Difference between revisions of "IlvA"
| Line 29: | Line 29: | ||
<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
|- | |- | ||
| − | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ilvA_2292769_2294037_-1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:ilvA_expression.png|500px]] | + | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ilvA_2292769_2294037_-1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:ilvA_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU21770]] |
|- | |- | ||
|} | |} | ||
Revision as of 13:41, 16 May 2013
- Description: threonine dehydratase
| Gene name | ilvA |
| Synonyms | |
| Essential | no |
| Product | threonine dehydratase |
| Function | biosynthesis of branched-chain amino acids |
| Gene expression levels in SubtiExpress: ilvA | |
| Metabolic function and regulation of this protein in SubtiPathways: Ile, Leu, Val | |
| MW, pI | 46 kDa, 5.538 |
| Gene length, protein length | 1266 bp, 422 aa |
| Immediate neighbours | ypmP, yplP |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU21770
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: L-threonine = 2-oxobutanoate + NH3 (according to Swiss-Prot)
- Protein family: ccmF/cycK/ccl1/nrfE/ccsA family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P37946
- KEGG entry: [3]
- E.C. number: 4.3.1.19
Additional information
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
Expression and regulation
- Sigma factor:
- Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed
Biological materials
- Mutant:
- Expression vector:
- 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)
