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: 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 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

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)