Propionyl-CoA carboxylase subunit beta

mammalian protein found in Homo sapiens
Protein protein Q21121843
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Propionyl-CoA carboxylase subunit beta

Summary

Propionyl-CoA carboxylase subunit beta is a protein[1].

Key Facts

  • Propionyl-CoA carboxylase subunit beta's instance of is recorded as protein[2].
  • Propionyl-CoA carboxylase subunit beta is part of ClpP/crotonase-like domain superfamily[3].
  • Propionyl-CoA carboxylase subunit beta is part of Acetyl-coenzyme A carboxyltransferase, C-terminal domain, protein family[4].
  • Propionyl-CoA carboxylase subunit beta is part of acetyl-coenzyme A carboxyltransferase, N-terminal domain, protein family[5].
  • Propionyl-CoA carboxylase subunit beta is part of Acetyl-CoA carboxylase family[6].
  • Propionyl-CoA carboxylase subunit beta comprises acetyl-coenzyme A carboxyltransferase, N-terminal[7].
  • Propionyl-CoA carboxylase subunit beta comprises acetyl-coenzyme A carboxyltransferase, C-terminal[8].
  • Propionyl-CoA carboxylase subunit beta comprises Acetyl-CoA carboxylase domain[9].
  • Propionyl-CoA carboxylase subunit beta's molecular function is recorded as nucleotide binding[10].
  • Propionyl-CoA carboxylase subunit beta's molecular function is recorded as ligase activity[11].
  • Propionyl-CoA carboxylase subunit beta's molecular function is recorded as ATP binding[12].
  • Propionyl-CoA carboxylase subunit beta's molecular function is recorded as propionyl-CoA carboxylase activity[13].
  • Propionyl-CoA carboxylase subunit beta's molecular function is recorded as CoA carboxylase activity[14].
  • Propionyl-CoA carboxylase subunit beta's molecular function is recorded as protein binding[15].
  • Propionyl-CoA carboxylase subunit beta's cell component is recorded as cytosol[16].
  • Propionyl-CoA carboxylase subunit beta's cell component is recorded as mitochondrial matrix[17].
  • Propionyl-CoA carboxylase subunit beta's cell component is recorded as mitochondrion[18].
  • Propionyl-CoA carboxylase subunit beta's biological process is recorded as biotin metabolic process[19].
  • Propionyl-CoA carboxylase subunit beta's biological process is recorded as fatty acid catabolic process[20].
  • Propionyl-CoA carboxylase subunit beta's biological process is recorded as short-chain fatty acid catabolic process[21].
  • Propionyl-CoA carboxylase subunit beta's encoded by is recorded as PCCB[22].
  • Propionyl-CoA carboxylase subunit beta's found in taxon is recorded as Homo sapiens[23].

References

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

Direct Wikidata claims

  1. [2] . Q905695. Retrieved . wikidata.org.
  2. [3] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  3. [4] . wikidata.org.
  4. [5] . wikidata.org.
  5. [6] . 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] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] . Correction of the metabolic defect in propionic acidemia fibroblasts by microinjection of a full-length cDNA or RNA transcript encoding the propionyl-CoA carboxylase beta subunit. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] . Crystal structure of the α6β6 holoenzyme of propionyl-coenzyme A carboxylase. 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] . Correction of the metabolic defect in propionic acidemia fibroblasts by microinjection of a full-length cDNA or RNA transcript encoding the propionyl-CoA carboxylase beta subunit. 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] . Q905695. Retrieved . wikidata.org.
  22. [23] . Q905695. Retrieved . wikidata.org.

Class ancestry

  1. [1] . Wikidata. wikidata.org.

📑 Cite this page

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). Propionyl-CoA carboxylase subunit beta. Retrieved May 3, 2026, from https://4ort.xyz/entity/propionyl-coa-carboxylase-subunit-beta
MLA “Propionyl-CoA carboxylase subunit beta.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/propionyl-coa-carboxylase-subunit-beta.
BibTeX @misc{4ortxyz_propionyl-coa-carboxylase-subunit-beta_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Propionyl-CoA carboxylase subunit beta}}, year = {2026}, url = {https://4ort.xyz/entity/propionyl-coa-carboxylase-subunit-beta}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Propionyl-CoA carboxylase subunit beta — https://4ort.xyz/entity/propionyl-coa-carboxylase-subunit-beta (retrieved 2026-05-03)

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Edit History

Rolling log of changes to this entity's Wikidata record. Values shown reflect the current state of each edited property — follow the history link to see the precise diff for any edit.

  1. 5w ago · Boghog · 2026-07-24 view diff on Wikidata ↗
    Imported from
    Encoded by PCCB
    Wikidata description mammalian protein found in Homo sapiens
    Molecular function nucleotide binding, ligase activity, ATP binding +3
    + 10 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ [[Property:P591]]: 6.4.1.3, [[:toollabs:quickstatements/#/batch/261491|batch #261491]]"
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