Difference between revisions of "YjmD"

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=References=
 
=References=
  
<pubmed> 9579062, 9882655, 10666464 17573341 </pubmed>
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<pubmed> 9579062, 9882655, 10666464 17573341 22900538 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 09:34, 29 August 2012

  • Description: galactitol-1-phosphate dehydrogenase

Gene name yjmD
Synonyms
Essential no
Product galactitol-1-phosphate dehydrogenase
Function utilization of dulcitol
Gene expression levels in SubtiExpress: yjmD
MW, pI 36 kDa, 6.115
Gene length, protein length 1017 bp, 339 aa
Immediate neighbours yjmC, uxuA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YjmD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YjmD expression.png















Categories containing this gene/protein

utilization of specific carbon sources, sporulation proteins

This gene is a member of the following regulons

CcpA regulon, ExuR regulon, SigE regulon

The gene

Basic information

  • Locus tag: BSU12330

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: zinc-containing alcohol dehydrogenase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • 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

Bogumiła C Marciniak, Monika Pabijaniak, Anne de Jong, Robert Dűhring, Gerald Seidel, Wolfgang Hillen, Oscar P Kuipers
High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis.
BMC Genomics: 2012, 13;401
[PubMed:22900538] [WorldCat.org] [DOI] (I e)

You-Kwan Oh, Bernhard O Palsson, Sung M Park, Christophe H Schilling, Radhakrishnan Mahadevan
Genome-scale reconstruction of metabolic network in Bacillus subtilis based on high-throughput phenotyping and gene essentiality data.
J Biol Chem: 2007, 282(39);28791-28799
[PubMed:17573341] [WorldCat.org] [DOI] (P p)

Y Miwa, A Nakata, A Ogiwara, M Yamamoto, Y Fujita
Evaluation and characterization of catabolite-responsive elements (cre) of Bacillus subtilis.
Nucleic Acids Res: 2000, 28(5);1206-10
[PubMed:10666464] [WorldCat.org] [DOI] (I p)

K R Mekjian, E M Bryan, B W Beall, C P Moran
Regulation of hexuronate utilization in Bacillus subtilis.
J Bacteriol: 1999, 181(2);426-33
[PubMed:9882655] [WorldCat.org] [DOI] (P p)

Carlo Rivolta, Blazenka Soldo, Vladimir Lazarevic, Bernard Joris, Catherine Mauël, Dimitri Karamat
A 35.7 kb DNA fragment from the Bacillus subtilis chromosome containing a putative 12.3 kb operon involved in hexuronate catabolism and a perfectly symmetrical hypothetical catabolite-responsive element.
Microbiology (Reading): 1998, 144 ( Pt 4);877-884
[PubMed:9579062] [WorldCat.org] [DOI] (P p)