protocatechuate catabolic process, ortho-cleavage

GO:0019618

The complete four-reaction ortho-cleavage branch converts protocatechuate to 3-oxoadipate through 3-carboxy-cis,cis-muconate, the R carboxymuconolactone and 3-oxoadipate enol-lactone. The selected Pseudomonas putida machinery retains historical native enzyme identities and assembly limitations; it does not assert occurrence in every strain. The exact native cycloisomerase preserves a stereospecific product absent from its Rhea cross-reference. Terminal CoA transfer and thiolysis belong to the separate downstream pathway.

Pathway type
aromatic compound catabolism
Organism scope

Read the source YAML

Pathway network

25 nodes · 37 asserted directed edges

Arrows show recorded subject → object relationships, not necessarily metabolic flow. Select a node for details or an arrow for evidence. Scroll, zoom or find a node to explore.

Pathway network: protocatechuate catabolic process, ortho-cleavage 25 nodes · 37 asserted directed edges. Every arrow links to its evidence table row; nodes link to their component details. Isolated declared components are retained. GO:0019618 — has_part → RHEA:10085; One of the four complete native core reactions; the GO scope is the protocatechuate branch ending at 3-oxoadipate.; Evidence: MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY, MetaCyc:PROTOCATECHUATE-34-DIOXYGENASE-RXN, GO:0019618has part CHEBI:15379 — consumes → RHEA:10085; Complete formal substrates side; coefficient 1.; Evidence: RHEA:10085consumes CHEBI:36241 — consumes → RHEA:10085; Complete formal substrates side; coefficient 1.; Evidence: RHEA:10085consumes RHEA:10085 — produces → CHEBI:15378; Complete formal products side; coefficient 2.; Evidence: RHEA:10085produces RHEA:10085 — produces → CHEBI:57496; Complete formal products side; coefficient 1.; Evidence: RHEA:10085produces GO:0019618 — has_part → MetaCyc:5.5.1.2-RXN; One of the four complete native core reactions; the GO scope is the protocatechuate branch ending at 3-oxoadipate.; Evidence: MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY, GO:0019618has part CHEBI:15378 — consumes → MetaCyc:5.5.1.2-RXN; Complete formal substrates side; coefficient 1.; Evidence: MetaCyc:5.5.1.2-RXN, MetaCyc:PROTONconsumes CHEBI:57496 — consumes → MetaCyc:5.5.1.2-RXN; Complete formal substrates side; coefficient 1.; Evidence: MetaCyc:5.5.1.2-RXN, MetaCyc:CPD-245consumes MetaCyc:5.5.1.2-RXN — produces → CHEBI:58771; Complete formal products side; coefficient 1. The native R lactone is retained; stereo-unspecified RHEA:23658/CHEBI:57979 is not an exact identity.; Evidence: MetaCyc:5.5.1.2-RXN, MetaCyc:CPD-7737produces GO:0019618 — has_part → RHEA:23349; One of the four complete native core reactions; the GO scope is the protocatechuate branch ending at 3-oxoadipate.; Evidence: MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY, MetaCyc:4-CARBOXYMUCONOLACTONE-DECARBOXYLASE-RXN, GO:0019618has part CHEBI:15378 — consumes → RHEA:23349; Complete formal substrates side; coefficient 1.; Evidence: RHEA:23349consumes CHEBI:58771 — consumes → RHEA:23349; Complete formal substrates side; coefficient 1.; Evidence: RHEA:23349consumes RHEA:23349 — produces → CHEBI:16526; Complete formal products side; coefficient 1.; Evidence: RHEA:23349produces RHEA:23349 — produces → CHEBI:58425; Complete formal products side; coefficient 1.; Evidence: RHEA:23349produces GO:0019618 — has_part → RHEA:10185; One of the four complete native core reactions; the GO scope is the protocatechuate branch ending at 3-oxoadipate.; Evidence: MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY, MetaCyc:3-OXOADIPATE-ENOL-LACTONASE-RXN, GO:0019618has part CHEBI:15377 — consumes → RHEA:10185; Complete formal substrates side; coefficient 1.; Evidence: RHEA:10185consumes CHEBI:58425 — consumes → RHEA:10185; Complete formal substrates side; coefficient 1.; Evidence: RHEA:10185consumes RHEA:10185 — produces → CHEBI:15378; Complete formal products side; coefficient 1.; Evidence: RHEA:10185produces RHEA:10185 — produces → CHEBI:15775; Complete formal products side; coefficient 1.; Evidence: RHEA:10185produces RHEA:10085 — provides_input_for → MetaCyc:5.5.1.2-RXN; The complete shared intermediate is CHEBI:57496. This material connection preserves the native reaction ordering.; Evidence: MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY, MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWYprovides input for MetaCyc:5.5.1.2-RXN — provides_input_for → RHEA:23349; The complete shared intermediate is CHEBI:58771. This material connection preserves the native reaction ordering.; Evidence: MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY, MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWYprovides input for RHEA:23349 — provides_input_for → RHEA:10185; The complete shared intermediate is CHEBI:58425. This material connection preserves the native reaction ordering.; Evidence: MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY, MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWYprovides input for MetaCyc:CPLX-2721 — catalyzes → RHEA:10085; Native Pseudomonas putida activity annotation. Its complex comment distinguishes the historical four-alpha/four-beta preparation from the ATCC23975 twelve-alpha/twelve-beta enzyme; native subunit frames are not exact cross-strain sequence assignments.; Evidence: MetaCyc:ENZRXN-3343, MetaCyc:PROTOCATECHUATE-34-DIOXYGENASE-RXNcatalyzes MetaCyc:CPLX-2762 — catalyzes → MetaCyc:5.5.1.2-RXN; Historical Pseudomonas putida PcaB enzyme; do not substitute catechol-branch muconate cycloisomerase.; Evidence: MetaCyc:ENZRXN-3366catalyzes MetaCyc:CPLX-2745 — catalyzes → RHEA:23349; Historical Pseudomonas putida decarboxylase accelerates the otherwise spontaneous decarboxylation; distinct from muconolactone isomerase.; Evidence: MetaCyc:ENZRXN-3367, MetaCyc:4-CARBOXYMUCONOLACTONE-DECARBOXYLASE-RXNcatalyzes MetaCyc:CPLX-2761 — catalyzes → RHEA:10185; Historical Pseudomonas putida hydrolase model shared with catechol cleavage; no exact sequence join to KT2440 Q88N36 is established.; Evidence: MetaCyc:ENZRXN-3368, MetaCyc:3-OXOADIPATE-ENOL-LACTONASE-RXNcatalyzes MetaCyc:CPLX-2721 — has_part → MetaCyc:MONOMER-3185; 4 beta subunits in the source assembly. The complex comment attributes this model to the historical purified preparation and distinguishes the ATCC23975 twelve-alpha/twelve-beta enzyme. Native subunit cross-references do not establish exact sequence equivalence.; Evidence: MetaCyc:CPLX-2721has part MetaCyc:CPLX-2721 — has_part → MetaCyc:MONOMER-3186; 4 alpha subunits in the source assembly. The complex comment attributes this model to the historical purified preparation and distinguishes the ATCC23975 twelve-alpha/twelve-beta enzyme. Native subunit cross-references do not establish exact sequence equivalence.; Evidence: MetaCyc:CPLX-2721has part MetaCyc:CPLX-2762 — has_part → MetaCyc:MONOMER-3222; 4 PcaB subunits in the source assembly. Native historical Pseudomonas putida assembly model.; Evidence: MetaCyc:CPLX-2762has part MetaCyc:CPLX-2745 — has_part → MetaCyc:MONOMER-3206; Six subunits in the native historical Pseudomonas putida assembly annotation. The source distinguishes this hexamer from the catechol-branch muconolactone isomerase decamer.; Evidence: MetaCyc:CPLX-2745has part MetaCyc:CPLX-2761 — has_part → MetaCyc:MONOMER-3221; Native historical three-copy assembly annotation. It is not a modern structure determination or evidence for three KT2440 Q88N36 proteins; historical mass and sequence limitations are retained in the research ledger.; Evidence: MetaCyc:CPLX-2761has part MetaCyc:CPLX-2721 — has_cofactor → CHEBI:29034; The native activity identifies ferric iron as a bound cofactor. The complex comment distinguishes preparations with different subunit counts; no universal iron occupancy is asserted. Dioxygen remains a reaction substrate.; Evidence: MetaCyc:ENZRXN-3343has cofactor CHEBI:36241 — regulates → MetaCyc:CPLX-2721; Protocatechuate induces enzyme expression in the source Pseudomonas putida pathway context; this does not assert direct catalytic activation or ligand binding to this purified assembly.; Evidence: MetaCyc:CPLX-2721regulates CHEBI:15775 — regulates → MetaCyc:CPLX-2762; 3-oxoadipate induces enzyme expression in the source Pseudomonas putida pathway context; this does not assert direct catalytic activation or ligand binding to this purified assembly.; Evidence: MetaCyc:CPLX-2762regulates CHEBI:15775 — regulates → MetaCyc:CPLX-2745; 3-oxoadipate induces enzyme expression in the source Pseudomonas putida pathway context; this does not assert direct catalytic activation or ligand binding to this purified assembly.; Evidence: MetaCyc:CPLX-2745regulates CHEBI:15775 — regulates → MetaCyc:CPLX-2761; 3-oxoadipate induces enzyme expression in the source Pseudomonas putida pathway context; this does not assert direct catalytic activation or ligand binding to this purified assembly.; Evidence: MetaCyc:CPLX-2761regulates RHEA:10185 — provides_input_for → MetaCyc:PWY-2361; The final core product, 3-oxoadipate, enters the separate downstream degradation module. Its CoA-transfer and thiolysis reactions are outside this record boundary.; Evidence: MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY, MetaCyc:PWY-2361provides input for 3,4-dihydroxybenzoate; CHEBI:36241; Declared type: small_molecule small molecule 3,4-dihydroxybenzoate 3-carboxy-cis,cis-muconate(3-); CHEBI:57496; Declared type: small_molecule small molecule 3-carboxy-cis,cis- muconate(3-) (R)-2-(carboxylatomethyl)-5-oxo-2,5-dihydro-2-furoate; CHEBI:58771; Declared type: small_molecule small molecule (R)-2-(carboxylatomethyl)-5- oxo-2,5-dihydro-2-furoate 5-oxo-4,5-dihydro-2-furylacetate; CHEBI:58425; Declared type: small_molecule small molecule 5-oxo-4,5-dihydro-2- furylacetate 3-oxoadipate(2-); CHEBI:15775; Declared type: small_molecule small molecule 3-oxoadipate(2-) dioxygen; CHEBI:15379; Declared type: small_molecule small molecule dioxygen hydron; CHEBI:15378; Declared type: small_molecule small molecule hydron water; CHEBI:15377; Declared type: small_molecule small molecule water carbon dioxide; CHEBI:16526; Declared type: small_molecule small molecule carbon dioxide protocatechuate 3,4-dioxygenase; MetaCyc:CPLX-2721; Declared type: complex complex protocatechuate 3,4-dioxygenase protocatechuate 3,4-dioxygenase β subunit; MetaCyc:MONOMER-3185; Declared type: protein protein protocatechuate 3,4-dioxygenase β subunit protocatechuate 3,4-dioxygenase α subunit; MetaCyc:MONOMER-3186; Declared type: protein protein protocatechuate 3,4-dioxygenase α subunit 3-carboxymuconate cycloisomerase; MetaCyc:CPLX-2762; Declared type: complex complex 3-carboxymuconate cycloisomerase subunit of 3-carboxymuconate cycloisomerase; MetaCyc:MONOMER-3222; Declared type: protein protein subunit of 3-carboxymuconate cycloisomerase 4-carboxymuconolactone decarboxylase; MetaCyc:CPLX-2745; Declared type: complex complex 4-carboxymuconolactone decarboxylase subunit of 4-carboxymuconolactone decarboxylase; MetaCyc:MONOMER-3206; Declared type: protein protein subunit of 4-carboxymuconolactone decarboxylase β-ketoadipate enol-lactone hydrolase; MetaCyc:CPLX-2761; Declared type: complex complex β-ketoadipate enol-lactone hydrolase subunit of 3-oxoadipate enol-lactone hydrolase; MetaCyc:MONOMER-3221; Declared type: protein protein subunit of 3-oxoadipate enol-lactone hydrolase iron(3+); CHEBI:29034; Declared type: cofactor cofactor iron(3+) 3,4-dihydroxybenzoate + O2 => 3-carboxy-cis,cis-muconate + 2 H(+); RHEA:10085; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity 3,4-dihydroxybenzoate + O2 => 3-carboxy-cis,cis- muconate + 2 H(+) 3-carboxymuconate cycloisomerization to the R lactone; MetaCyc:5.5.1.2-RXN; Declared type: molecular_activity; Source reaction direction: right_to_left molecular activity 3-carboxymuconate cycloisomerization to the R lactone (R)-2-(carboxymethyl)-5-oxo-2,5-dihydro-2-furoate + H(+) => (4,5-dihydro-5-oxofuran-2-yl)-acetate + CO2; RHEA:23349; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity (R)-2-(carboxymethyl)-5-oxo- 2,5-dihydro-2-furoate + H(+) => (4,5-dihydro-5-oxofuran- 2-yl)-acetate + CO2 (4,5-dihydro-5-oxofuran-2-yl)-acetate + H2O => 3-oxoadipate + H(+); RHEA:10185; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity (4,5-dihydro-5-oxofuran-2- yl)-acetate + H2O => 3-oxoadipate + H(+) 3-oxoadipate degradation; MetaCyc:PWY-2361; Declared type: pathway pathway 3-oxoadipate degradation protocatechuate catabolic process, ortho-cleavage; GO:0019618; Declared type: pathway pathway protocatechuate catabolic process, ortho-cleavage

Components and activities

Declared biological components and source reaction directions
NodeKind or roleSource direction
Pseudomonas putida
NCBITaxon:303		taxon
3,4-dihydroxybenzoate
CHEBI:36241		small molecule
3-carboxy-cis,cis-muconate(3-)
CHEBI:57496		small molecule
(R)-2-(carboxylatomethyl)-5-oxo-2,5-dihydro-2-furoate
CHEBI:58771		small molecule
5-oxo-4,5-dihydro-2-furylacetate
CHEBI:58425		small molecule
3-oxoadipate(2-)
CHEBI:15775		small molecule
dioxygen
CHEBI:15379		small molecule
hydron
CHEBI:15378		small molecule
water
CHEBI:15377		small molecule
carbon dioxide
CHEBI:16526		small molecule
protocatechuate 3,4-dioxygenase
MetaCyc:CPLX-2721		complex
protocatechuate 3,4-dioxygenase β subunit
MetaCyc:MONOMER-3185		protein
protocatechuate 3,4-dioxygenase α subunit
MetaCyc:MONOMER-3186		protein
3-carboxymuconate cycloisomerase
MetaCyc:CPLX-2762		complex
subunit of 3-carboxymuconate cycloisomerase
MetaCyc:MONOMER-3222		protein
4-carboxymuconolactone decarboxylase
MetaCyc:CPLX-2745		complex
subunit of 4-carboxymuconolactone decarboxylase
MetaCyc:MONOMER-3206		protein
β-ketoadipate enol-lactone hydrolase
MetaCyc:CPLX-2761		complex
subunit of 3-oxoadipate enol-lactone hydrolase
MetaCyc:MONOMER-3221		protein
iron(3+)
CHEBI:29034		cofactor
3,4-dihydroxybenzoate + O2 => 3-carboxy-cis,cis-muconate + 2 H(+)
RHEA:10085		molecular activityleft to right
3-carboxymuconate cycloisomerization to the R lactone
MetaCyc:5.5.1.2-RXN		molecular activityright to left
(R)-2-(carboxymethyl)-5-oxo-2,5-dihydro-2-furoate + H(+) => (4,5-dihydro-5-oxofuran-2-yl)-acetate + CO2
RHEA:23349		molecular activityleft to right
(4,5-dihydro-5-oxofuran-2-yl)-acetate + H2O => 3-oxoadipate + H(+)
RHEA:10185		molecular activityleft to right
3-oxoadipate degradation
MetaCyc:PWY-2361		pathway

Mechanistic edges

Mechanistic edges and their cited evidence
SubjectPredicate and descriptionObjectEvidence
GO:0019618has_part

One of the four complete native core reactions; the GO scope is the protocatechuate branch ending at 3-oxoadipate.

3,4-dihydroxybenzoate + O2 => 3-carboxy-cis,cis-muconate + 2 H(+)
RHEA:10085
  • MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY

    Source assertion: The native reaction-list contains PROTOCATECHUATE-34-DIOXYGENASE-RXN.

    Source location/ptools-xml/Pathway[@frameid='PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY']/reaction-list/Reaction[@frameid='PROTOCATECHUATE-34-DIOXYGENASE-RXN']
  • MetaCyc:PROTOCATECHUATE-34-DIOXYGENASE-RXN

    Source assertion: The native reaction has a RHEA unification cross-reference to 10085; complete compounds, coefficients and selected pathway direction agree.

    Source location/ptools-xml/Reaction/dblink[dblink-db='RHEA']; left; right; reaction-direction
  • GO:0019618

    Source assertion: The biological-process term denotes protocatechuate degradation to beta-ketoadipate and cross-references MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY; its logical input and output restrictions use CHEBI:36241 and CHEBI:15775.

    Source locationGO:0019618: IAO:0000115; oio:hasDbXref; owl:equivalentClass/owl:intersectionOf list members with owl:onProperty RO:0004009, owl:someValuesFrom CHEBI:36241, and owl:onProperty RO:0004008, owl:someValuesFrom CHEBI:15775
dioxygen
CHEBI:15379		consumes

Complete formal substrates side; coefficient 1.

3,4-dihydroxybenzoate + O2 => 3-carboxy-cis,cis-muconate + 2 H(+)
RHEA:10085
  • RHEA:10085

    Source assertion: RHEA:10085 places CHEBI:15379 on its substrates side with coefficient 1.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/10085 rh:substrates http://rdf.rhea-db.org/10084_L -> http://rdf.rhea-db.org/10084_L rh:contains1 http://rdf.rhea-db.org/Participant_10084_compound_1198 -> http://rdf.rhea-db.org/Participant_10084_compound_1198 rh:compound http://rdf.rhea-db.org/Compound_1198 -> http://rdf.rhea-db.org/Compound_1198 rh:chebi http://purl.obolibrary.org/obo/CHEBI_15379
3,4-dihydroxybenzoate
CHEBI:36241		consumes

Complete formal substrates side; coefficient 1.

3,4-dihydroxybenzoate + O2 => 3-carboxy-cis,cis-muconate + 2 H(+)
RHEA:10085
  • RHEA:10085

    Source assertion: RHEA:10085 places CHEBI:36241 on its substrates side with coefficient 1.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/10085 rh:substrates http://rdf.rhea-db.org/10084_L -> http://rdf.rhea-db.org/10084_L rh:contains1 http://rdf.rhea-db.org/Participant_10084_compound_3099 -> http://rdf.rhea-db.org/Participant_10084_compound_3099 rh:compound http://rdf.rhea-db.org/Compound_3099 -> http://rdf.rhea-db.org/Compound_3099 rh:chebi http://purl.obolibrary.org/obo/CHEBI_36241
3,4-dihydroxybenzoate + O2 => 3-carboxy-cis,cis-muconate + 2 H(+)
RHEA:10085		produces

Complete formal products side; coefficient 2.

hydron
CHEBI:15378
  • RHEA:10085

    Source assertion: RHEA:10085 places CHEBI:15378 on its products side with coefficient 2.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/10085 rh:products http://rdf.rhea-db.org/10084_R -> http://rdf.rhea-db.org/10084_R rh:contains2 http://rdf.rhea-db.org/Participant_10084_compound_3249 -> http://rdf.rhea-db.org/Participant_10084_compound_3249 rh:compound http://rdf.rhea-db.org/Compound_3249 -> http://rdf.rhea-db.org/Compound_3249 rh:chebi http://purl.obolibrary.org/obo/CHEBI_15378
3,4-dihydroxybenzoate + O2 => 3-carboxy-cis,cis-muconate + 2 H(+)
RHEA:10085		produces

Complete formal products side; coefficient 1.

3-carboxy-cis,cis-muconate(3-)
CHEBI:57496
  • RHEA:10085

    Source assertion: RHEA:10085 places CHEBI:57496 on its products side with coefficient 1.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/10085 rh:products http://rdf.rhea-db.org/10084_R -> http://rdf.rhea-db.org/10084_R rh:contains1 http://rdf.rhea-db.org/Participant_10084_compound_4372 -> http://rdf.rhea-db.org/Participant_10084_compound_4372 rh:compound http://rdf.rhea-db.org/Compound_4372 -> http://rdf.rhea-db.org/Compound_4372 rh:chebi http://purl.obolibrary.org/obo/CHEBI_57496
GO:0019618has_part

One of the four complete native core reactions; the GO scope is the protocatechuate branch ending at 3-oxoadipate.

3-carboxymuconate cycloisomerization to the R lactone
MetaCyc:5.5.1.2-RXN
  • MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY

    Source assertion: The native reaction-list contains 5.5.1.2-RXN.

    Source location/ptools-xml/Pathway[@frameid='PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY']/reaction-list/Reaction[@frameid='5.5.1.2-RXN']
  • GO:0019618

    Source assertion: The biological-process term denotes protocatechuate degradation to beta-ketoadipate and cross-references MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY; its logical input and output restrictions use CHEBI:36241 and CHEBI:15775.

    Source locationGO:0019618: IAO:0000115; oio:hasDbXref; owl:equivalentClass/owl:intersectionOf list members with owl:onProperty RO:0004009, owl:someValuesFrom CHEBI:36241, and owl:onProperty RO:0004008, owl:someValuesFrom CHEBI:15775
hydron
CHEBI:15378		consumes

Complete formal substrates side; coefficient 1.

3-carboxymuconate cycloisomerization to the R lactone
MetaCyc:5.5.1.2-RXN
  • MetaCyc:5.5.1.2-RXN

    Source assertion: The native right side contains PROTON once. Native RIGHT-TO-LEFT direction selects this as substrate.

    Source location/ptools-xml/Reaction[@frameid='5.5.1.2-RXN']/right[Compound/@frameid='PROTON']/Compound; /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PROTON

    Source assertion: The native compound has CHEBI unification cross-reference 15378. Its full InChI, formula and charge specify the mapped chemical state.

    Source location/ptools-xml/Compound/dblink[dblink-db='CHEBI']; inchi; inchi-key; cml/molecule/@formalCharge; cml/molecule/formula/@concise
3-carboxy-cis,cis-muconate(3-)
CHEBI:57496		consumes

Complete formal substrates side; coefficient 1.

3-carboxymuconate cycloisomerization to the R lactone
MetaCyc:5.5.1.2-RXN
  • MetaCyc:5.5.1.2-RXN

    Source assertion: The native right side contains CPD-245 once. Native RIGHT-TO-LEFT direction selects this as substrate.

    Source location/ptools-xml/Reaction[@frameid='5.5.1.2-RXN']/right[Compound/@frameid='CPD-245']/Compound; /ptools-xml/Reaction/reaction-direction
  • MetaCyc:CPD-245

    Source assertion: The native compound has CHEBI unification cross-reference 57496. Its full InChI, formula and charge specify the mapped chemical state.

    Source location/ptools-xml/Compound/dblink[dblink-db='CHEBI']; inchi; inchi-key; cml/molecule/@formalCharge; cml/molecule/formula/@concise
3-carboxymuconate cycloisomerization to the R lactone
MetaCyc:5.5.1.2-RXN		produces

Complete formal products side; coefficient 1. The native R lactone is retained; stereo-unspecified RHEA:23658/CHEBI:57979 is not an exact identity.

(R)-2-(carboxylatomethyl)-5-oxo-2,5-dihydro-2-furoate
CHEBI:58771
  • MetaCyc:5.5.1.2-RXN

    Source assertion: The native left side contains CPD-7737 once. Native RIGHT-TO-LEFT direction selects this as product.

    Source location/ptools-xml/Reaction[@frameid='5.5.1.2-RXN']/left[Compound/@frameid='CPD-7737']/Compound; /ptools-xml/Reaction/reaction-direction
  • MetaCyc:CPD-7737

    Source assertion: The native compound has CHEBI unification cross-reference 58771. Its full InChI, formula and charge specify the R-configured lactone dianion.

    Source location/ptools-xml/Compound/dblink[dblink-db='CHEBI']; inchi; inchi-key; cml/molecule/@formalCharge; cml/molecule/formula/@concise
GO:0019618has_part

One of the four complete native core reactions; the GO scope is the protocatechuate branch ending at 3-oxoadipate.

(R)-2-(carboxymethyl)-5-oxo-2,5-dihydro-2-furoate + H(+) => (4,5-dihydro-5-oxofuran-2-yl)-acetate + CO2
RHEA:23349
  • MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY

    Source assertion: The native reaction-list contains 4-CARBOXYMUCONOLACTONE-DECARBOXYLASE-RXN.

    Source location/ptools-xml/Pathway[@frameid='PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY']/reaction-list/Reaction[@frameid='4-CARBOXYMUCONOLACTONE-DECARBOXYLASE-RXN']
  • MetaCyc:4-CARBOXYMUCONOLACTONE-DECARBOXYLASE-RXN

    Source assertion: The native reaction has a RHEA unification cross-reference to 23349; complete compounds, coefficients and selected pathway direction agree.

    Source location/ptools-xml/Reaction/dblink[dblink-db='RHEA']; left; right; reaction-direction
  • GO:0019618

    Source assertion: The biological-process term denotes protocatechuate degradation to beta-ketoadipate and cross-references MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY; its logical input and output restrictions use CHEBI:36241 and CHEBI:15775.

    Source locationGO:0019618: IAO:0000115; oio:hasDbXref; owl:equivalentClass/owl:intersectionOf list members with owl:onProperty RO:0004009, owl:someValuesFrom CHEBI:36241, and owl:onProperty RO:0004008, owl:someValuesFrom CHEBI:15775
hydron
CHEBI:15378		consumes

Complete formal substrates side; coefficient 1.

(R)-2-(carboxymethyl)-5-oxo-2,5-dihydro-2-furoate + H(+) => (4,5-dihydro-5-oxofuran-2-yl)-acetate + CO2
RHEA:23349
  • RHEA:23349

    Source assertion: RHEA:23349 places CHEBI:15378 on its substrates side with coefficient 1.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/23349 rh:substrates http://rdf.rhea-db.org/23348_L -> http://rdf.rhea-db.org/23348_L rh:contains1 http://rdf.rhea-db.org/Participant_23348_compound_3249 -> http://rdf.rhea-db.org/Participant_23348_compound_3249 rh:compound http://rdf.rhea-db.org/Compound_3249 -> http://rdf.rhea-db.org/Compound_3249 rh:chebi http://purl.obolibrary.org/obo/CHEBI_15378
(R)-2-(carboxylatomethyl)-5-oxo-2,5-dihydro-2-furoate
CHEBI:58771		consumes

Complete formal substrates side; coefficient 1.

(R)-2-(carboxymethyl)-5-oxo-2,5-dihydro-2-furoate + H(+) => (4,5-dihydro-5-oxofuran-2-yl)-acetate + CO2
RHEA:23349
  • RHEA:23349

    Source assertion: RHEA:23349 places CHEBI:58771 on its substrates side with coefficient 1.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/23349 rh:substrates http://rdf.rhea-db.org/23348_L -> http://rdf.rhea-db.org/23348_L rh:contains1 http://rdf.rhea-db.org/Participant_23348_compound_5490 -> http://rdf.rhea-db.org/Participant_23348_compound_5490 rh:compound http://rdf.rhea-db.org/Compound_5490 -> http://rdf.rhea-db.org/Compound_5490 rh:chebi http://purl.obolibrary.org/obo/CHEBI_58771
(R)-2-(carboxymethyl)-5-oxo-2,5-dihydro-2-furoate + H(+) => (4,5-dihydro-5-oxofuran-2-yl)-acetate + CO2
RHEA:23349		produces

Complete formal products side; coefficient 1.

carbon dioxide
CHEBI:16526
  • RHEA:23349

    Source assertion: RHEA:23349 places CHEBI:16526 on its products side with coefficient 1.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/23349 rh:products http://rdf.rhea-db.org/23348_R -> http://rdf.rhea-db.org/23348_R rh:contains1 http://rdf.rhea-db.org/Participant_23348_compound_4391 -> http://rdf.rhea-db.org/Participant_23348_compound_4391 rh:compound http://rdf.rhea-db.org/Compound_4391 -> http://rdf.rhea-db.org/Compound_4391 rh:chebi http://purl.obolibrary.org/obo/CHEBI_16526
(R)-2-(carboxymethyl)-5-oxo-2,5-dihydro-2-furoate + H(+) => (4,5-dihydro-5-oxofuran-2-yl)-acetate + CO2
RHEA:23349		produces

Complete formal products side; coefficient 1.

5-oxo-4,5-dihydro-2-furylacetate
CHEBI:58425
  • RHEA:23349

    Source assertion: RHEA:23349 places CHEBI:58425 on its products side with coefficient 1.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/23349 rh:products http://rdf.rhea-db.org/23348_R -> http://rdf.rhea-db.org/23348_R rh:contains1 http://rdf.rhea-db.org/Participant_23348_compound_2258 -> http://rdf.rhea-db.org/Participant_23348_compound_2258 rh:compound http://rdf.rhea-db.org/Compound_2258 -> http://rdf.rhea-db.org/Compound_2258 rh:chebi http://purl.obolibrary.org/obo/CHEBI_58425
GO:0019618has_part

One of the four complete native core reactions; the GO scope is the protocatechuate branch ending at 3-oxoadipate.

(4,5-dihydro-5-oxofuran-2-yl)-acetate + H2O => 3-oxoadipate + H(+)
RHEA:10185
  • MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY

    Source assertion: The native reaction-list contains 3-OXOADIPATE-ENOL-LACTONASE-RXN.

    Source location/ptools-xml/Pathway[@frameid='PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY']/reaction-list/Reaction[@frameid='3-OXOADIPATE-ENOL-LACTONASE-RXN']
  • MetaCyc:3-OXOADIPATE-ENOL-LACTONASE-RXN

    Source assertion: The native reaction has a RHEA unification cross-reference to 10185; complete compounds, coefficients and selected pathway direction agree.

    Source location/ptools-xml/Reaction/dblink[dblink-db='RHEA']; left; right; reaction-direction
  • GO:0019618

    Source assertion: The biological-process term denotes protocatechuate degradation to beta-ketoadipate and cross-references MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY; its logical input and output restrictions use CHEBI:36241 and CHEBI:15775.

    Source locationGO:0019618: IAO:0000115; oio:hasDbXref; owl:equivalentClass/owl:intersectionOf list members with owl:onProperty RO:0004009, owl:someValuesFrom CHEBI:36241, and owl:onProperty RO:0004008, owl:someValuesFrom CHEBI:15775
water
CHEBI:15377		consumes

Complete formal substrates side; coefficient 1.

(4,5-dihydro-5-oxofuran-2-yl)-acetate + H2O => 3-oxoadipate + H(+)
RHEA:10185
  • RHEA:10185

    Source assertion: RHEA:10185 places CHEBI:15377 on its substrates side with coefficient 1.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/10185 rh:substrates http://rdf.rhea-db.org/10184_L -> http://rdf.rhea-db.org/10184_L rh:contains1 http://rdf.rhea-db.org/Participant_10184_compound_1283 -> http://rdf.rhea-db.org/Participant_10184_compound_1283 rh:compound http://rdf.rhea-db.org/Compound_1283 -> http://rdf.rhea-db.org/Compound_1283 rh:chebi http://purl.obolibrary.org/obo/CHEBI_15377
5-oxo-4,5-dihydro-2-furylacetate
CHEBI:58425		consumes

Complete formal substrates side; coefficient 1.

(4,5-dihydro-5-oxofuran-2-yl)-acetate + H2O => 3-oxoadipate + H(+)
RHEA:10185
  • RHEA:10185

    Source assertion: RHEA:10185 places CHEBI:58425 on its substrates side with coefficient 1.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/10185 rh:substrates http://rdf.rhea-db.org/10184_L -> http://rdf.rhea-db.org/10184_L rh:contains1 http://rdf.rhea-db.org/Participant_10184_compound_2258 -> http://rdf.rhea-db.org/Participant_10184_compound_2258 rh:compound http://rdf.rhea-db.org/Compound_2258 -> http://rdf.rhea-db.org/Compound_2258 rh:chebi http://purl.obolibrary.org/obo/CHEBI_58425
(4,5-dihydro-5-oxofuran-2-yl)-acetate + H2O => 3-oxoadipate + H(+)
RHEA:10185		produces

Complete formal products side; coefficient 1.

hydron
CHEBI:15378
  • RHEA:10185

    Source assertion: RHEA:10185 places CHEBI:15378 on its products side with coefficient 1.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/10185 rh:products http://rdf.rhea-db.org/10184_R -> http://rdf.rhea-db.org/10184_R rh:contains1 http://rdf.rhea-db.org/Participant_10184_compound_3249 -> http://rdf.rhea-db.org/Participant_10184_compound_3249 rh:compound http://rdf.rhea-db.org/Compound_3249 -> http://rdf.rhea-db.org/Compound_3249 rh:chebi http://purl.obolibrary.org/obo/CHEBI_15378
(4,5-dihydro-5-oxofuran-2-yl)-acetate + H2O => 3-oxoadipate + H(+)
RHEA:10185		produces

Complete formal products side; coefficient 1.

3-oxoadipate(2-)
CHEBI:15775
  • RHEA:10185

    Source assertion: RHEA:10185 places CHEBI:15775 on its products side with coefficient 1.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/10185 rh:products http://rdf.rhea-db.org/10184_R -> http://rdf.rhea-db.org/10184_R rh:contains1 http://rdf.rhea-db.org/Participant_10184_compound_1219 -> http://rdf.rhea-db.org/Participant_10184_compound_1219 rh:compound http://rdf.rhea-db.org/Compound_1219 -> http://rdf.rhea-db.org/Compound_1219 rh:chebi http://purl.obolibrary.org/obo/CHEBI_15775
3,4-dihydroxybenzoate + O2 => 3-carboxy-cis,cis-muconate + 2 H(+)
RHEA:10085		provides_input_for

The complete shared intermediate is CHEBI:57496. This material connection preserves the native reaction ordering.

3-carboxymuconate cycloisomerization to the R lactone
MetaCyc:5.5.1.2-RXN
  • MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY

    Source assertion: The native ordering names PROTOCATECHUATE-34-DIOXYGENASE-RXN as a predecessor of 5.5.1.2-RXN.

    Source location/ptools-xml/Pathway/reaction-ordering[Reaction/@frameid='5.5.1.2-RXN']/predecessor-reactions/Reaction[@frameid='PROTOCATECHUATE-34-DIOXYGENASE-RXN']
  • MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY

    Source assertion: The selected layouts join both reactions through CPD-245.

    Source location/ptools-xml/Pathway[@frameid='PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY']/reaction-layout[Reaction/@frameid='PROTOCATECHUATE-34-DIOXYGENASE-RXN']; /ptools-xml/Pathway[@frameid='PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY']/reaction-layout[Reaction/@frameid='5.5.1.2-RXN']
3-carboxymuconate cycloisomerization to the R lactone
MetaCyc:5.5.1.2-RXN		provides_input_for

The complete shared intermediate is CHEBI:58771. This material connection preserves the native reaction ordering.

(R)-2-(carboxymethyl)-5-oxo-2,5-dihydro-2-furoate + H(+) => (4,5-dihydro-5-oxofuran-2-yl)-acetate + CO2
RHEA:23349
  • MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY

    Source assertion: The native ordering names 5.5.1.2-RXN as a predecessor of 4-CARBOXYMUCONOLACTONE-DECARBOXYLASE-RXN.

    Source location/ptools-xml/Pathway/reaction-ordering[Reaction/@frameid='4-CARBOXYMUCONOLACTONE-DECARBOXYLASE-RXN']/predecessor-reactions/Reaction[@frameid='5.5.1.2-RXN']
  • MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY

    Source assertion: The selected layouts join both reactions through CPD-7737.

    Source location/ptools-xml/Pathway[@frameid='PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY']/reaction-layout[Reaction/@frameid='5.5.1.2-RXN']; /ptools-xml/Pathway[@frameid='PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY']/reaction-layout[Reaction/@frameid='4-CARBOXYMUCONOLACTONE-DECARBOXYLASE-RXN']
(R)-2-(carboxymethyl)-5-oxo-2,5-dihydro-2-furoate + H(+) => (4,5-dihydro-5-oxofuran-2-yl)-acetate + CO2
RHEA:23349		provides_input_for

The complete shared intermediate is CHEBI:58425. This material connection preserves the native reaction ordering.

(4,5-dihydro-5-oxofuran-2-yl)-acetate + H2O => 3-oxoadipate + H(+)
RHEA:10185
  • MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY

    Source assertion: The native ordering names 4-CARBOXYMUCONOLACTONE-DECARBOXYLASE-RXN as a predecessor of 3-OXOADIPATE-ENOL-LACTONASE-RXN.

    Source location/ptools-xml/Pathway/reaction-ordering[Reaction/@frameid='3-OXOADIPATE-ENOL-LACTONASE-RXN']/predecessor-reactions/Reaction[@frameid='4-CARBOXYMUCONOLACTONE-DECARBOXYLASE-RXN']
  • MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY

    Source assertion: The selected layouts join both reactions through 3-OXOADIPATE-ENOL-LACTONE.

    Source location/ptools-xml/Pathway[@frameid='PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY']/reaction-layout[Reaction/@frameid='4-CARBOXYMUCONOLACTONE-DECARBOXYLASE-RXN']; /ptools-xml/Pathway[@frameid='PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY']/reaction-layout[Reaction/@frameid='3-OXOADIPATE-ENOL-LACTONASE-RXN']
protocatechuate 3,4-dioxygenase
MetaCyc:CPLX-2721		catalyzes

Native Pseudomonas putida activity annotation. Its complex comment distinguishes the historical four-alpha/four-beta preparation from the ATCC23975 twelve-alpha/twelve-beta enzyme; native subunit frames are not exact cross-strain sequence assignments.

3,4-dihydroxybenzoate + O2 => 3-carboxy-cis,cis-muconate + 2 H(+)
RHEA:10085
  • MetaCyc:ENZRXN-3343

    Source assertion: ENZRXN-3343 links CPLX-2721 to PROTOCATECHUATE-34-DIOXYGENASE-RXN; its EV-EXP-IDA-PURIFIED-PROTEIN evidence cites PMID:6273403. This preserves the native activity annotation, not a newly read full-paper claim.

    Source locationEnzymatic-Reaction[@frameid="ENZRXN-3343"]/enzyme; /reaction; /evidence
  • MetaCyc:PROTOCATECHUATE-34-DIOXYGENASE-RXN

    Source assertion: The native RHEA cross-reference is RHEA:10085; complete sides, chemical structures, coefficients and the selected pathway direction agree.

    Source location/ptools-xml/Reaction/dblink[dblink-db="RHEA"]; left; right; reaction-direction
3-carboxymuconate cycloisomerase
MetaCyc:CPLX-2762		catalyzes

Historical Pseudomonas putida PcaB enzyme; do not substitute catechol-branch muconate cycloisomerase.

3-carboxymuconate cycloisomerization to the R lactone
MetaCyc:5.5.1.2-RXN
  • MetaCyc:ENZRXN-3366

    Source assertion: ENZRXN-3366 links CPLX-2762 to 5.5.1.2-RXN; its EV-EXP-IDA-PURIFIED-PROTEIN evidence cites PMID:4199895. This preserves the native activity annotation, not a newly read full-paper claim.

    Source locationEnzymatic-Reaction[@frameid="ENZRXN-3366"]/enzyme; /reaction; /evidence
4-carboxymuconolactone decarboxylase
MetaCyc:CPLX-2745		catalyzes

Historical Pseudomonas putida decarboxylase accelerates the otherwise spontaneous decarboxylation; distinct from muconolactone isomerase.

(R)-2-(carboxymethyl)-5-oxo-2,5-dihydro-2-furoate + H(+) => (4,5-dihydro-5-oxofuran-2-yl)-acetate + CO2
RHEA:23349
  • MetaCyc:ENZRXN-3367

    Source assertion: ENZRXN-3367 links CPLX-2745 to 4-CARBOXYMUCONOLACTONE-DECARBOXYLASE-RXN; its EV-EXP-IDA-PURIFIED-PROTEIN evidence cites PMID:4199896. This preserves the native activity annotation, not a newly read full-paper claim.

    Source locationEnzymatic-Reaction[@frameid="ENZRXN-3367"]/enzyme; /reaction; /evidence
  • MetaCyc:4-CARBOXYMUCONOLACTONE-DECARBOXYLASE-RXN

    Source assertion: The native RHEA cross-reference is RHEA:23349; complete sides, chemical structures, coefficients and the selected pathway direction agree.

    Source location/ptools-xml/Reaction/dblink[dblink-db="RHEA"]; left; right; reaction-direction
β-ketoadipate enol-lactone hydrolase
MetaCyc:CPLX-2761		catalyzes

Historical Pseudomonas putida hydrolase model shared with catechol cleavage; no exact sequence join to KT2440 Q88N36 is established.

(4,5-dihydro-5-oxofuran-2-yl)-acetate + H2O => 3-oxoadipate + H(+)
RHEA:10185
  • MetaCyc:ENZRXN-3368

    Source assertion: ENZRXN-3368 links CPLX-2761 to 3-OXOADIPATE-ENOL-LACTONASE-RXN; its EV-EXP-IDA-PURIFIED-PROTEIN evidence cites PMID:7391022. This preserves the native activity annotation, not a newly read full-paper claim.

    Source locationEnzymatic-Reaction[@frameid="ENZRXN-3368"]/enzyme; /reaction; /evidence
  • MetaCyc:3-OXOADIPATE-ENOL-LACTONASE-RXN

    Source assertion: The native RHEA cross-reference is RHEA:10185; complete sides, chemical structures, coefficients and the selected pathway direction agree.

    Source location/ptools-xml/Reaction/dblink[dblink-db="RHEA"]; left; right; reaction-direction
protocatechuate 3,4-dioxygenase
MetaCyc:CPLX-2721		has_part

4 beta subunits in the source assembly. The complex comment attributes this model to the historical purified preparation and distinguishes the ATCC23975 twelve-alpha/twelve-beta enzyme. Native subunit cross-references do not establish exact sequence equivalence.

protocatechuate 3,4-dioxygenase β subunit
MetaCyc:MONOMER-3185
  • MetaCyc:CPLX-2721

    Source assertion: Protein CPLX-2721 contains MONOMER-3185 with coefficient 4. This is the native source-scoped assembly; no cross-strain sequence identity is inferred.

    Source locationProtein[@frameid="CPLX-2721"]/component[Protein/@frameid="MONOMER-3185"]; coefficient
protocatechuate 3,4-dioxygenase
MetaCyc:CPLX-2721		has_part

4 alpha subunits in the source assembly. The complex comment attributes this model to the historical purified preparation and distinguishes the ATCC23975 twelve-alpha/twelve-beta enzyme. Native subunit cross-references do not establish exact sequence equivalence.

protocatechuate 3,4-dioxygenase α subunit
MetaCyc:MONOMER-3186
  • MetaCyc:CPLX-2721

    Source assertion: Protein CPLX-2721 contains MONOMER-3186 with coefficient 4. This is the native source-scoped assembly; no cross-strain sequence identity is inferred.

    Source locationProtein[@frameid="CPLX-2721"]/component[Protein/@frameid="MONOMER-3186"]; coefficient
3-carboxymuconate cycloisomerase
MetaCyc:CPLX-2762		has_part

4 PcaB subunits in the source assembly. Native historical Pseudomonas putida assembly model.

subunit of 3-carboxymuconate cycloisomerase
MetaCyc:MONOMER-3222
  • MetaCyc:CPLX-2762

    Source assertion: Protein CPLX-2762 contains MONOMER-3222 with coefficient 4. This is the native source-scoped assembly; no cross-strain sequence identity is inferred.

    Source locationProtein[@frameid="CPLX-2762"]/component[Protein/@frameid="MONOMER-3222"]; coefficient
4-carboxymuconolactone decarboxylase
MetaCyc:CPLX-2745		has_part

Six subunits in the native historical Pseudomonas putida assembly annotation. The source distinguishes this hexamer from the catechol-branch muconolactone isomerase decamer.

subunit of 4-carboxymuconolactone decarboxylase
MetaCyc:MONOMER-3206
  • MetaCyc:CPLX-2745

    Source assertion: Protein CPLX-2745 contains MONOMER-3206 with coefficient 6. This is the native source-scoped assembly; no cross-strain sequence identity is inferred.

    Source locationProtein[@frameid="CPLX-2745"]/component[Protein/@frameid="MONOMER-3206"]; coefficient
β-ketoadipate enol-lactone hydrolase
MetaCyc:CPLX-2761		has_part

Native historical three-copy assembly annotation. It is not a modern structure determination or evidence for three KT2440 Q88N36 proteins; historical mass and sequence limitations are retained in the research ledger.

subunit of 3-oxoadipate enol-lactone hydrolase
MetaCyc:MONOMER-3221
  • MetaCyc:CPLX-2761

    Source assertion: Protein CPLX-2761 contains MONOMER-3221 with coefficient 3. This is the native source-scoped assembly; no cross-strain sequence identity is inferred.

    Source locationProtein[@frameid="CPLX-2761"]/component[Protein/@frameid="MONOMER-3221"]; coefficient
protocatechuate 3,4-dioxygenase
MetaCyc:CPLX-2721		has_cofactor

The native activity identifies ferric iron as a bound cofactor. The complex comment distinguishes preparations with different subunit counts; no universal iron occupancy is asserted. Dioxygen remains a reaction substrate.

iron(3+)
CHEBI:29034
  • MetaCyc:ENZRXN-3343

    Source assertion: ENZRXN-3343 declares FE+3 as cofactor and cites PMID:6273403; its enzyme is CPLX-2721. Ferric iron is not consumed in the net intradiol-cleavage equation.

    Source locationEnzymatic-Reaction[@frameid="ENZRXN-3343"]/cofactor; /enzyme
3,4-dihydroxybenzoate
CHEBI:36241		regulates

Protocatechuate induces enzyme expression in the source Pseudomonas putida pathway context; this does not assert direct catalytic activation or ligand binding to this purified assembly.

protocatechuate 3,4-dioxygenase
MetaCyc:CPLX-2721
  • MetaCyc:CPLX-2721

    Source assertion: The CPLX-2721 comment states that the enzyme is induced by protocatechuate. This preserves expression-level induction in the curated Pseudomonas putida context, not direct enzyme activation.

    Source locationProtein[@frameid="CPLX-2721"]/comment: induction statement
3-oxoadipate(2-)
CHEBI:15775		regulates

3-oxoadipate induces enzyme expression in the source Pseudomonas putida pathway context; this does not assert direct catalytic activation or ligand binding to this purified assembly.

3-carboxymuconate cycloisomerase
MetaCyc:CPLX-2762
  • MetaCyc:CPLX-2762

    Source assertion: The CPLX-2762 comment states that the enzyme is induced by 3-oxoadipate. This preserves expression-level induction in the curated Pseudomonas putida context, not direct enzyme activation.

    Source locationProtein[@frameid="CPLX-2762"]/comment: induction statement
3-oxoadipate(2-)
CHEBI:15775		regulates

3-oxoadipate induces enzyme expression in the source Pseudomonas putida pathway context; this does not assert direct catalytic activation or ligand binding to this purified assembly.

4-carboxymuconolactone decarboxylase
MetaCyc:CPLX-2745
  • MetaCyc:CPLX-2745

    Source assertion: The CPLX-2745 comment states that the enzyme is induced by 3-oxoadipate. This preserves expression-level induction in the curated Pseudomonas putida context, not direct enzyme activation.

    Source locationProtein[@frameid="CPLX-2745"]/comment: induction statement
3-oxoadipate(2-)
CHEBI:15775		regulates

3-oxoadipate induces enzyme expression in the source Pseudomonas putida pathway context; this does not assert direct catalytic activation or ligand binding to this purified assembly.

β-ketoadipate enol-lactone hydrolase
MetaCyc:CPLX-2761
  • MetaCyc:CPLX-2761

    Source assertion: The CPLX-2761 comment states that the enzyme is induced by 3-oxoadipate. This preserves expression-level induction in the curated Pseudomonas putida context, not direct enzyme activation.

    Source locationProtein[@frameid="CPLX-2761"]/comment: induction statement
(4,5-dihydro-5-oxofuran-2-yl)-acetate + H2O => 3-oxoadipate + H(+)
RHEA:10185		provides_input_for

The final core product, 3-oxoadipate, enters the separate downstream degradation module. Its CoA-transfer and thiolysis reactions are outside this record boundary.

3-oxoadipate degradation
MetaCyc:PWY-2361
  • MetaCyc:PROTOCATECHUATE-ORTHO-CLEAVAGE-PWY

    Source assertion: The native pathway-link connects 3-KETO-ADIPATE with downstream PWY-2361.

    Source location/ptools-xml/Pathway/pathway-link[Compound/@frameid="3-KETO-ADIPATE"]/link-target/Pathway
  • MetaCyc:PWY-2361

    Source assertion: The downstream pathway includes 3-OXOADIPATE-COA-TRANSFERASE-RXN followed by RXN-3641; its first layout consumes 3-KETO-ADIPATE.

    Source location/ptools-xml/Pathway/reaction-list; reaction-ordering; reaction-layout

References

Curation history