protocatechuate 3,4-dioxygenase complex
A protein complex which is capable of protocatechuate 3,4-dioxygenase activity. It consists of an alpha subunit (PcaG) and a beta subunit (PcaH), with the non-heme iron active site formed at the alpha-beta interface. [GO:7770085]
Synonyms: PcaGH complex; PcaHG complex; protocatechuate 3,4-oxygenase complex
Components
| Component | Type | Part of / acts on | Grounding | Genes | Stoichiometry | Essential | Role |
|---|---|---|---|---|---|---|---|
| Protocatechuate 3,4-dioxygenase, alpha subunit | Protein | part of | InterPro:IPR012786 | pcaG | UNKNOWN | Alpha subunit of the two-component PcaGH intradiol ring-cleavage dioxygenase.
| |
| Protocatechuate 3,4-dioxygenase, beta subunit | Protein | part of | InterPro:IPR012785 | pcaH | UNKNOWN | Beta subunit of the PcaGH dioxygenase; the non-heme iron active site is formed at the alpha-beta interface.
|
Organism-specific protein examples
Named proteins in which each component's role was established, with the organism the evidence comes from. The component above is the taxon-agnostic family; these are the specific entries behind it.
Protocatechuate 3,4-dioxygenase, alpha subunit
| Accession | Protein | Gene | Organism | Entry |
|---|---|---|---|---|
UniProtKB:P00436 | Protocatechuate 3,4-dioxygenase alpha chain | pcaG | Pseudomonas putida (NCBITaxon:303) | REVIEWED |
Role and evidence (2 references)Reviewed Pseudomonas putida pcaG accession for the protocatechuate 3,4-dioxygenase alpha subunit.
| ||||
Protocatechuate 3,4-dioxygenase, beta subunit
| Accession | Protein | Gene | Organism | Entry |
|---|---|---|---|---|
UniProtKB:P00437 | Protocatechuate 3,4-dioxygenase beta chain | pcaH | Pseudomonas putida (NCBITaxon:303) | REVIEWED |
Role and evidence (2 references)Reviewed Pseudomonas putida pcaH accession for the protocatechuate 3,4-dioxygenase beta subunit.
| ||||
Canonical examples
NCBITaxon:101510Rhodococcus jostii RHA1 — Strain source of the PcaHG protocatechuate-branch in vitro reconstitution cited by GO:7770085. [PMID:25558786]NCBITaxon:303Pseudomonas putida — Source of the reviewed PcaG/PcaH protein examples and the pcaG-pcaH gene cloning and expression study. [PMID:8407791]
Functions
- protocatechuate 3,4-dioxygenase activity
GO:0018578— The PcaGH complex catalyzes ring cleavage of 3,4-dihydroxybenzoate to 3-carboxy-cis,cis-muconate.GO:7770085GO:7770085 is capable of GO:0018578 protocatechuate 3,4-dioxygenase activity.GO:0018578GO:0018578 is the molecular-function term for protocatechuate 3,4-dioxygenase activity.
Evidence
GO:7770085Gene Ontology cellular-component term for the protocatechuate 3,4-dioxygenase complex and its PcaGH, PcaHG and protocatechuate 3,4-oxygenase synonymy.GO:1990204QuickGO reports GO:7770085 as an is-a child of GO:1990204 oxidoreductase complex.GO:0018578Gene Ontology molecular-function term for protocatechuate 3,4-dioxygenase activity.InterPro:IPR012786InterPro family entry for protocatechuate 3,4-dioxygenase alpha subunits.InterPro:IPR012785InterPro family entry for protocatechuate 3,4-dioxygenase beta subunits.UniProtKB:P00436UniProtKB reviewed Pseudomonas putida PcaG entry.UniProtKB:P00437UniProtKB reviewed Pseudomonas putida PcaH entry.PMID:25558786PubMed identifier for Yamanashi et al. 2015, the Bioscience, Biotechnology, and Biochemistry PcaHG reconstitution paper cited by GO:7770085.DOI:10.1080/09168451.2014.993915DOI for Yamanashi et al. 2015, as reported by PubMed.PMID:8407791PubMed identifier for Frazee et al. 1993, the Journal of Bacteriology Pseudomonas putida pcaG-pcaH cloning paper cited by UniProtKB P00436 and P00437.DOI:10.1128/jb.175.19.6194-6202.1993DOI for Frazee et al. 1993, as reported by UniProtKB.
Curation history
2026-10-02T01:22:14Zcodex · CREATED_RECORD — Scaffolded by scripts/new_record.py2026-10-02T01:23:32Zcodex · EXPANDED_RECORD — Added PcaGH synonymy, oxidoreductase-complex parentage, exact InterPro-grounded PcaG and PcaH constituents with reviewed Pseudomonas putida UniProt examples, Rhodococcus jostii RHA1 and P. putida canonical examples, protocatechuate 3,4-dioxygenase activity, and GO/PubMed/DOI evidence.
Source: data/structures/other/protocatechuate_3_4_dioxygenase_complex.yaml