catechol degradation to β-ketoadipate

MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWY

The native four-reaction ortho-cleavage module converts catechol to 3-oxoadipate through cis,cis-muconate, (S)-muconolactone and 3-oxoadipate enol-lactone. This boundary ends before CoA transfer and thiolysis in the downstream 3-oxoadipate degradation module. The selected Pseudomonas putida scope follows the native species annotation; it does not assert occurrence in every strain. Native catalyst frames preserve historical assembly annotations; deleted CatA and discordant PcaD sequence cross-references are not propagated as modern protein identities.

Pathway type
aromatic compound catabolism
Organism scope

Read the source YAML

Pathway network

25 nodes · 32 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: catechol degradation to β-ketoadipate 25 nodes · 32 asserted directed edges. Every arrow links to its evidence table row; nodes link to their component details. Isolated declared components are retained. MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWY — has_part → RHEA:23853; Native core membership; the exact directional Rhea equation was checked against the native structures, charge, coefficients and selected pathway traversal.; Evidence: MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWY, MetaCyc:CATECHOL-12-DIOXYGENASE-RXNhas part CHEBI:18135 — consumes → RHEA:23853; Complete formal substrates side; coefficient 1.; Evidence: RHEA:23853consumes CHEBI:15379 — consumes → RHEA:23853; Complete formal substrates side; coefficient 1.; Evidence: RHEA:23853consumes RHEA:23853 — produces → CHEBI:32379; Complete formal products side; coefficient 1.; Evidence: RHEA:23853produces RHEA:23853 — produces → CHEBI:15378; Complete formal products side; coefficient 2.; Evidence: RHEA:23853produces MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWY — has_part → RHEA:30033; Native core membership; the exact directional Rhea equation was checked against the native structures, charge, coefficients and selected pathway traversal.; Evidence: MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWY, MetaCyc:MUCONATE-CYCLOISOMERASE-RXNhas part CHEBI:32379 — consumes → RHEA:30033; Complete formal substrates side; coefficient 1.; Evidence: RHEA:30033consumes CHEBI:15378 — consumes → RHEA:30033; Complete formal substrates side; coefficient 1.; Evidence: RHEA:30033consumes RHEA:30033 — produces → CHEBI:58736; Complete formal products side; coefficient 1.; Evidence: RHEA:30033produces MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWY — has_part → RHEA:12349; Native core membership; the exact directional Rhea equation was checked against the native structures, charge, coefficients and selected pathway traversal.; Evidence: MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWY, MetaCyc:MUCONOLACTONE-DELTA-ISOMERASE-RXNhas part CHEBI:58736 — consumes → RHEA:12349; Complete formal substrates side; coefficient 1.; Evidence: RHEA:12349consumes RHEA:12349 — produces → CHEBI:58425; Complete formal products side; coefficient 1.; Evidence: RHEA:12349produces MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWY — has_part → RHEA:10185; Native core membership; the exact directional Rhea equation was checked against the native structures, charge, coefficients and selected pathway traversal.; Evidence: MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWY, MetaCyc:3-OXOADIPATE-ENOL-LACTONASE-RXNhas part CHEBI:58425 — consumes → RHEA:10185; Complete formal substrates side; coefficient 1.; Evidence: RHEA:10185consumes CHEBI:15377 — consumes → RHEA:10185; Complete formal substrates side; coefficient 1.; Evidence: RHEA:10185consumes RHEA:10185 — produces → CHEBI:15775; Complete formal products side; coefficient 1.; Evidence: RHEA:10185produces RHEA:10185 — produces → CHEBI:15378; Complete formal products side; coefficient 1.; Evidence: RHEA:10185produces RHEA:23853 — provides_input_for → RHEA:30033; The common chemical product feeds the next native core transformation; this is material transfer, not a regulatory relation.; Evidence: MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWYprovides input for RHEA:30033 — provides_input_for → RHEA:12349; The common chemical product feeds the next native core transformation; this is material transfer, not a regulatory relation.; Evidence: MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWYprovides input for RHEA:12349 — provides_input_for → RHEA:10185; The common chemical product feeds the next native core transformation; this is material transfer, not a regulatory relation.; Evidence: MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWYprovides input for MetaCyc:CPLX-2842 — catalyzes → RHEA:23853; The native P. putida enzyme assignment is retained at its native frame scope. Database-curated assay attribution does not establish identity with a particular modern strain or sequence.; Evidence: MetaCyc:ENZRXN-3585, MetaCyc:CATECHOL-12-DIOXYGENASE-RXNcatalyzes MetaCyc:CPLX-2842 — has_part → MetaCyc:MONOMER-3422; Native assembly annotation, 2 subunits. This is a database-scoped assembly assertion, not proof of exact contemporary sequence or strain identity.; Evidence: MetaCyc:CPLX-2842has part MetaCyc:CPLX-2843 — catalyzes → RHEA:30033; The native P. putida enzyme assignment is retained at its native frame scope. Database-curated assay attribution does not establish identity with a particular modern strain or sequence.; Evidence: MetaCyc:ENZRXN-3586, MetaCyc:MUCONATE-CYCLOISOMERASE-RXNcatalyzes MetaCyc:CPLX-2843 — has_part → MetaCyc:MONOMER-3423; Native assembly annotation, 8 subunits. This is a database-scoped assembly assertion, not proof of exact contemporary sequence or strain identity.; Evidence: MetaCyc:CPLX-2843has part MetaCyc:CPLX-2844 — catalyzes → RHEA:12349; The native P. putida enzyme assignment is retained at its native frame scope. Database-curated assay attribution does not establish identity with a particular modern strain or sequence.; Evidence: MetaCyc:ENZRXN-3587, MetaCyc:MUCONOLACTONE-DELTA-ISOMERASE-RXNcatalyzes MetaCyc:CPLX-2844 — has_part → MetaCyc:MONOMER-3424; Native assembly annotation, 10 subunits. This is a database-scoped assembly assertion, not proof of exact contemporary sequence or strain identity.; Evidence: MetaCyc:CPLX-2844has part MetaCyc:CPLX-2761 — catalyzes → RHEA:10185; The native P. putida enzyme assignment is retained at its native frame scope. Database-curated assay attribution does not establish identity with a particular modern strain or sequence.; Evidence: MetaCyc:ENZRXN-3368, MetaCyc:3-OXOADIPATE-ENOL-LACTONASE-RXNcatalyzes MetaCyc:CPLX-2761 — has_part → MetaCyc:MONOMER-3221; Historical inferred trimer from the P. putida PRS2260 preparation (derivative of PRS2178): apparent native mass 30–33 kDa and apparent subunits 11 kDa after 8 M urea. This is the 1980 interpretation retained by the native frame, not a modern structure determination or evidence for three 263-residue Q88N36 proteins. Original figure pixels and complete miniprint were unavailable.; Evidence: MetaCyc:CPLX-2761, PMID:7391022has part MetaCyc:CPLX-2843 — has_cofactor → CHEBI:29035; Native muconate cycloisomerase annotation identifies a manganese ion near the active site in each subunit. This is a bound catalytic cofactor, not a consumed pathway substrate.; Evidence: MetaCyc:ENZRXN-3586, MetaCyc:CPLX-2843has cofactor 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:CATECHOL-ORTHO-CLEAVAGE-PWY, MetaCyc:PWY-2361provides input for CHEBI:15775 — regulates → MetaCyc:CPLX-2761; Native source reports induction of the P. putida hydrolase by 3-oxoadipate. This expression-level response does not assert direct ligand binding, catalytic activation, an identified regulatory gene or equivalence with a modern KT2440 sequence.; Evidence: MetaCyc:CPLX-2761regulates MetaCyc:CPLX-2842 — has_cofactor → CHEBI:29034; subject molecular state: Natural Pseudomonas putida (synonym P. arvilla) C-1 catechol 1,2-dioxygenase holoenzyme modeled in PDB 2AZQ. The native frame discusses C-1 isozyme variants; no exact sequence equivalence with MONOMER-3422 or deleted Q9AEQ0 is asserted.; Evidence DOI:10.2210/pdb2azq/pdb: The natural source is Pseudomonas putida, taxonomy 303, strain C-1; biological assembly 1 is dimeric and the model includes FE. (_entity_src_nat; _pdbx_struct_assembly[id=1]; _atom_site[label_comp_id=FE]); Evidence MetaCyc:CPLX-2842: The complex comment explicitly discusses the three C-1 catechol 1,2-dioxygenase isozyme assemblies alpha-alpha, alpha-beta and beta-beta. (/ptools-xml/Protein/comment, paragraph beginning "Some strains possess"); The C-1 structural model assigns a bound Fe(III) cofactor coordinated by two tyrosine and two histidine residues. The assignment applies to this modeled holoenzyme; it is not a new redox assay or a sequence-equivalence claim for the native generic component. Iron is not consumed by the core reaction.; Evidence: DOI:10.2210/pdb2azq/pdbhas cofactor catechol; CHEBI:18135; Declared type: small_molecule small molecule catechol O2; CHEBI:15379; Declared type: small_molecule small molecule O2 cis,cis-muconate; CHEBI:32379; Declared type: small_molecule small molecule cis,cis-muconate H(+); CHEBI:15378; Declared type: small_molecule small molecule H(+) (S)-muconolactone; CHEBI:58736; Declared type: small_molecule small molecule (S)-muconolactone (4,5-dihydro-5-oxofuran-2-yl)-acetate; CHEBI:58425; Declared type: small_molecule small molecule (4,5-dihydro-5-oxofuran-2- yl)-acetate H2O; CHEBI:15377; Declared type: small_molecule small molecule H2O 3-oxoadipate; CHEBI:15775; Declared type: small_molecule small molecule 3-oxoadipate catechol 1,2-dioxygenase; MetaCyc:CPLX-2842; Declared type: complex complex catechol 1,2-dioxygenase subunit of catechol 1,2-dioxygenase; MetaCyc:MONOMER-3422; Declared type: protein protein subunit of catechol 1,2-dioxygenase muconate cycloisomerase; MetaCyc:CPLX-2843; Declared type: complex complex muconate cycloisomerase muconate lactonizing enzyme subunit; MetaCyc:MONOMER-3423; Declared type: protein protein muconate lactonizing enzyme subunit muconolactone isomerase; MetaCyc:CPLX-2844; Declared type: complex complex muconolactone isomerase muconolactone isomerase subunit; MetaCyc:MONOMER-3424; Declared type: protein protein muconolactone isomerase subunit 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 manganese(2+); CHEBI:29035; Declared type: cofactor cofactor manganese(2+) iron(3+); CHEBI:29034; Declared type: cofactor cofactor iron(3+) catechol + O2 => cis,cis-muconate + 2 H(+); RHEA:23853; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity catechol + O2 => cis,cis- muconate + 2 H(+) cis,cis-muconate + H(+) => (S)-muconolactone; RHEA:30033; Declared type: molecular_activity; Source reaction direction: right_to_left molecular activity cis,cis-muconate + H(+) => (S)-muconolactone (S)-muconolactone => (4,5-dihydro-5-oxofuran-2-yl)-acetate; RHEA:12349; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity (S)-muconolactone => (4,5- dihydro-5-oxofuran-2-yl)- acetate (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 catechol degradation to β-ketoadipate; MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWY; Declared type: pathway pathway catechol degradation to β-ketoadipate catechol 1,2-dioxygenase; MetaCyc:CPLX-2842; Declared type: complex; molecular state: Natural Pseudomonas putida (synonym P. arvilla) C-1 catechol 1,2-dioxygenase holoenzyme modeled in PDB 2AZQ. The native frame discusses C-1 isozyme variants; no exact sequence equivalence with MONOMER-3422 or deleted Q9AEQ0 is asserted.; Evidence DOI:10.2210/pdb2azq/pdb: The natural source is Pseudomonas putida, taxonomy 303, strain C-1; biological assembly 1 is dimeric and the model includes FE. (_entity_src_nat; _pdbx_struct_assembly[id=1]; _atom_site[label_comp_id=FE]); Evidence MetaCyc:CPLX-2842: The complex comment explicitly discusses the three C-1 catechol 1,2-dioxygenase isozyme assemblies alpha-alpha, alpha-beta and beta-beta. (/ptools-xml/Protein/comment, paragraph beginning "Some strains possess") molecular state catechol 1,2-dioxygenase [molecular state: Natural Pseudomonas putida (synonym P. arvilla) C-1 catechol 1,2-dioxygenase holoenzyme modeled in…]

Components and activities

Declared biological components and source reaction directions
NodeKind or roleSource direction
Pseudomonas putida
NCBITaxon:303		taxon
catechol
CHEBI:18135		small molecule
O2
CHEBI:15379		small molecule
cis,cis-muconate
CHEBI:32379		small molecule
H(+)
CHEBI:15378		small molecule
(S)-muconolactone
CHEBI:58736		small molecule
(4,5-dihydro-5-oxofuran-2-yl)-acetate
CHEBI:58425		small molecule
H2O
CHEBI:15377		small molecule
3-oxoadipate
CHEBI:15775		small molecule
catechol 1,2-dioxygenase
MetaCyc:CPLX-2842		complex
subunit of catechol 1,2-dioxygenase
MetaCyc:MONOMER-3422		protein
muconate cycloisomerase
MetaCyc:CPLX-2843		complex
muconate lactonizing enzyme subunit
MetaCyc:MONOMER-3423		protein
muconolactone isomerase
MetaCyc:CPLX-2844		complex
muconolactone isomerase subunit
MetaCyc:MONOMER-3424		protein
β-ketoadipate enol-lactone hydrolase
MetaCyc:CPLX-2761		complex
subunit of 3-oxoadipate enol-lactone hydrolase
MetaCyc:MONOMER-3221		protein
manganese(2+)
CHEBI:29035		cofactor
iron(3+)
CHEBI:29034		cofactor
catechol + O2 => cis,cis-muconate + 2 H(+)
RHEA:23853		molecular activityleft to right
cis,cis-muconate + H(+) => (S)-muconolactone
RHEA:30033		molecular activityright to left
(S)-muconolactone => (4,5-dihydro-5-oxofuran-2-yl)-acetate
RHEA:12349		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
MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWYhas_part

Native core membership; the exact directional Rhea equation was checked against the native structures, charge, coefficients and selected pathway traversal.

catechol + O2 => cis,cis-muconate + 2 H(+)
RHEA:23853
  • MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWY

    Source assertion: The native reaction-list contains CATECHOL-12-DIOXYGENASE-RXN.

    Source location/ptools-xml/Pathway/reaction-list/Reaction[@frameid="CATECHOL-12-DIOXYGENASE-RXN"]
  • MetaCyc:CATECHOL-12-DIOXYGENASE-RXN

    Source assertion: The native reaction has a RHEA unification cross-reference to 23853; its complete sides and direction specify the selected reaction.

    Source location/ptools-xml/Reaction/dblink[dblink-db="RHEA"]; left; right; reaction-direction
catechol
CHEBI:18135		consumes

Complete formal substrates side; coefficient 1.

catechol + O2 => cis,cis-muconate + 2 H(+)
RHEA:23853
  • RHEA:23853

    Source assertion: RHEA:23853 places CHEBI:18135 on its substrates side with coefficient 1.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/23853/rh:substrates -> http://rdf.rhea-db.org/23852_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_23852_compound_2779/rh:compound -> http://rdf.rhea-db.org/Compound_2779/rh:chebi
O2
CHEBI:15379		consumes

Complete formal substrates side; coefficient 1.

catechol + O2 => cis,cis-muconate + 2 H(+)
RHEA:23853
  • RHEA:23853

    Source assertion: RHEA:23853 places CHEBI:15379 on its substrates side with coefficient 1.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/23853/rh:substrates -> http://rdf.rhea-db.org/23852_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_23852_compound_1198/rh:compound -> http://rdf.rhea-db.org/Compound_1198/rh:chebi
catechol + O2 => cis,cis-muconate + 2 H(+)
RHEA:23853		produces

Complete formal products side; coefficient 1.

cis,cis-muconate
CHEBI:32379
  • RHEA:23853

    Source assertion: RHEA:23853 places CHEBI:32379 on its products side with coefficient 1.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/23853/rh:products -> http://rdf.rhea-db.org/23852_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_23852_compound_3685/rh:compound -> http://rdf.rhea-db.org/Compound_3685/rh:chebi
catechol + O2 => cis,cis-muconate + 2 H(+)
RHEA:23853		produces

Complete formal products side; coefficient 2.

H(+)
CHEBI:15378
  • RHEA:23853

    Source assertion: RHEA:23853 places CHEBI:15378 on its products side with coefficient 2.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/23853/rh:products -> http://rdf.rhea-db.org/23852_R/rh:contains2 -> http://rdf.rhea-db.org/Participant_23852_compound_3249/rh:compound -> http://rdf.rhea-db.org/Compound_3249/rh:chebi
MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWYhas_part

Native core membership; the exact directional Rhea equation was checked against the native structures, charge, coefficients and selected pathway traversal.

cis,cis-muconate + H(+) => (S)-muconolactone
RHEA:30033
  • MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWY

    Source assertion: The native reaction-list contains MUCONATE-CYCLOISOMERASE-RXN.

    Source location/ptools-xml/Pathway/reaction-list/Reaction[@frameid="MUCONATE-CYCLOISOMERASE-RXN"]
  • MetaCyc:MUCONATE-CYCLOISOMERASE-RXN

    Source assertion: The native reaction has a RHEA unification cross-reference to 30033; its complete sides and direction specify the selected reaction.

    Source location/ptools-xml/Reaction/dblink[dblink-db="RHEA"]; left; right; reaction-direction
cis,cis-muconate
CHEBI:32379		consumes

Complete formal substrates side; coefficient 1.

cis,cis-muconate + H(+) => (S)-muconolactone
RHEA:30033
  • RHEA:30033

    Source assertion: RHEA:30033 places CHEBI:32379 on its substrates side with coefficient 1.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/30033/rh:substrates -> http://rdf.rhea-db.org/30031_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_30031_compound_3685/rh:compound -> http://rdf.rhea-db.org/Compound_3685/rh:chebi
H(+)
CHEBI:15378		consumes

Complete formal substrates side; coefficient 1.

cis,cis-muconate + H(+) => (S)-muconolactone
RHEA:30033
  • RHEA:30033

    Source assertion: RHEA:30033 places CHEBI:15378 on its substrates side with coefficient 1.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/30033/rh:substrates -> http://rdf.rhea-db.org/30031_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_30031_compound_3249/rh:compound -> http://rdf.rhea-db.org/Compound_3249/rh:chebi
cis,cis-muconate + H(+) => (S)-muconolactone
RHEA:30033		produces

Complete formal products side; coefficient 1.

(S)-muconolactone
CHEBI:58736
  • RHEA:30033

    Source assertion: RHEA:30033 places CHEBI:58736 on its products side with coefficient 1.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/30033/rh:products -> http://rdf.rhea-db.org/30031_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_30031_compound_5261/rh:compound -> http://rdf.rhea-db.org/Compound_5261/rh:chebi
MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWYhas_part

Native core membership; the exact directional Rhea equation was checked against the native structures, charge, coefficients and selected pathway traversal.

(S)-muconolactone => (4,5-dihydro-5-oxofuran-2-yl)-acetate
RHEA:12349
  • MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWY

    Source assertion: The native reaction-list contains MUCONOLACTONE-DELTA-ISOMERASE-RXN.

    Source location/ptools-xml/Pathway/reaction-list/Reaction[@frameid="MUCONOLACTONE-DELTA-ISOMERASE-RXN"]
  • MetaCyc:MUCONOLACTONE-DELTA-ISOMERASE-RXN

    Source assertion: The native reaction has a RHEA unification cross-reference to 12349; its complete sides and direction specify the selected reaction.

    Source location/ptools-xml/Reaction/dblink[dblink-db="RHEA"]; left; right; reaction-direction
(S)-muconolactone
CHEBI:58736		consumes

Complete formal substrates side; coefficient 1.

(S)-muconolactone => (4,5-dihydro-5-oxofuran-2-yl)-acetate
RHEA:12349
  • RHEA:12349

    Source assertion: RHEA:12349 places CHEBI:58736 on its substrates side with coefficient 1.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/12349/rh:substrates -> http://rdf.rhea-db.org/12348_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_12348_compound_5261/rh:compound -> http://rdf.rhea-db.org/Compound_5261/rh:chebi
(S)-muconolactone => (4,5-dihydro-5-oxofuran-2-yl)-acetate
RHEA:12349		produces

Complete formal products side; coefficient 1.

(4,5-dihydro-5-oxofuran-2-yl)-acetate
CHEBI:58425
  • RHEA:12349

    Source assertion: RHEA:12349 places CHEBI:58425 on its products side with coefficient 1.

    Source locationAggregate rdf:Description by rdf:about: http://rdf.rhea-db.org/12349/rh:products -> http://rdf.rhea-db.org/12348_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_12348_compound_2258/rh:compound -> http://rdf.rhea-db.org/Compound_2258/rh:chebi
MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWYhas_part

Native core membership; the exact directional Rhea equation was checked against the native structures, charge, coefficients and selected pathway traversal.

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

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

    Source location/ptools-xml/Pathway/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; its complete sides and direction specify the selected reaction.

    Source location/ptools-xml/Reaction/dblink[dblink-db="RHEA"]; left; right; reaction-direction
(4,5-dihydro-5-oxofuran-2-yl)-acetate
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/rh:contains1 -> http://rdf.rhea-db.org/Participant_10184_compound_2258/rh:compound -> http://rdf.rhea-db.org/Compound_2258/rh:chebi
H2O
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/rh:contains1 -> http://rdf.rhea-db.org/Participant_10184_compound_1283/rh:compound -> http://rdf.rhea-db.org/Compound_1283/rh:chebi
(4,5-dihydro-5-oxofuran-2-yl)-acetate + H2O => 3-oxoadipate + H(+)
RHEA:10185		produces

Complete formal products side; coefficient 1.

3-oxoadipate
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/rh:contains1 -> http://rdf.rhea-db.org/Participant_10184_compound_1219/rh:compound -> http://rdf.rhea-db.org/Compound_1219/rh:chebi
(4,5-dihydro-5-oxofuran-2-yl)-acetate + H2O => 3-oxoadipate + H(+)
RHEA:10185		produces

Complete formal products side; coefficient 1.

H(+)
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/rh:contains1 -> http://rdf.rhea-db.org/Participant_10184_compound_3249/rh:compound -> http://rdf.rhea-db.org/Compound_3249/rh:chebi
catechol + O2 => cis,cis-muconate + 2 H(+)
RHEA:23853		provides_input_for

The common chemical product feeds the next native core transformation; this is material transfer, not a regulatory relation.

cis,cis-muconate + H(+) => (S)-muconolactone
RHEA:30033
  • MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWY

    Source assertion: The native ordering lists CATECHOL-12-DIOXYGENASE-RXN as a predecessor of MUCONATE-CYCLOISOMERASE-RXN; the pathway layouts share the intermediate.

    Source location/ptools-xml/Pathway/reaction-ordering[Reaction/@frameid="MUCONATE-CYCLOISOMERASE-RXN"]/predecessor-reactions; reaction-layout
cis,cis-muconate + H(+) => (S)-muconolactone
RHEA:30033		provides_input_for

The common chemical product feeds the next native core transformation; this is material transfer, not a regulatory relation.

(S)-muconolactone => (4,5-dihydro-5-oxofuran-2-yl)-acetate
RHEA:12349
  • MetaCyc:CATECHOL-ORTHO-CLEAVAGE-PWY

    Source assertion: The native ordering lists MUCONATE-CYCLOISOMERASE-RXN as a predecessor of MUCONOLACTONE-DELTA-ISOMERASE-RXN; the pathway layouts share the intermediate.

    Source location/ptools-xml/Pathway/reaction-ordering[Reaction/@frameid="MUCONOLACTONE-DELTA-ISOMERASE-RXN"]/predecessor-reactions; reaction-layout
(S)-muconolactone => (4,5-dihydro-5-oxofuran-2-yl)-acetate
RHEA:12349		provides_input_for

The common chemical product feeds the next native core transformation; this is material transfer, not a regulatory relation.

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

    Source assertion: The native ordering lists MUCONOLACTONE-DELTA-ISOMERASE-RXN as a predecessor of 3-OXOADIPATE-ENOL-LACTONASE-RXN; the pathway layouts share the intermediate.

    Source location/ptools-xml/Pathway/reaction-ordering[Reaction/@frameid="3-OXOADIPATE-ENOL-LACTONASE-RXN"]/predecessor-reactions; reaction-layout
catechol 1,2-dioxygenase
MetaCyc:CPLX-2842		catalyzes

The native P. putida enzyme assignment is retained at its native frame scope. Database-curated assay attribution does not establish identity with a particular modern strain or sequence.

catechol + O2 => cis,cis-muconate + 2 H(+)
RHEA:23853
  • MetaCyc:ENZRXN-3585

    Source assertion: The activity links enzyme CPLX-2842 to CATECHOL-12-DIOXYGENASE-RXN. Native evidence: EV-EXP-IDA-PURIFIED-PROTEIN.

    Source location/ptools-xml/Enzymatic-Reaction/enzyme; reaction; evidence
  • MetaCyc:CATECHOL-12-DIOXYGENASE-RXN

    Source assertion: The native reaction cross-references RHEA:23853; complete structures, formal charges, sides and coefficients agree with the selected directional equation.

    Source location/ptools-xml/Reaction/dblink[dblink-db="RHEA"]; left; right; reaction-direction
catechol 1,2-dioxygenase
MetaCyc:CPLX-2842		has_part

Native assembly annotation, 2 subunits. This is a database-scoped assembly assertion, not proof of exact contemporary sequence or strain identity.

subunit of catechol 1,2-dioxygenase
MetaCyc:MONOMER-3422
  • MetaCyc:CPLX-2842

    Source assertion: The complex has component MONOMER-3422 with integer coefficient 2 and species TAX-303.

    Source location/ptools-xml/Protein/component; species/Organism[@frameid="TAX-303"]
muconate cycloisomerase
MetaCyc:CPLX-2843		catalyzes

The native P. putida enzyme assignment is retained at its native frame scope. Database-curated assay attribution does not establish identity with a particular modern strain or sequence.

cis,cis-muconate + H(+) => (S)-muconolactone
RHEA:30033
  • MetaCyc:ENZRXN-3586

    Source assertion: The activity links enzyme CPLX-2843 to MUCONATE-CYCLOISOMERASE-RXN. Native evidence: EV-EXP-IDA-PURIFIED-PROTEIN.

    Source location/ptools-xml/Enzymatic-Reaction/enzyme; reaction; evidence
  • MetaCyc:MUCONATE-CYCLOISOMERASE-RXN

    Source assertion: The native reaction cross-references RHEA:30033; complete structures, formal charges, sides and coefficients agree with the selected directional equation.

    Source location/ptools-xml/Reaction/dblink[dblink-db="RHEA"]; left; right; reaction-direction
muconate cycloisomerase
MetaCyc:CPLX-2843		has_part

Native assembly annotation, 8 subunits. This is a database-scoped assembly assertion, not proof of exact contemporary sequence or strain identity.

muconate lactonizing enzyme subunit
MetaCyc:MONOMER-3423
  • MetaCyc:CPLX-2843

    Source assertion: The complex has component MONOMER-3423 with integer coefficient 8 and species TAX-303.

    Source location/ptools-xml/Protein/component; species/Organism[@frameid="TAX-303"]
muconolactone isomerase
MetaCyc:CPLX-2844		catalyzes

The native P. putida enzyme assignment is retained at its native frame scope. Database-curated assay attribution does not establish identity with a particular modern strain or sequence.

(S)-muconolactone => (4,5-dihydro-5-oxofuran-2-yl)-acetate
RHEA:12349
  • MetaCyc:ENZRXN-3587

    Source assertion: The activity links enzyme CPLX-2844 to MUCONOLACTONE-DELTA-ISOMERASE-RXN. Native evidence: EV-EXP-IDA-PURIFIED-PROTEIN.

    Source location/ptools-xml/Enzymatic-Reaction/enzyme; reaction; evidence
  • MetaCyc:MUCONOLACTONE-DELTA-ISOMERASE-RXN

    Source assertion: The native reaction cross-references RHEA:12349; complete structures, formal charges, sides and coefficients agree with the selected directional equation.

    Source location/ptools-xml/Reaction/dblink[dblink-db="RHEA"]; left; right; reaction-direction
muconolactone isomerase
MetaCyc:CPLX-2844		has_part

Native assembly annotation, 10 subunits. This is a database-scoped assembly assertion, not proof of exact contemporary sequence or strain identity.

muconolactone isomerase subunit
MetaCyc:MONOMER-3424
  • MetaCyc:CPLX-2844

    Source assertion: The complex has component MONOMER-3424 with integer coefficient 10 and species TAX-303.

    Source location/ptools-xml/Protein/component; species/Organism[@frameid="TAX-303"]
β-ketoadipate enol-lactone hydrolase
MetaCyc:CPLX-2761		catalyzes

The native P. putida enzyme assignment is retained at its native frame scope. Database-curated assay attribution does not establish identity with a particular modern strain or sequence.

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

    Source assertion: The activity links enzyme CPLX-2761 to 3-OXOADIPATE-ENOL-LACTONASE-RXN. Native evidence: EV-EXP-IDA-PURIFIED-PROTEIN.

    Source location/ptools-xml/Enzymatic-Reaction/enzyme; reaction; evidence
  • MetaCyc:3-OXOADIPATE-ENOL-LACTONASE-RXN

    Source assertion: The native reaction cross-references RHEA:10185; complete structures, formal charges, sides and coefficients agree with the selected directional equation.

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

Historical inferred trimer from the P. putida PRS2260 preparation (derivative of PRS2178): apparent native mass 30–33 kDa and apparent subunits 11 kDa after 8 M urea. This is the 1980 interpretation retained by the native frame, not a modern structure determination or evidence for three 263-residue Q88N36 proteins. Original figure pixels and complete miniprint were unavailable.

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

    Source assertion: The complex has component MONOMER-3221 with integer coefficient 3 and species TAX-303.

    Source location/ptools-xml/Protein/component; species/Organism[@frameid="TAX-303"]
  • PMID:7391022
    a trimer formed by the association of identical subunits.
    Source locationJournal p. 6336, Discussion subsection: Pseudomonas beta-Ketoadipate Enol-Lactone Hydrolase Appears To Be a Trimer Composed of Identical Subunits; preparation p. 6339 and mass discussion p. 6340.
muconate cycloisomerase
MetaCyc:CPLX-2843		has_cofactor

Native muconate cycloisomerase annotation identifies a manganese ion near the active site in each subunit. This is a bound catalytic cofactor, not a consumed pathway substrate.

manganese(2+)
CHEBI:29035
  • MetaCyc:ENZRXN-3586

    Source assertion: The native cofactor slot names MN+2 and cites PMID:3999146.

    Source location/ptools-xml/Enzymatic-Reaction/cofactor
  • MetaCyc:CPLX-2843

    Source assertion: The complex comment states that each subunit contains an Mn2+ ion near its active site, citing PMID:3612800.

    Source location/ptools-xml/Protein/comment, paragraph beginning "Based on crystal structure"
(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:CATECHOL-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
3-oxoadipate
CHEBI:15775		regulates

Native source reports induction of the P. putida hydrolase by 3-oxoadipate. This expression-level response does not assert direct ligand binding, catalytic activation, an identified regulatory gene or equivalence with a modern KT2440 sequence.

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

    Source assertion: The first comment paragraph states that the P. putida enzyme is induced by 3-oxoadipate, citing PMID:5916393 and PMID:8905091.

    Source location/ptools-xml/Protein/comment, first paragraph, clause "which is induced by"
catechol 1,2-dioxygenase
MetaCyc:CPLX-2842

molecular state: Natural Pseudomonas putida (synonym P. arvilla) C-1 catechol 1,2-dioxygenase holoenzyme modeled in PDB 2AZQ. The native frame discusses C-1 isozyme variants; no exact sequence equivalence with MONOMER-3422 or deleted Q9AEQ0 is asserted.

Qualification evidence
  • DOI:10.2210/pdb2azq/pdb

    Source assertion: The natural source is Pseudomonas putida, taxonomy 303, strain C-1; biological assembly 1 is dimeric and the model includes FE.

    Source location_entity_src_nat; _pdbx_struct_assembly[id=1]; _atom_site[label_comp_id=FE]
  • MetaCyc:CPLX-2842

    Source assertion: The complex comment explicitly discusses the three C-1 catechol 1,2-dioxygenase isozyme assemblies alpha-alpha, alpha-beta and beta-beta.

    Source location/ptools-xml/Protein/comment, paragraph beginning "Some strains possess"
has_cofactor

The C-1 structural model assigns a bound Fe(III) cofactor coordinated by two tyrosine and two histidine residues. The assignment applies to this modeled holoenzyme; it is not a new redox assay or a sequence-equivalence claim for the native generic component. Iron is not consumed by the core reaction.

iron(3+)
CHEBI:29034
  • DOI:10.2210/pdb2azq/pdb

    Source assertion: The natural-source C-1 model names component FE as FE (III) ION and records four metal contacts to two TYR and two HIS residues; its FE atom has occupancy 1.00.

    Source location_entity_src_nat; _chem_comp[id=FE]; _struct_conn[conn_type_id=metalc]; _atom_site[label_comp_id=FE]

References

Curation history