Difference between revisions of "Tkt"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=tkt_1919861_1921864_1 tkt] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=tkt_1919861_1921864_1 tkt] {{PubMed|22383849}}
  
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==Original publications==
 
==Original publications==
<pubmed>14651647,16493705, 19603213 9068642 16143417 15375635 19193632 </pubmed>
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<pubmed>14651647,16493705, 19603213 9068642 16143417 15375635 19193632 23568212 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 10:57, 15 April 2013

  • Description: transketolase

Gene name tkt
Synonyms tktA
Essential no
Product transketolase
Function pentose phosphate pathway
Gene expression levels in SubtiExpress: tkt
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
Tkt context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Tkt expression.png















Categories containing this gene/protein

carbon core metabolism, phosphoproteins

This gene is a member of the following regulons

Spo0A regulon

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
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • repressed under conditions that trigger sporulation (Spo0A) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: BS4530 (aphA3), available in Stülke lab
  • Expression vector:
    • pGP94 (N-terminal Strep-tag, for SPINE, expression in B. subtilis, in pGP380), available in Stülke lab
    • for expression, purification in E. coli with N-terminal Strep-tag, in pGP172: pGP820, 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: GP1406 (spc, based on pGP1331), available in the Stülke lab

Labs working on this gene/protein

Your additional remarks

References

Reviews

Original publications

Yong-Cheol Park, Hae-Jin Lee, Chang Sup Kim, Jin-Ho Seo
Effects of oxygen supply and mixed sugar concentration on D-ribose production by a transketolase-deficient Bacillus subtilis SPK1.
J Microbiol Biotechnol: 2013, 23(4);560-4
[PubMed:23568212] [WorldCat.org] [DOI] (I p)

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)