Difference between revisions of "GlnA"
| Line 85: | Line 85: | ||
| * '''Domains:''' glutamate binding flap (aa 300 ... 306: protects unstable intermediates from abberant hydrolysis) | * '''Domains:''' glutamate binding flap (aa 300 ... 306: protects unstable intermediates from abberant hydrolysis) | ||
| − | * '''Modification:''' phosphorylated on ser/ thr/ tyr [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed] | + | * '''Modification:'''   | 
| + | ** phosphorylated on ser/ thr/ tyr [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed] | ||
| + | ** ''in vitro'' phosphorylated by [[PrkC]] on Thr-26, Thr-147, Ser-207, and Thr-286 {{PubMed|20389117}} | ||
| * '''Cofactor(s):''' Mg(2+) | * '''Cofactor(s):''' Mg(2+) | ||
| − | * '''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 | ||
| + | ** activity is inhibited upon interaction with [[TnrA]] {{PubMed|23535029}} | ||
| * '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
| Line 158: | Line 162: | ||
| ==Original publications== | ==Original publications== | ||
| − | <pubmed>19233925, 20389117,8799114,18195355, 11719184, 12139611, 2573733, 8636055, 19233925, 16493705, 16885465, 6141156 2906311 20656908 16055443 18331450 16547045 8093698 21435182</pubmed> | + | <pubmed>19233925, 20389117,8799114,18195355, 11719184, 12139611, 2573733, 8636055, 19233925, 16493705, 16885465, 6141156 2906311 20656908 16055443 18331450 16547045 8093698 21435182 23535029</pubmed> | 
| [[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 13:24, 29 March 2013
-  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 | 
| Gene expression levels in SubtiExpress: glnA | |
| Interactions involving this protein in SubtInteract: GlnA | |
| 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 | |
| Expression at a glance   PubMed   | |
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids, glutamate metabolism, transcription factors and their control, 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:
- Cofactor(s): Mg(2+)
- Effectors of protein activity:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
-  Structure:
- 3QAJ (complex with ATP)
- A general discussion of GS structure
 
- 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
Original publications

