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Gulonolactone (L-) oxidase

mammalian protein found in Rattus norvegicus
Protein protein Q28557039
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Gulonolactone (L-) oxidase

Summary

Gulonolactone (L-) oxidase is a protein[1].

Key Facts

  • Gulonolactone (L-) oxidase's instance of is recorded as protein[2].
  • Gulonolactone (L-) oxidase's UniProt protein ID is recorded as P10867[3].
  • Gulonolactone (L-) oxidase's part of is recorded as FAD-binding, type PCMH-like superfamily[4].
  • Gulonolactone (L-) oxidase's part of is recorded as FAD-binding, type PCMH, subdomain 1[5].
  • Gulonolactone (L-) oxidase's part of is recorded as Sugar 1,4-lactone oxidase[6].
  • Gulonolactone (L-) oxidase's part of is recorded as FAD-binding, type PCMH, subdomain 2[7].
  • Gulonolactone (L-) oxidase's part of is recorded as membrane protein[8].
  • Gulonolactone (L-) oxidase's part of is recorded as FAD-oxidase[9].
  • Gulonolactone (L-) oxidase's part of is recorded as D-arabinono-1,4-lactone oxidase[10].
  • Gulonolactone (L-) oxidase's part of is recorded as FAD-binding domain, PCMH-type, protein family[11].
  • Gulonolactone (L-) oxidase's part of is recorded as Oxygen oxidoreductase covalent FAD-binding site, protein family[12].
  • Gulonolactone (L-) oxidase's has part is recorded as FAD-binding domain, PCMH-type[13].
  • Gulonolactone (L-) oxidase's has part is recorded as Oxygen oxidoreductase covalent FAD-binding site[14].
  • Gulonolactone (L-) oxidase's has part is recorded as D-arabinono-1,4-lactone oxidase domain[15].
  • Gulonolactone (L-) oxidase's has part is recorded as FAD linked oxidase, N-terminal[16].
  • Gulonolactone (L-) oxidase's RefSeq protein ID is recorded as NP_071556[17].
  • Gulonolactone (L-) oxidase's molecular function is recorded as catalytic activity[18].
  • Gulonolactone (L-) oxidase's molecular function is recorded as D-arabinono-1,4-lactone oxidase activity[19].
  • Gulonolactone (L-) oxidase's molecular function is recorded as oxidoreductase activity[20].
  • Gulonolactone (L-) oxidase's molecular function is recorded as oxidoreductase activity, acting on CH-OH group of donors[21].
  • Gulonolactone (L-) oxidase's molecular function is recorded as oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor[22].
  • Gulonolactone (L-) oxidase's molecular function is recorded as L-gulonolactone oxidase activity[23].
  • Gulonolactone (L-) oxidase's molecular function is recorded as flavin adenine dinucleotide binding[24].
  • Gulonolactone (L-) oxidase's molecular function is recorded as FAD binding[25].
  • Gulonolactone (L-) oxidase's cell component is recorded as endoplasmic reticulum[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] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: 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] ↑ . 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] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . Q20641742. Retrieved . 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] ↑ . GOA. 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). Gulonolactone (L-) oxidase. Retrieved May 3, 2026, from https://4ort.xyz/entity/gulonolactone-l-oxidase
MLA “Gulonolactone (L-) oxidase.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/gulonolactone-l-oxidase.
BibTeX @misc{4ortxyz_gulonolactone-l-oxidase_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Gulonolactone (L-) oxidase}}, year = {2026}, url = {https://4ort.xyz/entity/gulonolactone-l-oxidase}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Gulonolactone (L-) oxidase — https://4ort.xyz/entity/gulonolactone-l-oxidase (retrieved 2026-05-03)

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