Difference between revisions of "PdhC"
| Line 93: | Line 93: | ||
=Expression and regulation= | =Expression and regulation= | ||
| − | * '''Operon:''' ''[[pdhA]]-[[pdhB]]-[[pdhC]]-[[pdhD]]'' | + | * '''Operon:''' |
| + | ** ''[[pdhA]]-[[pdhB]]-[[pdhC]]-[[pdhD]]'' {{PubMed|11976308}} | ||
| + | ** ''[[pdhC]]-[[pdhD]]'' {{PubMed|11976308}} | ||
| − | * '''Sigma factor:''' [[SigA]] | + | * '''Sigma factor:''' |
| + | ** ''[[pdhA]]'': [[SigA]] {{PubMed|11976308}} | ||
| + | ** ''[[pdhC]]'': [[SigA]] {{PubMed|11976308}} | ||
* '''Regulation:''' expression activated by glucose (1.9 fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed] | * '''Regulation:''' expression activated by glucose (1.9 fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed] | ||
| Line 125: | Line 129: | ||
=References= | =References= | ||
| − | <pubmed>9352926,,9352926,,12850135 18763711 6414463 </pubmed> | + | <pubmed>9352926,,9352926,,12850135 18763711 6414463 11976308</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 19:48, 8 October 2009
- Description: pyruvate dehydrogenase (dihydrolipoamide acetyltransferase E2 subunit)
| Gene name | pdhC |
| Synonyms | |
| Essential | no |
| Product | pyruvate dehydrogenase (dihydrolipoamide acetyltransferase E2 subunit) |
| Function | links glycolysis and TCA cycle |
| Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
| MW, pI | 47 kDa, 4.855 |
| Gene length, protein length | 1326 bp, 442 aa |
| Immediate neighbours | pdhB, pdhD |
| 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: BSU14600
Phenotypes of a mutant
- defects in sporulation and unable to grow on glucose as single carbon source PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine (according to Swiss-Prot)
- Protein family: lipoyl-binding domain (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information: Michaelis-Menten PubMed
- Domains:
- Modification: phosphorylated (Ser/Thr/Tyr) PubMed
- Cofactor(s):
- Effectors of protein activity:
- Inhibited thiamine 2-thiothiazolone diphosphate and NADH PubMed
- Low sensibility to NADPH
- Localization: membrane associated PubMed
Database entries
- Structure: 1W88 (E1 in complex with subunit binding domain of E2, Geobacillus stearothermophilus), 2PDE (peripheral subunit binding domain, Geobacillus stearothermophilus), 1LAC (lipoyl domain, Geobacillus stearothermophilus), 1B5S (catalytic domain (residues 184-425) , Geobacillus stearothermophilus)
- UniProt: P21883
- KEGG entry: [3]
- E.C. number: 2.3.1.12 2
Additional information
Expression and regulation
- Regulation: expression activated by glucose (1.9 fold) 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
