Difference between revisions of "IlvA"
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=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU21770&redirect=T BSU21770] | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ilvA-ypmP.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ilvA-ypmP.html] | ||
| Line 89: | Line 90: | ||
=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU21770&redirect=T BSU21770] | ||
* '''Structure:''' | * '''Structure:''' | ||
Revision as of 14:00, 2 April 2014
- 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: ilvA | |
| 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
- BsubCyc: BSU21770
- 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:
- Modification:
- Effectors of protein activity:
Database entries
- BsubCyc: BSU21770
- 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
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)
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)
