protocatechuate degradation I (meta-cleavage pathway)

MetaCyc:P184-PWY

The complete MetaCyc 27.0 eight-member protocatechuate 4,5-cleavage definition proceeds through a semialdehyde hemiacetal, pyrone dicarboxylate, oxalomesaconate, the source-defined E,E enol and stereochemically unspecified CHA to oxaloacetate and pyruvate, followed by oxaloacetate decarboxylation. This is a source-defined composite with enzyme and taxon assertions scoped individually; it is not an experimentally reconstituted eight-step route in one strain. Modern LigU/LigJ reactions use distinct KCH and stereospecific S-CHA and are not substituted under the historical native reaction IDs. Taxa also include the explicitly scoped enzyme-source contexts; KT2440 gallate-module activities do not establish complete pathway occurrence in that strain.

Pathway type
aromatic compound catabolism
Organism scope

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Pathway network

78 nodes · 127 asserted directed edges

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Pathway network: protocatechuate degradation I (meta-cleavage pathway) 78 nodes · 127 asserted directed edges. Every arrow links to its evidence table row; nodes link to their component details. Isolated declared components are retained. RHEA:24045 — part_of → MetaCyc:P184-PWY; Member of the complete eight-step source-defined pathway. Material edges use the pathway-selected forward conversion.; Evidence: MetaCyc:P184-PWYpart of CHEBI:15379 — consumes → RHEA:24045; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:PROTOCATECHUATE-45-DIOXYGENASE-RXN, RHEA:24045consumes CHEBI:36241 — consumes → RHEA:24045; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:PROTOCATECHUATE-45-DIOXYGENASE-RXN, RHEA:24045consumes RHEA:24045 — produces → CHEBI:15378; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:PROTOCATECHUATE-45-DIOXYGENASE-RXN, RHEA:24045produces RHEA:24045 — produces → CHEBI:58358; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:PROTOCATECHUATE-45-DIOXYGENASE-RXN, RHEA:24045produces MetaCyc:R107-RXN — part_of → MetaCyc:P184-PWY; Member of the complete eight-step source-defined pathway. Material edges use the pathway-selected forward conversion. Native spontaneous=true permits uncatalyzed conversion without asserting its physiological rate or excluding enzyme acceleration.; Evidence: MetaCyc:P184-PWYpart of CHEBI:58358 — consumes → MetaCyc:R107-RXN; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:R107-RXNconsumes MetaCyc:R107-RXN — produces → CHEBI:61985; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:R107-RXNproduces RHEA:29588 — part_of → MetaCyc:P184-PWY; Member of the complete eight-step source-defined pathway. Material edges use the pathway-selected forward conversion. The native obsolete RHEA:10889 cross-reference is replaced only after exact equation comparison by approved RHEA:29588.; Evidence: MetaCyc:P184-PWYpart of CHEBI:61985 — consumes → RHEA:29588; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:1.2.1.45-RXN, RHEA:29588consumes CHEBI:58349 — consumes → RHEA:29588; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:1.2.1.45-RXN, RHEA:29588consumes RHEA:29588 — produces → CHEBI:58304; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:1.2.1.45-RXN, RHEA:29588produces RHEA:29588 — produces → CHEBI:57783; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:1.2.1.45-RXN, RHEA:29588produces RHEA:29588 — produces → CHEBI:15378; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:1.2.1.45-RXN, RHEA:29588produces RHEA:10645 — part_of → MetaCyc:P184-PWY; Member of the complete eight-step source-defined pathway. Material edges use the pathway-selected forward conversion.; Evidence: MetaCyc:P184-PWYpart of CHEBI:58304 — consumes → RHEA:10645; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:RXN-2462, RHEA:10645consumes CHEBI:15377 — consumes → RHEA:10645; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:RXN-2462, RHEA:10645consumes RHEA:10645 — produces → CHEBI:57471; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:RXN-2462, RHEA:10645produces RHEA:10645 — produces → CHEBI:15378; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:RXN-2462, RHEA:10645produces RHEA:28932 — part_of → MetaCyc:P184-PWY; Member of the complete eight-step source-defined pathway. Material edges use the pathway-selected forward conversion. Native reversible metadata is retained alongside the selected forward Rhea equation identity. Native spontaneous=true permits uncatalyzed conversion without asserting its physiological rate or excluding enzyme acceleration.; Evidence: MetaCyc:P184-PWYpart of CHEBI:57471 — consumes → RHEA:28932; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:RXN-9983, RHEA:28932consumes RHEA:28932 — produces → CHEBI:58142; Coefficient 1 in the selected pathway flux. Exact native E,E enol; historical cis,cis display terminology does not equate it to KCH or the Z,Z enol.; Evidence: MetaCyc:RXN-9983, RHEA:28932produces RHEA:17403 — part_of → MetaCyc:P184-PWY; Member of the complete eight-step source-defined pathway. Material edges use the pathway-selected forward conversion. The selected hydration runs opposite to the native reaction object written as dehydration. Native reversible metadata is retained alongside the selected forward Rhea equation identity.; Evidence: MetaCyc:P184-PWYpart of CHEBI:58142 — consumes → RHEA:17403; Coefficient 1 in the selected pathway flux. Exact native E,E enol; historical cis,cis display terminology does not equate it to KCH or the Z,Z enol.; Evidence: MetaCyc:RXN-2463, RHEA:17403consumes CHEBI:15377 — consumes → RHEA:17403; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:RXN-2463, RHEA:17403consumes RHEA:17403 — produces → CHEBI:58075; Coefficient 1 in the selected pathway flux. Native structure leaves absolute configuration unspecified; no racemic mixture or S-specific product is inferred.; Evidence: MetaCyc:RXN-2463, RHEA:17403produces RHEA:28936 — part_of → MetaCyc:P184-PWY; Member of the complete eight-step source-defined pathway. Material edges use the pathway-selected forward conversion. Native reversible metadata is retained alongside the selected forward Rhea equation identity.; Evidence: MetaCyc:P184-PWYpart of CHEBI:58075 — consumes → RHEA:28936; Coefficient 1 in the selected pathway flux. Native structure leaves absolute configuration unspecified; no racemic mixture or S-specific product is inferred.; Evidence: MetaCyc:RXN-2464, RHEA:28936consumes RHEA:28936 — produces → CHEBI:15361; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:RXN-2464, RHEA:28936produces RHEA:28936 — produces → CHEBI:16452; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:RXN-2464, RHEA:28936produces RHEA:15642 — part_of → MetaCyc:P184-PWY; Member of the complete eight-step source-defined pathway. Material edges use the pathway-selected forward conversion.; Evidence: MetaCyc:P184-PWYpart of CHEBI:16452 — consumes → RHEA:15642; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:OXALODECARB-RXN, RHEA:15642consumes CHEBI:15378 — consumes → RHEA:15642; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:OXALODECARB-RXN, RHEA:15642consumes RHEA:15642 — produces → CHEBI:15361; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:OXALODECARB-RXN, RHEA:15642produces RHEA:15642 — produces → CHEBI:16526; Coefficient 1 in the selected pathway flux.; Evidence: MetaCyc:OXALODECARB-RXN, RHEA:15642produces RHEA:28936 — provides_input_for → RHEA:15642; Selected pathway material transfer through CHEBI:16452. This source ordering does not assert an additional regulatory effect.; Evidence: MetaCyc:P184-PWYprovides input for RHEA:28932 — provides_input_for → RHEA:17403; Selected pathway material transfer through CHEBI:58142. This source ordering does not assert an additional regulatory effect.; Evidence: MetaCyc:P184-PWYprovides input for RHEA:10645 — provides_input_for → RHEA:28932; Selected pathway material transfer through CHEBI:57471. This source ordering does not assert an additional regulatory effect.; Evidence: MetaCyc:P184-PWYprovides input for RHEA:24045 — provides_input_for → MetaCyc:R107-RXN; Selected pathway material transfer through CHEBI:58358. This source ordering does not assert an additional regulatory effect.; Evidence: MetaCyc:P184-PWYprovides input for MetaCyc:R107-RXN — provides_input_for → RHEA:29588; Selected pathway material transfer through CHEBI:61985. This source ordering does not assert an additional regulatory effect.; Evidence: MetaCyc:P184-PWYprovides input for RHEA:17403 — provides_input_for → RHEA:28936; Selected pathway material transfer through CHEBI:58075. This source ordering does not assert an additional regulatory effect.; Evidence: MetaCyc:P184-PWYprovides input for RHEA:29588 — provides_input_for → RHEA:10645; Selected pathway material transfer through CHEBI:58304. This source ordering does not assert an additional regulatory effect.; Evidence: MetaCyc:P184-PWYprovides input for MetaCyc:MONOMER-10723 — catalyzes → RHEA:10645; Unpurified PDC-hydrolase from P. putida PDC selected on PDC. This strain uses ortho cleavage for PCA in the 1982 primary; no full P184 occurrence inference.; Evidence: MetaCyc:ENZRXN-11003catalyzes MetaCyc:CPLX-7917 — catalyzes → RHEA:28936; Historical Comamonas/Pseudomonas testosteroni HMG/CHA aldolase, source experimental evidence includes crude/part-purified assays; R-HMG preference does not assign CHA absolute chirality.; Evidence: MetaCyc:ENZRXN-11041catalyzes MetaCyc:CPLX-7916 — enables → RHEA:24045; Native SYK6 LigAB complex assignment is supported by functional complementation, not independent purified subunit catalysis. Later His-tagged/synthetic preparations are separate.; Evidence: MetaCyc:ENZRXN-16927enables MetaCyc:CPLX-2865 — catalyzes → RHEA:15642; Recombinant SYK6 LigK native-gene pETK in E. coli BL21(DE3), near-homogeneous hexamer. Native broad CHA assignment does not assert absolute substrate configuration; terminal OAA decarboxylation separately supported.; Evidence: MetaCyc:ENZRXN-16934catalyzes MetaCyc:CPLX-2782 — catalyzes → RHEA:15642; Historical P. straminea/P. ochraceae homohexamer and separately recombinant proA observations; broad CHA node does not mean racemic substrate, and reported L-substrate preference is retained.; Evidence: MetaCyc:ENZRXN-16935catalyzes MetaCyc:G1G01-2697-MONOMER — catalyzes → RHEA:28932; subject experimental construct: KT2440 GalD expressed in E. coli BL21(DE3), purified by Ni-NTA with retained His6 tag; an internal thrombin site prevented tag removal. No substitution of a SYK6 LigU homolog.; Evidence PMID:26867578: removal of the His6 tag was not attempted; KT2440 GalD shared gallate-module tautomerase. 2016 assays retained His6 tag due internal thrombin site; native exact reaction is E,E enol, while old narrative Z,Z link is rejected. No whole KT2440 P184 occurrence.; Evidence: MetaCyc:ENZRXN-18372, PMID:26867578catalyzes MetaCyc:CPLX-8178 — catalyzes → RHEA:17403; subject experimental construct: Source-native GalB assay preparation: KT2440 gene expressed with a His tag in KT2442/E. coli. Do not substitute the separate 2016 GalBNt crystal construct lacking four N-terminal residues or infer absolute CHA configuration.; Evidence MetaCyc:CPLX-8178: The native protein comment identifies His-tagged GalB expression and purification in KT2442 and E. coli. (/ptools-xml/Protein[@frameid="CPLX-8178"]/comment); KT2440 GalB gallate-module enzyme; native-host KT2442 and recombinant E. coli preparations are separate. Modern 2016 substrate assays support GalD-generated E,E-CHM and (-)-CHA without absolute product assignment; not whole KT2440 P184 occurrence.; Evidence: MetaCyc:ENZRXN-18373, PMID:26867578catalyzes MetaCyc:CPLX-2701 — catalyzes → RHEA:24045; Historical Comamonas/Pseudomonas testosteroni preparations; native species object spans reported strains. Do not equate the original preparations with modern BR6020 subunit accession sequences.; Evidence: MetaCyc:ENZRXN-3342catalyzes MetaCyc:MONOMER-3182 — catalyzes → RHEA:10645; Historical phthalate-grown P. straminea/P. ochraceae purified PDC hydrolase; later recombinant proL is distinct, and current native cross-reference does not prove old strain sequence identity.; Evidence: MetaCyc:ENZRXN-3363catalyzes MetaCyc:CPLX-2781 — catalyzes → RHEA:17403; Historical phthalate-grown P. straminea/P. ochraceae purified homodimer; retain native substrate assignment as a database assertion, not independent absolute stereochemical identification.; Evidence: MetaCyc:ENZRXN-3364catalyzes MetaCyc:CPLX-2782 — catalyzes → RHEA:28936; Historical P. straminea/P. ochraceae homohexamer and separately recombinant proA observations; broad CHA node does not mean racemic substrate, and reported L-substrate preference is retained.; Evidence: MetaCyc:ENZRXN-3365catalyzes MetaCyc:MONOMER-3463 — catalyzes → RHEA:10645; Purified native Pseudomonas/Comamonas testosteroni PDC hydrolase from 4-hydroxybenzoate-grown cells; reversible/pH-dependent reaction. Original 1982 source does not individually characterize all open-chain isomers.; Evidence: MetaCyc:ENZRXN-3623catalyzes MetaCyc:CPLX-2863 — catalyzes → RHEA:29588; Recombinant SYK6 LigC from native-gene pSM21 in E. coli BL21(DE3), purified near homogeneity. First 20 residues matched deduced gene; full paper reports both NAD/NADP support and 67 kDa homodimer.; Evidence: MetaCyc:ENZRXN-3624catalyzes MetaCyc:MONOMER-3467 — catalyzes → RHEA:10645; Recombinant SYK6 LigI near-homogeneous monomer from historical experiment. Later synthetic/tagged 2012 structural preparation is distinct.; Evidence: MetaCyc:ENZRXN-3625catalyzes MetaCyc:CPLX-2865 — catalyzes → RHEA:28936; Recombinant SYK6 LigK native-gene pETK in E. coli BL21(DE3), near-homogeneous hexamer. Native broad CHA assignment does not assert absolute substrate configuration; terminal OAA decarboxylation separately supported.; Evidence: MetaCyc:ENZRXN-3627catalyzes MetaCyc:CPLX-2881 — catalyzes → RHEA:28936; Historical P. putida HMG/CHA aldolase preparation; avoid identifying the original strain solely from later KT2440 galC sequence.; Evidence: MetaCyc:ENZRXN-3641catalyzes MetaCyc:CPLX-2861 — catalyzes → RHEA:29588; Historical P. straminea/P. ochraceae purified CHMS dehydrogenase homodimer; both NAD and NADP are supported, with higher apparent affinity for NADP.; Evidence: MetaCyc:ENZRXN-8701catalyzes MetaCyc:CPLX1G01-155 — catalyzes → RHEA:28936; KT2440 GalC/gllC gallate-module activity; native/heterologous assays and historical species-level enzyme are distinct. Does not establish the whole protocatechuate meta-cleavage pathway in KT2440.; Evidence: MetaCyc:ENZRXN1G01-1112catalyzes MetaCyc:MONOMER-3165 — part_of → MetaCyc:CPLX-2701; Native complex membership; subunit membership alone is not an assertion of independent catalysis.; Evidence: MetaCyc:CPLX-2701part of MetaCyc:MONOMER-3166 — part_of → MetaCyc:CPLX-2701; Native complex membership; subunit membership alone is not an assertion of independent catalysis.; Evidence: MetaCyc:CPLX-2701part of MetaCyc:MONOMER-3243 — part_of → MetaCyc:CPLX-2781; Native complex membership; subunit membership alone is not an assertion of independent catalysis.; Evidence: MetaCyc:CPLX-2781part of MetaCyc:MONOMER-3244 — part_of → MetaCyc:CPLX-2782; Native complex membership; subunit membership alone is not an assertion of independent catalysis.; Evidence: MetaCyc:CPLX-2782part of MetaCyc:MONOMER-8501 — part_of → MetaCyc:CPLX-2861; Native complex membership; subunit membership alone is not an assertion of independent catalysis.; Evidence: MetaCyc:CPLX-2861part of MetaCyc:MONOMER-3466 — part_of → MetaCyc:CPLX-2863; Native complex membership; subunit membership alone is not an assertion of independent catalysis.; Evidence: MetaCyc:CPLX-2863part of MetaCyc:MONOMER-3469 — part_of → MetaCyc:CPLX-2865; Native complex membership; subunit membership alone is not an assertion of independent catalysis.; Evidence: MetaCyc:CPLX-2865part of MetaCyc:MONOMER-3481 — part_of → MetaCyc:CPLX-2881; Native complex membership; subunit membership alone is not an assertion of independent catalysis.; Evidence: MetaCyc:CPLX-2881part of MetaCyc:MONOMER-15117 — part_of → MetaCyc:CPLX-7916; Native complex membership; subunit membership alone is not an assertion of independent catalysis.; Evidence: MetaCyc:CPLX-7916part of MetaCyc:MONOMER-15116 — part_of → MetaCyc:CPLX-7916; Native complex membership; subunit membership alone is not an assertion of independent catalysis.; Evidence: MetaCyc:CPLX-7916part of MetaCyc:MONOMER-3184 — part_of → MetaCyc:CPLX-7917; Native complex membership; subunit membership alone is not an assertion of independent catalysis.; Evidence: MetaCyc:CPLX-7917part of MetaCyc:G1G01-2699-MONOMER — part_of → MetaCyc:CPLX-8178; Native complex membership; subunit membership alone is not an assertion of independent catalysis.; Evidence: MetaCyc:CPLX-8178part of MetaCyc:G1G01-2698-MONOMER — part_of → MetaCyc:CPLX1G01-155; Native complex membership; subunit membership alone is not an assertion of independent catalysis.; Evidence: MetaCyc:CPLX1G01-155part of MetaCyc:CPLX-2865 — has_cofactor → CHEBI:18420; subject experimental construct: Purified recombinant SYK6 LigK from pETK in E. coli BL21(DE3), observed as a homohexamer. The measured N-terminus lacks the initial native methionine; unreported vector-derived residues are not inferred absent.; Evidence PMID:12486039: first methionine (PMC141877, Results / Purification of CHA aldolase, N-terminal sequence; Methods / Expression and purification of LigK; Results / Enzyme properties, gel filtration); The source annotates Mg as a LigK cofactor. In the reported recombinant assays, CHA activity with 1 mM Co, Zn, Ca or Mn was 85%, 65%, 20% or 0% of the 1 mM Mg control. OAA activity showed qualitatively similar metal dependence; those exact percentages were not reported for OAA. At 0.5 mM, phosphate enhanced CHA and OAA activities by 3.0 and 1.7 fold, respectively. These assay observations do not identify the physiological metal.; Evidence: MetaCyc:ENZRXN-16934, MetaCyc:ENZRXN-3627, PMID:12486039, PMID:12486039has cofactor MetaCyc:CPLX-8178 — has_cofactor → CHEBI:29105; subject experimental construct: Source-native GalB assay preparation: KT2440 gene expressed with a His tag in KT2442/E. coli. Do not substitute the separate 2016 GalBNt crystal construct lacking four N-terminal residues or infer absolute CHA configuration.; Evidence MetaCyc:CPLX-8178: The native protein comment identifies His-tagged GalB expression and purification in KT2442 and E. coli. (/ptools-xml/Protein[@frameid="CPLX-8178"]/comment); Source-scoped cofactor annotation. Alternative metals and assay-specific effects must not be generalized across distinct aldolases or hydratases.; Evidence: MetaCyc:ENZRXN-18373has cofactor MetaCyc:CPLX-2701 — has_cofactor → CHEBI:29033; Source-scoped cofactor annotation. Alternative metals and assay-specific effects must not be generalized across distinct aldolases or hydratases.; Evidence: MetaCyc:ENZRXN-3342has cofactor MetaCyc:CPLX-2782 — has_cofactor → CHEBI:18420; Source-scoped cofactor annotation. Alternative metals and assay-specific effects must not be generalized across distinct aldolases or hydratases.; Evidence: MetaCyc:ENZRXN-3365has cofactor MetaCyc:CPLX-2881 — has_cofactor → CHEBI:29035; Source-scoped cofactor annotation. Alternative metals and assay-specific effects must not be generalized across distinct aldolases or hydratases.; Evidence: MetaCyc:ENZRXN-3641has cofactor MetaCyc:CPLX-2881 — has_cofactor → CHEBI:18420; Source-scoped cofactor annotation. Alternative metals and assay-specific effects must not be generalized across distinct aldolases or hydratases.; Evidence: MetaCyc:ENZRXN-3641has cofactor MetaCyc:CPLX1G01-155 — has_cofactor → CHEBI:29035; Source-scoped cofactor annotation. Alternative metals and assay-specific effects must not be generalized across distinct aldolases or hydratases.; Evidence: MetaCyc:ENZRXN1G01-1112has cofactor CHEBI:16452 — inhibits → MetaCyc:CPLX-2865; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-10400inhibits MetaCyc:N-ETHYLMALEIMIDE — inhibits → MetaCyc:CPLX-2865; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-10401inhibits MetaCyc:CPD-29 — inhibits → MetaCyc:CPLX-2861; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-10405inhibits MetaCyc:IODOACETATE — inhibits → MetaCyc:CPLX-2861; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-10406inhibits MetaCyc:N-ETHYLMALEIMIDE — inhibits → MetaCyc:CPLX-2861; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-10407inhibits CHEBI:16452 — inhibits → MetaCyc:CPLX-2881; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-10724inhibits CHEBI:48828 — inhibits → MetaCyc:MONOMER-3463; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-11529inhibits CHEBI:29035 — inhibits → MetaCyc:MONOMER-3463; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-11530inhibits CHEBI:29036 — inhibits → MetaCyc:MONOMER-3463; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-11531inhibits CHEBI:29105 — inhibits → MetaCyc:MONOMER-3463; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-11532inhibits CHEBI:29035 — regulates → MetaCyc:CPLX-2701; Native source leaves the effect sign unspecified; this edge does not assert activation or inhibition.; Evidence: MetaCyc:REG-11747regulates CHEBI:49786 — regulates → MetaCyc:CPLX-2701; Native source leaves the effect sign unspecified; this edge does not assert activation or inhibition.; Evidence: MetaCyc:REG-11748regulates CHEBI:48828 — regulates → MetaCyc:CPLX-2701; Native source leaves the effect sign unspecified; this edge does not assert activation or inhibition.; Evidence: MetaCyc:REG-11749regulates CHEBI:16793 — inhibits → MetaCyc:CPLX-2861; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-12625inhibits CHEBI:16793 — inhibits → MetaCyc:CPLX-2865; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-12626inhibits CHEBI:16793 — inhibits → MetaCyc:CPLX-2863; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred. LigC 2000 assayed purified recombinant pSM21 protein; Hg was delivered as HgCl2, pCMB at 10 μM: 78%; HgCl2 at 10 μM: 83%; DTNB at 100 μM: 98% inhibition after 1 h. These are separate treatments.; Evidence: MetaCyc:REG-12627inhibits CHEBI:16793 — inhibits → MetaCyc:CPLX-2781; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-12629inhibits CHEBI:16793 — inhibits → MetaCyc:MONOMER-3182; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-12637inhibits CHEBI:16793 — inhibits → MetaCyc:CPLX-2782; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-12638inhibits CHEBI:29105 — inhibits → MetaCyc:CPLX-2781; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-12669inhibits CHEBI:29105 — inhibits → MetaCyc:MONOMER-3467; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-8378inhibits MetaCyc:N-ETHYLMALEIMIDE — inhibits → MetaCyc:MONOMER-3467; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-8379inhibits MetaCyc:DITHIO-NITROBENZOATE — inhibits → MetaCyc:MONOMER-3467; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-8380inhibits CHEBI:16452 — inhibits → MetaCyc:CPLX-2782; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-8391inhibits MetaCyc:CPD-29 — inhibits → MetaCyc:CPLX-2782; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-8393inhibits CHEBI:29036 — inhibits → MetaCyc:MONOMER-3182; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-8394inhibits CHEBI:29105 — inhibits → MetaCyc:MONOMER-3182; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-8395inhibits CHEBI:29035 — inhibits → MetaCyc:MONOMER-3182; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-8396inhibits CHEBI:48828 — inhibits → MetaCyc:MONOMER-3182; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-8397inhibits MetaCyc:CPD-29 — inhibits → MetaCyc:MONOMER-3182; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-8398inhibits MetaCyc:CPD-29 — inhibits → MetaCyc:CPLX-2781; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-9531inhibits MetaCyc:CUSO4 — inhibits → MetaCyc:CPLX-2781; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.; Evidence: MetaCyc:REG-9532inhibits MetaCyc:CPD-29 — inhibits → MetaCyc:CPLX-2863; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred. LigC 2000 assayed purified recombinant pSM21 protein; Hg was delivered as HgCl2, pCMB at 10 μM: 78%; HgCl2 at 10 μM: 83%; DTNB at 100 μM: 98% inhibition after 1 h. These are separate treatments.; Evidence: MetaCyc:REG-9956inhibits MetaCyc:DITHIO-NITROBENZOATE — inhibits → MetaCyc:CPLX-2863; Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred. LigC 2000 assayed purified recombinant pSM21 protein; Hg was delivered as HgCl2, pCMB at 10 μM: 78%; HgCl2 at 10 μM: 83%; DTNB at 100 μM: 98% inhibition after 1 h. These are separate treatments.; Evidence: MetaCyc:REG-9957inhibits MetaCyc:CPLX-2861 — has_cofactor → CHEBI:57540; Historical enzyme supports either nicotinamide coenzyme; higher apparent NADP affinity does not mean exclusive NADP usage.; Evidence: MetaCyc:CPLX-2861has cofactor MetaCyc:CPLX-2861 — has_cofactor → CHEBI:58349; Historical enzyme supports either nicotinamide coenzyme; higher apparent NADP affinity does not mean exclusive NADP usage.; Evidence: MetaCyc:CPLX-2861has cofactor MetaCyc:CPLX-2863 — has_cofactor → CHEBI:57540; Purified recombinant SYK6 LigC supports NAD and NADP. Primary Table 3 values supersede transposed UniProt kinetic substrate labels.; Evidence: PMID:11073908has cofactor MetaCyc:CPLX-2863 — has_cofactor → CHEBI:58349; Purified recombinant SYK6 LigC supports NAD and NADP. Primary Table 3 values supersede transposed UniProt kinetic substrate labels.; Evidence: PMID:11073908has cofactor MetaCyc:CPLX-8178 — has_cofactor → CHEBI:29033; subject molecular state: EDTA-treated GalB apoenzyme subsequently incubated with the named divalent metal; compare separately from zinc-rich aerobically purified KT2442 material.; Evidence PMID:26867578: Table2 contrasts the named metal reconstitutions, Apo, EDTA, Native, and Native+Co2+ conditions. (Table2 condition rows and caption); 2016 apoenzyme reconstitution supports this alternative metal; native-host aerobic purification was zinc-rich, and physiological metal identity remains unresolved.; Evidence: PMID:26867578has cofactor MetaCyc:CPLX-8178 — has_cofactor → CHEBI:48828; subject molecular state: EDTA-treated GalB apoenzyme subsequently incubated with the named divalent metal; compare separately from zinc-rich aerobically purified KT2442 material.; Evidence PMID:26867578: Table2 contrasts the named metal reconstitutions, Apo, EDTA, Native, and Native+Co2+ conditions. (Table2 condition rows and caption); 2016 apoenzyme reconstitution supports this alternative metal; native-host aerobic purification was zinc-rich, and physiological metal identity remains unresolved.; Evidence: PMID:26867578has cofactor MetaCyc:CPLX-2782 — has_cofactor → CHEBI:29035; Historical P. straminea/P. ochraceae aldolase metal alternative; do not transfer this result to SYK6 LigK, whose assay metal preferences differ.; Evidence: MetaCyc:CPLX-2782has cofactor MetaCyc:CPLX-2782 — has_cofactor → CHEBI:48828; Historical P. straminea/P. ochraceae aldolase metal alternative; do not transfer this result to SYK6 LigK, whose assay metal preferences differ.; Evidence: MetaCyc:CPLX-2782has cofactor MetaCyc:CPLX-2782 — has_cofactor → CHEBI:29105; Historical P. straminea/P. ochraceae aldolase metal alternative; do not transfer this result to SYK6 LigK, whose assay metal preferences differ.; Evidence: MetaCyc:CPLX-2782has cofactor MetaCyc:CPLX-2782 — has_cofactor → CHEBI:48775; Historical P. straminea/P. ochraceae aldolase metal alternative; do not transfer this result to SYK6 LigK, whose assay metal preferences differ.; Evidence: MetaCyc:CPLX-2782has cofactor UniProtKB:Q8RQV9 — regulates → MetaCyc:P184-PWY; In SYK6, LigR activates ligK-orf1-ligI-lsdA and ligJABC transcription with PCA/gallate and autorepresses ligR. This regulatory evidence does not validate every chemical step of the composite native eight-member definition; promoter DNA identifiers and cooperative-binding hypotheses are not invented.; Evidence: PMID:20435721regulates CHEBI:16240 — inhibits → MetaCyc:CPLX-2701; Historical native P. testosteroni dioxygenase is inactivated when its Fe2+ is oxidized; this is assay-induced redox inactivation, not inferred physiological regulation.; Evidence: PMID:6317682, PMID:6317682inhibits CHEBI:22651 — activates → MetaCyc:CPLX-2701; object molecular state: Previously oxidized, inactive Fe3+-containing native P. testosteroni dioxygenase; reduction recovers activity.; Evidence PMID:6317682: In the oxidized state; Ascorbate restores activity by reducing the oxidized iron site in the historical native preparation; it is not generalized activation of already-active dioxygenase.; Evidence: PMID:6317682activates dioxygen; CHEBI:15379; Declared type: small_molecule small molecule dioxygen 3,4-dihydroxybenzoate; CHEBI:36241; Declared type: small_molecule small molecule 3,4-dihydroxybenzoate hydron; CHEBI:15378; Declared type: small_molecule small molecule hydron 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde(2-); CHEBI:58358; Declared type: small_molecule small molecule 4-carboxy-2-hydroxy-cis,cis- muconate 6-semialdehyde(2-) 4-carboxy-2-hydroxymuconate semialdehyde hemiacetal(2-); CHEBI:61985; Declared type: small_molecule small molecule 4-carboxy-2-hydroxymuconate semialdehyde hemiacetal(2-) NADP(3-); CHEBI:58349; Declared type: cofactor cofactor NADP(3-) 2-oxo-2H-pyran-4,6-dicarboxylate; CHEBI:58304; Declared type: small_molecule small molecule 2-oxo-2H-pyran-4,6- dicarboxylate NADPH(4-); CHEBI:57783; Declared type: small_molecule small molecule NADPH(4-) water; CHEBI:15377; Declared type: small_molecule small molecule water (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate; CHEBI:57471; Declared type: small_molecule small molecule (1E)-4-oxobut-1-ene-1,2,4- tricarboxylate 4-carboxy-2-hydroxy-cis,cis-muconate(3-); CHEBI:58142; Declared type: small_molecule small molecule 4-carboxy-2-hydroxy-cis,cis- muconate(3-) 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate; CHEBI:58075; Declared type: small_molecule small molecule 2-hydroxy-4-oxobutane-1,2,4- tricarboxylate pyruvate; CHEBI:15361; Declared type: small_molecule small molecule pyruvate oxaloacetate(2-); CHEBI:16452; Declared type: small_molecule small molecule oxaloacetate(2-) carbon dioxide; CHEBI:16526; Declared type: small_molecule small molecule carbon dioxide protocatechuate 4,5-dioxygenase; MetaCyc:CPLX-2701; Declared type: complex complex protocatechuate 4,5-dioxygenase 4-oxalomesaconate hydratase; MetaCyc:CPLX-2781; Declared type: complex complex 4-oxalomesaconate hydratase HMG aldolase; MetaCyc:CPLX-2782; Declared type: complex complex HMG aldolase 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase; MetaCyc:CPLX-2861; Declared type: complex complex 4-carboxy-2-hydroxymuconate- 6-semialdehyde dehydrogenase 2-hydroxy-4-carboxymuconate-6-semialdehyde dehydrogenase; MetaCyc:CPLX-2863; Declared type: complex complex 2-hydroxy-4-carboxymuconate- 6-semialdehyde dehydrogenase 4-carboxy-4-hydroxy-2-oxoadipate aldolase; MetaCyc:CPLX-2865; Declared type: complex complex 4-carboxy-4-hydroxy-2- oxoadipate aldolase HMG aldolase; MetaCyc:CPLX-2881; Declared type: complex complex HMG aldolase protocatechuate 4,5-dioxygenase; MetaCyc:CPLX-7916; Declared type: complex complex protocatechuate 4,5-dioxygenase HMG aldolase; MetaCyc:CPLX-7917; Declared type: complex complex HMG aldolase 4-oxalmesaconate hydratase; MetaCyc:CPLX-8178; Declared type: complex complex 4-oxalmesaconate hydratase 4-hydroxy-4-methyl-2-oxoglutarate aldolase; MetaCyc:CPLX1G01-155; Declared type: complex complex 4-hydroxy-4-methyl-2- oxoglutarate aldolase 4-oxalomesaconate tautomerase; MetaCyc:G1G01-2697-MONOMER; Declared type: protein protein 4-oxalomesaconate tautomerase 4-hydroxy-4-methyl-2-oxoglutarate aldolase aldolase; MetaCyc:G1G01-2698-MONOMER; Declared type: protein protein 4-hydroxy-4-methyl-2- oxoglutarate aldolase aldolase 4-oxalmesaconate hydratase monomer; MetaCyc:G1G01-2699-MONOMER; Declared type: protein protein 4-oxalmesaconate hydratase monomer 2-pyrone-4,6-dicarboxylate hydrolase; MetaCyc:MONOMER-10723; Declared type: protein protein 2-pyrone-4,6-dicarboxylate hydrolase protocatechuate 4,5-dioxygenase alpha chain; MetaCyc:MONOMER-15116; Declared type: protein protein protocatechuate 4,5-dioxygenase alpha chain protocatechuate 4,5-dioxygenase beta chain; MetaCyc:MONOMER-15117; Declared type: protein protein protocatechuate 4,5-dioxygenase beta chain protocatechuate 4,5-dioxygenase α subunit; MetaCyc:MONOMER-3165; Declared type: protein protein protocatechuate 4,5-dioxygenase α subunit protocatechuate 4,5-dioxygenase β subunit; MetaCyc:MONOMER-3166; Declared type: protein protein protocatechuate 4,5-dioxygenase β subunit 2-pyrone-4,6-dicarboxylate hydrolase; MetaCyc:MONOMER-3182; Declared type: protein protein 2-pyrone-4,6-dicarboxylate hydrolase HMG aldolase monomer; MetaCyc:MONOMER-3184; Declared type: protein protein HMG aldolase monomer subunit of 4-oxalomesaconate hydratase; MetaCyc:MONOMER-3243; Declared type: protein protein subunit of 4-oxalomesaconate hydratase 4-oxalocitramalate aldolase subunit; MetaCyc:MONOMER-3244; Declared type: protein protein 4-oxalocitramalate aldolase subunit 2-pyrone-4,6-dicarboxylate hydrolase; MetaCyc:MONOMER-3463; Declared type: protein protein 2-pyrone-4,6-dicarboxylate hydrolase LigC; MetaCyc:MONOMER-3466; Declared type: protein protein LigC 2-pyrone-4,6-dicarboxylate hydrolase; MetaCyc:MONOMER-3467; Declared type: protein protein 2-pyrone-4,6-dicarboxylate hydrolase LigK; MetaCyc:MONOMER-3469; Declared type: protein protein LigK subunit of 4-hydroxy-4-methyl-2-oxoglutarate aldolase; MetaCyc:MONOMER-3481; Declared type: protein protein subunit of 4-hydroxy-4- methyl-2-oxoglutarate aldolase α-hydroxy-γ-carboxymuconate ε-semialdehyde dehydrogenase subunit; MetaCyc:MONOMER-8501; Declared type: protein protein α-hydroxy-γ-carboxymuconate ε-semialdehyde dehydrogenase subunit magnesium(2+); CHEBI:18420; Declared type: cofactor cofactor magnesium(2+) zinc(2+); CHEBI:29105; Declared type: cofactor cofactor zinc(2+) iron(2+); CHEBI:29033; Declared type: cofactor cofactor iron(2+) manganese(2+); CHEBI:29035; Declared type: cofactor cofactor manganese(2+) N-ethylmaleimide; MetaCyc:N-ETHYLMALEIMIDE; Declared type: small_molecule small molecule N-ethylmaleimide p-chloromercuribenzoate; MetaCyc:CPD-29; Declared type: small_molecule small molecule p-chloromercuribenzoate iodoacetate; MetaCyc:IODOACETATE; Declared type: small_molecule small molecule iodoacetate cobalt(2+); CHEBI:48828; Declared type: cofactor cofactor cobalt(2+) copper(2+); CHEBI:29036; Declared type: small_molecule small molecule copper(2+) nickel(2+); CHEBI:49786; Declared type: small_molecule small molecule nickel(2+) mercury(2+); CHEBI:16793; Declared type: small_molecule small molecule mercury(2+) 5,5'-dithio-bis-2-nitrobenzoate; MetaCyc:DITHIO-NITROBENZOATE; Declared type: small_molecule small molecule 5,5'-dithio- bis-2-nitrobenzoate copper sulfate; MetaCyc:CUSO4; Declared type: small_molecule small molecule copper sulfate NAD(1-); CHEBI:57540; Declared type: cofactor cofactor NAD(1-) cadmium(2+); CHEBI:48775; Declared type: cofactor cofactor cadmium(2+) LigR protein; UniProtKB:Q8RQV9; Declared type: protein protein LigR protein hydrogen peroxide; CHEBI:16240; Declared type: small_molecule small molecule hydrogen peroxide ascorbate; CHEBI:22651; Declared type: chemical_entity chemical entity ascorbate 3,4-dihydroxybenzoate + O2 => 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + H(+); RHEA:24045; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity 3,4-dihydroxybenzoate + O2 => 4-carboxy-2-hydroxy- cis,cis-muconate 6-semialdehyde + H(+) 4-carboxy-2-hydroxymuconate semialdehyde hemiacetal formation; MetaCyc:R107-RXN; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity 4-carboxy-2-hydroxymuconate semialdehyde hemiacetal formation 4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP(+) => 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H(+); RHEA:29588; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity 4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP(+) => 2-oxo-2H-pyran- 4,6-dicarboxylate + NADPH + H(+) 2-oxo-2H-pyran-4,6-dicarboxylate + H2O => (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate + H(+); RHEA:10645; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity 2-oxo-2H-pyran-4,6- dicarboxylate + H2O => (1E)- 4-oxobut-1-ene-1,2,4- tricarboxylate + H(+) (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate => 4-carboxy-2-hydroxy-cis,cis-muconate; RHEA:28932; Declared type: molecular_activity; Source reaction direction: reversible molecular activity (1E)-4-oxobut-1-ene-1,2,4- tricarboxylate => 4-carboxy-2-hydroxy-cis,cis- muconate 4-carboxy-2-hydroxy-cis,cis-muconate + H2O => 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate; RHEA:17403; Declared type: molecular_activity; Source reaction direction: reversible molecular activity 4-carboxy-2-hydroxy-cis,cis- muconate + H2O => 2-hydroxy- 4-oxobutane-1,2,4- tricarboxylate 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate => oxaloacetate + pyruvate; RHEA:28936; Declared type: molecular_activity; Source reaction direction: reversible molecular activity 2-hydroxy-4-oxobutane-1,2,4- tricarboxylate => oxaloacetate + pyruvate oxaloacetate + H(+) => pyruvate + CO2; RHEA:15642; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity oxaloacetate + H(+) => pyruvate + CO2 protocatechuate degradation I (meta-cleavage pathway); MetaCyc:P184-PWY; Declared type: pathway pathway protocatechuate degradation I (meta-cleavage pathway) 4-oxalomesaconate tautomerase; MetaCyc:G1G01-2697-MONOMER; Declared type: protein; experimental construct: KT2440 GalD expressed in E. coli BL21(DE3), purified by Ni-NTA with retained His6 tag; an internal thrombin site prevented tag removal. No substitution of a SYK6 LigU homolog.; Evidence PMID:26867578: removal of the His6 tag was not attempted experimental construct 4-oxalomesaconate tautomerase [experimental construct: KT2440 GalD expressed in E. coli BL21(DE3), purified by Ni- NTA with retained His6 tag; an internal…] 4-oxalmesaconate hydratase; MetaCyc:CPLX-8178; Declared type: complex; experimental construct: Source-native GalB assay preparation: KT2440 gene expressed with a His tag in KT2442/E. coli. Do not substitute the separate 2016 GalBNt crystal construct lacking four N-terminal residues or infer absolute CHA configuration.; Evidence MetaCyc:CPLX-8178: The native protein comment identifies His-tagged GalB expression and purification in KT2442 and E. coli. (/ptools-xml/Protein[@frameid="CPLX-8178"]/comment) experimental construct 4-oxalmesaconate hydratase [experimental construct: Source-native GalB assay preparation: KT2440 gene expressed with a His tag in KT2442/E. coli. Do…] 4-carboxy-4-hydroxy-2-oxoadipate aldolase; MetaCyc:CPLX-2865; Declared type: complex; experimental construct: Purified recombinant SYK6 LigK from pETK in E. coli BL21(DE3), observed as a homohexamer. The measured N-terminus lacks the initial native methionine; unreported vector-derived residues are not inferred absent.; Evidence PMID:12486039: first methionine (PMC141877, Results / Purification of CHA aldolase, N-terminal sequence; Methods / Expression and purification of LigK; Results / Enzyme properties, gel filtration) experimental construct 4-carboxy-4-hydroxy-2- oxoadipate aldolase [experimental construct: Purified recombinant SYK6 LigK from pETK in E. coli BL21(DE3), observed as a homohexamer. The…] 4-oxalmesaconate hydratase; MetaCyc:CPLX-8178; Declared type: complex; experimental construct: Source-native GalB assay preparation: KT2440 gene expressed with a His tag in KT2442/E. coli. Do not substitute the separate 2016 GalBNt crystal construct lacking four N-terminal residues or infer absolute CHA configuration.; Evidence MetaCyc:CPLX-8178: The native protein comment identifies His-tagged GalB expression and purification in KT2442 and E. coli. (/ptools-xml/Protein[@frameid="CPLX-8178"]/comment) experimental construct 4-oxalmesaconate hydratase [experimental construct: Source-native GalB assay preparation: KT2440 gene expressed with a His tag in KT2442/E. coli. Do…] 4-oxalmesaconate hydratase; MetaCyc:CPLX-8178; Declared type: complex; molecular state: EDTA-treated GalB apoenzyme subsequently incubated with the named divalent metal; compare separately from zinc-rich aerobically purified KT2442 material.; Evidence PMID:26867578: Table2 contrasts the named metal reconstitutions, Apo, EDTA, Native, and Native+Co2+ conditions. (Table2 condition rows and caption) molecular state 4-oxalmesaconate hydratase [molecular state: EDTA- treated GalB apoenzyme subsequently incubated with the named divalent metal; compare…] 4-oxalmesaconate hydratase; MetaCyc:CPLX-8178; Declared type: complex; molecular state: EDTA-treated GalB apoenzyme subsequently incubated with the named divalent metal; compare separately from zinc-rich aerobically purified KT2442 material.; Evidence PMID:26867578: Table2 contrasts the named metal reconstitutions, Apo, EDTA, Native, and Native+Co2+ conditions. (Table2 condition rows and caption) molecular state 4-oxalmesaconate hydratase [molecular state: EDTA- treated GalB apoenzyme subsequently incubated with the named divalent metal; compare…] protocatechuate 4,5-dioxygenase; MetaCyc:CPLX-2701; Declared type: complex; molecular state: Previously oxidized, inactive Fe3+-containing native P. testosteroni dioxygenase; reduction recovers activity.; Evidence PMID:6317682: In the oxidized state molecular state protocatechuate 4,5-dioxygenase [molecular state: Previously oxidized, inactive Fe3+-containing native P. testosteroni dioxygenase; reduction…]

Components and activities

Declared biological components and source reaction directions
NodeKind or roleSource direction
Comamonas testosteroni
NCBITaxon:285		taxon
Delftia acidovorans
NCBITaxon:80866		taxon
Phytopseudomonas straminea
NCBITaxon:47882		taxon
Sphingomonas sp. SYK6
NCBITaxon:502559		taxon
Pseudomonas putida
NCBITaxon:303		taxon
Pseudomonas putida KT2440
NCBITaxon:160488		taxon
dioxygen
CHEBI:15379		small molecule
3,4-dihydroxybenzoate
CHEBI:36241		small molecule
hydron
CHEBI:15378		small molecule
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde(2-)
CHEBI:58358		small molecule
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal(2-)
CHEBI:61985		small molecule
NADP(3-)
CHEBI:58349		cofactor
2-oxo-2H-pyran-4,6-dicarboxylate
CHEBI:58304		small molecule
NADPH(4-)
CHEBI:57783		small molecule
water
CHEBI:15377		small molecule
(1E)-4-oxobut-1-ene-1,2,4-tricarboxylate
CHEBI:57471		small molecule
4-carboxy-2-hydroxy-cis,cis-muconate(3-)
CHEBI:58142		small molecule
2-hydroxy-4-oxobutane-1,2,4-tricarboxylate
CHEBI:58075		small molecule
pyruvate
CHEBI:15361		small molecule
oxaloacetate(2-)
CHEBI:16452		small molecule
carbon dioxide
CHEBI:16526		small molecule
protocatechuate 4,5-dioxygenase
MetaCyc:CPLX-2701		complex
4-oxalomesaconate hydratase
MetaCyc:CPLX-2781		complex
HMG aldolase
MetaCyc:CPLX-2782		complex
4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase
MetaCyc:CPLX-2861		complex
2-hydroxy-4-carboxymuconate-6-semialdehyde dehydrogenase
MetaCyc:CPLX-2863		complex
4-carboxy-4-hydroxy-2-oxoadipate aldolase
MetaCyc:CPLX-2865		complex
HMG aldolase
MetaCyc:CPLX-2881		complex
protocatechuate 4,5-dioxygenase
MetaCyc:CPLX-7916		complex
HMG aldolase
MetaCyc:CPLX-7917		complex
4-oxalmesaconate hydratase
MetaCyc:CPLX-8178		complex
4-hydroxy-4-methyl-2-oxoglutarate aldolase
MetaCyc:CPLX1G01-155		complex
4-oxalomesaconate tautomerase
MetaCyc:G1G01-2697-MONOMER		protein
4-hydroxy-4-methyl-2-oxoglutarate aldolase aldolase
MetaCyc:G1G01-2698-MONOMER		protein
4-oxalmesaconate hydratase monomer
MetaCyc:G1G01-2699-MONOMER		protein
2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-10723		protein
protocatechuate 4,5-dioxygenase alpha chain
MetaCyc:MONOMER-15116		protein
protocatechuate 4,5-dioxygenase beta chain
MetaCyc:MONOMER-15117		protein
protocatechuate 4,5-dioxygenase α subunit
MetaCyc:MONOMER-3165		protein
protocatechuate 4,5-dioxygenase β subunit
MetaCyc:MONOMER-3166		protein
2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-3182		protein
HMG aldolase monomer
MetaCyc:MONOMER-3184		protein
subunit of 4-oxalomesaconate hydratase
MetaCyc:MONOMER-3243		protein
4-oxalocitramalate aldolase subunit
MetaCyc:MONOMER-3244		protein
2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-3463		protein
LigC
MetaCyc:MONOMER-3466		protein
2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-3467		protein
LigK
MetaCyc:MONOMER-3469		protein
subunit of 4-hydroxy-4-methyl-2-oxoglutarate aldolase
MetaCyc:MONOMER-3481		protein
α-hydroxy-γ-carboxymuconate ε-semialdehyde dehydrogenase subunit
MetaCyc:MONOMER-8501		protein
magnesium(2+)
CHEBI:18420		cofactor
zinc(2+)
CHEBI:29105		cofactor
iron(2+)
CHEBI:29033		cofactor
manganese(2+)
CHEBI:29035		cofactor
N-ethylmaleimide
MetaCyc:N-ETHYLMALEIMIDE		small molecule
p-chloromercuribenzoate
MetaCyc:CPD-29		small molecule
iodoacetate
MetaCyc:IODOACETATE		small molecule
cobalt(2+)
CHEBI:48828		cofactor
copper(2+)
CHEBI:29036		small molecule
nickel(2+)
CHEBI:49786		small molecule
mercury(2+)
CHEBI:16793		small molecule
5,5'-dithio-bis-2-nitrobenzoate
MetaCyc:DITHIO-NITROBENZOATE		small molecule
copper sulfate
MetaCyc:CUSO4		small molecule
NAD(1-)
CHEBI:57540		cofactor
cadmium(2+)
CHEBI:48775		cofactor
LigR protein
UniProtKB:Q8RQV9		protein
hydrogen peroxide
CHEBI:16240		small molecule
ascorbate
CHEBI:22651		chemical entity
3,4-dihydroxybenzoate + O2 => 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + H(+)
RHEA:24045		molecular activityleft to right
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal formation
MetaCyc:R107-RXN		molecular activityleft to right
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP(+) => 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H(+)
RHEA:29588		molecular activityleft to right
2-oxo-2H-pyran-4,6-dicarboxylate + H2O => (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate + H(+)
RHEA:10645		molecular activityleft to right
(1E)-4-oxobut-1-ene-1,2,4-tricarboxylate => 4-carboxy-2-hydroxy-cis,cis-muconate
RHEA:28932		molecular activityreversible
4-carboxy-2-hydroxy-cis,cis-muconate + H2O => 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate
RHEA:17403		molecular activityreversible
2-hydroxy-4-oxobutane-1,2,4-tricarboxylate => oxaloacetate + pyruvate
RHEA:28936		molecular activityreversible
oxaloacetate + H(+) => pyruvate + CO2
RHEA:15642		molecular activityleft to right

Mechanistic edges

Mechanistic edges and their cited evidence
SubjectPredicate and descriptionObjectEvidence
3,4-dihydroxybenzoate + O2 => 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + H(+)
RHEA:24045		part_of

Member of the complete eight-step source-defined pathway. Material edges use the pathway-selected forward conversion.

MetaCyc:P184-PWY
  • MetaCyc:P184-PWY

    Source assertion: The native pathway explicitly lists PROTOCATECHUATE-45-DIOXYGENASE-RXN and selects L2R layout flux.

    Source location/ptools-xml/Pathway/reaction-list/Reaction[@frameid='PROTOCATECHUATE-45-DIOXYGENASE-RXN']; /ptools-xml/Pathway/reaction-layout[Reaction/@frameid='PROTOCATECHUATE-45-DIOXYGENASE-RXN']
dioxygen
CHEBI:15379		consumes

Coefficient 1 in the selected pathway flux.

3,4-dihydroxybenzoate + O2 => 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + H(+)
RHEA:24045
  • MetaCyc:PROTOCATECHUATE-45-DIOXYGENASE-RXN

    Source assertion: The complete native reaction left side contains OXYGEN-MOLECULE with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='PROTOCATECHUATE-45-DIOXYGENASE-RXN']/left[Compound/@frameid='OXYGEN-MOLECULE']
  • RHEA:24045

    Source assertion: RHEA:24045 substrates contain CHEBI:15379 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/24045 rh:substrates http://rdf.rhea-db.org/24044_L; http://rdf.rhea-db.org/24044_L rh:contains1 http://rdf.rhea-db.org/Participant_24044_compound_1198; http://rdf.rhea-db.org/Participant_24044_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

Coefficient 1 in the selected pathway flux.

3,4-dihydroxybenzoate + O2 => 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + H(+)
RHEA:24045
  • MetaCyc:PROTOCATECHUATE-45-DIOXYGENASE-RXN

    Source assertion: The complete native reaction left side contains 3-4-DIHYDROXYBENZOATE with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='PROTOCATECHUATE-45-DIOXYGENASE-RXN']/left[Compound/@frameid='3-4-DIHYDROXYBENZOATE']
  • RHEA:24045

    Source assertion: RHEA:24045 substrates contain CHEBI:36241 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/24045 rh:substrates http://rdf.rhea-db.org/24044_L; http://rdf.rhea-db.org/24044_L rh:contains1 http://rdf.rhea-db.org/Participant_24044_compound_3099; http://rdf.rhea-db.org/Participant_24044_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 => 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + H(+)
RHEA:24045		produces

Coefficient 1 in the selected pathway flux.

hydron
CHEBI:15378
  • MetaCyc:PROTOCATECHUATE-45-DIOXYGENASE-RXN

    Source assertion: The complete native reaction right side contains PROTON with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='PROTOCATECHUATE-45-DIOXYGENASE-RXN']/right[Compound/@frameid='PROTON']
  • RHEA:24045

    Source assertion: RHEA:24045 products contain CHEBI:15378 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/24045 rh:products http://rdf.rhea-db.org/24044_R; http://rdf.rhea-db.org/24044_R rh:contains1 http://rdf.rhea-db.org/Participant_24044_compound_3249; http://rdf.rhea-db.org/Participant_24044_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 => 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + H(+)
RHEA:24045		produces

Coefficient 1 in the selected pathway flux.

4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde(2-)
CHEBI:58358
  • MetaCyc:PROTOCATECHUATE-45-DIOXYGENASE-RXN

    Source assertion: The complete native reaction right side contains CPD-87 with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='PROTOCATECHUATE-45-DIOXYGENASE-RXN']/right[Compound/@frameid='CPD-87']
  • RHEA:24045

    Source assertion: RHEA:24045 products contain CHEBI:58358 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/24045 rh:products http://rdf.rhea-db.org/24044_R; http://rdf.rhea-db.org/24044_R rh:contains1 http://rdf.rhea-db.org/Participant_24044_compound_1799; http://rdf.rhea-db.org/Participant_24044_compound_1799 rh:compound http://rdf.rhea-db.org/Compound_1799; http://rdf.rhea-db.org/Compound_1799 rh:chebi http://purl.obolibrary.org/obo/CHEBI_58358
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal formation
MetaCyc:R107-RXN		part_of

Member of the complete eight-step source-defined pathway. Material edges use the pathway-selected forward conversion. Native spontaneous=true permits uncatalyzed conversion without asserting its physiological rate or excluding enzyme acceleration.

MetaCyc:P184-PWY
  • MetaCyc:P184-PWY

    Source assertion: The native pathway explicitly lists R107-RXN and selects L2R layout flux.

    Source location/ptools-xml/Pathway/reaction-list/Reaction[@frameid='R107-RXN']; /ptools-xml/Pathway/reaction-layout[Reaction/@frameid='R107-RXN']
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde(2-)
CHEBI:58358		consumes

Coefficient 1 in the selected pathway flux.

4-carboxy-2-hydroxymuconate semialdehyde hemiacetal formation
MetaCyc:R107-RXN
  • MetaCyc:R107-RXN

    Source assertion: The complete native reaction left side contains CPD-87 with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='R107-RXN']/left[Compound/@frameid='CPD-87']
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal formation
MetaCyc:R107-RXN		produces

Coefficient 1 in the selected pathway flux.

4-carboxy-2-hydroxymuconate semialdehyde hemiacetal(2-)
CHEBI:61985
  • MetaCyc:R107-RXN

    Source assertion: The complete native reaction right side contains CPD-2542 with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='R107-RXN']/right[Compound/@frameid='CPD-2542']
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP(+) => 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H(+)
RHEA:29588		part_of

Member of the complete eight-step source-defined pathway. Material edges use the pathway-selected forward conversion. The native obsolete RHEA:10889 cross-reference is replaced only after exact equation comparison by approved RHEA:29588.

MetaCyc:P184-PWY
  • MetaCyc:P184-PWY

    Source assertion: The native pathway explicitly lists 1.2.1.45-RXN and selects L2R layout flux.

    Source location/ptools-xml/Pathway/reaction-list/Reaction[@frameid='1.2.1.45-RXN']; /ptools-xml/Pathway/reaction-layout[Reaction/@frameid='1.2.1.45-RXN']
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal(2-)
CHEBI:61985		consumes

Coefficient 1 in the selected pathway flux.

4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP(+) => 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H(+)
RHEA:29588
  • MetaCyc:1.2.1.45-RXN

    Source assertion: The complete native reaction left side contains CPD-2542 with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='1.2.1.45-RXN']/left[Compound/@frameid='CPD-2542']
  • RHEA:29588

    Source assertion: RHEA:29588 substrates contain CHEBI:61985 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/29588 rh:substrates http://rdf.rhea-db.org/29587_L; http://rdf.rhea-db.org/29587_L rh:contains1 http://rdf.rhea-db.org/Participant_29587_compound_6580; http://rdf.rhea-db.org/Participant_29587_compound_6580 rh:compound http://rdf.rhea-db.org/Compound_6580; http://rdf.rhea-db.org/Compound_6580 rh:chebi http://purl.obolibrary.org/obo/CHEBI_61985
NADP(3-)
CHEBI:58349		consumes

Coefficient 1 in the selected pathway flux.

4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP(+) => 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H(+)
RHEA:29588
  • MetaCyc:1.2.1.45-RXN

    Source assertion: The complete native reaction left side contains NADP with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='1.2.1.45-RXN']/left[Compound/@frameid='NADP']
  • RHEA:29588

    Source assertion: RHEA:29588 substrates contain CHEBI:58349 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/29588 rh:substrates http://rdf.rhea-db.org/29587_L; http://rdf.rhea-db.org/29587_L rh:contains1 http://rdf.rhea-db.org/Participant_29587_compound_5188; http://rdf.rhea-db.org/Participant_29587_compound_5188 rh:compound http://rdf.rhea-db.org/Compound_5188; http://rdf.rhea-db.org/Compound_5188 rh:chebi http://purl.obolibrary.org/obo/CHEBI_58349
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP(+) => 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H(+)
RHEA:29588		produces

Coefficient 1 in the selected pathway flux.

2-oxo-2H-pyran-4,6-dicarboxylate
CHEBI:58304
  • MetaCyc:1.2.1.45-RXN

    Source assertion: The complete native reaction right side contains CPD-184 with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='1.2.1.45-RXN']/right[Compound/@frameid='CPD-184']
  • RHEA:29588

    Source assertion: RHEA:29588 products contain CHEBI:58304 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/29588 rh:products http://rdf.rhea-db.org/29587_R; http://rdf.rhea-db.org/29587_R rh:contains1 http://rdf.rhea-db.org/Participant_29587_compound_1788; http://rdf.rhea-db.org/Participant_29587_compound_1788 rh:compound http://rdf.rhea-db.org/Compound_1788; http://rdf.rhea-db.org/Compound_1788 rh:chebi http://purl.obolibrary.org/obo/CHEBI_58304
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP(+) => 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H(+)
RHEA:29588		produces

Coefficient 1 in the selected pathway flux.

NADPH(4-)
CHEBI:57783
  • MetaCyc:1.2.1.45-RXN

    Source assertion: The complete native reaction right side contains NADPH with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='1.2.1.45-RXN']/right[Compound/@frameid='NADPH']
  • RHEA:29588

    Source assertion: RHEA:29588 products contain CHEBI:57783 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/29588 rh:products http://rdf.rhea-db.org/29587_R; http://rdf.rhea-db.org/29587_R rh:contains1 http://rdf.rhea-db.org/Participant_29587_compound_3438; http://rdf.rhea-db.org/Participant_29587_compound_3438 rh:compound http://rdf.rhea-db.org/Compound_3438; http://rdf.rhea-db.org/Compound_3438 rh:chebi http://purl.obolibrary.org/obo/CHEBI_57783
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP(+) => 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H(+)
RHEA:29588		produces

Coefficient 1 in the selected pathway flux.

hydron
CHEBI:15378
  • MetaCyc:1.2.1.45-RXN

    Source assertion: The complete native reaction right side contains PROTON with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='1.2.1.45-RXN']/right[Compound/@frameid='PROTON']
  • RHEA:29588

    Source assertion: RHEA:29588 products contain CHEBI:15378 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/29588 rh:products http://rdf.rhea-db.org/29587_R; http://rdf.rhea-db.org/29587_R rh:contains1 http://rdf.rhea-db.org/Participant_29587_compound_3249; http://rdf.rhea-db.org/Participant_29587_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
2-oxo-2H-pyran-4,6-dicarboxylate + H2O => (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate + H(+)
RHEA:10645		part_of

Member of the complete eight-step source-defined pathway. Material edges use the pathway-selected forward conversion.

MetaCyc:P184-PWY
  • MetaCyc:P184-PWY

    Source assertion: The native pathway explicitly lists RXN-2462 and selects L2R layout flux.

    Source location/ptools-xml/Pathway/reaction-list/Reaction[@frameid='RXN-2462']; /ptools-xml/Pathway/reaction-layout[Reaction/@frameid='RXN-2462']
2-oxo-2H-pyran-4,6-dicarboxylate
CHEBI:58304		consumes

Coefficient 1 in the selected pathway flux.

2-oxo-2H-pyran-4,6-dicarboxylate + H2O => (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate + H(+)
RHEA:10645
  • MetaCyc:RXN-2462

    Source assertion: The complete native reaction left side contains CPD-184 with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='RXN-2462']/left[Compound/@frameid='CPD-184']
  • RHEA:10645

    Source assertion: RHEA:10645 substrates contain CHEBI:58304 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/10645 rh:substrates http://rdf.rhea-db.org/10644_L; http://rdf.rhea-db.org/10644_L rh:contains1 http://rdf.rhea-db.org/Participant_10644_compound_1788; http://rdf.rhea-db.org/Participant_10644_compound_1788 rh:compound http://rdf.rhea-db.org/Compound_1788; http://rdf.rhea-db.org/Compound_1788 rh:chebi http://purl.obolibrary.org/obo/CHEBI_58304
water
CHEBI:15377		consumes

Coefficient 1 in the selected pathway flux.

2-oxo-2H-pyran-4,6-dicarboxylate + H2O => (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate + H(+)
RHEA:10645
  • MetaCyc:RXN-2462

    Source assertion: The complete native reaction left side contains WATER with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='RXN-2462']/left[Compound/@frameid='WATER']
  • RHEA:10645

    Source assertion: RHEA:10645 substrates contain CHEBI:15377 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/10645 rh:substrates http://rdf.rhea-db.org/10644_L; http://rdf.rhea-db.org/10644_L rh:contains1 http://rdf.rhea-db.org/Participant_10644_compound_1283; http://rdf.rhea-db.org/Participant_10644_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
2-oxo-2H-pyran-4,6-dicarboxylate + H2O => (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate + H(+)
RHEA:10645		produces

Coefficient 1 in the selected pathway flux.

(1E)-4-oxobut-1-ene-1,2,4-tricarboxylate
CHEBI:57471
  • MetaCyc:RXN-2462

    Source assertion: The complete native reaction right side contains 4-OXALOMESACONATE with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='RXN-2462']/right[Compound/@frameid='4-OXALOMESACONATE']
  • RHEA:10645

    Source assertion: RHEA:10645 products contain CHEBI:57471 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/10645 rh:products http://rdf.rhea-db.org/10644_R; http://rdf.rhea-db.org/10644_R rh:contains1 http://rdf.rhea-db.org/Participant_10644_compound_1770; http://rdf.rhea-db.org/Participant_10644_compound_1770 rh:compound http://rdf.rhea-db.org/Compound_1770; http://rdf.rhea-db.org/Compound_1770 rh:chebi http://purl.obolibrary.org/obo/CHEBI_57471
2-oxo-2H-pyran-4,6-dicarboxylate + H2O => (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate + H(+)
RHEA:10645		produces

Coefficient 1 in the selected pathway flux.

hydron
CHEBI:15378
  • MetaCyc:RXN-2462

    Source assertion: The complete native reaction right side contains PROTON with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='RXN-2462']/right[Compound/@frameid='PROTON']
  • RHEA:10645

    Source assertion: RHEA:10645 products contain CHEBI:15378 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/10645 rh:products http://rdf.rhea-db.org/10644_R; http://rdf.rhea-db.org/10644_R rh:contains1 http://rdf.rhea-db.org/Participant_10644_compound_3249; http://rdf.rhea-db.org/Participant_10644_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
(1E)-4-oxobut-1-ene-1,2,4-tricarboxylate => 4-carboxy-2-hydroxy-cis,cis-muconate
RHEA:28932		part_of

Member of the complete eight-step source-defined pathway. Material edges use the pathway-selected forward conversion. Native reversible metadata is retained alongside the selected forward Rhea equation identity. Native spontaneous=true permits uncatalyzed conversion without asserting its physiological rate or excluding enzyme acceleration.

MetaCyc:P184-PWY
  • MetaCyc:P184-PWY

    Source assertion: The native pathway explicitly lists RXN-9983 and selects L2R layout flux.

    Source location/ptools-xml/Pathway/reaction-list/Reaction[@frameid='RXN-9983']; /ptools-xml/Pathway/reaction-layout[Reaction/@frameid='RXN-9983']
(1E)-4-oxobut-1-ene-1,2,4-tricarboxylate
CHEBI:57471		consumes

Coefficient 1 in the selected pathway flux.

(1E)-4-oxobut-1-ene-1,2,4-tricarboxylate => 4-carboxy-2-hydroxy-cis,cis-muconate
RHEA:28932
  • MetaCyc:RXN-9983

    Source assertion: The complete native reaction left side contains 4-OXALOMESACONATE with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='RXN-9983']/left[Compound/@frameid='4-OXALOMESACONATE']
  • RHEA:28932

    Source assertion: RHEA:28932 substrates contain CHEBI:57471 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/28932 rh:substrates http://rdf.rhea-db.org/28931_L; http://rdf.rhea-db.org/28931_L rh:contains1 http://rdf.rhea-db.org/Participant_28931_compound_1770; http://rdf.rhea-db.org/Participant_28931_compound_1770 rh:compound http://rdf.rhea-db.org/Compound_1770; http://rdf.rhea-db.org/Compound_1770 rh:chebi http://purl.obolibrary.org/obo/CHEBI_57471
(1E)-4-oxobut-1-ene-1,2,4-tricarboxylate => 4-carboxy-2-hydroxy-cis,cis-muconate
RHEA:28932		produces

Coefficient 1 in the selected pathway flux. Exact native E,E enol; historical cis,cis display terminology does not equate it to KCH or the Z,Z enol.

4-carboxy-2-hydroxy-cis,cis-muconate(3-)
CHEBI:58142
  • MetaCyc:RXN-9983

    Source assertion: The complete native reaction right side contains CPD-12849 with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='RXN-9983']/right[Compound/@frameid='CPD-12849']
  • RHEA:28932

    Source assertion: RHEA:28932 products contain CHEBI:58142 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/28932 rh:products http://rdf.rhea-db.org/28931_R; http://rdf.rhea-db.org/28931_R rh:contains1 http://rdf.rhea-db.org/Participant_28931_compound_3844; http://rdf.rhea-db.org/Participant_28931_compound_3844 rh:compound http://rdf.rhea-db.org/Compound_3844; http://rdf.rhea-db.org/Compound_3844 rh:chebi http://purl.obolibrary.org/obo/CHEBI_58142
4-carboxy-2-hydroxy-cis,cis-muconate + H2O => 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate
RHEA:17403		part_of

Member of the complete eight-step source-defined pathway. Material edges use the pathway-selected forward conversion. The selected hydration runs opposite to the native reaction object written as dehydration. Native reversible metadata is retained alongside the selected forward Rhea equation identity.

MetaCyc:P184-PWY
  • MetaCyc:P184-PWY

    Source assertion: The native pathway explicitly lists RXN-2463 and selects R2L layout flux.

    Source location/ptools-xml/Pathway/reaction-list/Reaction[@frameid='RXN-2463']; /ptools-xml/Pathway/reaction-layout[Reaction/@frameid='RXN-2463']
4-carboxy-2-hydroxy-cis,cis-muconate(3-)
CHEBI:58142		consumes

Coefficient 1 in the selected pathway flux. Exact native E,E enol; historical cis,cis display terminology does not equate it to KCH or the Z,Z enol.

4-carboxy-2-hydroxy-cis,cis-muconate + H2O => 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate
RHEA:17403
  • MetaCyc:RXN-2463

    Source assertion: The complete native reaction right side contains CPD-12849 with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='RXN-2463']/right[Compound/@frameid='CPD-12849']
  • RHEA:17403

    Source assertion: RHEA:17403 substrates contain CHEBI:58142 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/17403 rh:substrates http://rdf.rhea-db.org/17401_R; http://rdf.rhea-db.org/17401_R rh:contains1 http://rdf.rhea-db.org/Participant_17401_compound_3844; http://rdf.rhea-db.org/Participant_17401_compound_3844 rh:compound http://rdf.rhea-db.org/Compound_3844; http://rdf.rhea-db.org/Compound_3844 rh:chebi http://purl.obolibrary.org/obo/CHEBI_58142
water
CHEBI:15377		consumes

Coefficient 1 in the selected pathway flux.

4-carboxy-2-hydroxy-cis,cis-muconate + H2O => 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate
RHEA:17403
  • MetaCyc:RXN-2463

    Source assertion: The complete native reaction right side contains WATER with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='RXN-2463']/right[Compound/@frameid='WATER']
  • RHEA:17403

    Source assertion: RHEA:17403 substrates contain CHEBI:15377 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/17403 rh:substrates http://rdf.rhea-db.org/17401_R; http://rdf.rhea-db.org/17401_R rh:contains1 http://rdf.rhea-db.org/Participant_17401_compound_1283; http://rdf.rhea-db.org/Participant_17401_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
4-carboxy-2-hydroxy-cis,cis-muconate + H2O => 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate
RHEA:17403		produces

Coefficient 1 in the selected pathway flux. Native structure leaves absolute configuration unspecified; no racemic mixture or S-specific product is inferred.

2-hydroxy-4-oxobutane-1,2,4-tricarboxylate
CHEBI:58075
  • MetaCyc:RXN-2463

    Source assertion: The complete native reaction left side contains 4-OH-4-ACETYL-2-OXOGLUTARATE with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='RXN-2463']/left[Compound/@frameid='4-OH-4-ACETYL-2-OXOGLUTARATE']
  • RHEA:17403

    Source assertion: RHEA:17403 products contain CHEBI:58075 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/17403 rh:products http://rdf.rhea-db.org/17401_L; http://rdf.rhea-db.org/17401_L rh:contains1 http://rdf.rhea-db.org/Participant_17401_compound_2617; http://rdf.rhea-db.org/Participant_17401_compound_2617 rh:compound http://rdf.rhea-db.org/Compound_2617; http://rdf.rhea-db.org/Compound_2617 rh:chebi http://purl.obolibrary.org/obo/CHEBI_58075
2-hydroxy-4-oxobutane-1,2,4-tricarboxylate => oxaloacetate + pyruvate
RHEA:28936		part_of

Member of the complete eight-step source-defined pathway. Material edges use the pathway-selected forward conversion. Native reversible metadata is retained alongside the selected forward Rhea equation identity.

MetaCyc:P184-PWY
  • MetaCyc:P184-PWY

    Source assertion: The native pathway explicitly lists RXN-2464 and selects L2R layout flux.

    Source location/ptools-xml/Pathway/reaction-list/Reaction[@frameid='RXN-2464']; /ptools-xml/Pathway/reaction-layout[Reaction/@frameid='RXN-2464']
2-hydroxy-4-oxobutane-1,2,4-tricarboxylate
CHEBI:58075		consumes

Coefficient 1 in the selected pathway flux. Native structure leaves absolute configuration unspecified; no racemic mixture or S-specific product is inferred.

2-hydroxy-4-oxobutane-1,2,4-tricarboxylate => oxaloacetate + pyruvate
RHEA:28936
  • MetaCyc:RXN-2464

    Source assertion: The complete native reaction left side contains 4-OH-4-ACETYL-2-OXOGLUTARATE with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='RXN-2464']/left[Compound/@frameid='4-OH-4-ACETYL-2-OXOGLUTARATE']
  • RHEA:28936

    Source assertion: RHEA:28936 substrates contain CHEBI:58075 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/28936 rh:substrates http://rdf.rhea-db.org/28935_L; http://rdf.rhea-db.org/28935_L rh:contains1 http://rdf.rhea-db.org/Participant_28935_compound_2617; http://rdf.rhea-db.org/Participant_28935_compound_2617 rh:compound http://rdf.rhea-db.org/Compound_2617; http://rdf.rhea-db.org/Compound_2617 rh:chebi http://purl.obolibrary.org/obo/CHEBI_58075
2-hydroxy-4-oxobutane-1,2,4-tricarboxylate => oxaloacetate + pyruvate
RHEA:28936		produces

Coefficient 1 in the selected pathway flux.

pyruvate
CHEBI:15361
  • MetaCyc:RXN-2464

    Source assertion: The complete native reaction right side contains PYRUVATE with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='RXN-2464']/right[Compound/@frameid='PYRUVATE']
  • RHEA:28936

    Source assertion: RHEA:28936 products contain CHEBI:15361 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/28936 rh:products http://rdf.rhea-db.org/28935_R; http://rdf.rhea-db.org/28935_R rh:contains1 http://rdf.rhea-db.org/Participant_28935_compound_3719; http://rdf.rhea-db.org/Participant_28935_compound_3719 rh:compound http://rdf.rhea-db.org/Compound_3719; http://rdf.rhea-db.org/Compound_3719 rh:chebi http://purl.obolibrary.org/obo/CHEBI_15361
2-hydroxy-4-oxobutane-1,2,4-tricarboxylate => oxaloacetate + pyruvate
RHEA:28936		produces

Coefficient 1 in the selected pathway flux.

oxaloacetate(2-)
CHEBI:16452
  • MetaCyc:RXN-2464

    Source assertion: The complete native reaction right side contains OXALACETIC_ACID with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='RXN-2464']/right[Compound/@frameid='OXALACETIC_ACID']
  • RHEA:28936

    Source assertion: RHEA:28936 products contain CHEBI:16452 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/28936 rh:products http://rdf.rhea-db.org/28935_R; http://rdf.rhea-db.org/28935_R rh:contains1 http://rdf.rhea-db.org/Participant_28935_compound_5219; http://rdf.rhea-db.org/Participant_28935_compound_5219 rh:compound http://rdf.rhea-db.org/Compound_5219; http://rdf.rhea-db.org/Compound_5219 rh:chebi http://purl.obolibrary.org/obo/CHEBI_16452
oxaloacetate + H(+) => pyruvate + CO2
RHEA:15642		part_of

Member of the complete eight-step source-defined pathway. Material edges use the pathway-selected forward conversion.

MetaCyc:P184-PWY
  • MetaCyc:P184-PWY

    Source assertion: The native pathway explicitly lists OXALODECARB-RXN and selects L2R layout flux.

    Source location/ptools-xml/Pathway/reaction-list/Reaction[@frameid='OXALODECARB-RXN']; /ptools-xml/Pathway/reaction-layout[Reaction/@frameid='OXALODECARB-RXN']
oxaloacetate(2-)
CHEBI:16452		consumes

Coefficient 1 in the selected pathway flux.

oxaloacetate + H(+) => pyruvate + CO2
RHEA:15642
  • MetaCyc:OXALODECARB-RXN

    Source assertion: The complete native reaction left side contains OXALACETIC_ACID with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='OXALODECARB-RXN']/left[Compound/@frameid='OXALACETIC_ACID']
  • RHEA:15642

    Source assertion: RHEA:15642 substrates contain CHEBI:16452 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/15642 rh:substrates http://rdf.rhea-db.org/15641_L; http://rdf.rhea-db.org/15641_L rh:contains1 http://rdf.rhea-db.org/Participant_15641_compound_5219; http://rdf.rhea-db.org/Participant_15641_compound_5219 rh:compound http://rdf.rhea-db.org/Compound_5219; http://rdf.rhea-db.org/Compound_5219 rh:chebi http://purl.obolibrary.org/obo/CHEBI_16452
hydron
CHEBI:15378		consumes

Coefficient 1 in the selected pathway flux.

oxaloacetate + H(+) => pyruvate + CO2
RHEA:15642
  • MetaCyc:OXALODECARB-RXN

    Source assertion: The complete native reaction left side contains PROTON with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='OXALODECARB-RXN']/left[Compound/@frameid='PROTON']
  • RHEA:15642

    Source assertion: RHEA:15642 substrates contain CHEBI:15378 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/15642 rh:substrates http://rdf.rhea-db.org/15641_L; http://rdf.rhea-db.org/15641_L rh:contains1 http://rdf.rhea-db.org/Participant_15641_compound_3249; http://rdf.rhea-db.org/Participant_15641_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
oxaloacetate + H(+) => pyruvate + CO2
RHEA:15642		produces

Coefficient 1 in the selected pathway flux.

pyruvate
CHEBI:15361
  • MetaCyc:OXALODECARB-RXN

    Source assertion: The complete native reaction right side contains PYRUVATE with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='OXALODECARB-RXN']/right[Compound/@frameid='PYRUVATE']
  • RHEA:15642

    Source assertion: RHEA:15642 products contain CHEBI:15361 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/15642 rh:products http://rdf.rhea-db.org/15641_R; http://rdf.rhea-db.org/15641_R rh:contains1 http://rdf.rhea-db.org/Participant_15641_compound_3719; http://rdf.rhea-db.org/Participant_15641_compound_3719 rh:compound http://rdf.rhea-db.org/Compound_3719; http://rdf.rhea-db.org/Compound_3719 rh:chebi http://purl.obolibrary.org/obo/CHEBI_15361
oxaloacetate + H(+) => pyruvate + CO2
RHEA:15642		produces

Coefficient 1 in the selected pathway flux.

carbon dioxide
CHEBI:16526
  • MetaCyc:OXALODECARB-RXN

    Source assertion: The complete native reaction right side contains CARBON-DIOXIDE with coefficient 1.

    Source location/ptools-xml/Reaction[@frameid='OXALODECARB-RXN']/right[Compound/@frameid='CARBON-DIOXIDE']
  • RHEA:15642

    Source assertion: RHEA:15642 products contain CHEBI:16526 with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/15642 rh:products http://rdf.rhea-db.org/15641_R; http://rdf.rhea-db.org/15641_R rh:contains1 http://rdf.rhea-db.org/Participant_15641_compound_4391; http://rdf.rhea-db.org/Participant_15641_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
2-hydroxy-4-oxobutane-1,2,4-tricarboxylate => oxaloacetate + pyruvate
RHEA:28936		provides_input_for

Selected pathway material transfer through CHEBI:16452. This source ordering does not assert an additional regulatory effect.

oxaloacetate + H(+) => pyruvate + CO2
RHEA:15642
  • MetaCyc:P184-PWY

    Source assertion: The pathway names RXN-2464 as a predecessor of OXALODECARB-RXN; selected reaction layouts transfer CHEBI:16452.

    Source location/ptools-xml/Pathway/reaction-ordering[Reaction/@frameid='OXALODECARB-RXN']/predecessor-reactions/Reaction[@frameid='RXN-2464']; /ptools-xml/Pathway/reaction-layout
(1E)-4-oxobut-1-ene-1,2,4-tricarboxylate => 4-carboxy-2-hydroxy-cis,cis-muconate
RHEA:28932		provides_input_for

Selected pathway material transfer through CHEBI:58142. This source ordering does not assert an additional regulatory effect.

4-carboxy-2-hydroxy-cis,cis-muconate + H2O => 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate
RHEA:17403
  • MetaCyc:P184-PWY

    Source assertion: The pathway names RXN-9983 as a predecessor of RXN-2463; selected reaction layouts transfer CHEBI:58142.

    Source location/ptools-xml/Pathway/reaction-ordering[Reaction/@frameid='RXN-2463']/predecessor-reactions/Reaction[@frameid='RXN-9983']; /ptools-xml/Pathway/reaction-layout
2-oxo-2H-pyran-4,6-dicarboxylate + H2O => (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate + H(+)
RHEA:10645		provides_input_for

Selected pathway material transfer through CHEBI:57471. This source ordering does not assert an additional regulatory effect.

(1E)-4-oxobut-1-ene-1,2,4-tricarboxylate => 4-carboxy-2-hydroxy-cis,cis-muconate
RHEA:28932
  • MetaCyc:P184-PWY

    Source assertion: The pathway names RXN-2462 as a predecessor of RXN-9983; selected reaction layouts transfer CHEBI:57471.

    Source location/ptools-xml/Pathway/reaction-ordering[Reaction/@frameid='RXN-9983']/predecessor-reactions/Reaction[@frameid='RXN-2462']; /ptools-xml/Pathway/reaction-layout
3,4-dihydroxybenzoate + O2 => 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + H(+)
RHEA:24045		provides_input_for

Selected pathway material transfer through CHEBI:58358. This source ordering does not assert an additional regulatory effect.

4-carboxy-2-hydroxymuconate semialdehyde hemiacetal formation
MetaCyc:R107-RXN
  • MetaCyc:P184-PWY

    Source assertion: The pathway names PROTOCATECHUATE-45-DIOXYGENASE-RXN as a predecessor of R107-RXN; selected reaction layouts transfer CHEBI:58358.

    Source location/ptools-xml/Pathway/reaction-ordering[Reaction/@frameid='R107-RXN']/predecessor-reactions/Reaction[@frameid='PROTOCATECHUATE-45-DIOXYGENASE-RXN']; /ptools-xml/Pathway/reaction-layout
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal formation
MetaCyc:R107-RXN		provides_input_for

Selected pathway material transfer through CHEBI:61985. This source ordering does not assert an additional regulatory effect.

4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP(+) => 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H(+)
RHEA:29588
  • MetaCyc:P184-PWY

    Source assertion: The pathway names R107-RXN as a predecessor of 1.2.1.45-RXN; selected reaction layouts transfer CHEBI:61985.

    Source location/ptools-xml/Pathway/reaction-ordering[Reaction/@frameid='1.2.1.45-RXN']/predecessor-reactions/Reaction[@frameid='R107-RXN']; /ptools-xml/Pathway/reaction-layout
4-carboxy-2-hydroxy-cis,cis-muconate + H2O => 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate
RHEA:17403		provides_input_for

Selected pathway material transfer through CHEBI:58075. This source ordering does not assert an additional regulatory effect.

2-hydroxy-4-oxobutane-1,2,4-tricarboxylate => oxaloacetate + pyruvate
RHEA:28936
  • MetaCyc:P184-PWY

    Source assertion: The pathway names RXN-2463 as a predecessor of RXN-2464; selected reaction layouts transfer CHEBI:58075.

    Source location/ptools-xml/Pathway/reaction-ordering[Reaction/@frameid='RXN-2464']/predecessor-reactions/Reaction[@frameid='RXN-2463']; /ptools-xml/Pathway/reaction-layout
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP(+) => 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H(+)
RHEA:29588		provides_input_for

Selected pathway material transfer through CHEBI:58304. This source ordering does not assert an additional regulatory effect.

2-oxo-2H-pyran-4,6-dicarboxylate + H2O => (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate + H(+)
RHEA:10645
  • MetaCyc:P184-PWY

    Source assertion: The pathway names 1.2.1.45-RXN as a predecessor of RXN-2462; selected reaction layouts transfer CHEBI:58304.

    Source location/ptools-xml/Pathway/reaction-ordering[Reaction/@frameid='RXN-2462']/predecessor-reactions/Reaction[@frameid='1.2.1.45-RXN']; /ptools-xml/Pathway/reaction-layout
2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-10723		catalyzes

Unpurified PDC-hydrolase from P. putida PDC selected on PDC. This strain uses ortho cleavage for PCA in the 1982 primary; no full P184 occurrence inference.

2-oxo-2H-pyran-4,6-dicarboxylate + H2O => (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate + H(+)
RHEA:10645
  • MetaCyc:ENZRXN-11003

    Source assertion: The enzymatic-reaction object assigns MetaCyc:MONOMER-10723 to MetaCyc:RXN-2462; source evidence: EV-EXP-IDA-UNPURIFIED-PROTEIN.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-11003']/enzyme; reaction; evidence
HMG aldolase
MetaCyc:CPLX-7917		catalyzes

Historical Comamonas/Pseudomonas testosteroni HMG/CHA aldolase, source experimental evidence includes crude/part-purified assays; R-HMG preference does not assign CHA absolute chirality.

2-hydroxy-4-oxobutane-1,2,4-tricarboxylate => oxaloacetate + pyruvate
RHEA:28936
  • MetaCyc:ENZRXN-11041

    Source assertion: The enzymatic-reaction object assigns MetaCyc:CPLX-7917 to MetaCyc:RXN-2464; source evidence: EV-EXP-IDA-UNPURIFIED-PROTEIN, EV-EXP-IDA-PART-PURIFIED-PROTEIN.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-11041']/enzyme; reaction; evidence
protocatechuate 4,5-dioxygenase
MetaCyc:CPLX-7916		enables

Native SYK6 LigAB complex assignment is supported by functional complementation, not independent purified subunit catalysis. Later His-tagged/synthetic preparations are separate.

3,4-dihydroxybenzoate + O2 => 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + H(+)
RHEA:24045
  • MetaCyc:ENZRXN-16927

    Source assertion: The enzymatic-reaction object assigns MetaCyc:CPLX-7916 to MetaCyc:PROTOCATECHUATE-45-DIOXYGENASE-RXN; source evidence: EV-EXP-IGI-FUNC-COMPLEMENTATION.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-16927']/enzyme; reaction; evidence
4-carboxy-4-hydroxy-2-oxoadipate aldolase
MetaCyc:CPLX-2865		catalyzes

Recombinant SYK6 LigK native-gene pETK in E. coli BL21(DE3), near-homogeneous hexamer. Native broad CHA assignment does not assert absolute substrate configuration; terminal OAA decarboxylation separately supported.

oxaloacetate + H(+) => pyruvate + CO2
RHEA:15642
  • MetaCyc:ENZRXN-16934

    Source assertion: The enzymatic-reaction object assigns MetaCyc:CPLX-2865 to MetaCyc:OXALODECARB-RXN; source evidence: EV-EXP-IDA-PURIFIED-PROTEIN-HH.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-16934']/enzyme; reaction; evidence
HMG aldolase
MetaCyc:CPLX-2782		catalyzes

Historical P. straminea/P. ochraceae homohexamer and separately recombinant proA observations; broad CHA node does not mean racemic substrate, and reported L-substrate preference is retained.

oxaloacetate + H(+) => pyruvate + CO2
RHEA:15642
  • MetaCyc:ENZRXN-16935

    Source assertion: The enzymatic-reaction object assigns MetaCyc:CPLX-2782 to MetaCyc:OXALODECARB-RXN; source evidence: EV-EXP-IDA-PURIFIED-PROTEIN-HH.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-16935']/enzyme; reaction; evidence
4-oxalomesaconate tautomerase
MetaCyc:G1G01-2697-MONOMER

experimental construct: KT2440 GalD expressed in E. coli BL21(DE3), purified by Ni-NTA with retained His6 tag; an internal thrombin site prevented tag removal. No substitution of a SYK6 LigU homolog.

Qualification evidence
catalyzes

KT2440 GalD shared gallate-module tautomerase. 2016 assays retained His6 tag due internal thrombin site; native exact reaction is E,E enol, while old narrative Z,Z link is rejected. No whole KT2440 P184 occurrence.

(1E)-4-oxobut-1-ene-1,2,4-tricarboxylate => 4-carboxy-2-hydroxy-cis,cis-muconate
RHEA:28932
  • MetaCyc:ENZRXN-18372

    Source assertion: The enzymatic-reaction object assigns MetaCyc:G1G01-2697-MONOMER to MetaCyc:RXN-9983; source evidence: EV-EXP-IDA-PART-PURIFIED-PROTEIN-HH.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-18372']/enzyme; reaction; evidence
  • PMID:26867578

    Source assertion: Figure1A draws GalD conversion of OMA into(2E,4E)-CHM and GalB hydration of that CHM to CHA; product absolute configuration is not specified by these experiments.

    Source locationFigure1A, gallate branch; Figure5A/C optical-rotation comparison; Discussion, stereochemical specificity.
4-oxalmesaconate hydratase
MetaCyc:CPLX-8178

experimental construct: Source-native GalB assay preparation: KT2440 gene expressed with a His tag in KT2442/E. coli. Do not substitute the separate 2016 GalBNt crystal construct lacking four N-terminal residues or infer absolute CHA configuration.

Qualification evidence
  • MetaCyc:CPLX-8178

    Source assertion: The native protein comment identifies His-tagged GalB expression and purification in KT2442 and E. coli.

    Source location/ptools-xml/Protein[@frameid="CPLX-8178"]/comment
catalyzes

KT2440 GalB gallate-module enzyme; native-host KT2442 and recombinant E. coli preparations are separate. Modern 2016 substrate assays support GalD-generated E,E-CHM and (-)-CHA without absolute product assignment; not whole KT2440 P184 occurrence.

4-carboxy-2-hydroxy-cis,cis-muconate + H2O => 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate
RHEA:17403
  • MetaCyc:ENZRXN-18373

    Source assertion: The enzymatic-reaction object assigns MetaCyc:CPLX-8178 to MetaCyc:RXN-2463; source evidence: EV-EXP-IDA-PURIFIED-PROTEIN-HH.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-18373']/enzyme; reaction; evidence
  • PMID:26867578

    Source assertion: Figure1A draws GalD conversion of OMA into(2E,4E)-CHM and GalB hydration of that CHM to CHA; product absolute configuration is not specified by these experiments.

    Source locationFigure1A, gallate branch; Figure5A/C optical-rotation comparison; Discussion, stereochemical specificity.
protocatechuate 4,5-dioxygenase
MetaCyc:CPLX-2701		catalyzes

Historical Comamonas/Pseudomonas testosteroni preparations; native species object spans reported strains. Do not equate the original preparations with modern BR6020 subunit accession sequences.

3,4-dihydroxybenzoate + O2 => 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + H(+)
RHEA:24045
  • MetaCyc:ENZRXN-3342

    Source assertion: The enzymatic-reaction object assigns MetaCyc:CPLX-2701 to MetaCyc:PROTOCATECHUATE-45-DIOXYGENASE-RXN; source evidence: EV-EXP-IDA-PURIFIED-PROTEIN.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-3342']/enzyme; reaction; evidence
2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-3182		catalyzes

Historical phthalate-grown P. straminea/P. ochraceae purified PDC hydrolase; later recombinant proL is distinct, and current native cross-reference does not prove old strain sequence identity.

2-oxo-2H-pyran-4,6-dicarboxylate + H2O => (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate + H(+)
RHEA:10645
  • MetaCyc:ENZRXN-3363

    Source assertion: The enzymatic-reaction object assigns MetaCyc:MONOMER-3182 to MetaCyc:RXN-2462; source evidence: EV-EXP-IDA-PURIFIED-PROTEIN.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-3363']/enzyme; reaction; evidence
4-oxalomesaconate hydratase
MetaCyc:CPLX-2781		catalyzes

Historical phthalate-grown P. straminea/P. ochraceae purified homodimer; retain native substrate assignment as a database assertion, not independent absolute stereochemical identification.

4-carboxy-2-hydroxy-cis,cis-muconate + H2O => 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate
RHEA:17403
  • MetaCyc:ENZRXN-3364

    Source assertion: The enzymatic-reaction object assigns MetaCyc:CPLX-2781 to MetaCyc:RXN-2463; source evidence: EV-EXP-IDA-PURIFIED-PROTEIN.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-3364']/enzyme; reaction; evidence
HMG aldolase
MetaCyc:CPLX-2782		catalyzes

Historical P. straminea/P. ochraceae homohexamer and separately recombinant proA observations; broad CHA node does not mean racemic substrate, and reported L-substrate preference is retained.

2-hydroxy-4-oxobutane-1,2,4-tricarboxylate => oxaloacetate + pyruvate
RHEA:28936
  • MetaCyc:ENZRXN-3365

    Source assertion: The enzymatic-reaction object assigns MetaCyc:CPLX-2782 to MetaCyc:RXN-2464; source evidence: EV-EXP-IDA-PURIFIED-PROTEIN, EV-EXP-IDA-PURIFIED-PROTEIN-HH.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-3365']/enzyme; reaction; evidence
2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-3463		catalyzes

Purified native Pseudomonas/Comamonas testosteroni PDC hydrolase from 4-hydroxybenzoate-grown cells; reversible/pH-dependent reaction. Original 1982 source does not individually characterize all open-chain isomers.

2-oxo-2H-pyran-4,6-dicarboxylate + H2O => (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate + H(+)
RHEA:10645
  • MetaCyc:ENZRXN-3623

    Source assertion: The enzymatic-reaction object assigns MetaCyc:MONOMER-3463 to MetaCyc:RXN-2462; source evidence: EV-EXP-IDA-PURIFIED-PROTEIN.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-3623']/enzyme; reaction; evidence
2-hydroxy-4-carboxymuconate-6-semialdehyde dehydrogenase
MetaCyc:CPLX-2863		catalyzes

Recombinant SYK6 LigC from native-gene pSM21 in E. coli BL21(DE3), purified near homogeneity. First 20 residues matched deduced gene; full paper reports both NAD/NADP support and 67 kDa homodimer.

4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP(+) => 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H(+)
RHEA:29588
  • MetaCyc:ENZRXN-3624

    Source assertion: The enzymatic-reaction object assigns MetaCyc:CPLX-2863 to MetaCyc:1.2.1.45-RXN; source evidence: EV-EXP-IDA-PURIFIED-PROTEIN.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-3624']/enzyme; reaction; evidence
2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-3467		catalyzes

Recombinant SYK6 LigI near-homogeneous monomer from historical experiment. Later synthetic/tagged 2012 structural preparation is distinct.

2-oxo-2H-pyran-4,6-dicarboxylate + H2O => (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate + H(+)
RHEA:10645
  • MetaCyc:ENZRXN-3625

    Source assertion: The enzymatic-reaction object assigns MetaCyc:MONOMER-3467 to MetaCyc:RXN-2462; source evidence: EV-EXP-IDA-PURIFIED-PROTEIN.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-3625']/enzyme; reaction; evidence
4-carboxy-4-hydroxy-2-oxoadipate aldolase
MetaCyc:CPLX-2865		catalyzes

Recombinant SYK6 LigK native-gene pETK in E. coli BL21(DE3), near-homogeneous hexamer. Native broad CHA assignment does not assert absolute substrate configuration; terminal OAA decarboxylation separately supported.

2-hydroxy-4-oxobutane-1,2,4-tricarboxylate => oxaloacetate + pyruvate
RHEA:28936
  • MetaCyc:ENZRXN-3627

    Source assertion: The enzymatic-reaction object assigns MetaCyc:CPLX-2865 to MetaCyc:RXN-2464; source evidence: EV-EXP-IDA-PURIFIED-PROTEIN.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-3627']/enzyme; reaction; evidence
HMG aldolase
MetaCyc:CPLX-2881		catalyzes

Historical P. putida HMG/CHA aldolase preparation; avoid identifying the original strain solely from later KT2440 galC sequence.

2-hydroxy-4-oxobutane-1,2,4-tricarboxylate => oxaloacetate + pyruvate
RHEA:28936
  • MetaCyc:ENZRXN-3641

    Source assertion: The enzymatic-reaction object assigns MetaCyc:CPLX-2881 to MetaCyc:RXN-2464; source evidence: EV-EXP-IDA-PURIFIED-PROTEIN, EV-EXP-IDA-PURIFIED-PROTEIN-NH.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-3641']/enzyme; reaction; evidence
4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase
MetaCyc:CPLX-2861		catalyzes

Historical P. straminea/P. ochraceae purified CHMS dehydrogenase homodimer; both NAD and NADP are supported, with higher apparent affinity for NADP.

4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP(+) => 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H(+)
RHEA:29588
  • MetaCyc:ENZRXN-8701

    Source assertion: The enzymatic-reaction object assigns MetaCyc:CPLX-2861 to MetaCyc:1.2.1.45-RXN; source evidence: EV-EXP-IDA-PURIFIED-PROTEIN.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-8701']/enzyme; reaction; evidence
4-hydroxy-4-methyl-2-oxoglutarate aldolase
MetaCyc:CPLX1G01-155		catalyzes

KT2440 GalC/gllC gallate-module activity; native/heterologous assays and historical species-level enzyme are distinct. Does not establish the whole protocatechuate meta-cleavage pathway in KT2440.

2-hydroxy-4-oxobutane-1,2,4-tricarboxylate => oxaloacetate + pyruvate
RHEA:28936
  • MetaCyc:ENZRXN1G01-1112

    Source assertion: The enzymatic-reaction object assigns MetaCyc:CPLX1G01-155 to MetaCyc:RXN-2464; source evidence: EV-EXP-IMP-REACTION-BLOCKED, EV-EXP-IDA-UNPURIFIED-PROTEIN-HH, EV-EXP-IDA-PURIFIED-PROTEIN-NH.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN1G01-1112']/enzyme; reaction; evidence
protocatechuate 4,5-dioxygenase α subunit
MetaCyc:MONOMER-3165		part_of

Native complex membership; subunit membership alone is not an assertion of independent catalysis.

protocatechuate 4,5-dioxygenase
MetaCyc:CPLX-2701
  • MetaCyc:CPLX-2701

    Source assertion: The native protein object lists component MetaCyc:MONOMER-3165. Explicit source value (source value 4).

    Source location/ptools-xml/Protein[@frameid='CPLX-2701']/component
protocatechuate 4,5-dioxygenase β subunit
MetaCyc:MONOMER-3166		part_of

Native complex membership; subunit membership alone is not an assertion of independent catalysis.

protocatechuate 4,5-dioxygenase
MetaCyc:CPLX-2701
  • MetaCyc:CPLX-2701

    Source assertion: The native protein object lists component MetaCyc:MONOMER-3166. Explicit source value (source value 4).

    Source location/ptools-xml/Protein[@frameid='CPLX-2701']/component
subunit of 4-oxalomesaconate hydratase
MetaCyc:MONOMER-3243		part_of

Native complex membership; subunit membership alone is not an assertion of independent catalysis.

4-oxalomesaconate hydratase
MetaCyc:CPLX-2781
  • MetaCyc:CPLX-2781

    Source assertion: The native protein object lists component MetaCyc:MONOMER-3243. Explicit source value (source value 2).

    Source location/ptools-xml/Protein[@frameid='CPLX-2781']/component
4-oxalocitramalate aldolase subunit
MetaCyc:MONOMER-3244		part_of

Native complex membership; subunit membership alone is not an assertion of independent catalysis.

HMG aldolase
MetaCyc:CPLX-2782
  • MetaCyc:CPLX-2782

    Source assertion: The native protein object lists component MetaCyc:MONOMER-3244. Explicit source value (source value 6).

    Source location/ptools-xml/Protein[@frameid='CPLX-2782']/component
α-hydroxy-γ-carboxymuconate ε-semialdehyde dehydrogenase subunit
MetaCyc:MONOMER-8501		part_of

Native complex membership; subunit membership alone is not an assertion of independent catalysis.

4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase
MetaCyc:CPLX-2861
  • MetaCyc:CPLX-2861

    Source assertion: The native protein object lists component MetaCyc:MONOMER-8501. Explicit source value (source value 2).

    Source location/ptools-xml/Protein[@frameid='CPLX-2861']/component
LigC
MetaCyc:MONOMER-3466		part_of

Native complex membership; subunit membership alone is not an assertion of independent catalysis.

2-hydroxy-4-carboxymuconate-6-semialdehyde dehydrogenase
MetaCyc:CPLX-2863
  • MetaCyc:CPLX-2863

    Source assertion: The native protein object lists component MetaCyc:MONOMER-3466. Explicit source value (source value 2).

    Source location/ptools-xml/Protein[@frameid='CPLX-2863']/component
LigK
MetaCyc:MONOMER-3469		part_of

Native complex membership; subunit membership alone is not an assertion of independent catalysis.

4-carboxy-4-hydroxy-2-oxoadipate aldolase
MetaCyc:CPLX-2865
  • MetaCyc:CPLX-2865

    Source assertion: The native protein object lists component MetaCyc:MONOMER-3469. Explicit source value (source value 6).

    Source location/ptools-xml/Protein[@frameid='CPLX-2865']/component
subunit of 4-hydroxy-4-methyl-2-oxoglutarate aldolase
MetaCyc:MONOMER-3481		part_of

Native complex membership; subunit membership alone is not an assertion of independent catalysis.

HMG aldolase
MetaCyc:CPLX-2881
  • MetaCyc:CPLX-2881

    Source assertion: The native protein object lists component MetaCyc:MONOMER-3481. Explicit source value (source value 6).

    Source location/ptools-xml/Protein[@frameid='CPLX-2881']/component
protocatechuate 4,5-dioxygenase beta chain
MetaCyc:MONOMER-15117		part_of

Native complex membership; subunit membership alone is not an assertion of independent catalysis.

protocatechuate 4,5-dioxygenase
MetaCyc:CPLX-7916
  • MetaCyc:CPLX-7916

    Source assertion: The native protein object lists component MetaCyc:MONOMER-15117. One source occurrence; oligomer stoichiometry is not independently established (source value 1).

    Source location/ptools-xml/Protein[@frameid='CPLX-7916']/component
protocatechuate 4,5-dioxygenase alpha chain
MetaCyc:MONOMER-15116		part_of

Native complex membership; subunit membership alone is not an assertion of independent catalysis.

protocatechuate 4,5-dioxygenase
MetaCyc:CPLX-7916
  • MetaCyc:CPLX-7916

    Source assertion: The native protein object lists component MetaCyc:MONOMER-15116. One source occurrence; oligomer stoichiometry is not independently established (source value 1).

    Source location/ptools-xml/Protein[@frameid='CPLX-7916']/component
HMG aldolase monomer
MetaCyc:MONOMER-3184		part_of

Native complex membership; subunit membership alone is not an assertion of independent catalysis.

HMG aldolase
MetaCyc:CPLX-7917
  • MetaCyc:CPLX-7917

    Source assertion: The native protein object lists component MetaCyc:MONOMER-3184. Explicit source value (source value 6).

    Source location/ptools-xml/Protein[@frameid='CPLX-7917']/component
4-oxalmesaconate hydratase monomer
MetaCyc:G1G01-2699-MONOMER		part_of

Native complex membership; subunit membership alone is not an assertion of independent catalysis.

4-oxalmesaconate hydratase
MetaCyc:CPLX-8178
  • MetaCyc:CPLX-8178

    Source assertion: The native protein object lists component MetaCyc:G1G01-2699-MONOMER. Explicit source value (source value 6).

    Source location/ptools-xml/Protein[@frameid='CPLX-8178']/component
4-hydroxy-4-methyl-2-oxoglutarate aldolase aldolase
MetaCyc:G1G01-2698-MONOMER		part_of

Native complex membership; subunit membership alone is not an assertion of independent catalysis.

4-hydroxy-4-methyl-2-oxoglutarate aldolase
MetaCyc:CPLX1G01-155
  • MetaCyc:CPLX1G01-155

    Source assertion: The native protein object lists component MetaCyc:G1G01-2698-MONOMER. Explicit source value (source value 6).

    Source location/ptools-xml/Protein[@frameid='CPLX1G01-155']/component
4-carboxy-4-hydroxy-2-oxoadipate aldolase
MetaCyc:CPLX-2865

experimental construct: Purified recombinant SYK6 LigK from pETK in E. coli BL21(DE3), observed as a homohexamer. The measured N-terminus lacks the initial native methionine; unreported vector-derived residues are not inferred absent.

Qualification evidence
  • PMID:12486039
    first methionine
    Source locationPMC141877, Results / Purification of CHA aldolase, N-terminal sequence; Methods / Expression and purification of LigK; Results / Enzyme properties, gel filtration
has_cofactor

The source annotates Mg as a LigK cofactor. In the reported recombinant assays, CHA activity with 1 mM Co, Zn, Ca or Mn was 85%, 65%, 20% or 0% of the 1 mM Mg control. OAA activity showed qualitatively similar metal dependence; those exact percentages were not reported for OAA. At 0.5 mM, phosphate enhanced CHA and OAA activities by 3.0 and 1.7 fold, respectively. These assay observations do not identify the physiological metal.

magnesium(2+)
CHEBI:18420
  • MetaCyc:ENZRXN-16934

    Source assertion: The enzymatic-reaction cofactor slot identifies MG+2 for enzyme MetaCyc:CPLX-2865.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-16934']/cofactor
  • MetaCyc:ENZRXN-3627

    Source assertion: The enzymatic-reaction cofactor slot identifies MG+2 for enzyme MetaCyc:CPLX-2865.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-3627']/cofactor
  • PMID:12486039
    85, 65, 20, or 0% of the activity
    Source locationPMC141877, Results / Enzyme properties, first paragraph; 1 mM divalent-cation comparison
  • PMID:12486039
    3.0- and 1.7-fold activation of CHA aldolase and oxaloacetate decarboxylase activity, respectively.
    Source locationPMC141877, Results / Enzyme properties, first paragraph; 0.5 mM phosphate experiment
4-oxalmesaconate hydratase
MetaCyc:CPLX-8178

experimental construct: Source-native GalB assay preparation: KT2440 gene expressed with a His tag in KT2442/E. coli. Do not substitute the separate 2016 GalBNt crystal construct lacking four N-terminal residues or infer absolute CHA configuration.

Qualification evidence
  • MetaCyc:CPLX-8178

    Source assertion: The native protein comment identifies His-tagged GalB expression and purification in KT2442 and E. coli.

    Source location/ptools-xml/Protein[@frameid="CPLX-8178"]/comment
has_cofactor

Source-scoped cofactor annotation. Alternative metals and assay-specific effects must not be generalized across distinct aldolases or hydratases.

zinc(2+)
CHEBI:29105
  • MetaCyc:ENZRXN-18373

    Source assertion: The enzymatic-reaction cofactor slot identifies ZN+2 for enzyme MetaCyc:CPLX-8178.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-18373']/cofactor
protocatechuate 4,5-dioxygenase
MetaCyc:CPLX-2701		has_cofactor

Source-scoped cofactor annotation. Alternative metals and assay-specific effects must not be generalized across distinct aldolases or hydratases.

iron(2+)
CHEBI:29033
  • MetaCyc:ENZRXN-3342

    Source assertion: The enzymatic-reaction cofactor slot identifies FE+2 for enzyme MetaCyc:CPLX-2701.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-3342']/cofactor
HMG aldolase
MetaCyc:CPLX-2782		has_cofactor

Source-scoped cofactor annotation. Alternative metals and assay-specific effects must not be generalized across distinct aldolases or hydratases.

magnesium(2+)
CHEBI:18420
  • MetaCyc:ENZRXN-3365

    Source assertion: The enzymatic-reaction cofactor slot identifies MG+2 for enzyme MetaCyc:CPLX-2782.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-3365']/cofactor
HMG aldolase
MetaCyc:CPLX-2881		has_cofactor

Source-scoped cofactor annotation. Alternative metals and assay-specific effects must not be generalized across distinct aldolases or hydratases.

manganese(2+)
CHEBI:29035
  • MetaCyc:ENZRXN-3641

    Source assertion: The enzymatic-reaction cofactor slot identifies MN+2 for enzyme MetaCyc:CPLX-2881.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-3641']/cofactor
HMG aldolase
MetaCyc:CPLX-2881		has_cofactor

Source-scoped cofactor annotation. Alternative metals and assay-specific effects must not be generalized across distinct aldolases or hydratases.

magnesium(2+)
CHEBI:18420
  • MetaCyc:ENZRXN-3641

    Source assertion: The enzymatic-reaction cofactor slot identifies MG+2 for enzyme MetaCyc:CPLX-2881.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN-3641']/cofactor
4-hydroxy-4-methyl-2-oxoglutarate aldolase
MetaCyc:CPLX1G01-155		has_cofactor

Source-scoped cofactor annotation. Alternative metals and assay-specific effects must not be generalized across distinct aldolases or hydratases.

manganese(2+)
CHEBI:29035
  • MetaCyc:ENZRXN1G01-1112

    Source assertion: The enzymatic-reaction cofactor slot identifies MN+2 for enzyme MetaCyc:CPLX1G01-155.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid='ENZRXN1G01-1112']/cofactor
oxaloacetate(2-)
CHEBI:16452		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

4-carboxy-4-hydroxy-2-oxoadipate aldolase
MetaCyc:CPLX-2865
  • MetaCyc:REG-10400

    Source assertion: Regulation object: regulator OXALACETIC_ACID; regulated-entity ENZRXN-3627; mode -. The target activity names enzyme MetaCyc:CPLX-2865.

    Source location/ptools-xml/Regulation[@frameid='REG-10400']/regulator; regulated-entity; mode
N-ethylmaleimide
MetaCyc:N-ETHYLMALEIMIDE		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

4-carboxy-4-hydroxy-2-oxoadipate aldolase
MetaCyc:CPLX-2865
  • MetaCyc:REG-10401

    Source assertion: Regulation object: regulator N-ETHYLMALEIMIDE; regulated-entity ENZRXN-3627; mode -. The target activity names enzyme MetaCyc:CPLX-2865.

    Source location/ptools-xml/Regulation[@frameid='REG-10401']/regulator; regulated-entity; mode
p-chloromercuribenzoate
MetaCyc:CPD-29		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase
MetaCyc:CPLX-2861
  • MetaCyc:REG-10405

    Source assertion: Regulation object: regulator CPD-29; regulated-entity ENZRXN-8701; mode -. The target activity names enzyme MetaCyc:CPLX-2861.

    Source location/ptools-xml/Regulation[@frameid='REG-10405']/regulator; regulated-entity; mode
iodoacetate
MetaCyc:IODOACETATE		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase
MetaCyc:CPLX-2861
  • MetaCyc:REG-10406

    Source assertion: Regulation object: regulator IODOACETATE; regulated-entity ENZRXN-8701; mode -. The target activity names enzyme MetaCyc:CPLX-2861.

    Source location/ptools-xml/Regulation[@frameid='REG-10406']/regulator; regulated-entity; mode
N-ethylmaleimide
MetaCyc:N-ETHYLMALEIMIDE		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase
MetaCyc:CPLX-2861
  • MetaCyc:REG-10407

    Source assertion: Regulation object: regulator N-ETHYLMALEIMIDE; regulated-entity ENZRXN-8701; mode -. The target activity names enzyme MetaCyc:CPLX-2861.

    Source location/ptools-xml/Regulation[@frameid='REG-10407']/regulator; regulated-entity; mode
oxaloacetate(2-)
CHEBI:16452		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

HMG aldolase
MetaCyc:CPLX-2881
  • MetaCyc:REG-10724

    Source assertion: Regulation object: regulator OXALACETIC_ACID; regulated-entity ENZRXN-3641; mode -. The target activity names enzyme MetaCyc:CPLX-2881.

    Source location/ptools-xml/Regulation[@frameid='REG-10724']/regulator; regulated-entity; mode
cobalt(2+)
CHEBI:48828		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-3463
  • MetaCyc:REG-11529

    Source assertion: Regulation object: regulator CO+2; regulated-entity ENZRXN-3623; mode -. The target activity names enzyme MetaCyc:MONOMER-3463.

    Source location/ptools-xml/Regulation[@frameid='REG-11529']/regulator; regulated-entity; mode
manganese(2+)
CHEBI:29035		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-3463
  • MetaCyc:REG-11530

    Source assertion: Regulation object: regulator MN+2; regulated-entity ENZRXN-3623; mode -. The target activity names enzyme MetaCyc:MONOMER-3463.

    Source location/ptools-xml/Regulation[@frameid='REG-11530']/regulator; regulated-entity; mode
copper(2+)
CHEBI:29036		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-3463
  • MetaCyc:REG-11531

    Source assertion: Regulation object: regulator CU+2; regulated-entity ENZRXN-3623; mode -. The target activity names enzyme MetaCyc:MONOMER-3463.

    Source location/ptools-xml/Regulation[@frameid='REG-11531']/regulator; regulated-entity; mode
zinc(2+)
CHEBI:29105		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-3463
  • MetaCyc:REG-11532

    Source assertion: Regulation object: regulator ZN+2; regulated-entity ENZRXN-3623; mode -. The target activity names enzyme MetaCyc:MONOMER-3463.

    Source location/ptools-xml/Regulation[@frameid='REG-11532']/regulator; regulated-entity; mode
manganese(2+)
CHEBI:29035		regulates

Native source leaves the effect sign unspecified; this edge does not assert activation or inhibition.

protocatechuate 4,5-dioxygenase
MetaCyc:CPLX-2701
  • MetaCyc:REG-11747

    Source assertion: Regulation object: regulator MN+2; regulated-entity ENZRXN-3342; mode unspecified. The target activity names enzyme MetaCyc:CPLX-2701.

    Source location/ptools-xml/Regulation[@frameid='REG-11747']/regulator; regulated-entity; mode
nickel(2+)
CHEBI:49786		regulates

Native source leaves the effect sign unspecified; this edge does not assert activation or inhibition.

protocatechuate 4,5-dioxygenase
MetaCyc:CPLX-2701
  • MetaCyc:REG-11748

    Source assertion: Regulation object: regulator NI+2; regulated-entity ENZRXN-3342; mode unspecified. The target activity names enzyme MetaCyc:CPLX-2701.

    Source location/ptools-xml/Regulation[@frameid='REG-11748']/regulator; regulated-entity; mode
cobalt(2+)
CHEBI:48828		regulates

Native source leaves the effect sign unspecified; this edge does not assert activation or inhibition.

protocatechuate 4,5-dioxygenase
MetaCyc:CPLX-2701
  • MetaCyc:REG-11749

    Source assertion: Regulation object: regulator CO+2; regulated-entity ENZRXN-3342; mode unspecified. The target activity names enzyme MetaCyc:CPLX-2701.

    Source location/ptools-xml/Regulation[@frameid='REG-11749']/regulator; regulated-entity; mode
mercury(2+)
CHEBI:16793		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase
MetaCyc:CPLX-2861
  • MetaCyc:REG-12625

    Source assertion: Regulation object: regulator HG+2; regulated-entity ENZRXN-8701; mode -. The target activity names enzyme MetaCyc:CPLX-2861.

    Source location/ptools-xml/Regulation[@frameid='REG-12625']/regulator; regulated-entity; mode
mercury(2+)
CHEBI:16793		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

4-carboxy-4-hydroxy-2-oxoadipate aldolase
MetaCyc:CPLX-2865
  • MetaCyc:REG-12626

    Source assertion: Regulation object: regulator HG+2; regulated-entity ENZRXN-3627; mode -. The target activity names enzyme MetaCyc:CPLX-2865.

    Source location/ptools-xml/Regulation[@frameid='REG-12626']/regulator; regulated-entity; mode
mercury(2+)
CHEBI:16793		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred. LigC 2000 assayed purified recombinant pSM21 protein; Hg was delivered as HgCl2, pCMB at 10 μM: 78%; HgCl2 at 10 μM: 83%; DTNB at 100 μM: 98% inhibition after 1 h. These are separate treatments.

2-hydroxy-4-carboxymuconate-6-semialdehyde dehydrogenase
MetaCyc:CPLX-2863
  • MetaCyc:REG-12627

    Source assertion: Regulation object: regulator HG+2; regulated-entity ENZRXN-3624; mode -. The target activity names enzyme MetaCyc:CPLX-2863.

    Source location/ptools-xml/Regulation[@frameid='REG-12627']/regulator; regulated-entity; mode
mercury(2+)
CHEBI:16793		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

4-oxalomesaconate hydratase
MetaCyc:CPLX-2781
  • MetaCyc:REG-12629

    Source assertion: Regulation object: regulator HG+2; regulated-entity ENZRXN-3364; mode -. The target activity names enzyme MetaCyc:CPLX-2781.

    Source location/ptools-xml/Regulation[@frameid='REG-12629']/regulator; regulated-entity; mode
mercury(2+)
CHEBI:16793		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-3182
  • MetaCyc:REG-12637

    Source assertion: Regulation object: regulator HG+2; regulated-entity ENZRXN-3363; mode -. The target activity names enzyme MetaCyc:MONOMER-3182.

    Source location/ptools-xml/Regulation[@frameid='REG-12637']/regulator; regulated-entity; mode
mercury(2+)
CHEBI:16793		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

HMG aldolase
MetaCyc:CPLX-2782
  • MetaCyc:REG-12638

    Source assertion: Regulation object: regulator HG+2; regulated-entity ENZRXN-3365; mode -. The target activity names enzyme MetaCyc:CPLX-2782.

    Source location/ptools-xml/Regulation[@frameid='REG-12638']/regulator; regulated-entity; mode
zinc(2+)
CHEBI:29105		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

4-oxalomesaconate hydratase
MetaCyc:CPLX-2781
  • MetaCyc:REG-12669

    Source assertion: Regulation object: regulator ZN+2; regulated-entity ENZRXN-3364; mode -. The target activity names enzyme MetaCyc:CPLX-2781.

    Source location/ptools-xml/Regulation[@frameid='REG-12669']/regulator; regulated-entity; mode
zinc(2+)
CHEBI:29105		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-3467
  • MetaCyc:REG-8378

    Source assertion: Regulation object: regulator ZN+2; regulated-entity ENZRXN-3625; mode -. The target activity names enzyme MetaCyc:MONOMER-3467.

    Source location/ptools-xml/Regulation[@frameid='REG-8378']/regulator; regulated-entity; mode
N-ethylmaleimide
MetaCyc:N-ETHYLMALEIMIDE		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-3467
  • MetaCyc:REG-8379

    Source assertion: Regulation object: regulator N-ETHYLMALEIMIDE; regulated-entity ENZRXN-3625; mode -. The target activity names enzyme MetaCyc:MONOMER-3467.

    Source location/ptools-xml/Regulation[@frameid='REG-8379']/regulator; regulated-entity; mode
5,5'-dithio-bis-2-nitrobenzoate
MetaCyc:DITHIO-NITROBENZOATE		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-3467
  • MetaCyc:REG-8380

    Source assertion: Regulation object: regulator DITHIO-NITROBENZOATE; regulated-entity ENZRXN-3625; mode -. The target activity names enzyme MetaCyc:MONOMER-3467.

    Source location/ptools-xml/Regulation[@frameid='REG-8380']/regulator; regulated-entity; mode
oxaloacetate(2-)
CHEBI:16452		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

HMG aldolase
MetaCyc:CPLX-2782
  • MetaCyc:REG-8391

    Source assertion: Regulation object: regulator OXALACETIC_ACID; regulated-entity ENZRXN-3365; mode -. The target activity names enzyme MetaCyc:CPLX-2782.

    Source location/ptools-xml/Regulation[@frameid='REG-8391']/regulator; regulated-entity; mode
p-chloromercuribenzoate
MetaCyc:CPD-29		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

HMG aldolase
MetaCyc:CPLX-2782
  • MetaCyc:REG-8393

    Source assertion: Regulation object: regulator CPD-29; regulated-entity ENZRXN-3365; mode -. The target activity names enzyme MetaCyc:CPLX-2782.

    Source location/ptools-xml/Regulation[@frameid='REG-8393']/regulator; regulated-entity; mode
copper(2+)
CHEBI:29036		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-3182
  • MetaCyc:REG-8394

    Source assertion: Regulation object: regulator CU+2; regulated-entity ENZRXN-3363; mode -. The target activity names enzyme MetaCyc:MONOMER-3182.

    Source location/ptools-xml/Regulation[@frameid='REG-8394']/regulator; regulated-entity; mode
zinc(2+)
CHEBI:29105		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-3182
  • MetaCyc:REG-8395

    Source assertion: Regulation object: regulator ZN+2; regulated-entity ENZRXN-3363; mode -. The target activity names enzyme MetaCyc:MONOMER-3182.

    Source location/ptools-xml/Regulation[@frameid='REG-8395']/regulator; regulated-entity; mode
manganese(2+)
CHEBI:29035		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-3182
  • MetaCyc:REG-8396

    Source assertion: Regulation object: regulator MN+2; regulated-entity ENZRXN-3363; mode -. The target activity names enzyme MetaCyc:MONOMER-3182.

    Source location/ptools-xml/Regulation[@frameid='REG-8396']/regulator; regulated-entity; mode
cobalt(2+)
CHEBI:48828		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-3182
  • MetaCyc:REG-8397

    Source assertion: Regulation object: regulator CO+2; regulated-entity ENZRXN-3363; mode -. The target activity names enzyme MetaCyc:MONOMER-3182.

    Source location/ptools-xml/Regulation[@frameid='REG-8397']/regulator; regulated-entity; mode
p-chloromercuribenzoate
MetaCyc:CPD-29		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

2-pyrone-4,6-dicarboxylate hydrolase
MetaCyc:MONOMER-3182
  • MetaCyc:REG-8398

    Source assertion: Regulation object: regulator CPD-29; regulated-entity ENZRXN-3363; mode -. The target activity names enzyme MetaCyc:MONOMER-3182.

    Source location/ptools-xml/Regulation[@frameid='REG-8398']/regulator; regulated-entity; mode
p-chloromercuribenzoate
MetaCyc:CPD-29		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

4-oxalomesaconate hydratase
MetaCyc:CPLX-2781
  • MetaCyc:REG-9531

    Source assertion: Regulation object: regulator CPD-29; regulated-entity ENZRXN-3364; mode -. The target activity names enzyme MetaCyc:CPLX-2781.

    Source location/ptools-xml/Regulation[@frameid='REG-9531']/regulator; regulated-entity; mode
copper sulfate
MetaCyc:CUSO4		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred.

4-oxalomesaconate hydratase
MetaCyc:CPLX-2781
  • MetaCyc:REG-9532

    Source assertion: Regulation object: regulator CUSO4; regulated-entity ENZRXN-3364; mode -. The target activity names enzyme MetaCyc:CPLX-2781.

    Source location/ptools-xml/Regulation[@frameid='REG-9532']/regulator; regulated-entity; mode
p-chloromercuribenzoate
MetaCyc:CPD-29		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred. LigC 2000 assayed purified recombinant pSM21 protein; Hg was delivered as HgCl2, pCMB at 10 μM: 78%; HgCl2 at 10 μM: 83%; DTNB at 100 μM: 98% inhibition after 1 h. These are separate treatments.

2-hydroxy-4-carboxymuconate-6-semialdehyde dehydrogenase
MetaCyc:CPLX-2863
  • MetaCyc:REG-9956

    Source assertion: Regulation object: regulator CPD-29; regulated-entity ENZRXN-3624; mode -. The target activity names enzyme MetaCyc:CPLX-2863.

    Source location/ptools-xml/Regulation[@frameid='REG-9956']/regulator; regulated-entity; mode
5,5'-dithio-bis-2-nitrobenzoate
MetaCyc:DITHIO-NITROBENZOATE		inhibits

Source-reported in-vitro enzyme effect; the chemical source node is retained exactly. No physiological regulatory role or unreported dose is inferred. LigC 2000 assayed purified recombinant pSM21 protein; Hg was delivered as HgCl2, pCMB at 10 μM: 78%; HgCl2 at 10 μM: 83%; DTNB at 100 μM: 98% inhibition after 1 h. These are separate treatments.

2-hydroxy-4-carboxymuconate-6-semialdehyde dehydrogenase
MetaCyc:CPLX-2863
  • MetaCyc:REG-9957

    Source assertion: Regulation object: regulator DITHIO-NITROBENZOATE; regulated-entity ENZRXN-3624; mode -. The target activity names enzyme MetaCyc:CPLX-2863.

    Source location/ptools-xml/Regulation[@frameid='REG-9957']/regulator; regulated-entity; mode
4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase
MetaCyc:CPLX-2861		has_cofactor

Historical enzyme supports either nicotinamide coenzyme; higher apparent NADP affinity does not mean exclusive NADP usage.

NAD(1-)
CHEBI:57540
  • MetaCyc:CPLX-2861

    Source assertion: The native protein/comment reports support by both NAD and NADP; the selected graph equation uses NADP without claiming exclusivity.

    Source location/ptools-xml/Protein[@frameid='CPLX-2861']/comment
4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase
MetaCyc:CPLX-2861		has_cofactor

Historical enzyme supports either nicotinamide coenzyme; higher apparent NADP affinity does not mean exclusive NADP usage.

NADP(3-)
CHEBI:58349
  • MetaCyc:CPLX-2861

    Source assertion: The native protein/comment reports support by both NAD and NADP; the selected graph equation uses NADP without claiming exclusivity.

    Source location/ptools-xml/Protein[@frameid='CPLX-2861']/comment
2-hydroxy-4-carboxymuconate-6-semialdehyde dehydrogenase
MetaCyc:CPLX-2863		has_cofactor

Purified recombinant SYK6 LigC supports NAD and NADP. Primary Table 3 values supersede transposed UniProt kinetic substrate labels.

NAD(1-)
CHEBI:57540
  • PMID:11073908

    Source assertion: Table 3 lists SYK6 LigC rates and Km values for NAD+ and NADP+ separately:252±3.9μM and24.6±1.5μM; CHMS Km20.6±1.0μM with200μM NAD+ and26.0±0.5μM with200μM NADP+.

    Source locationTable3, SYK-6 four rows; column headings identify the varied substrate and fixed cosubstrate.
2-hydroxy-4-carboxymuconate-6-semialdehyde dehydrogenase
MetaCyc:CPLX-2863		has_cofactor

Purified recombinant SYK6 LigC supports NAD and NADP. Primary Table 3 values supersede transposed UniProt kinetic substrate labels.

NADP(3-)
CHEBI:58349
  • PMID:11073908

    Source assertion: Table 3 lists SYK6 LigC rates and Km values for NAD+ and NADP+ separately:252±3.9μM and24.6±1.5μM; CHMS Km20.6±1.0μM with200μM NAD+ and26.0±0.5μM with200μM NADP+.

    Source locationTable3, SYK-6 four rows; column headings identify the varied substrate and fixed cosubstrate.
4-oxalmesaconate hydratase
MetaCyc:CPLX-8178

molecular state: EDTA-treated GalB apoenzyme subsequently incubated with the named divalent metal; compare separately from zinc-rich aerobically purified KT2442 material.

Qualification evidence
  • PMID:26867578

    Source assertion: Table2 contrasts the named metal reconstitutions, Apo, EDTA, Native, and Native+Co2+ conditions.

    Source locationTable2 condition rows and caption
has_cofactor

2016 apoenzyme reconstitution supports this alternative metal; native-host aerobic purification was zinc-rich, and physiological metal identity remains unresolved.

iron(2+)
CHEBI:29033
  • PMID:26867578

    Source assertion: Table2 reports iron(2+) restoration of GalB CHM hydration to relativeactivity 100±4.6%, with Fe2+setto100%; the native-aerobically-purified sample is a distinct preparation.

    Source locationTable2, named-metal row; tablecaption: native before EDTA treatment.
4-oxalmesaconate hydratase
MetaCyc:CPLX-8178

molecular state: EDTA-treated GalB apoenzyme subsequently incubated with the named divalent metal; compare separately from zinc-rich aerobically purified KT2442 material.

Qualification evidence
  • PMID:26867578

    Source assertion: Table2 contrasts the named metal reconstitutions, Apo, EDTA, Native, and Native+Co2+ conditions.

    Source locationTable2 condition rows and caption
has_cofactor

2016 apoenzyme reconstitution supports this alternative metal; native-host aerobic purification was zinc-rich, and physiological metal identity remains unresolved.

cobalt(2+)
CHEBI:48828
  • PMID:26867578

    Source assertion: Table2 reports cobalt(2+) restoration of GalB CHM hydration to relativeactivity 79±4.0%, with Fe2+setto100%; the native-aerobically-purified sample is a distinct preparation.

    Source locationTable2, named-metal row; tablecaption: native before EDTA treatment.
HMG aldolase
MetaCyc:CPLX-2782		has_cofactor

Historical P. straminea/P. ochraceae aldolase metal alternative; do not transfer this result to SYK6 LigK, whose assay metal preferences differ.

manganese(2+)
CHEBI:29035
  • MetaCyc:CPLX-2782

    Source assertion: The native protein/comment lists Mg2+,Mn2+,Co2+,Zn2+andCd2+ as divalent ions supporting the historical aldolase.

    Source location/ptools-xml/Protein[@frameid="CPLX-2782"]/comment
HMG aldolase
MetaCyc:CPLX-2782		has_cofactor

Historical P. straminea/P. ochraceae aldolase metal alternative; do not transfer this result to SYK6 LigK, whose assay metal preferences differ.

cobalt(2+)
CHEBI:48828
  • MetaCyc:CPLX-2782

    Source assertion: The native protein/comment lists Mg2+,Mn2+,Co2+,Zn2+andCd2+ as divalent ions supporting the historical aldolase.

    Source location/ptools-xml/Protein[@frameid="CPLX-2782"]/comment
HMG aldolase
MetaCyc:CPLX-2782		has_cofactor

Historical P. straminea/P. ochraceae aldolase metal alternative; do not transfer this result to SYK6 LigK, whose assay metal preferences differ.

zinc(2+)
CHEBI:29105
  • MetaCyc:CPLX-2782

    Source assertion: The native protein/comment lists Mg2+,Mn2+,Co2+,Zn2+andCd2+ as divalent ions supporting the historical aldolase.

    Source location/ptools-xml/Protein[@frameid="CPLX-2782"]/comment
HMG aldolase
MetaCyc:CPLX-2782		has_cofactor

Historical P. straminea/P. ochraceae aldolase metal alternative; do not transfer this result to SYK6 LigK, whose assay metal preferences differ.

cadmium(2+)
CHEBI:48775
  • MetaCyc:CPLX-2782

    Source assertion: The native protein/comment lists Mg2+,Mn2+,Co2+,Zn2+andCd2+ as divalent ions supporting the historical aldolase.

    Source location/ptools-xml/Protein[@frameid="CPLX-2782"]/comment
LigR protein
UniProtKB:Q8RQV9		regulates

In SYK6, LigR activates ligK-orf1-ligI-lsdA and ligJABC transcription with PCA/gallate and autorepresses ligR. This regulatory evidence does not validate every chemical step of the composite native eight-member definition; promoter DNA identifiers and cooperative-binding hypotheses are not invented.

MetaCyc:P184-PWY
  • PMID:20435721
    LigR activates the transcription of the ligK and ligJ operons in the presence of PCA or GA
hydrogen peroxide
CHEBI:16240		inhibits

Historical native P. testosteroni dioxygenase is inactivated when its Fe2+ is oxidized; this is assay-induced redox inactivation, not inferred physiological regulation.

protocatechuate 4,5-dioxygenase
MetaCyc:CPLX-2701
  • PMID:6317682
    oxidized, for instance by H2O2
  • PMID:6317682
    In the oxidized state, protocatechuate 4,5-dioxygenase is inactive
ascorbate
CHEBI:22651		activates

Ascorbate restores activity by reducing the oxidized iron site in the historical native preparation; it is not generalized activation of already-active dioxygenase.

protocatechuate 4,5-dioxygenase
MetaCyc:CPLX-2701

molecular state: Previously oxidized, inactive Fe3+-containing native P. testosteroni dioxygenase; reduction recovers activity.

Qualification evidence

References

Curation history