Kbl
Revision as of 10:02, 19 April 2012 by 134.76.70.252 (talk)
- 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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
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
- UniProt: O31777
- KEGG entry: [2]
- E.C. number: 2.3.1.29
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)