Difference between revisions of "GlnA"

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* '''Description:''' [[trigger enzymes|trigger enzyme]]: glutamine synthetase and effector of [[TnrA]] and [[GlnR]] <br/><br/>
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=[http://ycybesav.co.cc UNDER COSTRUCTION, PLEASE SEE THIS POST IN RESERVE COPY]=
 
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=[http://ycybesav.co.cc CLICK HERE]=
 
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* '''Description:''' [[trigger enzymes|trigger enzyme]]: glutamine synthetase and effector of [[TnrA]] and [[GlnR]] &lt;br/>&lt;br/>
 
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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|style="background:#ABCDEF;" align="center"|'''Function''' || glutamine biosynthesis, control of [[TnrA]] and [[GlnR]] activity
 
|style="background:#ABCDEF;" align="center"|'''Function''' || glutamine biosynthesis, control of [[TnrA]] and [[GlnR]] activity
 
|-
 
|-
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: &lt;br/>[http://subtiwiki.uni-goettingen.de/pathways/glutamate.html Ammonium/ glutamate]'''
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/glutamate.html Ammonium/ glutamate]'''
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 50 kDa, 4.874   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 50 kDa, 4.874   
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[glnR]]'', ''[[ynxB]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[glnR]]'', ''[[ynxB]]''
 
|-
 
|-
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&amp;#91;EMBLCDS:CAB13630&amp;#93;+-newId sequences] &lt;br/> (Barbe ''et al.'', 2009)'''
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|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB13630&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
 
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|colspan="2" | '''Genetic context''' &lt;br/> [[Image:glnA_context.gif]]
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|colspan="2" | '''Genetic context''' <br/> [[Image:glnA_context.gif]]
  &lt;div align="right"> &lt;small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]&lt;/small>&lt;/div>
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  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
|-
 
|-
 
|}
 
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__TOC__
 
__TOC__
  
&lt;br/>&lt;br/>&lt;br/>&lt;br/>&lt;br/>&lt;br/>
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<br/><br/><br/><br/><br/><br/>
  
 
=The gene=
 
=The gene=
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=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
* '''Catalyzed reaction/ biological activity:''' ATP + L-glutamate + NH&lt;sub>3&lt;/sub> = ADP + phosphate + L-glutamine (according to Swiss-Prot)  
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* '''Catalyzed reaction/ biological activity:''' ATP + L-glutamate + NH<sub>3</sub> = ADP + phosphate + L-glutamine (according to Swiss-Prot)  
  
 
* '''Protein family:''' glutamine synthetase family (according to Swiss-Prot)
 
* '''Protein family:''' glutamine synthetase family (according to Swiss-Prot)
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=References=
 
=References=
 
==Reviews==
 
==Reviews==
&lt;pubmed> 10231480 18086213 &lt;/pubmed>
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<pubmed> 10231480 18086213 </pubmed>
 
==Original publications==
 
==Original publications==
&lt;pubmed>19233925, 20389117,8799114,18195355, 11719184, 12139611, 2573733, 8636055, 19233925, 16493705, 16885465, 6141156 2906311 20656908 16055443 18331450 16547045 8093698 &lt;/pubmed>
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<pubmed>19233925, 20389117,8799114,18195355, 11719184, 12139611, 2573733, 8636055, 19233925, 16493705, 16885465, 6141156 2906311 20656908 16055443 18331450 16547045 8093698 </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 04:58, 24 November 2010

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
GlnA context.gif
This image was kindly provided by SubtiList







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
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

  • Structure: 2GLS (enzyme from Salmonella typhimurium)
  • KEGG entry: [3]

Additional information

GlnA is a homooligomer of 12 subunits

Expression and regulation

  • Regulation:
    • expressed in the absence of glutamine (GlnR) PubMed
    • repressed in the absence of good nitrogen sources (glutamine or ammonium) (TnrA) PubMed
  • Additional information:

Biological materials

  • Mutant: GP247 (cat), available in Stülke lab
  • Expression vector:
    • expression/ purification from E. coli, with N-terminal Strep-tag (in pGP172): pGP174, available in Stülke lab
  • GFP fusion:
  • two-hybrid system:

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