Difference between revisions of "YwjH"
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=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU37110&redirect=T BSU37110] | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/fbaA-ywjH.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/fbaA-ywjH.html] | ||
| Line 93: | Line 94: | ||
=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU37110&redirect=T BSU37110] | ||
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=3R8R 3R8R] {{PubMed|22212631}} | * '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=3R8R 3R8R] {{PubMed|22212631}} | ||
Revision as of 15:03, 2 April 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 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
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
- BsubCyc: BSU37110
- 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:
- Effectors of protein activity:
- Interactions:
- forms decamers (dimer of pentamers) PubMed
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- BsubCyc: BSU37110
- UniProt: P19669
- KEGG entry: [3]
- E.C. number: 2.2.1.2
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
- belongs to the 100 most abundant proteins PubMed
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:
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)
