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Alcohol dehydrogenase ADH2 YMR303C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27548023
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Summary

Alcohol dehydrogenase ADH2 YMR303C is a protein[1].

Key Facts

  • Alcohol dehydrogenase ADH2 YMR303C's instance of is recorded as protein[2].
  • Alcohol dehydrogenase ADH2 YMR303C's subclass of is recorded as protein[3].
  • Alcohol dehydrogenase ADH2 YMR303C's UniProt protein ID is recorded as P00331[4].
  • Alcohol dehydrogenase ADH2 YMR303C's part of is recorded as NAD(P)-binding domain superfamily[5].
  • Alcohol dehydrogenase ADH2 YMR303C's part of is recorded as GroES-like superfamily[6].
  • Alcohol dehydrogenase ADH2 YMR303C's part of is recorded as Polyketide synthase, enoylreductase domain, protein family[7].
  • Alcohol dehydrogenase ADH2 YMR303C's part of is recorded as Alcohol dehydrogenase, C-terminal domain, protein family[8].
  • Alcohol dehydrogenase ADH2 YMR303C's part of is recorded as Alcohol dehydrogenase, N-terminal domain, protein family[9].
  • Alcohol dehydrogenase ADH2 YMR303C's part of is recorded as Alcohol dehydrogenase, zinc-type, conserved site, protein family[10].
  • Alcohol dehydrogenase ADH2 YMR303C's has part is recorded as Polyketide synthase, enoylreductase domain[11].
  • Alcohol dehydrogenase ADH2 YMR303C's has part is recorded as Alcohol dehydrogenase, zinc-type, conserved site[12].
  • Alcohol dehydrogenase ADH2 YMR303C's has part is recorded as Alcohol dehydrogenase, C-terminal[13].
  • Alcohol dehydrogenase ADH2 YMR303C's has part is recorded as Alcohol dehydrogenase, N-terminal[14].
  • Alcohol dehydrogenase ADH2 YMR303C's RefSeq protein ID is recorded as NP_014032[15].
  • Alcohol dehydrogenase ADH2 YMR303C's molecular function is recorded as metal ion binding[16].
  • Alcohol dehydrogenase ADH2 YMR303C's molecular function is recorded as alcohol dehydrogenase (NAD+) activity[17].
  • Alcohol dehydrogenase ADH2 YMR303C's molecular function is recorded as zinc ion binding[18].
  • Alcohol dehydrogenase ADH2 YMR303C's molecular function is recorded as oxidoreductase activity[19].
  • Alcohol dehydrogenase ADH2 YMR303C's molecular function is recorded as alcohol dehydrogenase (NAD+) activity[20].
  • Alcohol dehydrogenase ADH2 YMR303C's cell component is recorded as cytoplasm[21].
  • Alcohol dehydrogenase ADH2 YMR303C's cell component is recorded as cytoplasm[22].
  • Alcohol dehydrogenase ADH2 YMR303C's cell component is recorded as cytoplasm[23].
  • Alcohol dehydrogenase ADH2 YMR303C's biological process is recorded as ethanol metabolic process[24].
  • Alcohol dehydrogenase ADH2 YMR303C's biological process is recorded as amino acid catabolic process to alcohol via Ehrlich pathway[25].
  • Alcohol dehydrogenase ADH2 YMR303C's biological process is recorded as NADH oxidation[26].

References

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

Direct Wikidata claims

  1. [2] ↑ . UniProt. Retrieved . wikidata.org.
  2. [3] ↑ . UniProt. Retrieved . wikidata.org.
  3. [4] ↑ . UniProt. 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] ↑ . wikidata.org.
  8. [9] ↑ . wikidata.org.
  9. [10] ↑ . wikidata.org.
  10. [11] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . Q20641742. Retrieved . wikidata.org.
  15. [16] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . GOA. 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] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity.. Retrieved . ebi.ac.uk. Provenance: 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). Alcohol dehydrogenase ADH2 YMR303C. Retrieved May 3, 2026, from https://4ort.xyz/entity/alcohol-dehydrogenase-adh2-ymr303c
MLA “Alcohol dehydrogenase ADH2 YMR303C.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/alcohol-dehydrogenase-adh2-ymr303c.
BibTeX @misc{4ortxyz_alcohol-dehydrogenase-adh2-ymr303c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Alcohol dehydrogenase ADH2 YMR303C}}, year = {2026}, url = {https://4ort.xyz/entity/alcohol-dehydrogenase-adh2-ymr303c}, note = {Accessed: 2026-05-03}}
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