gapA [2017-08-19 17:15:41]

glyceraldehyde 3-phosphate dehydrogenase, NAD-dependent, glycolytic enzyme, forms a transhydrogenation cycle with GapB for balancing of NADPH

Locus: BSU33940

Isoelectric point: 5.03

Molecular weight: 35.68 kDa

Protein length: 335 aa

Gene length: 1005 bp

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

• Metabolism → Carbon metabolism → Carbon core metabolism → Glycolysis
• Groups of genes → Essential genes
• Groups of genes → Phosphoproteins → Phosphorylation on an Arg residue
• Groups of genes → Phosphoproteins → Phosphorylation on either a Ser, Thr or Tyr residue

Gene

Coordinates: 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)

• GapB

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

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
• belongs to the 100 most abundant proteins PubMed
• the protein is stable under both glycolytic and gluconeogenic conditions PubMed

Expression and Regulation

Operons

• Genes: cggR-gapA-pgk-tpi-pgm-eno
  Description: PubMed

  Sigma factors

  • SigA: sigma factor, PubMed, in SigA regulon

  Regulatory mechanism

  • CggR: repression, PubMed, in CggR regulon

  Regulation

  • expression induced by glycolytic intermediates (CggR) CggR PubMed
  • the mRNA is processed between cggR and gapA by RNase Y, this requires the YmcA-YlbF-YaaT complex PubMed

• Genes: cggR-gapA
  Description: PubMed

  Sigma factors

  • SigA: sigma factor, PubMed, in SigA regulon

  Regulatory mechanism

  • CggR: repression, PubMed, in CggR regulon

  Regulation

  • expression induced by glucose (10 fold) (CggR) PubMed
  • the mRNA is processed between cggR and gapA by RNase Y, this requires the YmcA-YlbF-YaaT complex 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), PubMed
• 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, PubMed

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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