Difference between revisions of "NfrA"
Line 54: | Line 54: | ||
=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
− | * '''Catalyzed reaction/ biological activity:''' | + | * '''Catalyzed reaction/ biological activity:''' possesses an NADH oxidase activity that leads to high concentrations of oxygen peroxide and an NAD(+) degrading activity leading to free nicotinamide {{PubMed|20727352}} |
* '''Protein family:''' flavin oxidoreductase frp family (according to Swiss-Prot) | * '''Protein family:''' flavin oxidoreductase frp family (according to Swiss-Prot) | ||
Line 122: | Line 122: | ||
=References= | =References= | ||
− | <pubmed>9535080,16847875,10913069, 12642660,14651647, </pubmed> | + | <pubmed>9535080,16847875,10913069, 12642660,14651647, 20727352 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 12:47, 24 August 2010
- Description: Spx-dependent FMN-containing NADPH-linked nitro/flavin reductase, stress protein
Gene name | nfrA |
Synonyms | ywcG, ipa-43d |
Essential | no |
Product | FMN-containing NADPH-linked nitro/flavin reductase |
Function | unknown |
Metabolic function and regulation of this protein in SubtiPathways: Stress | |
MW, pI | 28 kDa, 5.732 |
Gene length, protein length | 747 bp, 249 aa |
Immediate neighbours | ywcH, rodA |
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: BSU38110
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: possesses an NADH oxidase activity that leads to high concentrations of oxygen peroxide and an NAD(+) degrading activity leading to free nicotinamide PubMed
- Protein family: flavin oxidoreductase frp 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:
Database entries
- Structure:
- UniProt: P39605
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- 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
Sylvie Cortial, Philippe Chaignon, Bogdan I Iorga, Stéphane Aymerich, Gilles Truan, Virginie Gueguen-Chaignon, Philippe Meyer, Solange Moréra, Jamal Ouazzani
NADH oxidase activity of Bacillus subtilis nitroreductase NfrA1: insight into its biological role.
FEBS Lett: 2010, 584(18);3916-22
[PubMed:20727352]
[WorldCat.org]
[DOI]
(I p)
Le Thi Tam, Haike Antelmann, Christine Eymann, Dirk Albrecht, Jörg Bernhardt, Michael Hecker
Proteome signatures for stress and starvation in Bacillus subtilis as revealed by a 2-D gel image color coding approach.
Proteomics: 2006, 6(16);4565-85
[PubMed:16847875]
[WorldCat.org]
[DOI]
(P p)
Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647]
[WorldCat.org]
[DOI]
(P p)
Shunji Nakano, Michiko M Nakano, Ying Zhang, Montira Leelakriangsak, Peter Zuber
A regulatory protein that interferes with activator-stimulated transcription in bacteria.
Proc Natl Acad Sci U S A: 2003, 100(7);4233-8
[PubMed:12642660]
[WorldCat.org]
[DOI]
(P p)
C Moch, O Schrögel, R Allmansberger
Transcription of the nfrA-ywcH operon from Bacillus subtilis is specifically induced in response to heat.
J Bacteriol: 2000, 182(16);4384-93
[PubMed:10913069]
[WorldCat.org]
[DOI]
(P p)
C Moch, O Schrögel, R Allmansberger
The sigmaD-dependent transcription of the ywcG gene from Bacillus subtilis is dependent on an excess of glucose and glutamate.
Mol Microbiol: 1998, 27(5);889-98
[PubMed:9535080]
[WorldCat.org]
[DOI]
(P p)