IolG

• Description: inositol 2-dehydrogenase
  
  

Gene name	iolG
Synonyms	idh, iol
Essential	no
Product	inositol 2-dehydrogenase
Function	myo-inositol catabolism
Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism
MW, pI	38 kDa, 4.865
Gene length, protein length	1032 bp, 344 aa
Immediate neighbours	iolH, iolF
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: BSU39700

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Myo-inositol + NAD⁺ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH (according to Swiss-Prot)

• Protein family: gfo/idh/mocA family (according to Swiss-Prot)

• Paralogous protein(s): YfiI, NtdC, YrbE, YteT, YulF, IolW, IolX

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s): NAD(+) PubMed

• Effectors of protein activity:

• Interactions: the protein forms a tetramer PubMed

• Localization:

Database entries

• Structure: PubMed

• UniProt: P26935

• KEGG entry: [3]

• E.C. number: 1.1.1.18

Expression and regulation

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

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by glucose (CcpA) PubMed
  • induced by inositol (IolR) PubMed

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

Karin E van Straaten, Hongyan Zheng, David R J Palmer, David A R Sanders
Structural investigation of myo-inositol dehydrogenase from Bacillus subtilis: implications for catalytic mechanism and inositol dehydrogenase subfamily classification.
Biochem J: 2010, 432(2);237-47
[PubMed:20809899] [WorldCat.org] [DOI] (I p)

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)

Y Fujita, K Shindo, Y Miwa, K Yoshida
Bacillus subtilis inositol dehydrogenase-encoding gene (idh): sequence and expression in Escherichia coli.
Gene: 1991, 108(1);121-5
[PubMed:1761221] [WorldCat.org] [DOI] (P p)

J Nihashi, Y Fujita
Catabolite repression of inositol dehydrogenase and gluconate kinase syntheses in Bacillus subtilis.
Biochim Biophys Acta: 1984, 798(1);88-95
[PubMed:6322857] [WorldCat.org] [DOI] (P p)

R Ramaley, Y Fujita, E Freese
Purification and properties of Bacillus subtilis inositol dehydrogenase.
J Biol Chem: 1979, 254(16);7684-90
[PubMed:112095] [WorldCat.org] (P p)