Difference between revisions of "YhdN"
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=== Database entries ===  | === Database entries ===  | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU09530&redirect=T BSU09530]  | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yhdNO.html]  | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yhdNO.html]  | ||
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=== Database entries ===  | === Database entries ===  | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU09530&redirect=T BSU09530]  | ||
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1PZ1 1PZ1]	  | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1PZ1 1PZ1]	  | ||
Revision as of 13:18, 2 April 2014
-  Description: general stress protein, broad specificity aldo-keto reductase that converts MG to acetol 
 
| Gene name | yhdN | 
| Synonyms | |
| Essential | no | 
| Product | aldo/keto reductase, specific for NADP | 
| Function | detoxification of methylglyoxal | 
| Gene expression levels in SubtiExpress: yhdN | |
|  Metabolic function and regulation of this protein in SubtiPathways:  yhdN  | |
| MW, pI | 37 kDa, 4.77 | 
| Gene length, protein length | 993 bp, 331 aa | 
| Immediate neighbours | sigM, plsC | 
| Sequences | Protein DNA DNA_with_flanks | 
 Genetic context  
  This image was kindly provided by SubtiList 
 | |
Expression at a glance   PubMed 
 | |
Contents
Categories containing this gene/protein
biosynthesis of lipids, general stress proteins (controlled by SigB), resistance against oxidative and electrophile stress
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU09530
 
Phenotypes of a mutant
- increased sensitivity to methylglyoxal PubMed
 
Database entries
- BsubCyc: BSU09530
 
- DBTBS entry: [1]
 
- SubtiList entry: [2]
 
Additional information
The protein
Basic information/ Evolution
-  Catalyzed reaction/ biological activity: 
- methylglyoxal --> acetol PubMed
 
 
- Protein family: aldo/keto reductase 2 family (according to Swiss-Prot)
 
- Paralogous protein(s):
 
Extended information on the protein
- Kinetic information:
 
- Modification:
 
- Effectors of protein activity:
 
Database entries
- BsubCyc: BSU09530
 
- Structure: 1PZ1
 
- UniProt: P80874
 
- KEGG entry: [3]
 
- E.C. number:
 
Additional information
Expression and regulation
- 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
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)
Dirk Höper, Uwe Völker, Michael Hecker  
Comprehensive characterization of the contribution of individual SigB-dependent general stress genes to stress resistance of Bacillus subtilis. 
J Bacteriol: 2005, 187(8);2810-26 
[PubMed:15805528]
  [WorldCat.org]
 [DOI]
 (P p)
Andreas H Ehrensberger, David K Wilson  
Structural and catalytic diversity in the two family 11 aldo-keto reductases. 
J Mol Biol: 2004, 337(3);661-73 
[PubMed:15019785]
  [WorldCat.org]
 [DOI]
 (P p)
Gustavo E Schujman, Luciana Paoletti, Alan D Grossman, Diego de Mendoza  
FapR, a bacterial transcription factor involved in global regulation of membrane lipid biosynthesis. 
Dev Cell: 2003, 4(5);663-72 
[PubMed:12737802]
  [WorldCat.org]
 [DOI]
 (P p)
Anja Petersohn, Haike Antelmann, Ulf Gerth, Michael Hecker  
Identification and transcriptional analysis of new members of the sigmaB regulon in Bacillus subtilis. 
Microbiology (Reading): 1999, 145 ( Pt 4);869-880 
[PubMed:10220166]
  [WorldCat.org]
 [DOI]
 (P p)

