Difference between revisions of "GapB"
| Line 35: | Line 35: | ||
=== Basic information === | === Basic information === | ||
| − | * '''Locus tag:''' | + | * '''Locus tag:''' BSU29020 |
===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
| Line 81: | Line 81: | ||
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O34425 O34425] | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O34425 O34425] | ||
| − | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+ | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU29020] |
* '''E.C. number:''' [http://www.expasy.org/enzyme/1.2.1.59 1.2.1.59] 2 1.2.1.12] | * '''E.C. number:''' [http://www.expasy.org/enzyme/1.2.1.59 1.2.1.59] 2 1.2.1.12] | ||
Revision as of 11:37, 3 June 2009
- 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
| |
Contents
The gene
Basic information
- Locus tag: BSU29020
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
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) D-glyceraldehyde 3-phosphate + phosphate + NAD(P)(+) = 3-phospho-D-glyceroyl phosphate + NAD(P)H.
- Protein family: glyceraldehyde-3-phosphate dehydrogenase family (according to Swiss-Prot) 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: 1.2.1.59 2 1.2.1.12]
Additional information
Expression and regulation
- 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
Your additional remarks
References
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)
