Difference between revisions of "IlvD"
Line 102: | Line 102: | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
** [[CodY]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/12618455 PubMed1] [http://www.ncbi.nlm.nih.gov/sites/entrez/18083814 PubMed2] | ** [[CodY]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/12618455 PubMed1] [http://www.ncbi.nlm.nih.gov/sites/entrez/18083814 PubMed2] | ||
− | |||
* '''Additional information:''' | * '''Additional information:''' | ||
Line 112: | Line 111: | ||
* '''Expression vector:''' | * '''Expression vector:''' | ||
− | * '''lacZ fusion:''' | + | * '''lacZ fusion:''' pGP522 (in [[pAC5]]), pGP235 (in [[pAC5]]), both available in [[Stülke]] lab; a series of promoter deletions in [[pAC6]] is available in [[Stülke]] lab |
* '''GFP fusion:''' | * '''GFP fusion:''' |
Revision as of 18:19, 29 October 2009
- Description: dihydroxy-acid dehydratase (2,3-dihydroxy-3-methylbutanoate, 2,3-dihydroxy-3-methylpentanoate)
Gene name | ilvD |
Synonyms | |
Essential | no |
Product | dihydroxy-acid dehydratase (2,3-dihydroxy-3-methylbutanoate, 2,3-dihydroxy-3-methylpentanoate) |
Function | biosynthesis of branched-chain amino acids |
Metabolic function and regulation of this protein in SubtiPathways: Ile, Leu, Val, Coenzyme A | |
MW, pI | 59 kDa, 5.315 |
Gene length, protein length | 1674 bp, 558 aa |
Immediate neighbours | yphP, ypgR |
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: BSU21870
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: 2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O (according to Swiss-Prot)
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- UniProt: P51785
- KEGG entry: [3]
- E.C. number: 4.2.1.9
Additional information
Expression and regulation
- Regulation:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion: pGP522 (in pAC5), pGP235 (in pAC5), both available in Stülke lab; a series of promoter deletions in pAC6 is available in Stülke lab
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Boris R Belitsky, Abraham L Sonenshein
Genetic and biochemical analysis of CodY-binding sites in Bacillus subtilis.
J Bacteriol: 2008, 190(4);1224-36
[PubMed:18083814]
[WorldCat.org]
[DOI]
(I p)
Ulrike Mäder, Susanne Hennig, Michael Hecker, Georg Homuth
Transcriptional organization and posttranscriptional regulation of the Bacillus subtilis branched-chain amino acid biosynthesis genes.
J Bacteriol: 2004, 186(8);2240-52
[PubMed:15060025]
[WorldCat.org]
[DOI]
(P p)
Virginie Molle, Yoshiko Nakaura, Robert P Shivers, Hirotake Yamaguchi, Richard Losick, Yasutaro Fujita, Abraham L Sonenshein
Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis.
J Bacteriol: 2003, 185(6);1911-22
[PubMed:12618455]
[WorldCat.org]
[DOI]
(P p)
Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147]
[WorldCat.org]
[DOI]
(P p)