IolG

• Description: inositol 2-dehydrogenase
  
  

Gene name	iolG
Synonyms	idh, iol
Essential	no
Product	inositol 2-dehydrogenase
Function	myo-inositol catabolism
Gene expression levels in SubtiExpress: iolG
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
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

CcpA regulon, IolR regulon

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: 3MZ0 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

• Expression browser: iolG 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

Hongyan Zheng, Drew Bertwistle, David A R Sanders, David R J Palmer
Converting NAD-specific inositol dehydrogenase to an efficient NADP-selective catalyst, with a surprising twist.
Biochemistry: 2013, 52(34);5876-83
[PubMed:23952058] [WorldCat.org] [DOI] (I p)

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)