Histidine decarboxylase

mammalian protein found in Mus musculus
Protein protein Q14888536
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Summary

Histidine decarboxylase is a protein[1].

Key Facts

  • Histidine decarboxylase's instance of is recorded as protein[2].
  • Histidine decarboxylase's subclass of is recorded as protein[3].
  • Histidine decarboxylase's UniProt protein ID is recorded as P23738[4].
  • Histidine decarboxylase's part of is recorded as Pyridoxal phosphate-dependent transferase domain 1[5].
  • Histidine decarboxylase's part of is recorded as Pyridoxal phosphate-dependent transferase, major domain[6].
  • Histidine decarboxylase's part of is recorded as Aromatic-L-amino-acid decarboxylase[7].
  • Histidine decarboxylase's part of is recorded as Pyridoxal phosphate-dependent transferase[8].
  • Histidine decarboxylase's part of is recorded as Pyridoxal-phosphate binding site, protein family[9].
  • Histidine decarboxylase's has part is recorded as Pyridoxal-phosphate binding site[10].
  • Histidine decarboxylase's RefSeq protein ID is recorded as NP_032256[11].
  • Histidine decarboxylase's RefSeq protein ID is recorded as XP_006498847[12].
  • Histidine decarboxylase's molecular function is recorded as histidine decarboxylase activity[13].
  • Histidine decarboxylase's molecular function is recorded as carboxy-lyase activity[14].
  • Histidine decarboxylase's molecular function is recorded as catalytic activity[15].
  • Histidine decarboxylase's molecular function is recorded as lyase activity[16].
  • Histidine decarboxylase's molecular function is recorded as amino acid binding[17].
  • Histidine decarboxylase's molecular function is recorded as pyridoxal phosphate binding[18].
  • Histidine decarboxylase's molecular function is recorded as protein homodimerization activity[19].
  • Histidine decarboxylase's cell component is recorded as cytosol[20].
  • Histidine decarboxylase's cell component is recorded as dendrite[21].
  • Histidine decarboxylase's cell component is recorded as soma[22].
  • Histidine decarboxylase's biological process is recorded as cellular amino acid metabolic process[23].
  • Histidine decarboxylase's biological process is recorded as catecholamine biosynthetic process[24].
  • Histidine decarboxylase's biological process is recorded as histidine catabolic process[25].
  • Histidine decarboxylase's biological process is recorded as histamine biosynthetic process[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] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  7. [8] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . wikidata.org.
  9. [10] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . Q20641742. Retrieved . wikidata.org.
  11. [12] ↑ . Q20641742. Retrieved . wikidata.org.
  12. [13] ↑ . Gastric acid secretion in L-histidine decarboxylase-deficient mice. 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] ↑ . 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] ↑ . Gastric acid secretion in L-histidine decarboxylase-deficient mice. 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). Histidine decarboxylase. Retrieved May 3, 2026, from https://4ort.xyz/entity/histidine-decarboxylase-q14888536
MLA “Histidine decarboxylase.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/histidine-decarboxylase-q14888536.
BibTeX @misc{4ortxyz_histidine-decarboxylase-q14888536_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Histidine decarboxylase}}, year = {2026}, url = {https://4ort.xyz/entity/histidine-decarboxylase-q14888536}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Histidine decarboxylase — https://4ort.xyz/entity/histidine-decarboxylase-q14888536 (retrieved 2026-05-03)

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