Difference between revisions of "SpeD"

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|style="background:#ABCDEF;" align="center"|'''Function''' || spermidine, polyamine biosynthesis
 
|style="background:#ABCDEF;" align="center"|'''Function''' || spermidine, polyamine biosynthesis
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU29010 speD]
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/cys_meth_and_sulfate_assimilation.html Cys, Met & Sulfate assimilation], [http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]'''
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/cys_meth_and_sulfate_assimilation.html Cys, Met & Sulfate assimilation], [http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]'''

Revision as of 14:48, 7 August 2012

  • Description: S-adenosylmethionine decarboxylase

Gene name speD
Synonyms ytcF
Essential no
Product S-adenosylmethionine decarboxylase
Function spermidine, polyamine biosynthesis
Gene expression levels in SubtiExpress: speD
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
Expression at a glance   PubMed
SpeD expression.png




























Categories containing this gene/protein

miscellaneous metabolic pathways

This gene is a member of the following regulons

CcpN regulon

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:

Database entries

  • Structure: 1VR7 (from Thermotoga maritima, 47% identity, 72% similarity)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information:
    • speD: the mRNA is substantially stabilized upon depletion of RNase Y (the half-life of the monocistronic speD mRNA increases from 1.4 to 36 min) PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J  
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. 
Mol Microbiol. 2011 81(6): 1459-1473. 
PubMed:21815947

Pascale Servant, Dominique Le Coq, Stéphane Aymerich
CcpN (YqzB), a novel regulator for CcpA-independent catabolite repression of Bacillus subtilis gluconeogenic genes.
Mol Microbiol: 2005, 55(5);1435-51
[PubMed:15720552] [WorldCat.org] [DOI] (P p)

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)

A Sekowska, P Bertin, A Danchin
Characterization of polyamine synthesis pathway in Bacillus subtilis 168.
Mol Microbiol: 1998, 29(3);851-8
[PubMed:9723923] [WorldCat.org] [DOI] (P p)