Difference between revisions of "GapB"

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(Database entries)
(Database entries)
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=== Database entries ===
 
=== Database entries ===
  
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/rocG.html]
+
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/gapB-speD.html]
  
 
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG12592]
 
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG12592]

Revision as of 09:37, 7 January 2009

  • Description: glyceraldehyde-3-phosphate dehydrogenase catalyses the syntheseis of 1,3 Bisphosphoglycerat, phosphorylation of ADP and reduction of NAD

Gene name gapB
Synonyms
Essential no
Product glyceraldehyde-3-phosphate dehydrogenase2
Function syntheseis of 1,3 Bisphosphoglycerat
MW, pI 37,3 kDa, 6.47
Gene length, protein length 1020 bp, 340 amino acids
Immediate neighbours ytcD, speD
Gene sequence (+200bp) Protein sequence
Genetic context
File:GenE context.gif












The gene

Basic information

  • Coordinates:

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: D-glyceraldehyde 3-phosphate + phosphate + NAD(P)(+) = 3-phospho-D-glyceroyl phosphate + NAD(P)H.
  • Protein family: glyceraldehyde-3-phosphate dehydrogenase family
  • Paralogous protein(s): GapA

Extended information on the protein

  • Kinetic information:
  • Domains:
    • Nucleotid binding Domain (12-13)
    • 2x Glyceraldehyde 3-phosphate binding Domain (151-153) & (210-211)
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: Cytoplasm

Database entries

  • Structure:
  • Swiss prot entry: [3]
  • KEGG entry: [4]
  • E.C. number: [5]

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation: repressed (70-times) by Glc, repressor CcpN, pos. regulated by RocR
  • Regulatory mechanism:
  • Additional information:

Biological materials

Labs working on this gene/protein

Your additional remarks

References

  1. Author1, Author2 & Author3 (year) Title Journal volume: page-page. [6]
  2. Meile JC, Wu LJ, Ehrlich SD (2006) Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory Proteomics 6(7): 2135-46. PubMed
  3. Servant P, Le Coq D & Aymerich S. (2005) CcpN (YqzB), a novel regulator for CcpA-independent catabolite repression of Bacillus subtilis gluconeogenic genes. Mol Microbiol. 55(5): 1435-51 PubMed