Difference between revisions of "Bcd"
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=== Database entries === | === Database entries === | ||
− | * '''Structure:''' | + | * '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?pdbId=1LEH 1LEH] (from '' Lysinibacillus sphaericus'', 71% identity, 82% similarity) {{PubMed|8591046}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P54531 P54531] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P54531 P54531] |
Revision as of 10:19, 4 February 2010
- Description: valine dehydrogenase, isoleucine dehydrogenase, L-leucine dehydrogenase
Gene name | bcd |
Synonyms | bkd, yqiT |
Essential | no |
Product | valine dehydrogenase, isoleucine dehydrogenase, L-leucine dehydrogenase |
Function | utilization of branched-chain keto acids |
Metabolic function and regulation of this protein in SubtiPathways: Ile, Leu, Val | |
MW, pI | 39 kDa, 4.942 |
Gene length, protein length | 1092 bp, 364 aa |
Immediate neighbours | buk, ptb |
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: BSU24080
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: L-leucine + H2O + NAD+ = 4-methyl-2-oxopentanoate + NH3 + NADH (according to Swiss-Prot)
- Protein family: Glu/Leu/Phe/Val dehydrogenases 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:
Database entries
- UniProt: P54531
- KEGG entry: [3]
- E.C. number: 1.4.1.9
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
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)
Ken-ichi Yoshida, Hirotake Yamaguchi, Masaki Kinehara, Yo-hei Ohki, Yoshiko Nakaura, Yasutaro Fujita
Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box.
Mol Microbiol: 2003, 49(1);157-65
[PubMed:12823818]
[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)