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]] =
 
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{{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:'''  
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* '''[[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]
  
* '''Cofactor(s):'''
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* '''[[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:'''  
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* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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** repressed during growth in the presence of branched chain amino acids ([[CodY]]) {{PubMed|24163341}}
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
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** [[CodY]]: transcription repression {{PubMed|24163341}}
  
 
* '''Additional information:'''
 
* '''Additional information:'''
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=References=
 
=References=
  
<pubmed>12670965,17611193,, </pubmed>
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<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
YwaA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YwaA expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of amino acids

This gene is a member of the following regulons

CodY regulon

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

  • Structure: 3HT5 (from Mycobacterium tuberculosis, 42% identity, 58% similarity) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • repressed during growth in the presence of branched chain amino acids (CodY) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • 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)