Difference between revisions of "IlvC"
| Line 133: | Line 133: | ||
** number of protein molecules per cell (minimal medium with glucose and ammonium): 21254 {{PubMed|24696501}} | ** number of protein molecules per cell (minimal medium with glucose and ammonium): 21254 {{PubMed|24696501}} | ||
** number of protein molecules per cell (complex medium with amino acids, without glucose): 2878 {{PubMed|24696501}} | ** number of protein molecules per cell (complex medium with amino acids, without glucose): 2878 {{PubMed|24696501}} | ||
| + | ** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 75395 {{PubMed|21395229}} | ||
| + | ** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 36887 {{PubMed|21395229}} | ||
| + | ** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 50694 {{PubMed|21395229}} | ||
=Biological materials = | =Biological materials = | ||
| − | |||
* '''Mutant:''' | * '''Mutant:''' | ||
Revision as of 15:09, 17 April 2014
- Description: ketol-acid reductoisomerase (2,3-dihydroxy-3-methylbutanoate, 2-acetolactate)
| Gene name | ilvC |
| Synonyms | |
| Essential | no |
| Product | ketol-acid reductoisomerase (2,3-dihydroxy-3-methylbutanoate, 2-acetolactate) |
| Function | biosynthesis of branched-chain amino acids |
| Gene expression levels in SubtiExpress: ilvC | |
| Metabolic function and regulation of this protein in SubtiPathways: ilvC | |
| MW, pI | 37 kDa, 5.37 |
| Gene length, protein length | 1026 bp, 342 aa |
| Immediate neighbours | leuA, ilvH |
| 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, phosphoproteins, most abundant proteins
This gene is a member of the following regulons
CcpA regulon, CodY regulon, T-box, TnrA regulon
The gene
Basic information
- Locus tag: BSU28290
Phenotypes of a mutant
Database entries
- BsubCyc: BSU28290
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: (R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH (according to Swiss-Prot)
- Protein family: ketol-acid reductoisomerase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Effectors of protein activity:
Database entries
- BsubCyc: BSU28290
- UniProt: P37253
- KEGG entry: [3]
- E.C. number: 1.1.1.86
Additional information
Expression and regulation
- Regulation:
- for a complete overview on the regulation of the ilv operon, see Brinsmade et al.
- repressed by casamino acids PubMed
- expression is stimulated in the presence of glucose PubMed
- repressed in the absence of good nitrogen sources (glutamine or ammonium) (TnrA) PubMed
- repressed during growth in the presence of branched chain amino acids (CodY, T-box) PubMed
- Regulatory mechanism:
- Additional information:
- belongs to the 100 most abundant proteins PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium): 21254 PubMed
- number of protein molecules per cell (complex medium with amino acids, without glucose): 2878 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 75395 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 36887 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 50694 PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion: pGP521 (in pAC5), available in Jörg Stülke's lab
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Allison Kriel, Shaun R Brinsmade, Jessica L Tse, Ashley K Tehranchi, Alycia N Bittner, Abraham L Sonenshein, Jue D Wang
GTP dysregulation in Bacillus subtilis cells lacking (p)ppGpp results in phenotypic amino acid auxotrophy and failure to adapt to nutrient downshift and regulate biosynthesis genes.
J Bacteriol: 2014, 196(1);189-201
[PubMed:24163341]
[WorldCat.org]
[DOI]
(I p)
Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742]
[WorldCat.org]
[DOI]
(I p)
Shaun R Brinsmade, Roelco J Kleijn, Uwe Sauer, Abraham L Sonenshein
Regulation of CodY activity through modulation of intracellular branched-chain amino acid pools.
J Bacteriol: 2010, 192(24);6357-68
[PubMed:20935095]
[WorldCat.org]
[DOI]
(I p)
Boumediene Soufi, Chanchal Kumar, Florian Gnad, Matthias Mann, Ivan Mijakovic, Boris Macek
Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis.
J Proteome Res: 2010, 9(7);3638-46
[PubMed:20509597]
[WorldCat.org]
[DOI]
(I p)
Ana Gutiérrez-Preciado, Tina M Henkin, Frank J Grundy, Charles Yanofsky, Enrique Merino
Biochemical features and functional implications of the RNA-based T-box regulatory mechanism.
Microbiol Mol Biol Rev: 2009, 73(1);36-61
[PubMed:19258532]
[WorldCat.org]
[DOI]
(I p)
Shigeo Tojo, Takenori Satomura, Kanako Kumamoto, Kazutake Hirooka, Yasutaro Fujita
Molecular mechanisms underlying the positive stringent response of the Bacillus subtilis ilv-leu operon, involved in the biosynthesis of branched-chain amino acids.
J Bacteriol: 2008, 190(18);6134-47
[PubMed:18641142]
[WorldCat.org]
[DOI]
(I p)
Shigeo Tojo, Takenori Satomura, Kaori Morisaki, Ken-Ichi Yoshida, Kazutake Hirooka, Yasutaro Fujita
Negative transcriptional regulation of the ilv-leu operon for biosynthesis of branched-chain amino acids through the Bacillus subtilis global regulator TnrA.
J Bacteriol: 2004, 186(23);7971-9
[PubMed:15547269]
[WorldCat.org]
[DOI]
(P p)
Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759]
[WorldCat.org]
[DOI]
(P 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)
Holger Ludwig, Christoph Meinken, Anastasija Matin, Jörg Stülke
Insufficient expression of the ilv-leu operon encoding enzymes of branched-chain amino acid biosynthesis limits growth of a Bacillus subtilis ccpA mutant.
J Bacteriol: 2002, 184(18);5174-8
[PubMed:12193635]
[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)
F J Grundy, T M Henkin
Conservation of a transcription antitermination mechanism in aminoacyl-tRNA synthetase and amino acid biosynthesis genes in gram-positive bacteria.
J Mol Biol: 1994, 235(2);798-804
[PubMed:8289305]
[WorldCat.org]
[DOI]
(P p)
