Difference between revisions of "Kbl"

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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=kbl_1771517_1772695_1 kbl] {{PubMed|22383849}}
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=Biological materials =
 
=Biological materials =

Revision as of 09:25, 13 April 2012

  • Description: 2-amino-3-ketobutyrate CoA ligase

Gene name kbl
Synonyms
Essential no
Product 2-amino-3-ketobutyrate CoA ligase
Function threonine utilization
Metabolic function and regulation of this protein in SubtiPathways:
Lys, Thr
MW, pI 43 kDa, 6.25
Gene length, protein length 1176 bp, 392 aa
Immediate neighbours tdh, ymcB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Kbl context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

utilization of amino acids

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU17000

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Acetyl-CoA + glycine = CoA + 2-amino-3-oxobutanoate (according to Swiss-Prot)
  • Protein family: class-II pyridoxal-phosphate-dependent aminotransferase family (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: 1FC4 (from Escherichia coli, 40% identity, 60% similarity) PubMed
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
  • 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

A Schmidt, J Sivaraman, Y Li, R Larocque, J A Barbosa, C Smith, A Matte, J D Schrag, M Cygler
Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism.
Biochemistry: 2001, 40(17);5151-60
[PubMed:11318637] [WorldCat.org] [DOI] (P p)