Glyceraldehyde 3-phosphate dehydrogenase, NAD-dependent, glycolytic enzyme, forms a transhydrogenation cycle with GapB for balancing of NADPH
function
catabolic enzyme in glycolysis
product
glyceraldehyde 3-phosphate dehydrogenase
Genomic Context
categories
[category|SW 2|Metabolism] → [category|SW 2.2|Carbon metabolism] → [category|SW 2.2.1|Carbon core metabolism] → [category|SW 2.2.1.1|Glycolysis][category|SW 6|Groups of genes] → [category|SW 6.1|Essential genes][category|SW 6|Groups of genes] → [category|SW 6.4|Phosphoproteins] → [category|SW 6.4.1|Phosphorylation on an Arg residue][category|SW 6|Groups of genes] → [category|SW 6.4|Phosphoproteins] → [category|SW 6.4.8|Phosphorylation on either a Ser, Thr or Tyr residue][SW|Categories] containing this gene/protein
[SW|carbon core metabolism], [SW|essential genes], [SW|membrane proteins], [SW|phosphoproteins], [SW|most abundant proteins]This gene is a member of the following [SW|regulons]
[SW|CggR regulon]Gene
Coordinates on the chromosome (coding sequence)
3,481,698 -> 3,482,705
Phenotypes of a mutant
Essential [Pubmed|17114254]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)
[protein|search|GapB]Kinetic information
Michaelis-Menten [Pubmed|10799476]Modification
phosphorylated on Arg-199 [Pubmed|22517742]Phosphorylation on (Ser-148 OR Ser-151 OR Thr-153 OR Thr-154) [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed1], [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed2]Reversible thiol modifications after exposure to toxic quinones [Pubmed|18673455]Cys152-Cys156 form intramolecular disulfide in response to disulfide stress (diamide, NaOCl-stress) [Pubmed|21749987][SW|Cofactors]
NAD (does not accept NADP ) [Pubmed|10799476]Structure
[PDB|1GD1] (from ''Geobacillus stearothermophilus'')[PDB|1NQO] (from ''Geobacillus stearothermophilus'', mutant with cys 149 replaced by ser, complex with NAD und D-Glyceraldehyde-3-Phosphate)[SW|Localization]
cytoplasm (Homogeneous) [Pubmed|16479537] [Pubmed|14600241]loosely membrane associated [Pubmed|18763711][SW|Interactions]
[protein|search|GapA]-[protein|search|PtsH]: [PtsH|search|HPr(Ser-46-P)] binds GapA resulting in a slight inhibition of enzymatic activity [Pubmed|17142398][protein|search|GapA]-[protein|search|Crh]: [Crh|search|Crh(Ser-46-P)] binds GapA resulting in a slight inhibition of enzymatic activity.[Pubmed|17142398][protein|search|GapA]-[protein|search|YkzW] [Pubmed|23034808][SW|GapA]-[SW|RnjA] [Pubmed|27449348], about 1% of all [SW|GapA] molecules participate in this interaction [Pubmed|27449348][SW|GapA]-[SW|Rny] [Pubmed|27449348], about 2% of all [SW|GapA] molecules participate in this interaction [Pubmed|27449348]Additional information
GAP dehydrogenases from different sources (incl. ''Geobacillus stearothermophilus'') were shown to cleave RNA ([Pubmed|12359717])Moreover, mutations in ''gapA'' from ''B. subtilis'' can suppress mutations in genes involved in DNA replication ([Pubmed|17505547]).extensive information on the structure and enzymatic properties of GapA can be found at [http://www.proteopedia.org/wiki/index.php/Glyceraldehyde-3-Phosphate_Dehydrogenase Proteopedia]Expression and Regulation
Operon
''[protein|search|cggR]-[protein|search|gapA]-[protein|search|pgk]-[protein|search|tpi]-[protein|search|pgm]-[protein|search|eno]'' [Pubmed|11489127]''[protein|search|cggR]-[protein|search|gapA]'' [Pubmed|11489127][SW|Sigma factor]
[protein|search|SigA] [Pubmed|11489127]Regulation
expression activated by glucose (10 fold) ([protein|search|CggR]) [Pubmed|12850135,12622823]Regulatory mechanism
[protein|search|CggR]: transcription repression [Pubmed|11489127]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 ([http://www.ncbi.nlm.nih.gov/sites/entrez/12634343 PubMed])belongs to the 100 [SW|most abundant proteins] [PubMed|15378759]The primary mRNAs of the operon are highly unstable. The primary mRNA is subject to processing at the very end of the '[protein|search|cggR]' open reading frame. This results in stable mature '[protein|search|gapA]' and '[protein|search|gapA]-[protein|search|pgk]-[protein|search|tpiA]-[protein|search|pgm]-[protein|search|eno]' mRNAs. [PubMed|11489127] The processing event requires the [Rny|search|RNase Y] [PubMed|19193632].The accumulation of the '[protein|search|cggR]-[protein|search|gapA]' mRNA is strongly dependent on the presence of the [protein|search|YkzW] peptide, due to stabilization of the mRNA [PubMed|20444087].the mRNA is substantially stabilized upon depletion of [Rny|search|RNase Y] [PubMed|21815947]Biological materials
Mutant
GP592 (''gapA''::''cat''), available in [SW|Jörg Stülke]'s lab, [Pubmed|23420519]GP597 (''gapA''::''erm''), available in [SW|Jörg Stülke]'s lab, [Pubmed|23420519]GP703 (''gapA''::''cat'' ''[protein|search|gapB]''::''spec''), available in [SW|Jörg Stülke]'s lab, [Pubmed|23420519]GM1501 (under p(spac) control), available in [SW|Stephane Aymerich]'s lab1A1003 ( ''gapA''::''erm''), available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A1003&Search=1A1003 BGSC]Expression vector
pGP1424 (expression in ''B. subtilis'', in [SW|pBQ200]) (available in [SW|Jörg Stülke]'s lab)pGP90 (N-terminal Strep-tag, for [SW|SPINE], purification from ''B. subtilis'', in [SW|pGP380]) (available in [SW|Jörg Stülke]'s lab)pGP704 (N-terminal His-tag, in [SW|pWH844]) (available in [SW|Jörg Stülke]'s lab)lacZ fusion
pGP506 (in [protein|search|pAC7]), pGP512 (in [protein|search|pAC6]) (available in [SW|Jörg Stülke]'s lab)two-hybrid system
''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([SW|BACTH]), available in [SW|Jörg Stülke]'s labAntibody
available in [SW|Jörg Stülke]'s labLabs working on this gene/protein
[SW|Stephane Aymerich], Microbiology and Molecular Genetics, INRA Paris-Grignon, France[SW|Jörg Stülke], University of Göttingen, Germany[http://wwwuser.gwdg.de/~genmibio/stuelke.html homepage]References
Reviews
Original publications
22517742,23420519,22740702,23034808,21815947,21749987,12850135,19193632,18673455,20444087,17726680,16479537,12622823,12359717,10799476,17505547,11489127,12123463,17218307,12634343,17142398,17114254,10559165,15378759,27449348