| Standard Name | PDA1 |
|---|---|
| Systematic Name | YER178W |
| Feature Type | ORF, Verified |
| Description | E1 alpha subunit of the pyruvate dehydrogenase (PDH) complex, catalyzes the direct oxidative decarboxylation of pyruvate to acetyl-CoA; phosphorylated; regulated by glucose (1, 2, 3, 4 and see Summary Paragraph) |
| Name Description | Pyruvate Dehydrogenase Alpha 1 |
| Chromosomal Location | |
|---|---|
| Genetic position: 143 cM |
| View Computational GO annotations for PDA1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated | |
| High-throughput |
| Pathways |
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| 310 total interaction(s) for 217 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
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| Genetic position: 143 cM | |||||||||||||
| Last Update | Coordinates: 2011-02-03 | Sequence: 2003-09-22 | ||||||||||||
| Subfeature details |
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| S288C only | |
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| S288C vs. other species | |
| S288C vs. other strains |
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000000980 |
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PDA1 encodes the alpha subunit of pyruvate dehydrogenase (5, 1). Pyruvate dehydrogenase, consisting of alpha (Pda1p) and beta (Pdb1p) subunits, is the E1 component of the large multienzyme pyruvate dehydrogenase complex (3). This mitochondrial complex consists of an E2 (Lat1p) core that binds E1 (Pda1p and Pdb1p ), E3 (Lpd1p), and Protein X (Pdx1p) components (3). E1 (pyruvate dehydrogenase), E2 (dihydrolipoamide acetyltransferase), and E3 (dihydrolipoamide dehydrogenase) act in concert to convert pyruvate into acetyl-CoA (3). Cells lacking PDA1 are viable but lack pyruvate dehydrogenase activity, show slower growth on glucose, and exhibit increased formation of petites that lack mitochondrial DNA (rho0) (1, 6). The yeast PDA1 gene shows strong similarity to human PDHA1, mutations in which are responsible for most cases of
| 1) | Steensma HY, et al. (1990) Molecular cloning of the gene for the E1 alpha subunit of the pyruvate dehydrogenase complex from Saccharomyces cerevisiae. Eur J Biochem 191(3):769-74 |
| 2) | Sierkstra LN, et al. (1992) Analysis of transcription and translation of glycolytic enzymes in glucose-limited continuous cultures of Saccharomyces cerevisiae. J Gen Microbiol 138(12):2559-66 |
| 3) | Pronk JT, et al. (1996) Pyruvate metabolism in Saccharomyces cerevisiae. Yeast 12(16):1607-33 |
| 4) | Reinders J, et al. (2007) Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Mol Cell Proteomics 6(11):1896-906 |
| 5) | Behal RH, et al. (1989) Nucleotide and deduced amino acid sequence of the alpha subunit of yeast pyruvate dehydrogenase. Biochem Biophys Res Commun 164(2):941-6 |
| 6) | Wenzel TJ, et al. (1992) Characterization of Saccharomyces cerevisiae mutants lacking the E1 alpha subunit of the pyruvate dehydrogenase complex. Eur J Biochem 209(2):697-705 |
| 7) | Foury F (1997) Human genetic diseases: a cross-talk between man and yeast. Gene 195(1):1-10 |





