Difference between revisions of "MtnD"

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(Extended information on the protein)
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=== Database entries ===
 
=== Database entries ===

Revision as of 18:12, 2 December 2011

  • Description: 1,2,-dihydroxy-3-keto-5-methylthiopentene dioxygenase

Gene name mtnD
Synonyms ykrZ
Essential no
Product 1,2,-dihydroxy-3-keto-5-methylthiopentene dioxygenase
Function methionine salvage
Metabolic function and regulation of this protein in SubtiPathways:
Cys, Met & Sulfate assimilation
MW, pI 20 kDa, 4.408
Gene length, protein length 534 bp, 178 aa
Immediate neighbours mtnB, ykvA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YkrZ context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

biosynthesis/ acquisition of amino acids

This gene is a member of the following regulons

S-box

The gene

Basic information

  • Locus tag: BSU13620

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 3-(methylthio)propanoate + formate + CO (according to Swiss-Prot)
  • Protein family: acireductone dioxygenase (ARD) 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

  • Regulation:
  • Regulatory mechanism: S-box: transcription termination/ antitermination, the S-box riboswitch binds S-adenosylmethionine resulting in termination PubMed
  • 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

Jerneja Tomsic, Brooke A McDaniel, Frank J Grundy, Tina M Henkin
Natural variability in S-adenosylmethionine (SAM)-dependent riboswitches: S-box elements in bacillus subtilis exhibit differential sensitivity to SAM In vivo and in vitro.
J Bacteriol: 2008, 190(3);823-33
[PubMed:18039762] [WorldCat.org] [DOI] (I p)

Agnieszka Sekowska, Valérie Dénervaud, Hiroki Ashida, Karine Michoud, Dieter Haas, Akiho Yokota, Antoine Danchin
Bacterial variations on the methionine salvage pathway.
BMC Microbiol: 2004, 4;9
[PubMed:15102328] [WorldCat.org] [DOI] (I e)

Maumita Mandal, Benjamin Boese, Jeffrey E Barrick, Wade C Winkler, Ronald R Breaker
Riboswitches control fundamental biochemical pathways in Bacillus subtilis and other bacteria.
Cell: 2003, 113(5);577-86
[PubMed:12787499] [WorldCat.org] [DOI] (P p)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)

Agnieszka Sekowska, Antoine Danchin
The methionine salvage pathway in Bacillus subtilis.
BMC Microbiol: 2002, 2;8
[PubMed:12022921] [WorldCat.org] [DOI] (I e)

Brooke A Murphy, Frank J Grundy, Tina M Henkin
Prediction of gene function in methylthioadenosine recycling from regulatory signals.
J Bacteriol: 2002, 184(8);2314-8
[PubMed:11914366] [WorldCat.org] [DOI] (P p)