Difference between revisions of "YoaD"

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* '''Operon:''' ''[[yoaD]]-[[yoaC]]-[[yoaB]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/10094622 PubMed]
 
* '''Operon:''' ''[[yoaD]]-[[yoaC]]-[[yoaB]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/10094622 PubMed]
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yoaD_2024042_2025076_-1 yoaD] {{PubMed|22383849}}
  
 
* '''Sigma factor:'''  
 
* '''Sigma factor:'''  

Revision as of 10:08, 13 April 2012

  • Description: similar to phosphoglycerate dehydrogenase

Gene name yoaD
Synonyms
Essential no
Product unknown
Function methionine biosynthesis
Metabolic function and regulation of this protein in SubtiPathways:
Cys, Met & Sulfate assimilation
MW, pI 38 kDa, 5.62
Gene length, protein length 1032 bp, 344 aa
Immediate neighbours yoaC, yoaE
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YoaD context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

biosynthesis/ acquisition of amino acids

This gene is a member of the following regulons

S-box

The gene

Basic information

  • Locus tag: BSU18560

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: YoaD is likely to convert 3-phosphoglycerate to serine for use in methionine biosynthesis (based on S-box regulation)
  • Protein family:
  • 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: [2]
  • E.C. number:

Additional information

The gene is annotated in KEGG as an ortholog of D-3-phosphoglycerate dehydrogenase EC 1.1.1.95. No EC annotation is available in Swiss-Prot. In MetaCyc the protein is marked as “similar to phosphorglycerate dehydrogenase”. No literature/experimental evidence supporting the annotation is available. PubMed

Expression and regulation

  • Sigma factor:
  • 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

References

Ana Gutiérrez-Preciado, Tina M Henkin, Frank J Grundy, Charles Yanofsky, Enrique Merino
Biochemical features and functional implications of the RNA-based T-box regulatory mechanism.
Microbiol Mol Biol Rev: 2009, 73(1);36-61
[PubMed:19258532] [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)

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)

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)