Difference between revisions of "YlaM"

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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=glsB_1551385_1552314_1 ylaM] {{PubMed|22383849}}
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=Biological materials =
 
=Biological materials =

Revision as of 08:15, 13 April 2012

  • Description: glutaminase, high affinity for glutamine

Gene name ylaM
Synonyms
Essential no
Product glutaminase
Function glutamine degradation
MW, pI 33 kDa, 5.676
Gene length, protein length 927 bp, 309 aa
Immediate neighbours ylaL, ylaN
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YlaM context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

utilization of amino acids

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU14830

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: L-glutamine + H2O = L-glutamate + NH3 (according to Swiss-Prot)
  • Protein family: glutaminase family (according to Swiss-Prot)
  • Paralogous protein(s): GlsA

Extended information on the protein

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

Database entries

  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • 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

Greg Brown, Alex Singer, Michael Proudfoot, Tatiana Skarina, Youngchang Kim, Changsoo Chang, Irina Dementieva, Ekaterina Kuznetsova, Claudio F Gonzalez, Andrzej Joachimiak, Alexei Savchenko, Alexander F Yakunin
Functional and structural characterization of four glutaminases from Escherichia coli and Bacillus subtilis.
Biochemistry: 2008, 47(21);5724-35
[PubMed:18459799] [WorldCat.org] [DOI] (I p)