SPINE, expression in ''B. subtilis''), available in [[Jörg Stülke]]'s lab
 
 
 
* '''lacZ fusion:''' see ''[[gltA]]''
 
* '''lacZ fusion:''' see ''[[gltA]]''
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* '''GFP fusion:'''
 
* '''GFP fusion:'''
  
* '''two-hybrid system:''' ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Stülke]] lab
+
* '''two-hybrid system:''' ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Jörg Stülke]]'s lab
  
 
* '''Antibody:'''
 
* '''Antibody:'''

Revision as of 08:13, 24 September 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:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 1128 PubMed

Biological materials

  • Expression vector:
  • lacZ fusion: see gltA
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's 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

Gregory T Smaldone, Olga Revelles, Ahmed Gaballa, Uwe Sauer, Haike Antelmann, John D Helmann
A global investigation of the Bacillus subtilis iron-sparing response identifies major changes in metabolism.
J Bacteriol: 2012, 194(10);2594-605
[PubMed:22389480] [WorldCat.org] [DOI] (I p)

Frederik M Meyer, Jan Gerwig, Elke Hammer, Christina Herzberg, Fabian M Commichau, Uwe Völker, Jörg Stülke
Physical interactions between tricarboxylic acid cycle enzymes in Bacillus subtilis: evidence for a metabolon.
Metab Eng: 2011, 13(1);18-27
[PubMed:20933603] [WorldCat.org] [DOI] (I p)

Fabian M Commichau, Katrin Gunka, Jens J Landmann, Jörg Stülke
Glutamate metabolism in Bacillus subtilis: gene expression and enzyme activities evolved to avoid futile cycles and to allow rapid responses to perturbations of the system.
J Bacteriol: 2008, 190(10);3557-64
[PubMed:18326565] [WorldCat.org] [DOI] (I p)

Magali Cottevieille, Eric Larquet, Slavica Jonic, Maxim V Petoukhov, Gianluca Caprini, Stefano Paravisi, Dmitri I Svergun, Maria A Vanoni, Nicolas Boisset
The subnanometer resolution structure of the glutamate synthase 1.2-MDa hexamer by cryoelectron microscopy and its oligomerization behavior in solution: functional implications.
J Biol Chem: 2008, 283(13);8237-49
[PubMed:18199747] [WorldCat.org] [DOI] (P p)

Fabian M Commichau, Christina Herzberg, Philipp Tripal, Oliver Valerius, Jörg Stülke
A regulatory protein-protein interaction governs glutamate biosynthesis in Bacillus subtilis: the glutamate dehydrogenase RocG moonlights in controlling the transcription factor GltC.
Mol Microbiol: 2007, 65(3);642-54
[PubMed:17608797] [WorldCat.org] [DOI] (P p)

Fabian M Commichau, Ingrid Wacker, Jan Schleider, Hans-Matti Blencke, Irene Reif, Philipp Tripal, Jörg Stülke
Characterization of Bacillus subtilis mutants with carbon source-independent glutamate biosynthesis.
J Mol Microbiol Biotechnol: 2007, 12(1-2);106-13
[PubMed:17183217] [WorldCat.org] [DOI] (P p)

Silvia Picossi, Boris R Belitsky, Abraham L Sonenshein
Molecular mechanism of the regulation of Bacillus subtilis gltAB expression by GltC.
J Mol Biol: 2007, 365(5);1298-313
[PubMed:17134717] [WorldCat.org] [DOI] (P p)

Boris R Belitsky, Abraham L Sonenshein
Modulation of activity of Bacillus subtilis regulatory proteins GltC and TnrA by glutamate dehydrogenase.
J Bacteriol: 2004, 186(11);3399-407
[PubMed:15150225] [WorldCat.org] [DOI] (P p)

Ingrid Wacker, Holger Ludwig, Irene Reif, Hans-Matti Blencke, Christian Detsch, Jörg Stülke
The regulatory link between carbon and nitrogen metabolism in Bacillus subtilis: regulation of the gltAB operon by the catabolite control protein CcpA.
Microbiology (Reading): 2003, 149(Pt 10);3001-3009
[PubMed:14523131] [WorldCat.org] [DOI] (P p)

Ken-ichi Yoshida, Hirotake Yamaguchi, Masaki Kinehara, Yo-hei Ohki, Yoshiko Nakaura, Yasutaro Fujita
Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box.
Mol Microbiol: 2003, 49(1);157-65
[PubMed:12823818] [WorldCat.org] [DOI] (P p)

B R Belitsky, L V Wray, S H Fisher, D E Bohannon, A L Sonenshein
Role of TnrA in nitrogen source-dependent repression of Bacillus subtilis glutamate synthase gene expression.
J Bacteriol: 2000, 182(21);5939-47
[PubMed:11029411] [WorldCat.org] [DOI] (P p)

B R Belitsky, A L Sonenshein
Mutations in GltC that increase Bacillus subtilis gltA expression.
J Bacteriol: 1995, 177(19);5696-700
[PubMed:7559360] [WorldCat.org] [DOI] (P p)

D E Bohannon, A L Sonenshein
Positive regulation of glutamate biosynthesis in Bacillus subtilis.
J Bacteriol: 1989, 171(9);4718-27
[PubMed:2548995] [WorldCat.org] [DOI] (P p)