AraA

• Description: L-arabinose isomerase
  
  

Gene name	araA
Synonyms
Essential	no
Product	L-arabinose isomerase
Function	arabinose utilization
Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism
MW, pI	56 kDa, 5.474
Gene length, protein length	1494 bp, 498 aa
Immediate neighbours	araB, abnA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

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: BSU28800

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: L-arabinose = L-ribulose (according to Swiss-Prot)

• Protein family: arabinose isomerase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information: k (cat) of 14,504 min(-1) and k (cat)/K (m) of 121 min(-1) mM(-1) for L-arabinose PubMed

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 2AJT (from Escherichia coli, 51% identity, 71% similarity) PubMed

• UniProt: P94523

• KEGG entry: [3]

• E.C. number: 5.3.1.4

Expression and regulation

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

Jin-Ha Kim, Ponnandy Prabhu, Marimuthu Jeya, Manish Kumar Tiwari, Hee-Jung Moon, Raushan Kumar Singh, Jung-Kul Lee
Characterization of an L-arabinose isomerase from Bacillus subtilis.
Appl Microbiol Biotechnol: 2010, 85(6);1839-47
[PubMed:19727704] [WorldCat.org] [DOI] (I p)

Irina Saraiva Franco, Luís Jaime Mota, Cláudio Manuel Soares, Isabel de Sá-Nogueira
Functional domains of the Bacillus subtilis transcription factor AraR and identification of amino acids important for nucleoprotein complex assembly and effector binding.
J Bacteriol: 2006, 188(8);3024-36
[PubMed:16585763] [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, L M Sarmento, I de Sá-Nogueira
Control of the arabinose regulon in Bacillus subtilis by AraR in vivo: crucial roles of operators, cooperativity, and DNA looping.
J Bacteriol: 2001, 183(14);4190-201
[PubMed:11418559] [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)

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)