AlsD

• Description: acetolactate decarboxylase
  
  

Gene name	alsD
Synonyms
Essential	no
Product	acetolactate decarboxylase)
Function	overflow metabolism
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	28 kDa, 4.603
Gene length, protein length	765 bp, 255 aa
Immediate neighbours	ywrO, alsS
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU36000

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: (2S)-2-hydroxy-2-methyl-3-oxobutanoate = (3R)-3-hydroxybutan-2-one + CO₂ (according to Swiss-Prot)

• Protein family: alpha-acetolactate decarboxylase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylated on ser/ thr/ tyr PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• Swiss prot entry: Q04777

• KEGG entry: [3]

• E.C. number: 4.1.1.5

Expression and regulation

• Operon: alsS-alsD PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induction by acetate (AlsR) PubMed
  • induced under anaerobic conditions (Rex) PubMed

Note: since acetate formation requires ackA activation by CcpA there is an indirect effect of CcpA on the alsS-alsD operon: the operon is not expressed in ccpA mutants

• Regulatory mechanism:
  • AlsR: transcription activation in the presence of acetate PubMed
  • Rex: transcription repression if the ratio NADH2/NAD is high PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Takashi Inaoka, Takenori Satomura, Yasutaro Fujita, Kozo Ochi
Novel gene regulation mediated by overproduction of secondary metabolite neotrehalosadiamine in Bacillus subtilis.
FEMS Microbiol Lett: 2009, 291(2);151-6
[PubMed:19087206] [WorldCat.org] [DOI] (I p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)

Heike Reents, Richard Münch, Thorben Dammeyer, Dieter Jahn, Elisabeth Härtig
The Fnr regulon of Bacillus subtilis.
J Bacteriol: 2006, 188(3);1103-12
[PubMed:16428414] [WorldCat.org] [DOI] (P p)

A J Turinsky, T R Moir-Blais, F J Grundy, T M Henkin
Bacillus subtilis ccpA gene mutants specifically defective in activation of acetoin biosynthesis.
J Bacteriol: 2000, 182(19);5611-4
[PubMed:10986270] [WorldCat.org] [DOI] (P p)

M C Renna, N Najimudin, L R Winik, S A Zahler
Regulation of the Bacillus subtilis alsS, alsD, and alsR genes involved in post-exponential-phase production of acetoin.
J Bacteriol: 1993, 175(12);3863-75
[PubMed:7685336] [WorldCat.org] [DOI] (P p)

1. Lévine et al. (2006) Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes. Proteomics 6: 2157-2173 PubMed
2. Renna, M. C., Najimudin, N., Winik, L. R., and Zahler, S. A. (1993). Regulation of the Bacillus subtilis alsS, alsD, and alsR genes involved in post-exponential-phase production of acetoin. J. Bacteriol. 175, 3863-3875. PubMed
3. Reents, H., R. Münch, T. Dammeyer, D. Jahn, and E. Härtig. 2006. The Fnr regulon of Bacillus subtilis. J. Bacteriol. 188: 1103-1112. PubMed
4. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed