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:
Sugar catabolism
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
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

Additional publications: PubMed

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)

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)

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)