Difference between revisions of "YwaA"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
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= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
| − | + | {{SubtiWiki regulon|[[CodY regulon]]}} | |
=The gene= | =The gene= | ||
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=== Additional information=== | === Additional information=== | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' S-cysteinylation after diamide stress (C104) [http://www.ncbi.nlm.nih.gov/sites/entrez/17611193 PubMed] | * '''Modification:''' S-cysteinylation after diamide stress (C104) [http://www.ncbi.nlm.nih.gov/sites/entrez/17611193 PubMed] | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ilvK_3957391_3958482_1 ywaA] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ilvK_3957391_3958482_1 ywaA] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' |
* '''Regulation:''' | * '''Regulation:''' | ||
| + | ** repressed during growth in the presence of branched chain amino acids ([[CodY]]) {{PubMed|24163341}} | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| + | ** [[CodY]]: transcription repression {{PubMed|24163341}} | ||
* '''Additional information:''' | * '''Additional information:''' | ||
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=References= | =References= | ||
| − | <pubmed>12670965,17611193,, </pubmed> | + | <pubmed>12670965,17611193,24163341, </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 14:05, 22 December 2013
- Description: branched-chain amino acid aminotransferase
| Gene name | ywaA |
| Synonyms | ipa-0r |
| Essential | no |
| Product | branched-chain amino acid aminotransferase |
| Function | biosynthesis of branched-chain amino acids |
| Gene expression levels in SubtiExpress: ywaA | |
| Metabolic function and regulation of this protein in SubtiPathways: Lipid synthesis, Ile, Leu, Val | |
| MW, pI | 40 kDa, 4.952 |
| Gene length, protein length | 1089 bp, 363 aa |
| Immediate neighbours | dltE, licH |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
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Expression at a glance PubMed
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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: BSU38550
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate (according to Swiss-Prot)
- Protein family: class-IV pyridoxal-phosphate-dependent aminotransferase family (according to Swiss-Prot)
- Paralogous protein(s): YbgE
Extended information on the protein
- Kinetic information:
- Modification: S-cysteinylation after diamide stress (C104) PubMed
- Effectors of protein activity:
Database entries
- UniProt: P39576
- KEGG entry: [3]
- E.C. number: 2.6.1.42
Additional information
Expression and regulation
- Operon: ywaA PubMed
- Additional information:
Biological materials
- Mutant:
- a ywaA::spc mutant and a bcd ybgE ywaA triple mutant are available in Linc Sonenshein's lab
- Expression vector:
- lacZ fusion:
- 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)
Falko Hochgräfe, Jörg Mostertz, Dierk-Christoph Pöther, Dörte Becher, John D Helmann, Michael Hecker
S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress.
J Biol Chem: 2007, 282(36);25981-5
[PubMed:17611193]
[WorldCat.org]
[DOI]
(P p)
Bradley J Berger, Shane English, Gene Chan, Marvin H Knodel
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis.
J Bacteriol: 2003, 185(8);2418-31
[PubMed:12670965]
[WorldCat.org]
[DOI]
(P p)
