Difference between revisions of "PurA"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
 
{{SubtiWiki category|[[biosynthesis/ acquisition of nucleotides]]}},
 
{{SubtiWiki category|[[biosynthesis/ acquisition of nucleotides]]}},
{{SubtiWiki category|[[phosphoproteins]]}}
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{{SubtiWiki category|[[phosphoproteins]]}},
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[[most abundant proteins]]
  
 
= This gene is a member of the following [[regulons]] =
 
= This gene is a member of the following [[regulons]] =
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=== Additional information===
 
=== Additional information===
 
 
 
  
 
=The protein=
 
=The protein=
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:'''  
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* '''[[Domains]]:'''  
  
 
* '''Modification:'''
 
* '''Modification:'''
 
** phosphorylated on Arg-97 {{PubMed|22517742}}
 
** phosphorylated on Arg-97 {{PubMed|22517742}}
  
* '''Cofactor(s):'''
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* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=purA_4155433_4156725_-1 purA] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=purA_4155433_4156725_-1 purA] {{PubMed|22383849}}
  
* '''Sigma factor:''' [[SigA]] {{PubMed|1312531}}  
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* '''[[Sigma factor]]:''' [[SigA]] {{PubMed|1312531}}  
  
 
* '''Regulation:''' expression activated by glucose (4.9 fold) ([[CcpA]]) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]   
 
* '''Regulation:''' expression activated by glucose (4.9 fold) ([[CcpA]]) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]   
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* '''Additional information:'''
 
* '''Additional information:'''
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** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
  
 
=Biological materials =
 
=Biological materials =
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=References=
 
=References=
  
<pubmed>1722815,1312531 ,7638212,12850135, 21424839 22517742</pubmed>
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<pubmed>1722815,1312531 ,7638212,12850135, 21424839 22517742 15378759</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 17:56, 5 March 2014

  • Description: adenylosuccinate synthetase

Gene name purA
Synonyms
Essential no
Product adenylosuccinate synthetase
Function purine biosynthesis
Gene expression levels in SubtiExpress: purA
Metabolic function and regulation of this protein in SubtiPathways:
purA
MW, pI 47 kDa, 5.459
Gene length, protein length 1290 bp, 430 aa
Immediate neighbours trnY-Lys, yycE
Sequences Protein DNA DNA_with_flanks
Genetic context
PurA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PurA expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

PurR regulon

The gene

Basic information

  • Locus tag: BSU40420

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP (according to Swiss-Prot)
  • Protein family: adenylosuccinate synthetase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
    • phosphorylated on Arg-97 PubMed
  • Effectors of protein activity:

Database entries

  • Structure: 1KJX (from Escherichia coli k12, 46% identity, 64% similarity) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation: expression activated by glucose (4.9 fold) (CcpA) PubMed
    • repressed in the presence of purine nucleotides (PurR) PubMed
  • Regulatory mechanism:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc. Natl. Acad. Sci. U.S.A.: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Haojian Li, Guoqiang Zhang, Aihua Deng, Ning Chen, Tingyi Wen
De novo engineering and metabolic flux analysis of inosine biosynthesis in Bacillus subtilis.
Biotechnol. Lett.: 2011, 33(8);1575-80
[PubMed:21424839] [WorldCat.org] [DOI] (I p)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab. Eng.: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] (P p)

M Weng, P L Nagy, H Zalkin
Identification of the Bacillus subtilis pur operon repressor.
Proc. Natl. Acad. Sci. U.S.A.: 1995, 92(16);7455-9
[PubMed:7638212] [WorldCat.org] [DOI] (P p)

P Mäntsälä, H Zalkin
Cloning and sequence of Bacillus subtilis purA and guaA, involved in the conversion of IMP to AMP and GMP.
J. Bacteriol.: 1992, 174(6);1883-90
[PubMed:1312531] [WorldCat.org] [DOI] (P p)

H H Saxild, P Nygaard
Regulation of levels of purine biosynthetic enzymes in Bacillus subtilis: effects of changing purine nucleotide pools.
J. Gen. Microbiol.: 1991, 137(10);2387-94
[PubMed:1722815] [WorldCat.org] [DOI] (P p)