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gapA [Mon May 16 2016 15:50:11 GMT+0200 (CEST)]
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gapA [Mon May 16 2016 15:50:11 GMT+0200 (CEST)]

Glyceraldehyde 3-phosphate dehydrogenase, NAD-dependent, glycolytic enzyme, forms a transhydrogenation cycle with GapB for balancing of NADPH
Locus
BSU33940
Isoelectric point
5.00
Molecular weight
35.00 kDa
Function
catabolic enzyme in glycolysis
Product
glyceraldehyde 3-phosphate dehydrogenase
Essential
Yes
E.C.
1.2.1.12
Synonyms

Genomic Context

      
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Categories containing this gene/protein

Categories containing this gene/protein

This gene is a member of the following regulons

Gene

Coordinates on the chromosome (coding sequence)
3,481,698 -> 3,482,705

Phenotypes of a mutant

  • Essential PubMed
  • The protein

    Catalyzed reaction/ biological activity

  • D-glyceraldehyde 3-phosphate phosphate NAD = 3-phospho-D-glyceroyl phosphate NADH (according to Swiss-Prot)
  • This reaction is part of the glycolysis.
  • Protein family

  • glyceraldehyde-3-phosphate dehydrogenase family (according to Swiss-Prot)
  • Paralogous protein(s)

    Kinetic information

  • Michaelis-Menten PubMed
  • Modification

  • phosphorylated on Arg-199 PubMed
  • Phosphorylation on (Ser-148 OR Ser-151 OR Thr-153 OR Thr-154) PubMed1, PubMed2
  • Reversible thiol modifications after exposure to toxic quinones PubMed
  • Cys152-Cys156 form intramolecular disulfide in response to disulfide stress (diamide, NaOCl-stress) PubMed
  • Cofactors

  • NAD (does not accept NADP ) PubMed
  • Structure

  • 1GD1 (from Geobacillus stearothermophilus)
  • 1NQO (from Geobacillus stearothermophilus, mutant with cys 149 replaced by ser, complex with NAD und D-Glyceraldehyde-3-Phosphate)
  • Localization

  • cytoplasm (Homogeneous) PubMed PubMed
  • loosely membrane associated PubMed
  • Interactions

  • GapA-PtsH: [PtsH|search|HPr(Ser-46-P)] binds GapA resulting in a slight inhibition of enzymatic activity PubMed
  • GapA-Crh: [Crh|search|Crh(Ser-46-P)] binds GapA resulting in a slight inhibition of enzymatic activity.PubMed
  • GapA-YkzW PubMed
  • Additional information

  • GAP dehydrogenases from different sources (incl. Geobacillus stearothermophilus) were shown to cleave RNA (PubMed)
  • Moreover, mutations in gapA from B. subtilis can suppress mutations in genes involved in DNA replication (PubMed).
  • extensive information on the structure and enzymatic properties of GapA can be found at Proteopedia
  • Expression and Regulation

    Operon

    Sigma factor

    Regulation

  • expression activated by glucose (10 fold) (CggR) PubMed
  • Regulatory mechanism

  • CggR: transcription repression PubMed
  • Additional information

  • GapA is one of the most abundant proteins in the cell. In the presence of glucose, there are about 25,000 GapA molecules per cell (PubMed)
  • belongs to the 100 most abundant proteins PubMed
  • The primary mRNAs of the operon are highly unstable. The primary mRNA is subject to processing at the very end of the 'cggR' open reading frame. This results in stable mature 'gapA' and 'gapA-pgk-tpiA-pgm-eno' mRNAs. PubMed The processing event requires the [Rny|search|RNase Y] PubMed.
  • The accumulation of the 'cggR-gapA' mRNA is strongly dependent on the presence of the YkzW peptide, due to stabilization of the mRNA PubMed.
  • the mRNA is substantially stabilized upon depletion of [Rny|search|RNase Y] PubMed
  • Biological materials

    Mutant

  • GP592 (gapA::cat), available in Jörg Stülke's lab, PubMed
  • GP597 (gapA::erm), available in Jörg Stülke's lab, PubMed
  • GP703 (gapA::cat gapB::spec), available in Jörg Stülke's lab, PubMed
  • GM1501 (under p(spac) control), available in Stephane Aymerich's lab
  • 1A1003 ( gapA::erm), available at BGSC
  • Expression vector

  • pGP1424 (expression in B. subtilis, in pBQ200) (available in Jörg Stülke's lab)
  • pGP90 (N-terminal Strep-tag, for SPINE, purification from B. subtilis, in pGP380) (available in Jörg Stülke's lab)
  • pGP704 (N-terminal His-tag, in pWH844) (available in Jörg Stülke's lab)
  • LacZ fusion

  • pGP506 (in pAC7), pGP512 (in pAC6) (available in Jörg Stülke's lab)
  • Two-hybrid system

  • B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
  • Antibody

  • available in Jörg Stülke's lab
  • Labs working on this gene/protein

  • Stephane Aymerich, Microbiology and Molecular Genetics, INRA Paris-Grignon, France
  • Jörg Stülke, University of Göttingen, Germany
  • homepage
  • References

    Reviews

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    Original publications

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