ThrC

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• BsubCyc: BSU32250

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Domains:

• Modification:

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU32250

• Structure: 1UIN (from Thermus thermophilus, 51% identity, 69% similarity) PubMed

• UniProt: P04990

• KEGG entry: [2]

• E.C. number: 4.2.3.1

Expression and regulation

• Operon: hom-thrC-thrB PubMed

• Expression browser: thrC PubMed

• Sigma factor:

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

• Regulatory mechanism:
  • CodY: transcription repression PubMed

• Additional information:
  • belongs to the 100 most abundant proteins PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 5810 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 3216 PubMed

Biological materials

• Mutant:
  • 1A773 ( thrC::cat), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)