Difference between revisions of "GuaA"

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** number of protein molecules per cell (minimal medium with glucose and ammonium): 2612 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 2612 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 12454 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 12454 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 4578 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 5511 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 7521 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 14:07, 17 April 2014

  • Description: GMP synthase (glutamine-hydrolysing)

Gene name guaA
Synonyms guaB
Essential no
Product GMP synthetase (glutamine-hydrolysing)
Function biosynthesis of GMP
Gene expression levels in SubtiExpress: guaA
Metabolic function and regulation of this protein in SubtiPathways:
guaA
MW, pI 57 kDa, 4.747
Gene length, protein length 1539 bp, 513 aa
Immediate neighbours yebA, pbuG
Sequences Protein DNA DNA_with_flanks
Genetic context
GuaA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
GuaA expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides, most abundant proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU06360

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:

Database entries

  • Structure: 2YWB (from Thermus thermophilus hb8, 45% identity, 57% similarity)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • belongs to the 100 most abundant proteins PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 2612 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 12454 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 4578 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 5511 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 7521 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

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)

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)

T Mitani, J E Heinze, E Freese
Induction of sporulation in Bacillus subtilis by decoyinine or hadacidin.
Biochem Biophys Res Commun: 1977, 77(3);1118-25
[PubMed:409404] [WorldCat.org] [DOI] (P p)