Difference between revisions of "ThrC"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
{{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}}
+
{{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}},
 +
[[most abundant proteins]]
  
 
= This gene is a member of the following [[regulons]] =
 
= This gene is a member of the following [[regulons]] =
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* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
 
** [[CodY]]: transcription repression {{PubMed|24163341}}
 
** [[CodY]]: transcription repression {{PubMed|24163341}}
 +
 
* '''Additional information:'''
 
* '''Additional information:'''
 +
** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
  
 
=Biological materials =
 
=Biological materials =
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=References=
 
=References=
  
<pubmed>12107147 3098560, 24163341</pubmed>
+
<pubmed>12107147 3098560, 24163341 15378759</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 17:56, 5 March 2014

  • Description: threonine synthase

Gene name thrC
Synonyms thrB
Essential no
Product threonine synthase
Function biosynthesis of threonine
Gene expression levels in SubtiExpress: thrC
Metabolic function and regulation of this protein in SubtiPathways:
thrC
MW, pI 37 kDa, 5.185
Gene length, protein length 1056 bp, 352 aa
Immediate neighbours thrB, hom
Sequences Protein DNA DNA_with_flanks
Genetic context
ThrC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ThrC expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, most abundant proteins

This gene is a member of the following regulons

CodY regulon

The gene

Basic information

  • Locus tag: BSU32250

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: O-phospho-L-homoserine + H2O = L-threonine + phosphate (according to Swiss-Prot)
  • Protein family: serine/threonine dehydratase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure: 1UIN (from Thermus thermophilus, 51% identity, 69% similarity) PubMed
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Regulation:
    • repressed by casamino acids PubMed
    • repressed during growth in the presence of branched chain amino acids (CodY) PubMed
  • Regulatory mechanism:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Allison Kriel, Shaun R Brinsmade, Jessica L Tse, Ashley K Tehranchi, Alycia N Bittner, Abraham L Sonenshein, Jue D Wang
GTP dysregulation in Bacillus subtilis cells lacking (p)ppGpp results in phenotypic amino acid auxotrophy and failure to adapt to nutrient downshift and regulate biosynthesis genes.
J Bacteriol: 2014, 196(1);189-201
[PubMed:24163341] [WorldCat.org] [DOI] (I p)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [WorldCat.org] [DOI] (P 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)

C Parsot
Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase.
EMBO J: 1986, 5(11);3013-9
[PubMed:3098560] [WorldCat.org] [DOI] (P p)