GudB

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

Gene name	gudB
Synonyms	ypcA
Essential	no
Product	trigger enzyme: glutamate dehydrogenase
Function	glutamate utilization, control of GltC activity
Metabolic function and regulation of this protein in SubtiPathways: Ammonium/ glutamate
MW, pI	47 kDa, 5.582
Gene length, protein length	1278 bp, 426 aa
Immediate neighbours	ypdA, ypbH
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU22960

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: L-glutamate + H₂O + NAD⁺ = 2-oxoglutarate + NH₃ + NADH (according to Swiss-Prot)

• Protein family: Glu/Leu/Phe/Val dehydrogenases family (according to Swiss-Prot)

• Paralogous protein(s): RocG

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 3K8Z (enzymatically active GudB1)

• UniProt: P50735

• KEGG entry: [3]

• E.C. number: 1.4.1.2

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

• FLAG-tag construct: GP1194 (gudB, spc, based on pGP1331), GP1195 (gudB1, spc, based on pGP1331), 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

Your additional remarks

The GudB protein is active in other legacy B. subtilis strains (e.g. strain 122). Thus, it can be speculated that the ancestral gudB gene was not cryptic, but became so as a product of the "domestication" of B. subtilis 168 in the lab. PubMed

References

Daniel R Zeigler, Zoltán Prágai, Sabrina Rodriguez, Bastien Chevreux, Andrea Muffler, Thomas Albert, Renyuan Bai, Markus Wyss, John B Perkins
The origins of 168, W23, and other Bacillus subtilis legacy strains.
J Bacteriol: 2008, 190(21);6983-95
[PubMed:18723616] [WorldCat.org] [DOI] (I p)

Shigeki Kada, Masahiro Yabusaki, Takayuki Kaga, Hitoshi Ashida, Ken-ichi Yoshida
Identification of two major ammonia-releasing reactions involved in secondary natto fermentation.
Biosci Biotechnol Biochem: 2008, 72(7);1869-76
[PubMed:18603778] [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)

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)

B R Belitsky, A L Sonenshein
Role and regulation of Bacillus subtilis glutamate dehydrogenase genes.
J Bacteriol: 1998, 180(23);6298-305
[PubMed:9829940] [WorldCat.org] [DOI] (P p)