Difference between revisions of "MurAB"

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(Basic information/ Evolution)
(References)
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<pubmed>19270101  </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 20:51, 1 May 2010

  • Description: UDP-N-acetylglucosamine 1-carboxyvinyltransferase

Gene name murAB
Synonyms murZ, lssF, rev-4
Essential no
Product UDP-N-acetylglucosamine 1-carboxyvinyltransferase
Function peptidoglycan precursor biosynthesis
Metabolic function and regulation of this protein in SubtiPathways:
Cell wall
MW, pI 45 kDa, 5.831
Gene length, protein length 1287 bp, 429 aa
Immediate neighbours glpX, ywjH
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
MurAB context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU37100

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine (according to Swiss-Prot)
  • Protein family: MurA subfamily (according to Swiss-Prot)
  • Paralogous protein(s): MurAA

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

  • Structure: 1UAE (from Escherichia coli, 43% identity, 61% similarity) PubMed
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Regulation: constitutive PubMed
  • 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

Matthieu Jules, Ludovic Le Chat, Stéphane Aymerich, Dominique Le Coq
The Bacillus subtilis ywjI (glpX) gene encodes a class II fructose-1,6-bisphosphatase, functionally equivalent to the class III Fbp enzyme.
J Bacteriol: 2009, 191(9);3168-71
[PubMed:19270101] [WorldCat.org] [DOI] (I p)