Difference between revisions of "PdhD"
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** Low sensibility to NADPH [http://www.ncbi.nlm.nih.gov/pubmed/6414463 PubMed] | ** Low sensibility to NADPH [http://www.ncbi.nlm.nih.gov/pubmed/6414463 PubMed] | ||
− | * '''Interactions:''' [[OdhA]]-[[OdhB]]-[[PdhD]] | + | * '''Interactions:''' |
+ | ** [[OdhA]]-[[OdhB]]-[[PdhD]] {{PubMed|20933603}} | ||
+ | ** [[PdhA]]-[[PdhB]]-[[PdhC]]-[[PdhD]] | ||
* '''Localization:''' cytoplasm (according to Swiss-Prot) | * '''Localization:''' cytoplasm (according to Swiss-Prot) | ||
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<pubmed> 19476487 9655937 2227213 6805383 </pubmed> | <pubmed> 19476487 9655937 2227213 6805383 </pubmed> | ||
==Original publications== | ==Original publications== | ||
− | <pubmed>12850135 6414463 11976308 17726680 20081037 </pubmed> | + | <pubmed>12850135 6414463 11976308 17726680 20081037 20933603</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 08:05, 13 October 2010
- Description: dihydrolipoamide dehydrogenase E3 subunit of both pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
Gene name | pdhD |
Synonyms | citL |
Essential | no |
Product | dihydrolipoamide dehydrogenase E3 subunit of both pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes |
Function | links glycolysis and TCA cycle, enzyme in TCA cycle |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
MW, pI | 49 kDa, 4.76 |
Gene length, protein length | 1410 bp, 470 aa |
Immediate neighbours | pdhC, slp |
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: BSU14610
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: Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH (according to Swiss-Prot)
- Protein family: class-I pyridine nucleotide-disulfide oxidoreductase family (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:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure: 1EBD (complex with binding domain of dihydrolipoamide acetylase, Geobacillus stearothermophilus), 1EBD (complex with binding domain of dihydrolipoamide acetylase, Geobacillus stearothermophilus)
- UniProt: P21880
- KEGG entry: [3]
- E.C. number: 1.8.1.4
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- stringent response: due to presence of guanine at +1 position of the transcript PubMed
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Original publications