Difference between revisions of "PdhA"
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=Expression and regulation= | =Expression and regulation= | ||
| − | * '''Operon:''' ''[[pdhA]]-[[pdhB]]-[[pdhC]]-[[pdhD]]'' | + | * '''Operon:''' ''[[pdhA]]-[[pdhB]]-[[pdhC]]-[[pdhD]]'' {{PubMed|11976308}} |
| − | * '''Sigma factor:''' [[SigA]] | + | * '''Sigma factor:''' [[SigA]] {{PubMed|11976308}} |
* '''Regulation:''' expression activated by glucose (3.4) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed] | * '''Regulation:''' expression activated by glucose (3.4) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed] | ||
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=References= | =References= | ||
| − | <pubmed>9352926,,12850135 6414463 </pubmed> | + | <pubmed>9352926,,12850135 6414463 11976308</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 20:45, 8 October 2009
- Description: pyruvate dehydrogenase (E1 alpha subunit)
| Gene name | pdhA |
| Synonyms | aceA |
| Essential | yes |
| Product | pyruvate dehydrogenase (E1 alpha subunit) |
| Function | links glycolysis and TCA cycle |
| Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
| MW, pI | 41 kDa, 5.837 |
| Gene length, protein length | 1113 bp, 371 aa |
| Immediate neighbours | ykyA, pdhB |
| 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: BSU14580
Phenotypes of a mutant
- pdhA is essential PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2 (according to Swiss-Prot)
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information: Michaelis-Menten PubMed
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Inhibited thiamine 2-thiothiazolone diphosphate and NADH PubMed
- Low sensibility to NADPH
- Localization:
Database entries
- Structure: 1W88 (E1 in complex with subunit binding domain of E2, Geobacillus stearothermophilus)
- UniProt: P21881
- KEGG entry: [3]
- E.C. number: 1.2.4.1
Additional information
Expression and regulation
- Regulation: expression activated by glucose (3.4) PubMed
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Arthur Aronson, Purdue University, West Lafayette, USA homepage
Your additional remarks
References
Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135]
[WorldCat.org]
[DOI]
(P p)
Haichun Gao, Xin Jiang, Kit Pogliano, Arthur I Aronson
The E1beta and E2 subunits of the Bacillus subtilis pyruvate dehydrogenase complex are involved in regulation of sporulation.
J Bacteriol: 2002, 184(10);2780-8
[PubMed:11976308]
[WorldCat.org]
[DOI]
(P p)
M M Nakano, Y P Dailly, P Zuber, D P Clark
Characterization of anaerobic fermentative growth of Bacillus subtilis: identification of fermentation end products and genes required for growth.
J Bacteriol: 1997, 179(21);6749-55
[PubMed:9352926]
[WorldCat.org]
[DOI]
(P p)
P N Lowe, J A Hodgson, R N Perham
Dual role of a single multienzyme complex in the oxidative decarboxylation of pyruvate and branched-chain 2-oxo acids in Bacillus subtilis.
Biochem J: 1983, 215(1);133-40
[PubMed:6414463]
[WorldCat.org]
[DOI]
(P p)
