Difference between revisions of "KatA"

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* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1SI8 1SI8] (enzyme from Enterococcus faecalis, 68% identity)
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1SI8 1SI8] (enzyme from Enterococcus faecalis, 68% identity)
  
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P26901 P26901]
+
* '''UniProt:''' [http://www.uniprot.org/uniprot/P26901 P26901]
  
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU08820]
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU08820]

Revision as of 11:39, 20 July 2009

  • Description: vegetative catalase 1

Gene name katA
Synonyms kat-19
Essential no
Product vegetative catalase 1
Function detoxification (degradation) of hydrogen peroxide
Metabolic function and regulation of this protein in SubtiPathways:
Stress
MW, pI 54 kDa, 6.151
Gene length, protein length 1449 bp, 483 aa
Immediate neighbours senS, ssuB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
KatA context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU08820

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 2 H2O2 = O2 + 2 H2O (according to Swiss-Prot)
  • Protein family: catalase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

  • Structure: 1SI8 (enzyme from Enterococcus faecalis, 68% identity)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
    • repressed in the absence of hydrogen peroxide (PerR) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

A F Herbig, J D Helmann
Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA.
Mol Microbiol: 2001, 41(4);849-59
[PubMed:11532148] [WorldCat.org] [DOI] (P p)

L Casillas-Martinez, P Setlow
Alkyl hydroperoxide reductase, catalase, MrgA, and superoxide dismutase are not involved in resistance of Bacillus subtilis spores to heat or oxidizing agents.
J Bacteriol: 1997, 179(23);7420-5
[PubMed:9393707] [WorldCat.org] [DOI] (P p)

S Engelmann, M Hecker
Impaired oxidative stress resistance of Bacillus subtilis sigB mutants and the role of katA and katE.
FEMS Microbiol Lett: 1996, 145(1);63-9
[PubMed:8931328] [WorldCat.org] [DOI] (P p)

N Bsat, L Chen, J D Helmann
Mutation of the Bacillus subtilis alkyl hydroperoxide reductase (ahpCF) operon reveals compensatory interactions among hydrogen peroxide stress genes.
J Bacteriol: 1996, 178(22);6579-86
[PubMed:8932315] [WorldCat.org] [DOI] (P p)

L Chen, L Keramati, J D Helmann
Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions.
Proc Natl Acad Sci U S A: 1995, 92(18);8190-4
[PubMed:7667267] [WorldCat.org] [DOI] (P p)