IolJ

• Description: 2-deoxy-5-keto-gluconic acid-6-phosphate aldolase, formation of dihydroxyacetone phosphate and malonic semialdehyde (6th reaction)
  
  

Gene name	iolJ
Synonyms	fbaB, yxdI
Essential	no
Product	2-deoxy-5-keto-gluconic acid-6-phosphate aldolase, formation of dihydroxyacetone phosphate and malonic semialdehyde (6th reaction)
Function	myo-inositol catabolism
Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism
MW, pI	31 kDa, 4.854
Gene length, protein length	870 bp, 290 aa
Immediate neighbours	yxdJ, iolI
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: BSU39670

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: 5-dehydro-2-deoxy-D-gluconate 6-phosphate = glycerone phosphate + malonate semialdehyde (according to Swiss-Prot)

• Protein family: IolJ subfamily (according to Swiss-Prot)

• Paralogous protein(s): FbaA

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity: inhibited by alpha-keto acids PubMed

• Interactions:

• Localization:

Database entries

• Structure:

• Swiss prot entry: P42420

• KEGG entry: [3]

• E.C. number: 4.1.2.29

Expression and regulation

• Operon: iolA-iolB-iolC-iolD-iolE-iolF-iolG-iolH-iolJ PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed in the absence of inositol (IolR) PubMed
  • repressed by glucose (CcpA) PubMed
  • induced by inositol (IolR) PubMed

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

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

• Yasutaro Fujita, University of Fukuyama, Japan
• Ken-ichi Yoshida, Kobe University, Japan

References

Ken-ichi Yoshida, Masanori Yamaguchi, Tetsuro Morinaga, Masaki Kinehara, Maya Ikeuchi, Hitoshi Ashida, Yasutaro Fujita
myo-Inositol catabolism in Bacillus subtilis.
J Biol Chem: 2008, 283(16);10415-24
[PubMed:18310071] [WorldCat.org] [DOI] (P p)

K I Yoshida, T Shibayama, D Aoyama, Y Fujita
Interaction of a repressor and its binding sites for regulation of the Bacillus subtilis iol divergon.
J Mol Biol: 1999, 285(3);917-29
[PubMed:9887260] [WorldCat.org] [DOI] (P p)

K I Yoshida, D Aoyama, I Ishio, T Shibayama, Y Fujita
Organization and transcription of the myo-inositol operon, iol, of Bacillus subtilis.
J Bacteriol: 1997, 179(14);4591-8
[PubMed:9226270] [WorldCat.org] [DOI] (P p)

1. Yoshida K, Yamaguchi M, Morinaga T, Kinehara M, Ikeuchi M, Ashida H, Fujita Y. (2008) myo-Inositol catabolism in Bacillus subtilis. J Biol Chem. Apr 18;283(16): 10415-24. PubMed