Difference between revisions of "ThrB"

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(Extended information on the protein)
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* '''Operon:''' ''[[hom]]-[[thrC]]-[[thrB]]'' {{PubMed|12107147}}
 
* '''Operon:''' ''[[hom]]-[[thrC]]-[[thrB]]'' {{PubMed|12107147}}
  
* '''[[Sigma factor]]:'''  
+
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=thrB_3312844_3313773_-1 thrB] {{PubMed|22383849}}
 +
 
 +
* '''Sigma factor:'''  
  
 
* '''Regulation:''' repressed by casamino acids {{PubMed|12107147}}   
 
* '''Regulation:''' repressed by casamino acids {{PubMed|12107147}}   

Revision as of 16:39, 16 April 2012

  • Description: homoserine kinase

Gene name thrB
Synonyms thrA
Essential no
Product homoserine kinase
Function biosynthesis of threonine
Metabolic function and regulation of this protein in SubtiPathways:
Lys, Thr
MW, pI 33 kDa, 4.735
Gene length, protein length 927 bp, 309 aa
Immediate neighbours yuxL, thrC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
ThrB context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

biosynthesis/ acquisition of amino acids

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU32240

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + L-homoserine = ADP + O-phospho-L-homoserine (according to Swiss-Prot)
  • Protein family: Homoserine kinase subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 3HUL (from Listeria monocytogenes, 41% identity, 61% similarity)
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation: repressed by casamino acids PubMed
  • Regulatory mechanism:
  • 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

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)