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
Metabolic function and regulation of this protein in SubtiPathways: Cys, Met & Sulfate assimilation, Central C-metabolism
MW, pI	37,3 kDa, 6.47
Gene length, protein length	1020 bp, 340 amino acids
Immediate neighbours	speD, ytcD
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

carbon core metabolism

This gene is a member of the following regulons

CcpN regulon

The gene

Basic information

• Locus tag: BSU29020

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 (according to Swiss-Prot)
  • This reaction is part of the gluconeogenesis

• Protein family: glyceraldehyde-3-phosphate dehydrogenase family (according to Swiss-Prot)

• Paralogous protein(s): GapA

Extended information on the protein

• Kinetic information: Michaelis-Menten PubMed

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

• Modification:

• Cofactor(s): NADP (preferentially) and NAD PubMed

• Effectors of protein activity:

• Interactions:

• Localization: Cytoplasm (Homogeneous) PubMed

Database entries

• Structure: 3PRL (from B. halodurans)

• UniProt: O34425

• KEGG entry: [3]

• E.C. number: 1.2.1.59

Expression and regulation

• Operon: gapB-speD PubMed

• Expression browser: gapB PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed in the presence of glucose (70-fold) (CcpN) PubMed

• Regulatory mechanism:
  • CcpN: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:
  • GP701 (gapB::spec), available in Stülke lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

• Antibody:

Labs working on this gene/protein

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

References

Matthew L Ferguson, Dominique Le Coq, Matthieu Jules, Stéphane Aymerich, Ovidiu Radulescu, Nathalie Declerck, Catherine A Royer
Reconciling molecular regulatory mechanisms with noise patterns of bacterial metabolic promoters in induced and repressed states.
Proc Natl Acad Sci U S A: 2012, 109(1);155-60
[PubMed:22190493] [WorldCat.org] [DOI] (I p)

Simon Tännler, Eliane Fischer, Dominique Le Coq, Thierry Doan, Emmanuel Jamet, Uwe Sauer, Stéphane Aymerich
CcpN controls central carbon fluxes in Bacillus subtilis.
J Bacteriol: 2008, 190(18);6178-87
[PubMed:18586936] [WorldCat.org] [DOI] (I p)

Helena B Thomaides, Ella J Davison, Lisa Burston, Hazel Johnson, David R Brown, Alison C Hunt, Jeffery Errington, Lloyd Czaplewski
Essential bacterial functions encoded by gene pairs.
J Bacteriol: 2007, 189(2);591-602
[PubMed:17114254] [WorldCat.org] [DOI] (P p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

Pascale Servant, Dominique Le Coq, Stéphane Aymerich
CcpN (YqzB), a novel regulator for CcpA-independent catabolite repression of Bacillus subtilis gluconeogenic genes.
Mol Microbiol: 2005, 55(5);1435-51
[PubMed:15720552] [WorldCat.org] [DOI] (P p)

A Sekowska, J Y Coppée, J P Le Caer, I Martin-Verstraete, A Danchin
S-adenosylmethionine decarboxylase of Bacillus subtilis is closely related to archaebacterial counterparts.
Mol Microbiol: 2000, 36(5);1135-47
[PubMed:10844697] [WorldCat.org] [DOI] (P p)

S Fillinger, S Boschi-Muller, S Azza, E Dervyn, G Branlant, S Aymerich
Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium.
J Biol Chem: 2000, 275(19);14031-7
[PubMed:10799476] [WorldCat.org] [DOI] (P p)