Difference between revisions of "IolG"

From SubtiWiki
Jump to: navigation, search
(Extended information on the protein)
Line 52: Line 52:
  
  
 +
 +
= Categories containing this gene/protein =
 +
{{SubtiWiki category|[[utilization of specific carbon sources]]}}
 
=The protein=
 
=The protein=
  

Revision as of 17:26, 30 November 2010

  • 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
Idh context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU39700

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

Categories containing this gene/protein

utilization of specific carbon sources

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)

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Effectors of protein activity:
  • Interactions: the protein forms a tetramer PubMed
  • Localization:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

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)