Difference between revisions of "IolG"
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=== Basic information === | === Basic information === | ||
− | * '''Locus tag:''' | + | * '''Locus tag:''' BSU39700 |
===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
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* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P26935 P26935] | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P26935 P26935] | ||
− | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+ | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU39700] |
* '''E.C. number:''' [http://www.expasy.org/enzyme/1.1.1.18 1.1.1.18] | * '''E.C. number:''' [http://www.expasy.org/enzyme/1.1.1.18 1.1.1.18] |
Revision as of 13:53, 3 June 2009
- Description: inositol 2-dehydrogenase
Gene name | iolG |
Synonyms | idh, iol |
Essential | no |
Product | inositol 2-dehydrogenase |
Function | myo-inositol 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
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):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- Swiss prot entry: 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
- 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
- Ramaley R, Fujita Y, Freese E. (1979) Purification and properties of Bacillus subtilis inositol dehydrogenase. J Biol Chem. Aug 25;254(16): 7684-90. PubMed