Difference between revisions of "Ugd"

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=== Additional information===
 
=== Additional information===
 
 
 
  
 
=The protein=
 
=The protein=
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:'''  
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* '''[[Domains]]:'''  
  
 
* '''Modification:''' phosphorylation on Tyr-70 by [[PtkA]] {{PubMed|12970183}}, dephosphorylated by [[PtpZ]] {{PubMed|15866923}}
 
* '''Modification:''' phosphorylation on Tyr-70 by [[PtkA]] {{PubMed|12970183}}, dephosphorylated by [[PtpZ]] {{PubMed|15866923}}
  
* '''Cofactor(s):'''
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* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:''' phosphorylation by [[PtkA]] stimulates activity of Ugd {{PubMed|15741737}}
 
* '''Effectors of protein activity:''' phosphorylation by [[PtkA]] stimulates activity of Ugd {{PubMed|15741737}}
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=References=
 
=References=
  
<pubmed> 12970183, 19258708 15741737 15866923 20815827</pubmed>
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<pubmed> 12970183, 19258708 15741737 15866923 20815827 24728941 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 07:12, 15 April 2014

  • Description: UDP-glucose dehydrogenase

Gene name ugd
Synonyms ywqF
Essential no
Product UDP-glucose dehydrogenase
Function unknown
Gene expression levels in SubtiExpress: ugd
Interactions involving this protein in SubtInteract: Ugd
MW, pI 47 kDa, 5.03
Gene length, protein length 1320 bp, 440 aa
Immediate neighbours ywqG, ptpZ
Sequences Protein DNA DNA_with_flanks
Genetic context
YwqF context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Ugd expression.png















Categories containing this gene/protein

phosphoproteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU36230

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: UDP-glucose + 2 NAD+ + H2O = UDP-glucuronate + 2 NADH (according to Swiss-Prot)
  • Protein family: UDP-glucose/GDP-mannose dehydrogenase family (according to Swiss-Prot)

Extended information on the protein

  • Kinetic information:
  • Effectors of protein activity: phosphorylation by PtkA stimulates activity of Ugd PubMed

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • 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

Lei Shi, Boyang Ji, Lorena Kolar-Znika, Ana Boskovic, Fanny Jadeau, Christophe Combet, Christophe Grangeasse, Damjan Franjevic, Emmanuel Talla, Ivan Mijakovic
Evolution of bacterial protein-tyrosine kinases and their relaxed specificity toward substrates.
Genome Biol Evol: 2014, 6(4);800-17
[PubMed:24728941] [WorldCat.org] [DOI] (I p)

Taryn B Kiley, Nicola R Stanley-Wall
Post-translational control of Bacillus subtilis biofilm formation mediated by tyrosine phosphorylation.
Mol Microbiol: 2010, 78(4);947-63
[PubMed:20815827] [WorldCat.org] [DOI] (I p)

Dina Petranovic, Christophe Grangeasse, Boris Macek, Mohammad Abdillatef, Virginie Gueguen-Chaignon, Sylvie Nessler, Josef Deutscher, Ivan Mijakovic
Activation of Bacillus subtilis Ugd by the BY-kinase PtkA proceeds via phosphorylation of its residue tyrosine 70.
J Mol Microbiol Biotechnol: 2009, 17(2);83-9
[PubMed:19258708] [WorldCat.org] [DOI] (I p)

Ivan Mijakovic, Lucia Musumeci, Lutz Tautz, Dina Petranovic, Robert A Edwards, Peter Ruhdal Jensen, Tomas Mustelin, Josef Deutscher, Nunzio Bottini
In vitro characterization of the Bacillus subtilis protein tyrosine phosphatase YwqE.
J Bacteriol: 2005, 187(10);3384-90
[PubMed:15866923] [WorldCat.org] [DOI] (P p)

Ivan Mijakovic, Dina Petranovic, Josef Deutscher
How tyrosine phosphorylation affects the UDP-glucose dehydrogenase activity of Bacillus subtilis YwqF.
J Mol Microbiol Biotechnol: 2004, 8(1);19-25
[PubMed:15741737] [WorldCat.org] [DOI] (P p)

Ivan Mijakovic, Sandrine Poncet, Grégory Boël, Alain Mazé, Sylvie Gillet, Emmanuel Jamet, Paulette Decottignies, Christophe Grangeasse, Patricia Doublet, Pierre Le Maréchal, Josef Deutscher
Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases.
EMBO J: 2003, 22(18);4709-18
[PubMed:12970183] [WorldCat.org] [DOI] (P p)