Difference between revisions of "AmyE"
| Line 109: | Line 109: | ||
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=amyE_327618_329597_1 amyE] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=amyE_327618_329597_1 amyE] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' [[SigA]] {{PubMed|3123701}} | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|3123701}} |
* '''Regulation:''' | * '''Regulation:''' | ||
| Line 139: | Line 139: | ||
=References= | =References= | ||
| − | + | <pubmed>1904524 3123701,18957862 21948839 23262127,22900538,20817675,21512239</pubmed> | |
| − | <pubmed>1904524 3123701,18957862 21948839</pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 19:20, 18 June 2013
- Description: alpha-amylase
| Gene name | amyE |
| Synonyms | amyA |
| Essential | no |
| Product | alpha-amylase) |
| Function | starch degradation |
| Gene expression levels in SubtiExpress: amyE | |
| Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism | |
| MW, pI | 72 kDa, 5.85 |
| Gene length, protein length | 1980 bp, 660 aa |
| Immediate neighbours | ycgB, ldh |
| 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
utilization of specific carbon sources
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU03040
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides (according to Swiss-Prot)
- 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:
- Localization: secreted (according to Swiss-Prot), extracellular (signal peptide) PubMed
Database entries
- Structure: 1BAG (complex with maltopentaose)
- UniProt: P00691
- KEGG entry: [3]
- E.C. number: 3.2.1.1
Additional information
Expression and regulation
- Additional information:
Biological materials
- Mutant: GP550 (cat), available in Stülke lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Haiquan Yang, Long Liu, Hyun-dong Shin, Rachel R Chen, Jianghua Li, Guocheng Du, Jian Chen
Structure-based engineering of histidine residues in the catalytic domain of α-amylase from Bacillus subtilis for improved protein stability and catalytic efficiency under acidic conditions.
J Biotechnol: 2013, 164(1);59-66
[PubMed:23262127]
[WorldCat.org]
[DOI]
(I p)
Bogumiła C Marciniak, Monika Pabijaniak, Anne de Jong, Robert Dűhring, Gerald Seidel, Wolfgang Hillen, Oscar P Kuipers
High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis.
BMC Genomics: 2012, 13;401
[PubMed:22900538]
[WorldCat.org]
[DOI]
(I e)
Takashi Inaoka, Kozo Ochi
Scandium stimulates the production of amylase and bacilysin in Bacillus subtilis.
Appl Environ Microbiol: 2011, 77(22);8181-3
[PubMed:21948839]
[WorldCat.org]
[DOI]
(I p)
Wei Zhao, Jia Zheng, Hong-Bo Zhou
Hybrid on-line optimal control strategy for producing α-amylase by Bacillus subtilis.
Biosci Biotechnol Biochem: 2011, 75(4);694-9
[PubMed:21512239]
[WorldCat.org]
[DOI]
(I p)
Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675]
[WorldCat.org]
[DOI]
(I p)
Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862]
[WorldCat.org]
[DOI]
(I p)
T M Henkin, F J Grundy, W L Nicholson, G H Chambliss
Catabolite repression of alpha-amylase gene expression in Bacillus subtilis involves a trans-acting gene product homologous to the Escherichia coli lacl and galR repressors.
Mol Microbiol: 1991, 5(3);575-84
[PubMed:1904524]
[WorldCat.org]
[DOI]
(P p)
W L Nicholson, Y K Park, T M Henkin, M Won, M J Weickert, J A Gaskell, G H Chambliss
Catabolite repression-resistant mutations of the Bacillus subtilis alpha-amylase promoter affect transcription levels and are in an operator-like sequence.
J Mol Biol: 1987, 198(4);609-18
[PubMed:3123701]
[WorldCat.org]
[DOI]
(P p)
