Difference between revisions of "MtnW"

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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU13590&redirect=T BSU13590]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/mtnWXBD.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/mtnWXBD.html]
Line 95: Line 96:
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU13590&redirect=T BSU13590]
  
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=2ZVI 2ZVI] {{PubMed|19690372}}
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=2ZVI 2ZVI] {{PubMed|19690372}}

Revision as of 13:32, 2 April 2014

  • Description: 2,3-diketo-5-methylthiopentyl-1-phosphate enolase, Rubisco-like protein

Gene name mtnW
Synonyms ykrW
Essential no
Product 2,3-diketo-5-methylthiopentyl-1-phosphate enolase
Function methionine salvage
Gene expression levels in SubtiExpress: mtnW
Metabolic function and regulation of this protein in SubtiPathways:
mtnW
MW, pI 44 kDa, 5.284
Gene length, protein length 1242 bp, 414 aa
Immediate neighbours mtnE, mtnX
Sequences Protein DNA DNA_with_flanks
Genetic context
YkrW context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
MtnW expression.png




























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: BSU13590

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 5-(methylthio)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate (according to Swiss-Prot)
  • Protein family: Type IV subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • 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

Additional publications: PubMed

Haruka Tamura, Yohtaro Saito, Hiroki Ashida, Yasushi Kai, Tsuyoshi Inoue, Akiho Yokota, Hiroyoshi Matsumura
Structure of the apo decarbamylated form of 2,3-diketo-5-methylthiopentyl-1-phosphate enolase from Bacillus subtilis.
Acta Crystallogr D Biol Crystallogr: 2009, 65(Pt 9);942-51
[PubMed:19690372] [WorldCat.org] [DOI] (I p)

Yohtaro Saito, Hiroki Ashida, Tomoko Sakiyama, Nicole Tandeau de Marsac, Antoine Danchin, Agnieszka Sekowska, Akiho Yokota
Structural and functional similarities between a ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO)-like protein from Bacillus subtilis and photosynthetic RuBisCO.
J Biol Chem: 2009, 284(19);13256-64
[PubMed:19279009] [WorldCat.org] [DOI] (P p)

Haruka Tamura, Hiroki Ashida, Shogo Koga, Yohtaro Saito, Tomonori Yadani, Yasushi Kai, Tsuyoshi Inoue, Akiho Yokota, Hiroyoshi Matsumura
Crystallization and preliminary X-ray analysis of 2,3-diketo-5-methylthiopentyl-1-phosphate enolase from Bacillus subtilis.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2009, 65(Pt 2);147-50
[PubMed:19194007] [WorldCat.org] [DOI] (I p)

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)

Hiroki Ashida, Yohtaro Saito, Chojiro Kojima, Kazuo Kobayashi, Naotake Ogasawara, Akiho Yokota
A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO.
Science: 2003, 302(5643);286-90
[PubMed:14551435] [WorldCat.org] [DOI] (I p)

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)

F J Grundy, T M Henkin
The S box regulon: a new global transcription termination control system for methionine and cysteine biosynthesis genes in gram-positive bacteria.
Mol Microbiol: 1998, 30(4);737-49
[PubMed:10094622] [WorldCat.org] [DOI] (P p)