AmyE

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  • 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:
amyE
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
AmyE context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
AmyE expression.png















Categories containing this gene/protein

utilization of specific carbon sources

This gene is a member of the following regulons

AbrB regulon, CcpA regulon

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:

Database entries

  • Structure: 1BAG (complex with maltopentaose)
  • KEGG entry: [3]

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)