Difference between revisions of "YwaA"

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(Biological materials)
(Extended information on the protein)
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=== Database entries ===
 
=== Database entries ===

Revision as of 09:39, 2 November 2011

  • 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
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
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YwaA context.gif
This image was kindly provided by SubtiList









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:
  • Domains:
  • Modification: S-cysteinylation after diamide stress (C104) PubMed
  • Cofactor(s):
  • 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:
  • 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

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)