Difference between revisions of "SpeD"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ytcG]]'', ''[[gapB]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ytcG]]'', ''[[gapB]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU29010 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU29010 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU29010 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU29010 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU29010 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU29010 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:speD_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:speD_context.gif]]

Revision as of 11:58, 14 May 2013

  • 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
Sequences Protein DNA DNA_with_flanks
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)