Difference between revisions of "Abn2"

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=== Basic information ===
 
=== Basic information ===
  
* '''Locus tag:'''
+
* '''Locus tag:''' BSU39330
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===

Revision as of 13:41, 20 February 2014

  • Description: endo-1,5-alpha-L-arabinosidase

Gene name abn2
Synonyms yxiA
Essential no
Product endo-1,5-alpha-L-arabinosidase
Function arabinan degradation
Gene expression levels in SubtiExpress: abn2
MW, pI 52 kDa, 7.371
Gene length, protein length 1407 bp, 469 aa
Immediate neighbours yxiB, yxzL
Sequences Protein DNA DNA_with_flanks
Caution: The sequence for this gene in SubtiList contains errors
Genetic context
YxiA context.gif
Expression at a glance   PubMed
Abn2 expression.png



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: BSU39330

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: glycosyl hydrolase 43 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: With linear-alpha-1,5-l-arabinan as the preferred substrate, the enzyme exhibited an apparent K(m) of 2.0 mg ml(-1) and V(max) of 0.25 mmol min(-1) mg(-1) at pH 7.0 and 50°C. PubMed
  • Domains:
    • N-terminal catalytic domain with a characteristic β-propeller fold and a C-terminal domain whose function is unknown PubMed
  • Modification:
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]
  • E.C. number: 3.2.1.99

Additional information

Expression and regulation

  • Regulation:
    • repressed by glucose (4.3-fold) (CcpA) PubMed
    • expression is stimulated by arabinose and pectin and repressed by glucose PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Isabel de Sa-Nogueira, Lisboa, Portugal homepage

Your additional remarks

References

C E McVey, M J Ferreira, B Correia, S Lahiri, D de Sanctis, Maria Arménia Carrondo, P F Lindley, Isabel de Sá Nogueira, Cláudio Manuel Soares, Isabel Bento
The importance of the Abn2 calcium cluster in the endo-1,5-arabinanase activity from Bacillus subtilis.
J Biol Inorg Chem: 2014, 19(4-5);505-13
[PubMed:24549757] [WorldCat.org] [DOI] (I p)

Daniele de Sanctis, José M Inácio, Peter F Lindley, Isabel de Sá-Nogueira, Isabel Bento
New evidence for the role of calcium in the glycosidase reaction of GH43 arabinanases.
FEBS J: 2010, 277(21);4562-74
[PubMed:20883454] [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)

Daniele de Sanctis, Isabel Bento, José Manuel Inácio, Sónia Custódio, Isabel de Sá-Nogueira, Maria Arménia Carrondo
Overproduction, crystallization and preliminary X-ray characterization of Abn2, an endo-1,5-alpha-arabinanase from Bacillus subtilis.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2008, 64(Pt 7);636-8
[PubMed:18607095] [WorldCat.org] [DOI] (I p)

José Manuel Inácio, Isabel de Sá-Nogueira
Characterization of abn2 (yxiA), encoding a Bacillus subtilis GH43 arabinanase, Abn2, and its role in arabino-polysaccharide degradation.
J Bacteriol: 2008, 190(12);4272-80
[PubMed:18408032] [WorldCat.org] [DOI] (I p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)