Difference between revisions of "BkdB"
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=Expression and regulation= | =Expression and regulation= | ||
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* '''Operon:''' ''[[ptb]]-[[bcd]]-[[buk]]-[[lpdV]]-[[bkdAA]]-[[bkdAB]]-[[bkdB]]'' | * '''Operon:''' ''[[ptb]]-[[bcd]]-[[buk]]-[[lpdV]]-[[bkdAA]]-[[bkdAB]]-[[bkdB]]'' | ||
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* '''Regulation:''' | * '''Regulation:''' | ||
| − | ** | + | ** induced in the presence of isoleucine or valine ([[BkdR]]) {{PubMed|10094682}} |
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
** [[CodY]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/10094682 PubMed] | ** [[CodY]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/10094682 PubMed] | ||
| + | ** [[BkdR]]: transcription activation {{PubMed|10094682}} | ||
* '''Additional information:''' | * '''Additional information:''' | ||
Revision as of 21:22, 19 November 2009
- Description: 2-oxoisovalerate dehydrogenase (E2 subunit, lipoamide acyltransferase)
| Gene name | bkdB |
| Synonyms | bfmBB, bfmB2, bkd |
| Essential | no |
| Product | 2-oxoisovalerate dehydrogenase (E2 subunit, lipoamide acyltransferase) |
| Function | utilization of branched-chain keto acids |
| Metabolic function and regulation of this protein in SubtiPathways: Ile, Leu, Val | |
| MW, pI | 45 kDa, 5.301 |
| Gene length, protein length | 1272 bp, 424 aa |
| Immediate neighbours | bmrR, bkdAB |
| 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: BSU24030
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: 2-methylpropanoyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-(2-methylpropanoyl)dihydrolipoyl)lysine (according to Swiss-Prot)
- Protein family: 2-oxoacid dehydrogenase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: Nucleoid (Heterogeneous) PubMed
Database entries
- Structure:
- UniProt: P37942
- KEGG entry: [3]
- E.C. number: 2.3.1.168
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)
