Difference between revisions of "GlyA"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[upp]]'', ''[[ywlG]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[upp]]'', ''[[ywlG]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU36900 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU36900 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU36900 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU36900 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU36900 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU36900 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:glyA_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:glyA_context.gif]]

Revision as of 11:30, 14 May 2013

  • 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
Sequences Protein DNA DNA_with_flanks
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)