Difference between revisions of "YwjH"
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* '''Expression vector:'''  | * '''Expression vector:'''  | ||
** for expression, purification in ''E. coli'' with N-terminal Strep-tag, in [[pGP172]]: pGP819, available in [[Stülke]] lab  | ** 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  | ||
** GP1411 (''ywjH''-''Strep'' ''(cat)''), purification from ''B. subtilis'', for [[SPINE]], available in [[Stülke]] lab  | ** GP1411 (''ywjH''-''Strep'' ''(cat)''), purification from ''B. subtilis'', for [[SPINE]], available in [[Stülke]] lab  | ||
Revision as of 14:40, 22 February 2011
-  Description: transaldolase 
 
| Gene name | ywjH | 
| Synonyms | |
| Essential | no | 
| Product | transaldolase | 
| Function | pentose phosphate pathway | 
|  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 
 | |
Contents
Categories containing this gene/protein
carbon core metabolism, phosphoproteins
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:
 
- Domains:
 
- Cofactor(s):
 
- Effectors of protein activity:
 
- Interactions:
 
- Localization: cytoplasm (according to Swiss-Prot)
 
Database entries
- Structure: 1WX0 (from Thermus thermophilus hb8, 50% identity, 65% similarity)
 
- UniProt: P19669
 
- KEGG entry: [3]
 
- E.C. number: 2.2.1.2
 
Additional information
Expression and regulation
- Regulation:
 
- Regulatory mechanism:
 
- Additional information:
 
Biological materials
- Mutant:
 
- Expression vector:
 
- lacZ fusion:
 
- GFP fusion:
 
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
 
- Antibody:
 
Labs working on this gene/protein
Your additional remarks
References
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)
