Difference between revisions of "ThiG"

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(Expression and regulation)
(References)
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=References=
 
=References=
 
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==Reviews==
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<pubmed>19348578 </pubmed>
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==Original publications==
 
<pubmed>15362849,, 17726680, 16493705, 19216519 14567704  </pubmed>
 
<pubmed>15362849,, 17726680, 16493705, 19216519 14567704  </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 20:58, 19 January 2010

  • Description: hydroxyethylthiazole phosphate biosynthesis

Gene name thiG
Synonyms yjbT
Essential no
Product thiamin thiazole synthase
Function biosynthesis of thiamine
MW, pI 26 kDa, 4.718
Gene length, protein length 768 bp, 256 aa
Immediate neighbours thiS, thiF
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
ThiG context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU11690

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: thiG family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylated on ser/ thr/ tyr PubMed, PubMed
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Christopher T Jurgenson, Tadhg P Begley, Steven E Ealick
The structural and biochemical foundations of thiamin biosynthesis.
Annu Rev Biochem: 2009, 78;569-603
[PubMed:19348578] [WorldCat.org] [DOI] (I p)

Original publications

Amrita Hazra, Abhishek Chatterjee, Tadhg P Begley
Biosynthesis of the thiamin thiazole in Bacillus subtilis: identification of the product of the thiazole synthase-catalyzed reaction.
J Am Chem Soc: 2009, 131(9);3225-9
[PubMed:19216519] [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)

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)

Ethan C Settembre, Pieter C Dorrestein, Huili Zhai, Abhishek Chatterjee, Fred W McLafferty, Tadhg P Begley, Steven E Ealick
Thiamin biosynthesis in Bacillus subtilis: structure of the thiazole synthase/sulfur carrier protein complex.
Biochemistry: 2004, 43(37);11647-57
[PubMed:15362849] [WorldCat.org] [DOI] (P p)

Joo-Heon Park, Pieter C Dorrestein, Huili Zhai, Cynthia Kinsland, Fred W McLafferty, Tadhg P Begley
Biosynthesis of the thiazole moiety of thiamin pyrophosphate (vitamin B1).
Biochemistry: 2003, 42(42);12430-8
[PubMed:14567704] [WorldCat.org] [DOI] (P p)