GudB

• Description: glutamate dehydrogenase (cryptic in 168 and derivatives)
  
  

Gene name	gudB
Synonyms	ypcA
Essential	no
Product	glutamate dehydrogenase
Function
MW, pI	47 kDa, 5.582
Gene length, protein length	1278 bp, 426 aa
Immediate neighbours	ypdA, ypbH
Gene sequence (+200bp)	Protein sequence
Genetic context

The gene

Basic information

• Coordinates:

Phenotypes of a mutant

The gene is cryptic. If gudB is activated (gudB1 mutation), the bacteria are able to utilize glutamate as the only carbon source. PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s): RocG

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• Swiss prot entry:

• KEGG entry:

• E.C. number:

Expression and regulation

• Operon: gudB PubMed

• Sigma factor: SigA PubMed

• Regulation: constitutively expressed

• Regulatory mechanism:

• Additional information: GudB is subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

• Mutant: GP691 (cat), available in Stülke lab

• Expression vector:

• lacZ fusion: pGP651 (in pAC5), available in Stülke lab

• GFP fusion:

• two-hybrid system:

• Antibody: antibody against RocG recognizes GudB, available in Stülke lab

Labs working on this gene/protein

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

Jörg Stülke, University of Göttingen, Germany Homepage

References

1. Belitsky BR, Sonenshein AL (1998) Role and regulation of Bacillus subtilis glutamate dehydrogenase genes. J Bacteriol 180:6298-6305 PubMed
2. Commichau, F. M., Wacker, I., Schleider, J., Blencke, H.-M., Reif, I., Tripal, P., and Stülke, J. (2007) Characterization of Bacillus subtilis mutants with carbon source-independent glutamate biosynthesis. J Mol Microbiol Biotechnol 12: 106-113. PubMed
3. Commichau, F. M., Gunka, K., Landmann, J. J. & Stülke, J. (2008) Glutamate metabolism in Bacillus subtilis: Gene expression and enzyme activities evolved to avoid futile cycles and to allow rapid responses to perturbations in the system. J. Bacteriol. 190: 3557-3564. PubMed
4. Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 PubMed
5. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed