Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27551541
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Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C

Summary

Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C is a protein[1].

Key Facts

  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's instance of is recorded as protein[2].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's subclass of is recorded as protein[3].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's UniProt protein ID is recorded as P32473[4].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's part of is recorded as Pyruvate dehydrogenase E1 component subunit beta[5].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's part of is recorded as Thiamin diphosphate-binding fold[6].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's part of is recorded as Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II[7].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's part of is recorded as Transketolase-like, pyrimidine-binding domain, protein family[8].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's part of is recorded as Transketolase, C-terminal domain, protein family[9].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's has part is recorded as Transketolase, C-terminal domain[10].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's has part is recorded as Transketolase-like, pyrimidine-binding domain[11].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's RefSeq protein ID is recorded as NP_009780[12].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's molecular function is recorded as pyruvate dehydrogenase (acetyl-transferring) activity[13].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's molecular function is recorded as catalytic activity[14].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's molecular function is recorded as oxidoreductase activity[15].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's molecular function is recorded as protein binding[16].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's cell component is recorded as mitochondrial matrix[17].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's cell component is recorded as mitochondrial pyruvate dehydrogenase complex[18].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's cell component is recorded as mitochondrial nucleoid[19].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's cell component is recorded as mitochondrion[20].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's cell component is recorded as mitochondrion[21].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's biological process is recorded as glycolytic process[22].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's biological process is recorded as acetyl-CoA biosynthetic process from pyruvate[23].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's biological process is recorded as metabolism[24].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C's encoded by is recorded as PDB1[25].
  • Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C'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] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  7. [8] . wikidata.org.
  8. [9] . wikidata.org.
  9. [10] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [11] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  11. [12] . Q20641742. Retrieved . wikidata.org.
  12. [13] . Characterization of PDH beta 1, the structural gene for the pyruvate dehydrogenase beta subunit from Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] . Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . 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.
  18. [19] . Aconitase couples metabolic regulation to mitochondrial DNA maintenance. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . Characterization of PDH beta 1, the structural gene for the pyruvate dehydrogenase beta subunit from Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . Characterization of PDH beta 1, the structural gene for the pyruvate dehydrogenase beta subunit from Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . GOA. 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 beta YBR221C. Retrieved May 3, 2026, from https://4ort.xyz/entity/pyruvate-dehydrogenase-acetyl-transferring-subunit-e1-beta-ybr221c
MLA “Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/pyruvate-dehydrogenase-acetyl-transferring-subunit-e1-beta-ybr221c.
BibTeX @misc{4ortxyz_pyruvate-dehydrogenase-acetyl-transferring-subunit-e1-beta-ybr221c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Pyruvate dehydrogenase (acetyl-transferring) subunit E1 beta YBR221C}}, year = {2026}, url = {https://4ort.xyz/entity/pyruvate-dehydrogenase-acetyl-transferring-subunit-e1-beta-ybr221c}, note = {Accessed: 2026-05-03}}
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