D-lactate dehydrogenase YDL178W

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27549471
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D-lactate dehydrogenase YDL178W

Summary

D-lactate dehydrogenase YDL178W is a protein[1].

Key Facts

  • D-lactate dehydrogenase YDL178W's instance of is recorded as protein[2].
  • D-lactate dehydrogenase YDL178W's subclass of is recorded as protein[3].
  • D-lactate dehydrogenase YDL178W's UniProt protein ID is recorded as P46681[4].
  • D-lactate dehydrogenase YDL178W's part of is recorded as Vanillyl-alcohol oxidase, C-terminal subdomain 2[5].
  • D-lactate dehydrogenase YDL178W's part of is recorded as FAD-binding, type PCMH-like superfamily[6].
  • D-lactate dehydrogenase YDL178W's part of is recorded as FAD-linked oxidase-like, C-terminal[7].
  • D-lactate dehydrogenase YDL178W's part of is recorded as FAD-binding, type PCMH, subdomain 2[8].
  • D-lactate dehydrogenase YDL178W's part of is recorded as FAD-binding, type PCMH, subdomain 1[9].
  • D-lactate dehydrogenase YDL178W's part of is recorded as FAD-oxidase[10].
  • D-lactate dehydrogenase YDL178W's part of is recorded as FAD-linked oxidase, C-terminal domain, protein family[11].
  • D-lactate dehydrogenase YDL178W's part of is recorded as FAD-binding domain, PCMH-type, protein family[12].
  • D-lactate dehydrogenase YDL178W's has part is recorded as FAD linked oxidase, N-terminal[13].
  • D-lactate dehydrogenase YDL178W's has part is recorded as FAD-linked oxidase, C-terminal[14].
  • D-lactate dehydrogenase YDL178W's has part is recorded as FAD-binding domain, PCMH-type[15].
  • D-lactate dehydrogenase YDL178W's RefSeq protein ID is recorded as NP_010103[16].
  • D-lactate dehydrogenase YDL178W's molecular function is recorded as oxidoreductase activity, acting on CH-OH group of donors[17].
  • D-lactate dehydrogenase YDL178W's molecular function is recorded as FAD binding[18].
  • D-lactate dehydrogenase YDL178W's molecular function is recorded as catalytic activity[19].
  • D-lactate dehydrogenase YDL178W's molecular function is recorded as D-lactate dehydrogenase (cytochrome) activity[20].
  • D-lactate dehydrogenase YDL178W's molecular function is recorded as flavin adenine dinucleotide binding[21].
  • D-lactate dehydrogenase YDL178W's molecular function is recorded as oxidoreductase activity[22].
  • D-lactate dehydrogenase YDL178W's molecular function is recorded as (R)-2-hydroxyglutarate dehydrogenase activity[23].
  • D-lactate dehydrogenase YDL178W's molecular function is recorded as actin binding[24].
  • D-lactate dehydrogenase YDL178W's molecular function is recorded as FAD binding[25].
  • D-lactate dehydrogenase YDL178W's molecular function is recorded as D-lactate dehydrogenase (cytochrome) activity[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] . Q20641742. 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] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  8. [9] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  9. [10] . wikidata.org.
  10. [11] . wikidata.org.
  11. [12] . 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] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  15. [16] . Q20641742. Retrieved . wikidata.org.
  16. [17] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . Saccharomyces cerevisiae Forms D-2-Hydroxyglutarate and Couples Its Degradation to D-Lactate Formation via a Cytosolic Transhydrogenase. 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] . Saccharomyces cerevisiae Forms D-2-Hydroxyglutarate and Couples Its Degradation to D-Lactate Formation via a Cytosolic Transhydrogenase. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . Interaction of D-lactate dehydrogenase protein 2 (Dld2p) with F-actin: implication for an alternative function of Dld2p. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] . GOA. 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). D-lactate dehydrogenase YDL178W. Retrieved May 3, 2026, from https://4ort.xyz/entity/d-lactate-dehydrogenase-ydl178w
MLA “D-lactate dehydrogenase YDL178W.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/d-lactate-dehydrogenase-ydl178w.
BibTeX @misc{4ortxyz_d-lactate-dehydrogenase-ydl178w_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{D-lactate dehydrogenase YDL178W}}, year = {2026}, url = {https://4ort.xyz/entity/d-lactate-dehydrogenase-ydl178w}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): D-lactate dehydrogenase YDL178W — https://4ort.xyz/entity/d-lactate-dehydrogenase-ydl178w (retrieved 2026-05-03)

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