Sandbox

• Description: alpha-L-arabinofuranosidase
  
  

Gene name	abfA
Synonyms
Essential	no
Product	alpha-L-arabinofuranosidase
Function	arabinan degradation
MW, pI	56 kDa, 5.344
Gene length, protein length	1500 bp, 500 aa
Immediate neighbours	cstA, araQ
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU28720

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides (according to Swiss-Prot)

• Protein family: glycosyl hydrolase 51 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: cell membrane (according to Swiss-Prot)

Database entries

• Structure: 1QW8 (complex with Ara-alpha-Xyl, Geobacillus stearothermophilus), 1PZ3 (Geobacillus stearothermophilus)

• Swiss prot entry: P94531

• KEGG entry: [3]

• E.C. number: 3.2.1.55

Expression and regulation

• Operon: araA-araB-araD-araL-araM-araN-araP-araQ-abfA

• Sigma factor: SigA

• Regulation: repressed by glucose (CcpA)

• Regulatory mechanism: CcpA: transcription repression

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

José Manuel Inácio, Carla Costa, Isabel de Sá-Nogueira
Distinct molecular mechanisms involved in carbon catabolite repression of the arabinose regulon in Bacillus subtilis.
Microbiology (Reading): 2003, 149(Pt 9);2345-2355
[PubMed:12949161] [WorldCat.org] [DOI] (P p)

Isabel S-Nogueira, Teresa V Nogueira, Snia Soares, Hermnia de Lencastre
The Bacillus subtilis L-arabinose (ara) operon: nucleotide sequence, genetic organization and expression.
Microbiology (Reading): 1997, 143 ( Pt 3);957-969
[PubMed:9084180] [WorldCat.org] [DOI] (P p)