Difference between revisions of "GndA"

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* '''Operon:''' ''[[polY1]]-[[gndA]]'' (according to [http://dbtbs.hgc.jp/COG/prom/yqjHI.html DBTBS])
 
* '''Operon:''' ''[[polY1]]-[[gndA]]'' (according to [http://dbtbs.hgc.jp/COG/prom/yqjHI.html DBTBS])
  
* '''[[Sigma factor]]:'''  
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=gndA_2480750_2482159_-1 gndA] {{PubMed|22383849}}
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* '''Sigma factor:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
  
* '''Additional information:'''  
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* '''Additional information:'''
  
 
=Biological materials =
 
=Biological materials =

Revision as of 10:44, 16 April 2012

  • Description: NADP-dependent phosphogluconate dehydrogenase

Gene name gndA
Synonyms yqjI
Essential no
Product NADP-dependent phosphogluconate dehydrogenase
Function pentose phosphate pathway
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 51 kDa, 5.076
Gene length, protein length 1407 bp, 469 aa
Immediate neighbours zwf, polY1
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YqjI context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

carbon core metabolism, phosphoproteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU23860

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH (according to Swiss-Prot)
  • Protein family: 6-phosphogluconate dehydrogenase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: Reversible reaction PubMed
  • Domains:
  • Modification: phosphorylation on (Thr-15 OR Thr-17) PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 2W8Z (from Geobacillus stearothermophilus, 83% identity, 92% similarity) PubMed
  • KEGG entry: [3]

Additional information

It contains a cysteine on the active site. The enzyme is a dimer. PubMed

Expression and regulation

  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: GP1514 (gndA::kan), available in Stülke lab
  • Expression vector:
    • pGP1789 (N-terminal Strep-tag, for SPINE, purification from B. subtilis, in pGP1389) (available in Stülke lab)
    • GP1410 (gndA-Strep (cat)), purification from B. subtilis, for SPINE, available in Stülke lab
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:
  • FLAG-tag construct:
    • GP1403 (spc, based on pGP1331), available in the Stülke lab
    • GP1508 (kan, resistance cassette exchange in GP1403), available in the Stülke lab

Labs working on this gene/protein

Your additional remarks

References

Additional publications: PubMed

Scott Cameron, Viviane P Martini, Jorge Iulek, William N Hunter
Geobacillus stearothermophilus 6-phosphogluconate dehydrogenase complexed with 6-phosphogluconate.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2009, 65(Pt 5);450-4
[PubMed:19407374] [WorldCat.org] [DOI] (I p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)