Aminolevulinate dehydratase

mammalian protein found in Rattus norvegicus
Protein protein Q28559164
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Aminolevulinate dehydratase

Summary

Aminolevulinate dehydratase is a protein[1].

Key Facts

  • Aminolevulinate dehydratase's instance of is recorded as protein[2].
  • Aminolevulinate dehydratase's subclass of is recorded as protein[3].
  • Aminolevulinate dehydratase's UniProt protein ID is recorded as P06214[4].
  • Aminolevulinate dehydratase's part of is recorded as delta-aminolevulinic acid dehydratase[5].
  • Aminolevulinate dehydratase's part of is recorded as TIM barrel[6].
  • Aminolevulinate dehydratase's part of is recorded as Delta-aminolevulinic acid dehydratase, active site, protein family[7].
  • Aminolevulinate dehydratase's has part is recorded as Delta-aminolevulinic acid dehydratase, active site[8].
  • Aminolevulinate dehydratase's RefSeq protein ID is recorded as NP_037031[9].
  • Aminolevulinate dehydratase's RefSeq protein ID is recorded as XP_006238296[10].
  • Aminolevulinate dehydratase's RefSeq protein ID is recorded as XP_006238297[11].
  • Aminolevulinate dehydratase's molecular function is recorded as catalytic activity[12].
  • Aminolevulinate dehydratase's molecular function is recorded as porphobilinogen synthase activity[13].
  • Aminolevulinate dehydratase's molecular function is recorded as zinc ion binding[14].
  • Aminolevulinate dehydratase's molecular function is recorded as lyase activity[15].
  • Aminolevulinate dehydratase's molecular function is recorded as identical protein binding[16].
  • Aminolevulinate dehydratase's molecular function is recorded as metal ion binding[17].
  • Aminolevulinate dehydratase's molecular function is recorded as proteasome core complex binding[18].
  • Aminolevulinate dehydratase's cell component is recorded as extracellular space[19].
  • Aminolevulinate dehydratase's cell component is recorded as cytosol[20].
  • Aminolevulinate dehydratase's biological process is recorded as response to hypoxia[21].
  • Aminolevulinate dehydratase's biological process is recorded as porphyrin-containing compound biosynthetic process[22].
  • Aminolevulinate dehydratase's biological process is recorded as protoporphyrinogen IX biosynthetic process[23].
  • Aminolevulinate dehydratase's biological process is recorded as heme biosynthetic process[24].
  • Aminolevulinate dehydratase's biological process is recorded as response to oxidative stress[25].
  • Aminolevulinate dehydratase's biological process is recorded as response to nutrient[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] . Q20641742. Retrieved . wikidata.org.
  10. [11] . Q20641742. Retrieved . wikidata.org.
  11. [12] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] . GOA. 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] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . Delta-aminolevulinic dehydratase is a proteasome interacting protein. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . Effects of leaves extract of Ocimum sanctum L. on arsenic-induced toxicity in Wistar albino rats. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . delta-Aminolevulinic acid dehydratase in rat liver: studies on the effects of ethanol, acetaldehyde, and B6 vitamers. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . The regulation of porphobilinogen oxygenase and porphobilinogen deaminase activities in rat bone marrow under conditions of erythropoietic stress. 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] . Essential metal status, prooxidant/antioxidant effects of MiADMSA in male rats: age-related effects. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] . delta-Aminolevulinic acid dehydratase in rat liver: studies on the effects of ethanol, acetaldehyde, and B6 vitamers. 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). Aminolevulinate dehydratase. Retrieved May 3, 2026, from https://4ort.xyz/entity/aminolevulinate-dehydratase-q28559164
MLA “Aminolevulinate dehydratase.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/aminolevulinate-dehydratase-q28559164.
BibTeX @misc{4ortxyz_aminolevulinate-dehydratase-q28559164_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Aminolevulinate dehydratase}}, year = {2026}, url = {https://4ort.xyz/entity/aminolevulinate-dehydratase-q28559164}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Aminolevulinate dehydratase — https://4ort.xyz/entity/aminolevulinate-dehydratase-q28559164 (retrieved 2026-05-03)

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