Difference between revisions of "GlxA"

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* '''Additional information:'''
 
* '''Additional information:'''
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 229 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 229 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 3299 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1387 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 2906 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 14:22, 17 April 2014

  • Description: glyoxalase I

Gene name glxA
Synonyms ipa-18r, ywbC
Essential no
Product glyoxalase I
Function detoxification of methylglyoxal
Gene expression levels in SubtiExpress: glxA
Metabolic function and regulation of this protein in SubtiPathways:
glxA
MW, pI 14 kDa, 4.429
Gene length, protein length 378 bp, 126 aa
Immediate neighbours ywbD, ywbB
Sequences Protein DNA DNA_with_flanks
Genetic context
YwbC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YwbC expression.png















Categories containing this gene/protein

resistance against oxidative and electrophile stress

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU38370

Phenotypes of a mutant

  • increased sensitivity to methylglyoxal PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • methylglyoxal + BSH --> S-lactoyl-bacillithiol (BSH) PubMed
  • Protein family: glyoxalase I family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 229 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 3299 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1387 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 2906 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Pete Chandrangsu, Renata Dusi, Chris J Hamilton, John D Helmann
Methylglyoxal resistance in Bacillus subtilis: contributions of bacillithiol-dependent and independent pathways.
Mol Microbiol: 2014, 91(4);706-15
[PubMed:24330391] [WorldCat.org] [DOI] (I p)

E Presecan, I Moszer, L Boursier, H Cruz Ramos, V de la Fuente, M-F Hullo, C Lelong, S Schleich, A Sekowska, B H Song, G Villani, F Kunst, A Danchin, P Glaser
The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees).
Microbiology (Reading): 1997, 143 ( Pt 10);3313-3328
[PubMed:9353933] [WorldCat.org] [DOI] (P p)