SpeD

• 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 This image was kindly provided by SubtiList

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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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: 1VR7 (from Thermotoga maritima, 47% identity, 72% similarity)

• UniProt: O34426

• KEGG entry: [3]

• E.C. number: 4.1.1.50

Expression and regulation

• Operon:
  • gapB-speD PubMed
  • speD PubMed

• Expression browser: speD PubMed

• Sigma factor:
  • gapB: SigA PubMed
  • speD: SigA PubMed

• Regulation:
  • gapB: repressed in the presence of glucose (CcpN) PubMed

• Regulatory mechanism:
  • CcpN: transcription repression PubMed

• 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:

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