Difference between revisions of "YdeA"
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU05110&redirect=T BSU05110] | ||
* '''DBTBS entry:''' no entry | * '''DBTBS entry:''' no entry | ||
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU05110&redirect=T BSU05110] | ||
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=3F5D 3F5D] | * '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=3F5D 3F5D] |
Revision as of 13:03, 2 April 2014
- Description: glyoxalase III-like enzyme
Gene name | ydeA |
Synonyms | |
Essential | no |
Product | glyoxalase III-like enzyme |
Function | detoxification of methylglyoxal |
Gene expression levels in SubtiExpress: ydeA | |
MW, pI | 22 kDa, 5.644 |
Gene length, protein length | 591 bp, 197 aa |
Immediate neighbours | ydzN, cspC |
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
resistance against oxidative and electrophile stress
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU05110
Phenotypes of a mutant
Database entries
- BsubCyc: BSU05110
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- methylglyoxal --> D-lactate PubMed
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
Database entries
- BsubCyc: BSU05110
- Structure: 3F5D
- UniProt: P96658
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- 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)