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) | ||
− | * ''' | + | * '''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 This image was kindly provided by SubtiList
|
Contents
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)
- UniProt: P26901
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- 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)