Difference between revisions of "GlnA"
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|style="background:#ABCDEF;" align="center"| '''Product''' || glutamine synthetase (EC 6.3.1.2) | |style="background:#ABCDEF;" align="center"| '''Product''' || glutamine synthetase (EC 6.3.1.2) | ||
|- | |- | ||
| − | |style="background:#ABCDEF;" align="center"|'''Function''' || | + | |style="background:#ABCDEF;" align="center"|'''Function''' || glutamine biosynthesis, nitrogen assimilation |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 50 kDa, 4.874 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 50 kDa, 4.874 | ||
| Line 62: | Line 62: | ||
=== Extended information on the protein === | === Extended information on the protein === | ||
| − | * '''Kinetic information:''' | + | * '''Kinetic information:''' K(M) for: Glu: 27 mM, ATP: 2.4 mM, ammonium: 0.18 mM; v(max): 3.7 µmol/min/mg |
| − | * '''Domains:''' | + | * '''Domains:''' glutamate binding flap (aa 300 ... 306: protects unstable intermediates from abberant hydrolysis) |
* '''Modification:''' | * '''Modification:''' | ||
| − | * '''Cofactor(s):''' | + | * '''Cofactor(s):''' Mg(2+) |
| − | * '''Effectors of protein activity:''' | + | * '''Effectors of protein activity:''' feedback inhibition by glutamine, glutamine binds thhe entrance site for glutamate |
| − | * '''Interactions:''' [[GlnR]]-[[GlnA]], [[GlnA]]-[[TnrA]] | + | * '''Interactions:''' [[GlnR]]-[[GlnA]], [[GlnA]]-[[TnrA]] (only the feedback-inhibitted enzyme interacts with [[TnrA]] and [[GlnR]]) |
* '''Localization:''' | * '''Localization:''' | ||
| Line 87: | Line 87: | ||
=== Additional information=== | === Additional information=== | ||
| + | |||
| + | GlnA is a homooligomer of 12 subunits | ||
=Expression and regulation= | =Expression and regulation= | ||
Revision as of 19:44, 3 March 2009
- Description: glutamine synthetase
| Gene name | glnA |
| Synonyms | |
| Essential | no |
| Product | glutamine synthetase (EC 6.3.1.2) |
| Function | glutamine biosynthesis, nitrogen assimilation |
| MW, pI | 50 kDa, 4.874 |
| Gene length, protein length | 1332 bp, 444 aa |
| Immediate neighbours | glnR, ynxB |
| Gene sequence (+200bp) | Protein sequence |
Genetic context 
| |
Contents
The gene
Basic information
- Coordinates:
Phenotypes of a mutant
auxotrophic for glutamine
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information: K(M) for: Glu: 27 mM, ATP: 2.4 mM, ammonium: 0.18 mM; v(max): 3.7 µmol/min/mg
- Domains: glutamate binding flap (aa 300 ... 306: protects unstable intermediates from abberant hydrolysis)
- Modification:
- Cofactor(s): Mg(2+)
- Effectors of protein activity: feedback inhibition by glutamine, glutamine binds thhe entrance site for glutamate
- Interactions: GlnR-GlnA, GlnA-TnrA (only the feedback-inhibitted enzyme interacts with TnrA and GlnR)
- Localization:
Database entries
- Structure:
- Swiss prot entry:
- KEGG entry:
- E.C. number:
Additional information
GlnA is a homooligomer of 12 subunits
Expression and regulation
- Sigma factor:
- Regulation: expressed in the absence of glutamine PubMed
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody: available in Karl Forchhammer lab
Labs working on this gene/protein
Susan Fisher, Boston, USA homepage
Your additional remarks
References
- Brown, S. W., and A. L. Sonenshein. 1996. Autogenous regulation of the Bacillus subtilis glnRA operon. J. Bacteriol. 178: 2450-2454. PubMed
- Wray LV Jr, Zalieckas JM, Fisher SH. (2001) Bacillus subtilis glutamine synthetase controls gene expression through protein-protein interaction with transcription factor TnrA. Cell 107:427-435. PubMed
- Fisher, S. H., and Wray, L. V., Jr. (2006) Feedback-resistant mutations in Bacillus subtilis glutamine synthetase are clustered in the active site. J Bacteriol 188: 5966-5974. PubMed
- Fisher SH, Sonenshein AL (1984) Bacillus subtilis glutamine synthetase mutants pleiotropically altered in catabolite repression. J Bacteriol 157:612-621. PubMed
- Fisher, S. H., Brandenburg, J. L. & Wray, L. V. (2002). Mutations in Bacillus subtilis glutamine synthetase that block its interaction with transcription factor TnrA. Mol Microbiol 45, 627-635. PubMed
- Schreier, H. J., Brown, S. W., Hirschi, K. D., Nomellini, J. F. & Sonenshein, A. L. (1989). Regulation of Bacillus subtilis glutamine synthetase gene expression by the product of the glnR gene. J Mol Biol 210, 51-63. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
