Difference between revisions of "AmyE"
| Line 80: | Line 80: | ||
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P00691 P00691] | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P00691 P00691] | ||
| − | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU03040] | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU03040 BSU03040] |
* '''E.C. number:''' [http://www.expasy.org/enzyme/3.2.1.1 3.2.1.1] | * '''E.C. number:''' [http://www.expasy.org/enzyme/3.2.1.1 3.2.1.1] | ||
Revision as of 21:52, 13 May 2009
- Description: alpha-amylase
| Gene name | amyE |
| Synonyms | amyA |
| Essential | no |
| Product | alpha-amylase) |
| Function | starch degradation |
| MW, pI | 72 kDa, 5.85 |
| Gene length, protein length | 1980 bp, 660 aa |
| Immediate neighbours | ycgB, ldh |
| 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: glycosyl hydrolase 13 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: secreted (according to Swiss-Prot), extracellular (signal peptide) PubMed
Database entries
- Structure: 1BAG (complex with maltopentaose)
- Swiss prot entry: P00691
- KEGG entry: BSU03040
- E.C. number: 3.2.1.1
Additional information
Expression and regulation
- Operon: AmyE
- Regulation: repressed by glucose (CcpA)
- Regulatory mechanism: CcpA: transcription repression
- 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
- Voigt et al. (2009) Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis. J Mol Microbiol Biotechnol. 16: 53-68 PubMed
- Henkin, T. M., Grundy, F. J., Nicholson, W. L. and Chambliss, G. H. (1991) Catabolite repression of -amylase gene expression in Bacillus subtilis involves a trans-acting gene product homologous to the Escherichia coli lacI and galR repressors. Mol. Microbiol. 5, 575-584. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
