YwaA

• 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: ywaA
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
Expression at a glance   PubMed

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, most abundant proteins

This gene is a member of the following regulons

CodY regulon

The gene

Basic information

• Locus tag: BSU38550

Database entries

• BsubCyc: BSU38550

• DBTBS entry: [1]

• SubtiList entry: [2]

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

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU38550

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

• UniProt: P39576

• KEGG entry: [3]

• E.C. number: 2.6.1.42

Expression and regulation

• Operon: ywaA PubMed

• Expression browser: ywaA PubMed

• Sigma factor:

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

• Regulatory mechanism:
  • CodY: transcription repression PubMed

• Additional information:
  • belongs to the 100 most abundant proteins PubMed

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:

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)

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)

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)