Difference between revisions of "PdhA"
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|style="background:#ABCDEF;" align="center"|'''Function''' || links glycolysis and TCA cycle | |style="background:#ABCDEF;" align="center"|'''Function''' || links glycolysis and TCA cycle | ||
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+ | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU14580 pdhA] | ||
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/PdhA PdhA] | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/PdhA PdhA] |
Revision as of 09:10, 7 August 2012
- 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 |
Gene expression levels in SubtiExpress: pdhA | |
Interactions involving this protein in SubtInteract: PdhA | |
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
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
carbon core metabolism, essential genes
This gene is a member of the following regulons
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
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:
- Regulatory mechanism:
- stringent response: due to presence of guanine at +1 position of the transcript PubMed
- Additional information:
- The mRNA has a long 5' leader region. This may indicate RNA-based regulation PubMed
Biological materials
- Mutant:
- Expression vector:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Arthur Aronson, Purdue University, West Lafayette, USA homepage
Your additional remarks
References
Reviews
Original publications