Difference between revisions of "GlyA"

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|style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of glycine
 
|style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of glycine
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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/BSU36900 glyA]
 
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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/ala_gly_ser.html Ala, Gly, Ser]'''
 
|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/ala_gly_ser.html Ala, Gly, Ser]'''

Revision as of 16:54, 7 August 2012

  • Description: serine hydroxymethyltransferase

Gene name glyA
Synonyms glyC, ipc-34d
Essential yes PubMed
Product serine hydroxymethyltransferase
Function biosynthesis of glycine
Gene expression levels in SubtiExpress: glyA
Metabolic function and regulation of this protein in SubtiPathways:
Ala, Gly, Ser
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
Expression at a glance   PubMed
GlyA expression.png




























Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, essential genes, phosphoproteins

This gene is a member of the following regulons

PurR regulon, T-box

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:

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
    • induced by glycine limitation (T-box) 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

Anant Narayan Bhatt, Vinod Bhakuni, Ashutosh Kumar, M Yahiya Khan, Mohammad Imran Siddiqi
Alkaline pH-dependent differential unfolding characteristics of mesophilic and thermophilic homologs of dimeric serine hydroxymethyltransferase.
Biochim Biophys Acta: 2010, 1804(6);1294-300
[PubMed:20152942] [WorldCat.org] [DOI] (P p)

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)

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)

H H Saxild, K Brunstedt, K I Nielsen, H Jarmer, P Nygaard
Definition of the Bacillus subtilis PurR operator using genetic and bioinformatic tools and expansion of the PurR regulon with glyA, guaC, pbuG, xpt-pbuX, yqhZ-folD, and pbuO.
J Bacteriol: 2001, 183(21);6175-83
[PubMed:11591660] [WorldCat.org] [DOI] (P p)