Difference between revisions of "GlyA"

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=== Basic information ===
 
=== Basic information ===
  
* '''Locus tag:'''
+
* '''Locus tag:''' BSU36900
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
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* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P39148 P39148]
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P39148 P39148]
  
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU36900 BSU36900]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU36900]
  
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.1.2.1 2.1.2.1]
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.1.2.1 2.1.2.1]

Revision as of 09:33, 3 June 2009

  • Description: serine hydroxymethyltransferase

Gene name glyA
Synonyms glyC, ipc-34d
Essential yes PubMed
Product serine hydroxymethyltransferase
Function biosynthesis of glycine
MW, pI 45 kDa, 5.475
Gene length, protein length 1245 bp, 415 aa
Immediate neighbours upp, ywlG
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
GlyA context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU36900

Phenotypes of a mutant

essential PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine (according to Swiss-Prot)
  • Protein family: SHMT family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylated on ser/ thr/ tyr PubMed, PubMed
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

  • Structure: 2VGU (complex with L-serine, Geobacillus stearothermophilus), 2VI8 (Geobacillus stearothermophilus)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • repressed in the presence of adenine or adenosine(PurR) PubMed
  • Regulatory mechanism:
    • PurR: transcription repression (molecular inducer: PRPP) 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

Yann Duroc, Carmela Giglione, Thierry Meinnel
Mutations in three distinct loci cause resistance to peptide deformylase inhibitors in Bacillus subtilis.
Antimicrob Agents Chemother: 2009, 53(4);1673-8
[PubMed:19171795] [WorldCat.org] [DOI] (I p)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)


  1. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed