Difference between revisions of "AcoC"
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* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O31550 O31550] | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O31550 O31550] | ||
− | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU08080] | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU08080 BSU08080] |
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.3.1.12 2.3.1.12] | * '''E.C. number:''' [http://www.expasy.org/enzyme/2.3.1.12 2.3.1.12] |
Revision as of 21:48, 13 May 2009
- Description: acetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase)
Gene name | acoC |
Synonyms | yfjI |
Essential | no |
Product | acetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase) |
Function | acetoin utilization |
MW, pI | 42 kDa, 6.524 |
Gene length, protein length | 1194 bp, 398 aa |
Immediate neighbours | acoB, acoL |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Coordinates:
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: lipoyl-binding domain (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: Membrane-proximal (Spotty) PubMed
Database entries
- Structure:
- Swiss prot entry: O31550
- KEGG entry: BSU08080
- E.C. number: 2.3.1.12
Additional information
Expression and regulation
- Regulatory mechanism: CcpA: transcription repression, AcoR: transcription activation (interaction with SigL-containing RNA polymerase) PubMed
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Michel Debarbouille, Pasteur Institute, Paris, France Homepage
Your additional remarks
References
- Meile et al. (2006) Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory Proteomics 6: 2135-2146. PubMed
- Ali, N. O., Bignon, J., Rapoport, G., and Débarbouillé, M. (2001) Regulation of the acetoin catabolic pathway is controlled by sigma L in Bacillus subtilis. J. Bacteriol. 183, 2497-2504. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed