YwjH

• Description: transaldolase
  
  

Gene name	ywjH
Synonyms
Essential	no
Product	transaldolase
Function	pentose phosphate pathway
Gene expression levels in SubtiExpress: ywjH
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	22 kDa, 5.876
Gene length, protein length	636 bp, 212 aa
Immediate neighbours	murAB, fbaA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

carbon core metabolism, phosphoproteins

The gene

Basic information

• Locus tag: BSU37110

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate (according to Swiss-Prot)

• Protein family: Type 3B subfamily (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylation on Ser-39 PubMed, in vitro phosphorylated by PrkC PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • forms decamers (dimer of pentamers) PubMed

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure: 3R8R PubMed

• UniProt: P19669

• KEGG entry: [3]

• E.C. number: 2.2.1.2

Expression and regulation

• Operon: fbaA-ywjH PubMed

• Expression browser: ywjH PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:
  • for expression, purification in E. coli with N-terminal Strep-tag, in pGP172: pGP819, available in Stülke lab
  • pGP1790 (expression of ywjH in B. subtilis, in pGP1389), available in Stülke lab
  • GP1409 (ywjH-Strep (spc)) & GP1411 (ywjH-Strep (cat)), purification from B. subtilis, for SPINE, available in Stülke lab

• lacZ fusion:

• GFP fusion:

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab

• Antibody:

• FLAG-tag construct: GP1407 (spc, based on pGP1331), available in the Stülke lab

References

Additional publications: PubMed

Anja Lehwess-Litzmann, Piotr Neumann, Christoph Parthier, Stefan Lüdtke, Ralph Golbik, Ralf Ficner, Kai Tittmann
Twisted Schiff base intermediates and substrate locale revise transaldolase mechanism.
Nat Chem Biol: 2011, 7(10);678-84
[PubMed:21857661] [WorldCat.org] [DOI] (I e)

Nico Pietack, Dörte Becher, Sebastian R Schmidl, Milton H Saier, Michael Hecker, Fabian M Commichau, Jörg Stülke
In vitro phosphorylation of key metabolic enzymes from Bacillus subtilis: PrkC phosphorylates enzymes from different branches of basic metabolism.
J Mol Microbiol Biotechnol: 2010, 18(3);129-40
[PubMed:20389117] [WorldCat.org] [DOI] (I p)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)

H Ludwig, G Homuth, M Schmalisch, F M Dyka, M Hecker, J Stülke
Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon.
Mol Microbiol: 2001, 41(2);409-22
[PubMed:11489127] [WorldCat.org] [DOI] (P p)