Difference between revisions of "GudB"
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=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
| − | * '''Catalyzed reaction/ biological activity:''' | + | * '''Catalyzed reaction/ biological activity:''' L-glutamate + H<sub>2</sub>O + NAD<sup>+</sup> = 2-oxoglutarate + NH<sub>3</sub> + NADH (according to Swiss-Prot) |
* '''Protein family:''' Glu/Leu/Phe/Val dehydrogenases family (according to Swiss-Prot) | * '''Protein family:''' Glu/Leu/Phe/Val dehydrogenases family (according to Swiss-Prot) | ||
Revision as of 23:56, 23 May 2009
- Description: trigger enzyme: glutamate dehydrogenase (cryptic in 168 and derivatives)
| Gene name | gudB |
| Synonyms | ypcA |
| Essential | no |
| Product | glutamate dehydrogenase |
| Function | glutamate utilization, control of GltC activity |
| 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
| |
Contents
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]
Additional information
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:
- Swiss prot entry: P50735
- KEGG entry: BSU22960
- E.C. number: 1.4.1.2
Additional information
Expression and regulation
- Operon: gudB 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:
- GFP fusion:
- two-hybrid system:
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
- Belitsky BR, Sonenshein AL (1998) Role and regulation of Bacillus subtilis glutamate dehydrogenase genes. J Bacteriol 180:6298-6305 PubMed
- 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
- 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
- Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 PubMed
- Zeigler DR, Prágai Z, Rodriguez S, Chevreux B, Muffler A, Albert T, Bai R, Wyss M, Perkins JB (2008) The origins of 168, W23, and other Bacillus subtilis legacy strains. J Bacteriol 190(21):6983-95 PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
