Difference between revisions of "GlnA"
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=== Additional information=== | === Additional information=== | ||
− | |||
− | |||
− | |||
=The protein= | =The protein= | ||
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* '''Effectors of protein activity:''' feedback inhibition by glutamine, glutamine binds the entrance site for glutamate | * '''Effectors of protein activity:''' feedback inhibition by glutamine, glutamine binds the entrance site for glutamate | ||
− | * '''Interactions:''' [[TnrA]]-[[GlnA]] {{PubMed|11719184}} | + | * '''Interactions:''' |
+ | ** [[TnrA]]-[[GlnA]] {{PubMed|11719184}} | ||
+ | ** [[GlnR]]-[[GlnA]] {{PubMed|18195355}}, (only the feedback-inhibited enzyme interacts with [[TnrA]] and [[GlnR]]) | ||
+ | ** [[GlnA]]-[[NrgB]] {{PubMed|21435182}} | ||
* '''Localization:''' cytoplasm (according to Swiss-Prot) | * '''Localization:''' cytoplasm (according to Swiss-Prot) | ||
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<pubmed> 10231480 18086213 </pubmed> | <pubmed> 10231480 18086213 </pubmed> | ||
==Original publications== | ==Original publications== | ||
− | <pubmed>19233925, 20389117,8799114,18195355, 11719184, 12139611, 2573733, 8636055, 19233925, 16493705, 16885465, 6141156 2906311 20656908 16055443 18331450 16547045 8093698 </pubmed> | + | <pubmed>19233925, 20389117,8799114,18195355, 11719184, 12139611, 2573733, 8636055, 19233925, 16493705, 16885465, 6141156 2906311 20656908 16055443 18331450 16547045 8093698 21435182</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 08:10, 26 March 2011
- Description: trigger enzyme: glutamine synthetase and effector of TnrA and GlnR
Gene name | glnA |
Synonyms | |
Essential | no |
Product | trigger enzyme: glutamine synthetase |
Function | glutamine biosynthesis, control of TnrA and GlnR activity |
Metabolic function and regulation of this protein in SubtiPathways: Ammonium/ glutamate | |
MW, pI | 50 kDa, 4.874 |
Gene length, protein length | 1332 bp, 444 aa |
Immediate neighbours | glnR, ynxB |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids, trigger enzyme, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU17460
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: ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine (according to Swiss-Prot)
- Protein family: glutamine synthetase family (according to Swiss-Prot)
- 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: phosphorylated on ser/ thr/ tyr PubMed, in vitro phosphorylated by PrkC on Thr-26, Thr-147, Ser-207, and Thr-286 PubMed
- Cofactor(s): Mg(2+)
- Effectors of protein activity: feedback inhibition by glutamine, glutamine binds the entrance site for glutamate
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure: 2GLS (enzyme from Salmonella typhimurium)
- UniProt: P12425
- KEGG entry: [3]
- E.C. number: 6.3.1.2
Additional information
GlnA is a homooligomer of 12 subunits
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: GP247 (cat), available in Stülke lab
- Expression vector:
- 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
Reviews
Fabian M Commichau, Jörg Stülke
Trigger enzymes: bifunctional proteins active in metabolism and in controlling gene expression.
Mol Microbiol: 2008, 67(4);692-702
[PubMed:18086213]
[WorldCat.org]
[DOI]
(P p)
S H Fisher
Regulation of nitrogen metabolism in Bacillus subtilis: vive la différence!
Mol Microbiol: 1999, 32(2);223-32
[PubMed:10231480]
[WorldCat.org]
[DOI]
(P p)
Original publications