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Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27547319
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Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W

Summary

Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W is a protein[1].

Key Facts

  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's instance of is recorded as protein[2].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's subclass of is recorded as protein[3].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's UniProt protein ID is recorded as P16387[4].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's part of is recorded as Thiamin diphosphate-binding fold[5].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's part of is recorded as Pyruvate dehydrogenase (acetyl-transferring) E1 component, alpha subunit, subgroup y[6].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's part of is recorded as Dehydrogenase, E1 component domain, protein family[7].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's has part is recorded as Dehydrogenase, E1 component domain[8].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's RefSeq protein ID is recorded as NP_011105[9].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's molecular function is recorded as oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor[10].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's molecular function is recorded as pyruvate dehydrogenase (acetyl-transferring) activity[11].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's molecular function is recorded as oxidoreductase activity[12].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's molecular function is recorded as protein binding[13].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's cell component is recorded as mitochondrial pyruvate dehydrogenase complex[14].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's cell component is recorded as intracellular membrane-bounded organelle[15].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's cell component is recorded as mitochondrial matrix[16].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's cell component is recorded as mitochondrial nucleoid[17].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's cell component is recorded as mitochondrion[18].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's cell component is recorded as mitochondrion[19].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's cell component is recorded as mitochondrion[20].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's biological process is recorded as glycolytic process[21].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's biological process is recorded as pseudohyphal growth[22].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's biological process is recorded as metabolism[23].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's biological process is recorded as acetyl-CoA biosynthetic process from pyruvate[24].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's encoded by is recorded as PDA1[25].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W's found in taxon is recorded as Saccharomyces cerevisiae S288c[26].

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

  1. [2] ↑ . Q905695. Retrieved . wikidata.org.
  2. [3] ↑ . Q905695. Retrieved . wikidata.org.
  3. [4] ↑ . Q905695. Retrieved . wikidata.org.
  4. [5] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  6. [7] ↑ . wikidata.org.
  7. [8] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . Q20641742. Retrieved . wikidata.org.
  9. [10] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . Participation of acetaldehyde dehydrogenases in ethanol and pyruvate metabolism of the yeast Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . Disruption and mutagenesis of the Saccharomyces cerevisiae PDX1 gene encoding the protein X component of the pyruvate dehydrogenase complex. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . Aconitase couples metabolic regulation to mitochondrial DNA maintenance. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . The yeast Sks1p kinase signaling network regulates pseudohyphal growth and glucose response. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . Q905695. Retrieved . wikidata.org.
  25. [26] ↑ . Q905695. Retrieved . wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

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Use these citations when quoting this entity in research, articles, AI prompts, or wherever provenance matters. We aggregate Wikidata + Wikipedia + authoritative open-data sources; the stitched, scored, cross-referenced view is what 4ort.xyz contributes.

APA 4ort.xyz Knowledge Graph. (2026). Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W. Retrieved May 3, 2026, from https://4ort.xyz/entity/pyruvate-dehydrogenase-acetyl-transferring-subunit-e1-alpha-yer178w
MLA “Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/pyruvate-dehydrogenase-acetyl-transferring-subunit-e1-alpha-yer178w.
BibTeX @misc{4ortxyz_pyruvate-dehydrogenase-acetyl-transferring-subunit-e1-alpha-yer178w_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Pyruvate dehydrogenase (acetyl-transferring) subunit E1 alpha YER178W}}, year = {2026}, url = {https://4ort.xyz/entity/pyruvate-dehydrogenase-acetyl-transferring-subunit-e1-alpha-yer178w}, note = {Accessed: 2026-05-03}}
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