Difference between revisions of "Sandbox"

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−
* '''Description:''' alkyl hydroperoxide reductase (large subunit) / NADH dehydrogenase <br/><br/>
+
* '''Description:''' acetolactate decarboxylase <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"|'''Gene name'''
 
|style="background:#ABCDEF;" align="center"|'''Gene name'''
−
|''ahpF''
+
|''alsD''
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''ndh ''
+
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' ''
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Product''' || alkyl hydroperoxide reductase (large subunit) / NADH dehydrogenase
+
|style="background:#ABCDEF;" align="center"| '''Product''' || acetolactate decarboxylase)
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"|'''Function''' || resistance against peroxide stres
+
|style="background:#ABCDEF;" align="center"|'''Function''' || overflow metabolism
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 54 kDa, 4.705  
+
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 28 kDa, 4.603  
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1527 bp, 509 aa  
+
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 765 bp, 255 aa  
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ahpC]]'', ''[[bglA]]''
+
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ywrO]]'', ''[[alsS]]''
 
|-
 
|-
−
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB16047&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
+
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB15617&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
 
|-
 
|-
−
|colspan="2" | '''Genetic context''' <br/> [[Image:ahpF_context.gif]]
+
|colspan="2" | '''Genetic context''' <br/> [[Image:alsD_context.gif]]
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
|-
 
|-
Line 35: Line 35:
 
=== Basic information ===
 
=== Basic information ===
  
−
* '''Locus tag:''' BSU40100
+
* '''Locus tag:''' BSU36000
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
Line 41: Line 41:
 
=== Database entries ===
 
=== Database entries ===
  
−
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ahpCF.html]
+
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/alsSD.html]
  
−
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG11204]
+
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10472]
  
 
=== Additional information===
 
=== Additional information===
Line 52: Line 52:
 
=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
−
* '''Catalyzed reaction/ biological activity:''' NADH + acceptor = NAD<sup>+</sup> + reduced acceptor (according to Swiss-Prot)  
+
* '''Catalyzed reaction/ biological activity:''' (2S)-2-hydroxy-2-methyl-3-oxobutanoate = (3R)-3-hydroxybutan-2-one + CO<sub>2</sub> (according to Swiss-Prot)  
  
−
* '''Protein family:''' class-II pyridine nucleotide-disulfide oxidoreductase family (according to Swiss-Prot)
+
* '''Protein family:''' alpha-acetolactate decarboxylase family (according to Swiss-Prot)
  
 
* '''Paralogous protein(s):'''
 
* '''Paralogous protein(s):'''
Line 64: Line 64:
 
* '''Domains:'''  
 
* '''Domains:'''  
  
−
* '''Modification:''' phosphorylation on (Ser-48 OR Ser-49) [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed]
+
* '''Modification:''' phosphorylated on ser/ thr/ tyr [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed]  
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
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* '''Interactions:'''
 
* '''Interactions:'''
  
−
* '''Localization:''' cell membrane (according to Swiss-Prot)
+
* '''Localization:'''
  
 
=== Database entries ===
 
=== Database entries ===
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* '''Structure:'''
 
* '''Structure:'''
  
−
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P42974 P42974]
+
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/Q04777 Q04777]
  
−
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU40100]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU36000]
  
−
* '''E.C. number:'''
+
* '''E.C. number:''' [http://www.expasy.org/enzyme/4.1.1.5 4.1.1.5]
  
 
=== Additional information===
 
=== Additional information===
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=Expression and regulation=
 
=Expression and regulation=
  
−
* '''Operon:''' ''[[ahpC]]-[[ahpF]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/8932314 PubMed]
+
* '''Operon:''' ''[[alsS]]-[[alsD]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/7685336 PubMed]
  
−
* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/8932314 PubMed]
+
* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/7685336 PubMed]
  
−
* '''Regulation:''' induced by H2O2 ([[PerR]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/11532148 PubMed]
+
* '''Regulation:''' induction by acetate ([[AlsR]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/7685336 PubMed], repressed as long as terminal electron acceptors are available for respiration ([[Rex]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/16428414 PubMed]
 +
Note: since acetate formation requires ''[[ackA]]'' activation by [[CcpA]] there is an indirect effect of [[CcpA]] on the ''alsSD'' operon: the operon is not expressed in ''[[ccpA]]'' mutants
  
−
* '''Regulatory mechanism:''' [[PerR]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/11532148 PubMed]
+
* '''Regulatory mechanism:''' [[AlsR]]: transcription activation in the presence of acetate [http://www.ncbi.nlm.nih.gov/sites/entrez/7685336 PubMed], [[Rex]]: transcription repression if the ratio NADH2/NAD is high [http://www.ncbi.nlm.nih.gov/sites/entrez/16428414 PubMed]
  
 
* '''Additional information:'''
 
* '''Additional information:'''
Line 118: Line 119:
 
=References=
 
=References=
  
−
<pubmed>17218307, </pubmed>
+
<pubmed>16493705 7685336 16428414, </pubmed>
−
# Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model  bacterium ''Bacillus subtilis''. Mol. Cell. Proteomics 6: 697-707  [http://www.ncbi.nlm.nih.gov/pubmed/17218307 PubMed]
+
# L&#233;vine 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 [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed]
 +
# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/7685336 PubMed]
 +
# Reents, H., R. Münch, T. Dammeyer, D. Jahn, and E. Härtig. 2006. The Fnr regulon of ''Bacillus subtilis''. J. Bacteriol. 188: 1103-1112. [http://www.ncbi.nlm.nih.gov/sites/entrez/16428414 PubMed]
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]

Revision as of 13:56, 8 June 2009

  • Description: acetolactate decarboxylase

Gene name alsD
Synonyms
Essential no
Product acetolactate decarboxylase)
Function overflow 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
AlsD context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU36000

Phenotypes of a mutant

Database entries

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

Additional information

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:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation: induction by acetate (AlsR) PubMed, repressed as long as terminal electron acceptors are available for respiration (Rex) PubMed

Note: since acetate formation requires ackA activation by CcpA there is an indirect effect of CcpA on the alsSD 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:

Labs working on this gene/protein

Your additional remarks

References

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)

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
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