Difference between revisions of "GapA"
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− | + | * '''Description:''' Glyceraldehyde 3-phosphate dehydrogenase, NAD-dependent, glycolytic enzyme <br/><br/> | |
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− | * '''Description:''' Glyceraldehyde 3-phosphate dehydrogenase, NAD-dependent, glycolytic enzyme | ||
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
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|style="background:#ABCDEF;" align="center"|'''Function''' || catabolic enzyme in glycolysis | |style="background:#ABCDEF;" align="center"|'''Function''' || catabolic enzyme in glycolysis | ||
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− | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]''' |
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 35.7 kDa, 5.03 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 35.7 kDa, 5.03 | ||
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[pgk]]'', ''[[cggR]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[pgk]]'', ''[[cggR]]'' | ||
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− | |colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+& | + | |colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS:CAB15399]+-newId sequences] <br/> (Barbe ''et al.'', 2009)''' |
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− | |colspan="2" | '''Genetic context''' | + | |colspan="2" | '''Genetic context''' <br/> [[Image:gapA_context.gif]] |
− | + | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | |
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__TOC__ | __TOC__ | ||
− | + | <br/><br/><br/><br/><br/><br/> | |
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=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
− | * '''Catalyzed reaction/ biological activity:''' D-glyceraldehyde 3-phosphate + phosphate + NAD | + | * '''Catalyzed reaction/ biological activity:''' D-glyceraldehyde 3-phosphate + phosphate + NAD<sup>+</sup> = 3-phospho-D-glyceroyl phosphate + NADH (according to Swiss-Prot) |
** This reaction is part of the glycolysis. | ** This reaction is part of the glycolysis. | ||
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=References= | =References= | ||
− | + | <pubmed> 12850135,19193632, 18673455 , 20444087 17726680,16479537,12622823,12359717,10799476,17505547,11489127,12123463,17218307,12634343,17142398,17114254,10559165 </pubmed> | |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 04:49, 24 November 2010
- Description: Glyceraldehyde 3-phosphate dehydrogenase, NAD-dependent, glycolytic enzyme
Gene name | gapA |
Synonyms | |
Essential | Yes (PubMed) |
Product | glyceraldehyde 3-phosphate dehydrogenase |
Function | catabolic enzyme in glycolysis |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
MW, pI | 35.7 kDa, 5.03 |
Gene length, protein length | 1005 bp, 335 amino acids |
Immediate neighbours | pgk, cggR |
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: BSU33940
Phenotypes of a mutant
- Essential PubMed
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+ = 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
Extended information on the protein
- Kinetic information: Michaelis-Menten PubMed
- Domains:
- Modification:
- Cofactor(s): NAD+ (do not accept NADP+) PubMed
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot), Cytoplasm (Homogeneous) PubMed PubMed, loosely membrane associated PubMed
Database entries
- Structure:
- UniProt: P09124
- KEGG entry: [3]
- E.C. number: 1.2.1.12
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).
Expression and regulation
- Database entries: DBTBS
- 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 (PubMed).
- The primary mRNAs of the operon are highly unstable. The primary mRNA is subject to processing at the very end of the cggR open reading frame. This results in stable mature gapA and gapA-pgk-tpiA-pgm-eno mRNAs. PubMed The processing event requires the RNase Y PubMed.
- The accumulation of the cggR-gapA mRNA is strongly dependent on the presence of the YkzW peptide, due to stabilization of the mRNA PubMed.
Biological materials
- Mutant:
- GP592 (gapA::cat), available in Stülke lab
- GP597 (gapA::erm), available in Stülke lab
- GP703 (gapA::cat gapB::spec), available in Stülke lab
- GM1501 (under p(spac) control), available in Stephane Aymerich lab
- Expression vector:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody: available in Stülke lab
Labs working on this gene/protein
Stephane Aymerich, Microbiology and Molecular Genetics, INRA Paris-Grignon, France
Jörg Stülke, University of Göttingen, Germany homepage
Your additional remarks
References