Difference between revisions of "IolG"
| Line 83: | Line 83: | ||
=== Database entries === | === Database entries === | ||
| − | * '''Structure:''' {{PubMed|20809899}} | + | * '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=3MZ0 3MZ0] {{PubMed|20809899}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P26935 P26935] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P26935 P26935] | ||
| Line 132: | Line 132: | ||
=References= | =References= | ||
| − | <pubmed>9226270,6322857,1761221,112095,,9887260,18310071 112095 | + | <pubmed>9226270,6322857,1761221,112095,,9887260,18310071 112095 </pubmed> |
| − | + | '''Additional publications:''' {{PubMed|20809899}} | |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 18:10, 6 December 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 
This image was kindly provided by SubtiList
| |
Contents
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:
- Cofactor(s): NAD(+) PubMed
- Effectors of protein activity:
- Interactions: the protein forms a tetramer PubMed
- Localization:
Database entries
- UniProt: P26935
- KEGG entry: [3]
- E.C. number: 1.1.1.18
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
- Yasutaro Fujita, University of Fukuyama, Japan
- Ken-ichi Yoshida, Kobe University, Japan
Your additional remarks
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)
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)
Additional publications: PubMed
