AmyE

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:

• 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

Expression and regulation

• Operon: amyE PubMed

• Expression browser: amyE PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by glucose (CcpA) PubMed

• Regulatory mechanism:
  • CcpA: transcription repression PubMed
  • AbrB: transcription activation PubMed

• Additional information:

Biological materials

• Mutant: GP550 (cat), available in Stülke lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)