Kbl

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

Gene name	kbl
Synonyms
Essential	no
Product	2-amino-3-ketobutyrate CoA ligase
Function	threonine utilization
Gene expression levels in SubtiExpress: kbl
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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

utilization of amino acids

The gene

Basic information

• Locus tag: BSU17000

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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:
  • pyridoxal-phosphate (according to Swiss-Prot)

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 1FC4 (from Escherichia coli, 40% identity, 60% similarity) PubMed

• UniProt: O31777

• KEGG entry: [2]

• E.C. number: 2.3.1.29

Expression and regulation

• Operon:

• Expression browser: kbl PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Germán Plata, Tobias Fuhrer, Tzu-Lin Hsiao, Uwe Sauer, Dennis Vitkup
Global probabilistic annotation of metabolic networks enables enzyme discovery.
Nat Chem Biol: 2012, 8(10);848-54
[PubMed:22960854] [WorldCat.org] [DOI] (I p)

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)