PdhC
- 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 |
| Gene expression levels in SubtiExpress: pdhC | |
| Interactions involving this protein in SubtInteract: PdhC | |
| Metabolic function and regulation of this protein in SubtiPathways: pdhC | |
| MW, pI | 47 kDa, 4.855 |
| Gene length, protein length | 1326 bp, 442 aa |
| Immediate neighbours | pdhB, pdhD |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
carbon core metabolism, membrane proteins, most abundant proteins
This gene is a member of the following regulons
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
- BsubCyc: BSU14600
- 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)
Extended information on the protein
- Kinetic information: Michaelis-Menten PubMed
- Modification: phosphorylated (Ser/Thr/Tyr) PubMed
- Cofactors:
- lipoic acid
- Effectors of protein activity:
- Inhibited by thiamine 2-thiothiazolone diphosphate and NADH PubMed
- Low sensibility to NADPH
Database entries
- BsubCyc: BSU14600
- 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:
- Regulatory mechanism:
- stringent response: due to presence of guanine at +1 position of the transcript PubMed
- belongs to the 100 most abundant proteins PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium): 11281 PubMed
- number of protein molecules per cell (complex medium with amino acids, without glucose): 33899 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 10012 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 6860 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 6154 PubMed
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
Reviews
Original publications
Leigh G Monahan, Isabella V Hajduk, Sinead P Blaber, Ian G Charles, Elizabeth J Harry
Coordinating bacterial cell division with nutrient availability: a role for glycolysis.
mBio: 2014, 5(3);e00935-14
[PubMed:24825009]
[WorldCat.org]
[DOI]
(I e)
Shanshan Li, Di Huang, Yong Li, Jianping Wen, Xiaoqiang Jia
Rational improvement of the engineered isobutanol-producing Bacillus subtilis by elementary mode analysis.
Microb Cell Fact: 2012, 11;101
[PubMed:22862776]
[WorldCat.org]
[DOI]
(I e)
Shigeo Tojo, Kanako Kumamoto, Kazutake Hirooka, Yasutaro Fujita
Heavy involvement of stringent transcription control depending on the adenine or guanine species of the transcription initiation site in glucose and pyruvate metabolism in Bacillus subtilis.
J Bacteriol: 2010, 192(6);1573-85
[PubMed:20081037]
[WorldCat.org]
[DOI]
(I p)
Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711]
[WorldCat.org]
[DOI]
(I p)
Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680]
[WorldCat.org]
[DOI]
(P p)
Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759]
[WorldCat.org]
[DOI]
(P p)
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)
