Difference between revisions of "YwjH"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
 
{{SubtiWiki category|[[carbon core metabolism]]}},
 
{{SubtiWiki category|[[carbon core metabolism]]}},
{{SubtiWiki category|[[phosphoproteins]]}}
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{{SubtiWiki category|[[phosphoproteins]]}},
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[[most abundant proteins]]
  
 
= This gene is a member of the following [[regulons]] =
 
= This gene is a member of the following [[regulons]] =
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=== Additional information===
 
=== Additional information===
 
 
 
  
 
=The protein=
 
=The protein=
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:'''  
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* '''[[Domains]]:'''  
  
 
* '''Modification:''' phosphorylation on Ser-39 {{PubMed|17218307,16493705,17726680}}, ''in vitro'' phosphorylated by [[PrkC]] {{PubMed|20389117}}
 
* '''Modification:''' phosphorylation on Ser-39 {{PubMed|17218307,16493705,17726680}}, ''in vitro'' phosphorylated by [[PrkC]] {{PubMed|20389117}}
  
* '''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=ywjH_3807754_3808392_-1 ywjH] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ywjH_3807754_3808392_-1 ywjH] {{PubMed|22383849}}
  
* '''Sigma factor:'''  
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* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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* '''Additional information:'''
 
* '''Additional information:'''
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** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
  
 
=Biological materials =
 
=Biological materials =
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=References=
 
=References=
'''Additional publications:''' {{PubMed|22212631}}
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<pubmed> 17726680, 17218307, 16493705 11489127 20389117 21857661 22212631 15378759</pubmed>
<pubmed> 17726680, 17218307, 16493705 11489127 20389117 21857661 </pubmed>
 
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:01, 5 March 2014

  • 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:
ywjH
MW, pI 22 kDa, 5.876
Gene length, protein length 636 bp, 212 aa
Immediate neighbours murAB, fbaA
Sequences Protein DNA DNA_with_flanks
Genetic context
YwjH context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YwjH expression.png















Categories containing this gene/protein

carbon core metabolism, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU37110

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

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:
  • Modification: phosphorylation on Ser-39 PubMed, in vitro phosphorylated by PrkC PubMed
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:

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

Labs working on this gene/protein

Your additional remarks

References

Anne K Samland, Shiromi Baier, Melanie Schürmann, Tomoyuki Inoue, Sabine Huf, Gunter Schneider, Georg A Sprenger, Tatyana Sandalova
Conservation of structure and mechanism within the transaldolase enzyme family.
FEBS J: 2012, 279(5);766-78
[PubMed:22212631] [WorldCat.org] [DOI] (I p)

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)

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)

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)