Difference between revisions of "BkdAB"
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|style="background:#ABCDEF;" align="center"| '''Product''' || 2-oxoisovalerate dehydrogenase (E1 beta subunit) | |style="background:#ABCDEF;" align="center"| '''Product''' || 2-oxoisovalerate dehydrogenase (E1 beta subunit) | ||
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|style="background:#ABCDEF;" align="center"|'''Function''' || utilization of branched-chain keto acids | |style="background:#ABCDEF;" align="center"|'''Function''' || utilization of branched-chain keto acids |
Revision as of 13:05, 17 June 2009
- Description: 2-oxoisovalerate dehydrogenase (E1 beta subunit)
Gene name | bkdAB |
Synonyms | bfmBAB, bfmB1b, bkd |
Essential | no |
Product | 2-oxoisovalerate dehydrogenase (E1 beta subunit) |
Function | utilization of branched-chain keto acids |
MW, pI | 35 kDa, 4.791 |
Gene length, protein length | 981 bp, 327 aa |
Immediate neighbours | bkdB, bkdAA |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU24040
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2 (according to Swiss-Prot)
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: Cytoplasm (Homogeneous) PubMed
Database entries
- Structure:
- Swiss prot entry:
- KEGG entry: [3]
- E.C. number: 1.2.4.4
Additional information
Expression and regulation
- 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
Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537]
[WorldCat.org]
[DOI]
(P p)
M Nickel, G Homuth, C Böhnisch, U Mäder, T Schweder
Cold induction of the Bacillus subtilis bkd operon is mediated by increased mRNA stability.
Mol Genet Genomics: 2004, 272(1);98-107
[PubMed:15241682]
[WorldCat.org]
[DOI]
(P p)
Tanja Kaan, Georg Homuth, Ulrike Mäder, Julia Bandow, Thomas Schweder
Genome-wide transcriptional profiling of the Bacillus subtilis cold-shock response.
Microbiology (Reading): 2002, 148(Pt 11);3441-3455
[PubMed:12427936]
[WorldCat.org]
[DOI]
(P p)
M Debarbouille, R Gardan, M Arnaud, G Rapoport
Role of bkdR, a transcriptional activator of the sigL-dependent isoleucine and valine degradation pathway in Bacillus subtilis.
J Bacteriol: 1999, 181(7);2059-66
[PubMed:10094682]
[WorldCat.org]
[DOI]
(P p)