Difference between revisions of "AbfA"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
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* '''[[SubtInteract|Interactions]]:'''
 
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* '''[[Localization]]:''' cell membrane (according to Swiss-Prot)
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** forms hexamers {{PubMed|23797805}}
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** cell membrane (according to Swiss-Prot)
  
 
=== Database entries ===
 
=== Database entries ===
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=References=
 
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<pubmed>14973026,9084180,,18757805,10417639,12949161 9084180, </pubmed>
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<pubmed>14973026,9084180,,18757805,10417639,12949161 9084180, 23797805 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 08:54, 1 July 2013

  • Description: alpha-L-arabinofuranosidase

Gene name abfA
Synonyms
Essential no
Product alpha-L-arabinofuranosidase
Function arabinan degradation
Gene expression levels in SubtiExpress: abfA
Metabolic function and regulation of this protein in SubtiPathways:
Sugar catabolism
MW, pI 56 kDa, 5.344
Gene length, protein length 1500 bp, 500 aa
Immediate neighbours cstA, araQ
Sequences Protein DNA DNA_with_flanks
Genetic context
AbfA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
AbfA expression.png















Categories containing this gene/protein

utilization of specific carbon sources, membrane proteins

This gene is a member of the following regulons

AraR regulon, CcpA regulon

The gene

Basic information

  • Locus tag: BSU28720

Phenotypes of a mutant

Database entries

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

Additional information

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:

Database entries

  • Structure: 1QW8 (complex with Ara-alpha-Xyl, Geobacillus stearothermophilus), 1PZ3 (Geobacillus stearothermophilus)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Additional information:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Zaira B Hoffmam, Leandro C Oliveira, Junio Cota, Thabata M Alvarez, José A Diogo, Mario de Oliveira Neto, Ana Paula S Citadini, Vitor B P Leite, Fabio M Squina, Mario T Murakami, Roberto Ruller
Characterization of a hexameric exo-acting GH51 α-l-arabinofuranosidase from the mesophilic Bacillus subtilis.
Mol Biotechnol: 2013, 55(3);260-7
[PubMed:23797805] [WorldCat.org] [DOI] (I p)

José Manuel Inácio, Isabel Lopes Correia, Isabel de Sá-Nogueira
Two distinct arabinofuranosidases contribute to arabino-oligosaccharide degradation in Bacillus subtilis.
Microbiology (Reading): 2008, 154(Pt 9);2719-2729
[PubMed:18757805] [WorldCat.org] [DOI] (P p)

Maria Paiva Raposo, José Manuel Inácio, Luís Jaime Mota, Isabel de Sá-Nogueira
Transcriptional regulation of genes encoding arabinan-degrading enzymes in Bacillus subtilis.
J Bacteriol: 2004, 186(5);1287-96
[PubMed:14973026] [WorldCat.org] [DOI] (P p)

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)

L J Mota, P Tavares, I Sá-Nogueira
Mode of action of AraR, the key regulator of L-arabinose metabolism in Bacillus subtilis.
Mol Microbiol: 1999, 33(3);476-89
[PubMed:10417639] [WorldCat.org] [DOI] (P p)

Isabel Sa-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)