Difference between revisions of "SpeD"

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* '''Structure:'''
 
* '''Structure:'''
  
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O34426 O34426]
+
* '''UniProt:''' [http://www.uniprot.org/uniprot/O34426 O34426]
  
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU29010]
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU29010]

Revision as of 14:04, 20 July 2009

  • Description: S-adenosylmethionine decarboxylase

Gene name speD
Synonyms ytcF
Essential no
Product S-adenosylmethionine decarboxylase
Function spermidine, polyamine biosynthesis
Metabolic function and regulation of this protein in SubtiPathways:
Cys, Met & Sulfate assimilation, Central C-metabolism
MW, pI 13 kDa, 4.768
Gene length, protein length 384 bp, 128 aa
Immediate neighbours ytcG, gapB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
SpeD context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU29010

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO2 (according to Swiss-Prot)
  • Protein family: Type 1 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

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • 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

A Sekowska, J Y Coppée, J P Le Caer, I Martin-Verstraete, A Danchin
S-adenosylmethionine decarboxylase of Bacillus subtilis is closely related to archaebacterial counterparts.
Mol Microbiol: 2000, 36(5);1135-47
[PubMed:10844697] [WorldCat.org] [DOI] (P p)