GapB

• Description: glyceraldehyde-3-phosphate dehydrogenase, NADP-dependent, gluconeogenic enzyme
  
  

Gene name	gapB
Synonyms	ppc
Essential	no
Product	glyceraldehyde-3-phosphate dehydrogenase 2
Function	anabolic enzyme in gluconeogenesis
MW, pI	37,3 kDa, 6.47
Gene length, protein length	1020 bp, 340 amino acids
Immediate neighbours	ytcD, speD
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Coordinates: 2966075 - 2967094

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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 bindinge domain (12-13)
  • 2x Glyceraldehyde 3-phosphate binding domain (151-153) & (210-211)

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: Cytoplasm (Homogeneous) PubMed

Database entries

• Structure:

• Swiss prot entry: O34425

• KEGG entry: [3]

• E.C. number: 1.2.1.12

Expression and regulation

• Operon: gapB-speD

• Sigma factor: SigA PubMed

• Regulation: repressed (70-times) by Glc, repressor CcpN PubMed

• Regulatory mechanism: transcription repression

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• Antibody:

Labs working on this gene/protein

Stephane Aymerich, Microbiology and Molecular Genetics, INRA Paris-Grignon, France

References

1. Fillinger, S., Boschi-Muller, S., Azza, S., Dervyn, E., Branlant, G., and Aymerich, S. (2000) Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium. J Biol Chem 275, 14031-14037. PubMed
2. Meile et al. (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: 2135-2146. PubMed
3. Servant et al. (2005) CcpN (YqzB), a novel regulator for CcpA-independent catabolite repression of Bacillus subtilis gluconeogenic genes. Mol. Microbiol. 55: 1435-1451. PubMed
4. Tännler et al. (2008) CcpN controls central carbon fluxes in Bacillus subtilis. J. Bacteriol. 190: 6178-6187. PubMed
5. Thomaides, H. B., Davison, E. J., Burston, L., Johnson, H., Brown, D. R., Hunt, A. C., Errington, J., and Czaplewski, L. (2007) Essential bacterial functions encoded by gene pairs. J Bacteriol 189: 591-602. PubMed