AraD

• Description: L-ribulose-phosphate 4-epimerase
  
  

Gene name	araD
Synonyms
Essential	no
Product	L-ribulose-phosphate 4-epimerase
Function	arabinose utilization
Gene expression levels in SubtiExpress: araD
Metabolic function and regulation of this protein in SubtiPathways: araD
MW, pI	25 kDa, 5.243
Gene length, protein length	687 bp, 229 aa
Immediate neighbours	araL, araB
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

AraR regulon, CcpA regulon

The gene

Basic information

• Locus tag: BSU28780

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: L-ribulose 5-phosphate = D-xylulose 5-phosphate (according to Swiss-Prot)

• Protein family: AraD/fucA subfamily (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 1K0W (from Escherichia coli, 59% identity, 74% similarity) PubMed

• UniProt: P94525

• KEGG entry: [3]

• E.C. number: 5.1.3.4

Expression and regulation

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

• Expression browser: araD PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by glucose (CcpA) PubMed
  • induced by arabinose (AraR) PubMed

• Regulatory mechanism:
  • CcpA: transcription repression PubMed
  • AraR: transcription repression PubMed

• 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)

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 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)

I Sá-Nogueira, H de Lencastre
Cloning and characterization of araA, araB, and araD, the structural genes for L-arabinose utilization in Bacillus subtilis.
J Bacteriol: 1989, 171(7);4088-91
[PubMed:2500424] [WorldCat.org] [DOI] (P p)