Difference between revisions of "LpdV"

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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
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/fatty_acid_syn.html Lipid synthesis], [http://subtiwiki.uni-goettingen.de/pathways/ile_val_leu.html Ile, Leu, Val]'''
+
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/fatty_acid_synthesis.html Lipid synthesis], [http://subtiwiki.uni-goettingen.de/pathways/ile_val_leu.html Ile, Leu, Val]'''
 
|-
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 48 kDa, 4.893   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 48 kDa, 4.893   

Revision as of 13:50, 7 March 2010

  • Description: 2-oxoisovalerate dehydrogenase (E3 subunit, dihydrolipoamide dehydrogenase)

Gene name lpdV
Synonyms yqiV, bkd
Essential no
Product 2-oxoisovalerate dehydrogenase
(E3 subunit, dihydrolipoamide dehydrogenase)
Function utilization of branched-chain keto acids
Metabolic function and regulation of this protein in SubtiPathways:
Lipid synthesis, Ile, Leu, Val
MW, pI 48 kDa, 4.893
Gene length, protein length 1371 bp, 457 aa
Immediate neighbours bkdAA, buk
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
LpdV context.gif
This image was kindly provided by SubtiList









The gene

Basic information

  • Locus tag: BSU24060

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH (according to Swiss-Prot)
  • Protein family: class-I pyridine nucleotide-disulfide oxidoreductase 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

  • Structure: 2YQU (from Thermus thermophilus (hb8 mutant), 42% identity, 55% similarity)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • induced in the presence of isoleucine or valine (BkdR) PubMed
  • 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)