Difference between revisions of "Sandbox"

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−
* '''Description:''' alpha-amylase <br/><br/>
+
* '''Description:''' L-aspartase <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'''
−
|''amyE''
+
|''ansB''
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''amyA ''
+
|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''' || alpha-amylase)
+
|style="background:#ABCDEF;" align="center"| '''Product''' || L-aspartase
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"|'''Function''' || starch degradation  
+
|style="background:#ABCDEF;" align="center"|'''Function''' || aspartate degradation
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 72 kDa, 5.85  
+
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 52 kDa, 5.69  
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1980 bp, 660 aa  
+
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1425 bp, 475 aa  
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ycgB]]'', ''[[ldh]]''
+
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[mleN]]'', ''[[ansA]]''
 
|-
 
|-
−
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB12098&#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:CAB14289&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
 
|-
 
|-
−
|colspan="2" | '''Genetic context''' <br/> [[Image:amyE_context.gif]]
+
|-
 +
|-
 +
|colspan="2" | '''Genetic context''' <br/> [[Image:ansB_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>
 
|-
 
|-
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=== Basic information ===
 
=== Basic information ===
  
−
* '''Locus tag:''' BSU03040
+
* '''Locus tag:''' BSU23570
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
Line 41: Line 43:
 
=== Database entries ===
 
=== Database entries ===
  
−
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/amyE.html]
+
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ansAB.html]
  
−
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10473]
+
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10301]
  
 
=== Additional information===
 
=== Additional information===
Line 52: Line 54:
 
=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
−
* '''Catalyzed reaction/ biological activity:''' Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides (according to Swiss-Prot)  
+
* '''Catalyzed reaction/ biological activity:''' L-aspartate = fumarate + NH<sub>3</sub> (according to Swiss-Prot)  
  
−
* '''Protein family:''' glycosyl hydrolase 13 family (according to Swiss-Prot)
+
* '''Protein family:''' Aspartase subfamily (according to Swiss-Prot)
  
−
* '''Paralogous protein(s):'''
+
* '''Paralogous protein(s):''' [[CitG]]
  
 
=== Extended information on the protein ===
 
=== Extended information on the protein ===
Line 72: Line 74:
 
* '''Interactions:'''
 
* '''Interactions:'''
  
−
* '''Localization:''' secreted (according to Swiss-Prot),  extracellular (signal peptide) [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed]
+
* '''Localization:''' cell membrane (according to Swiss-Prot)
  
 
=== Database entries ===
 
=== Database entries ===
  
−
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1BAG 1BAG] (complex with maltopentaose)
+
* '''Structure:'''
  
−
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P00691 P00691]
+
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P26899 P26899]
  
−
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU03040]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU23570]
  
−
* '''E.C. number:''' [http://www.expasy.org/enzyme/3.2.1.1 3.2.1.1]
+
* '''E.C. number:''' [http://www.expasy.org/enzyme/4.3.1.1 4.3.1.1]  
  
 
=== Additional information===
 
=== Additional information===
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=Expression and regulation=
 
=Expression and regulation=
  
−
* '''Operon:''' [[AmyE]]
+
* '''Operon:''' ''[[ansA]]-[[ansB]]''
  
−
* '''[[Sigma factor]]:''' [[SigA]]
+
* '''Sigma factor:''' [[SigA]]
  
−
* '''Regulation:''' repressed by glucose ([[CcpA]]) 
+
* '''Regulation:'''  
  
−
* '''Regulatory mechanism:''' [[CcpA]]: transcription repression
+
* '''Regulatory mechanism:'''  
  
 
* '''Additional information:'''
 
* '''Additional information:'''
Line 118: Line 120:
 
=References=
 
=References=
  
−
<pubmed>18957862 1904524, </pubmed>
+
<pubmed>1711029, </pubmed>
−
# Voigt et al. (2009) Cell physiology and protein secretion of ''Bacillus licheniformis'' compared to ''Bacillus subtilis''. ''J Mol Microbiol Biotechnol.'' '''16:''' 53-68 [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed]
 
  
−
# Henkin, T. M., Grundy, F. J., Nicholson, W. L. and Chambliss, G. H. (1991) Catabolite repression of -amylase gene expression in Bacillus subtilis involves a trans-acting gene product homologous to the Escherichia coli lacI and galR repressors. Mol. Microbiol. 5, 575-584. [http://www.ncbi.nlm.nih.gov/sites/entrez/1904524 PubMed]
+
# Sun DX, Setlow P. (1991) Cloning, nucleotide sequence, and expression of the Bacillus subtilis ans operon, which codes for L-asparaginase and L-aspartase. ''J Bacteriol. '' '''Jun;173(12):''' 3831-45. [http://www.ncbi.nlm.nih.gov/sites/entrez/1711029 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 13:07, 8 June 2009

  • Description: L-aspartase

Gene name ansB
Synonyms
Essential no
Product L-aspartase
Function aspartate degradation
MW, pI 52 kDa, 5.69
Gene length, protein length 1425 bp, 475 aa
Immediate neighbours mleN, ansA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
AnsB context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU23570

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: L-aspartate = fumarate + NH3 (according to Swiss-Prot)
  • Protein family: Aspartase subfamily (according to Swiss-Prot)
  • Paralogous protein(s): CitG

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: cell membrane (according to Swiss-Prot)

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • 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

D X Sun, P Setlow
Cloning, nucleotide sequence, and expression of the Bacillus subtilis ans operon, which codes for L-asparaginase and L-aspartase.
J Bacteriol: 1991, 173(12);3831-45
[PubMed:1711029] [WorldCat.org] [DOI] (P p)


  1. Sun DX, Setlow P. (1991) Cloning, nucleotide sequence, and expression of the Bacillus subtilis ans operon, which codes for L-asparaginase and L-aspartase. J Bacteriol. Jun;173(12): 3831-45. PubMed
  2. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
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