Difference between revisions of "Tkt"
m (Reverted edits by 178.239.58.143 (talk) to last revision by 134.76.70.252) |
|||
Line 30: | Line 30: | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:tkt_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:tkt_context.gif]] | ||
<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
+ | |- | ||
+ | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=tkt_1919861_1921864_1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:tkt_expression.png|500px]] | ||
|- | |- | ||
|} | |} | ||
__TOC__ | __TOC__ | ||
+ | <br/><br/><br/><br/> | ||
+ | <br/><br/><br/><br/> | ||
+ | <br/><br/><br/><br/> | ||
+ | <br/><br/><br/><br/> | ||
+ | <br/><br/><br/><br/> | ||
+ | |||
<br/><br/><br/><br/><br/><br/> | <br/><br/><br/><br/><br/><br/> |
Revision as of 10:24, 19 April 2012
- Description: transketolase
Gene name | tkt |
Synonyms | tktA |
Essential | no |
Product | transketolase |
Function | pentose phosphate pathway |
Interactions involving this protein in SubtInteract: Tkt | |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
MW, pI | 72 kDa, 4.803 |
Gene length, protein length | 2001 bp, 667 aa |
Immediate neighbours | ynzC, sirA |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
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: BSU17890
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-ribose 5-phosphate + D-xylulose 5-phosphate (according to Swiss-Prot)
- Protein family: transketolase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: phosphorylated on ser/ thr/ tyr PubMed
- Cofactor(s): thiamine pyrophosphate
- Effectors of protein activity:
Database entries
- Structure: [3K95], complex with thiamine diphosphate, from B. anthracis
- UniProt: P45694
- KEGG entry: [3]
- E.C. number: 2.2.1.1
Additional information
Expression and regulation
- Operon: tkt PubMed
- Sigma factor:
- Additional information:
Biological materials
- Mutant: BS4530 (aphA3), available in Stülke lab
- 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
Reviews
G Schenk, R G Duggleby, P F Nixon
Properties and functions of the thiamin diphosphate dependent enzyme transketolase.
Int J Biochem Cell Biol: 1998, 30(12);1297-318
[PubMed:9924800]
[WorldCat.org]
[DOI]
(P p)
Original publications
Lin Wu, Zhimin Li, Qin Ye
Enhanced D-ribose biosynthesis in batch culture of a transketolase-deficient Bacillus subtilis strain by citrate.
J Ind Microbiol Biotechnol: 2009, 36(10);1289-96
[PubMed:19603213]
[WorldCat.org]
[DOI]
(I p)
Fabian M Commichau, Fabian M Rothe, Christina Herzberg, Eva Wagner, Daniel Hellwig, Martin Lehnik-Habrink, Elke Hammer, Uwe Völker, Jörg Stülke
Novel activities of glycolytic enzymes in Bacillus subtilis: interactions with essential proteins involved in mRNA processing.
Mol Cell Proteomics: 2009, 8(6);1350-60
[PubMed:19193632]
[WorldCat.org]
[DOI]
(I 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)
Yong-Cheol Park, Jin-Ho Choi, George N Bennett, Jin-Ho Seo
Characterization of D-ribose biosynthesis in Bacillus subtilis JY200 deficient in transketolase gene.
J Biotechnol: 2006, 121(4);508-16
[PubMed:16143417]
[WorldCat.org]
[DOI]
(P p)
Yong-Cheol Park, Sung-Gun Kim, Kyungmoon Park, Kelvin H Lee, Jin-Ho Seo
Fed-batch production of D-ribose from sugar mixtures by transketolase-deficient Bacillus subtilis SPK1.
Appl Microbiol Biotechnol: 2004, 66(3);297-302
[PubMed:15375635]
[WorldCat.org]
[DOI]
(P p)
Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647]
[WorldCat.org]
[DOI]
(P p)
T Schiött, C von Wachenfeldt, L Hederstedt
Identification and characterization of the ccdA gene, required for cytochrome c synthesis in Bacillus subtilis.
J Bacteriol: 1997, 179(6);1962-73
[PubMed:9068642]
[WorldCat.org]
[DOI]
(P p)