pyruvate dehydrogenase (E1 alpha subunit), required for Z-ring assembly in a pyruvate-dependent manner
function
links glycolysis and TCA cycle
product
pyruvate dehydrogenase (E1 alpha subunit)
Genomic Context
categories
[category|SW 2|Metabolism] → [category|SW 2.2|Carbon metabolism] → [category|SW 2.2.1|Carbon core metabolism] → [category|SW 2.2.1.4|TCA cycle]Gene
Coordinates
1,528,326 → 1,529,441
Phenotypes of a mutant
''pdhA'' is essential according to Kobayashi ''et al''. [Pubmed|12682299], non-essential according to [Pubmed|28189581]the mutant grows slowly but is viable [Pubmed|24825009]depletion of ''[gene|953DE0F0B81894ECFF4C0693511AC238BF3D0C0A|pdhA]'' and deletion of ''[gene|B317D7E51824DD70EF84E4D5D7290D601BF4FAB6|ezrA]'' have a strong synthetic defect in [SW|cell division] [Pubmed|24825009]The protein
Catalyzed reaction/ biological activity
Pyruvate [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine CO2 (according to Swiss-Prot)Paralogous protein(s)
[protein|B0A333BDFAE816B48B856A1DD91B73C41584A8E4|AcoA], [protein|9F298088C0A9EB7FE140C935AFC9243C6D4DE8AE|BkdAA]Kinetic information
Michaelis-Menten [Pubmed|6414463][SW|Cofactors]
thiamine pyrophosphateEffectors of protein activity
Inhibited thiamine 2-thiothiazolone diphosphate and NADH [Pubmed|6414463]Low sensibility to NADPHStructure
[PDB|1W88] (E1 in complex with subunit binding domain of E2, ''Geobacillus stearothermophilus'')[SW|Localization]
colocalizes with the nucleoid (depending on the availability of pyruvate) [Pubmed|24825009]additional information
belongs to the 100 [SW|most abundant proteins] [PubMed|15378759]Expression and Regulation
Operons
genes
[gene|953DE0F0B81894ECFF4C0693511AC238BF3D0C0A|pdhA]-[gene|458E967052D1093A0F48AE0E6B6CCA0F52EAC44D|pdhB]-[gene|2F40086E35FA32136B9A89C530A86D714FE9460C|pdhC]-[gene|E9BBAE86DF3E536A987179CC394B472F6F710498|pdhD]
description
[Pubmed|11976308]
sigma factors
[protein|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA]: sigma factor, [Pubmed|20081037], in [regulon|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|SigA regulon]regulatory mechanism
[regulon|stringent response|stringent response]: negative regulation, due to presence of guanine at 1 position of the transcript [Pubmed|20081037], in [regulon|stringent response|stringent response]regulation
''[protein|search|pdhA]'': expression activated by glucose (1.9-fold) [Pubmed|12850135]view in new tabBiological materials
lacZ fusion
pGP721 (in [protein|search|pAC5]), available in [SW|Stülke] lab, pGP186 (in [protein|search|pAC7]), available in [SW|Stülke] labLabs working on this gene/protein
[SW|Arthur Aronson], Purdue University, West Lafayette, USA [http://wwwdev.gradschool.purdue.edu/PULSe/faculty.cfm?fid=5&range=0 homepage]References
Reviews
19476487,9655937,2227213,6805383,24798336 Original publications
9352926,20525796,12850135,6414463,11976308,20081037,15378759,24825009,28189581,28516784