Difference between revisions of "MtnW"

From SubtiWiki
Jump to: navigation, search
(Undo revision 129389 by Awynalaxa (talk))
Line 50: Line 50:
= Categories containing this gene/protein =
{{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}}
=The protein=
=The protein=

Revision as of 18:14, 30 November 2010

  • 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
Metabolic function and regulation of this protein in SubtiPathways:
Cys, Met & Sulfate assimilation
MW, pI 44 kDa, 5.284
Gene length, protein length 1242 bp, 414 aa
Immediate neighbours mtnE, mtnX
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YkrW context.gif
This image was kindly provided by SubtiList

The gene

Basic information

  • Locus tag: BSU13590

Phenotypes of a mutant

Database entries

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

Additional information

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids

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:
  • Interactions:
  • Localization:

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


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)