quinate degradation II

MetaCyc:PWY-6416

The MetaCyc 27.0 quinate degradation II definition converts L-quinate through 3-dehydroquinate and 3-dehydroshikimate to protocatechuate. Its first reaction retains the native NAD(P) and NAD(P)H classes. Individual enzyme evidence distinguishes NAD preference, assay constructs, native assemblies and species or strain scope. This three-step route is separate from the PQQ-dependent quinate degradation I and the two-step shikimate degradation routes. The separately displayed NAD-specific reaction is a molecular realization of the first step, not an additional sequential fourth step.

Pathway type

aromatic compound catabolism

Organism scope

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Pathway network

63 nodes · 60 asserted directed edges

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Components and activities

Declared biological components and source reaction directions
Node	Kind or role	Source direction
Corynebacterium glutamicum R `NCBITaxon:340322`	taxon
Corynebacterium glutamicum `NCBITaxon:1718`	taxon
Amycolatopsis methanolica `NCBITaxon:1814`	taxon
Aspergillus nidulans `NCBITaxon:162425`	taxon
Neurospora crassa `NCBITaxon:5141`	taxon
(-)-quinate `CHEBI:29751`	small molecule
3-dehydroquinate `CHEBI:32364`	small molecule
3-dehydroshikimate `CHEBI:16630`	small molecule
3,4-dihydroxybenzoate `CHEBI:36241`	small molecule
water `CHEBI:15377`	small molecule
hydron `CHEBI:15378`	small molecule
NAD(P)+ `MetaCyc:NAD-P-OR-NOP`	chemical entity
NAD(P)H `MetaCyc:NADH-P-OR-NOP`	chemical entity
NAD(1-) `CHEBI:57540`	small molecule
NADH(2-) `CHEBI:57945`	small molecule
magnesium(2+) `CHEBI:18420`	cofactor
manganese(2+) `CHEBI:29035`	cofactor
zinc(2+) `CHEBI:29105`	cofactor
chorismate(2-) `CHEBI:29748`	small molecule
cobalt(2+) `CHEBI:48828`	cofactor
qa-1F `Entrez:3875756`	gene
qa-2 `Entrez:3875772`	gene
qa-3 `Entrez:3875774`	gene
3-dehydroquinate dehydratase `MetaCyc:CPLX-7980`	complex
quinate/shikimate dehydrogenase `MetaCyc:CPLX-7981`	complex
qsuB `MetaCyc:G-11737`	gene
qsuC `MetaCyc:G-11738`	gene
4-hydroxyphenylpyruvate dioxygenase [Corynebacterium glutamicum] `NCBIProtein:ANU32720.1`	protein
hypothetical protein cgR_0491 [Corynebacterium glutamicum R] `NCBIProtein:BAF53458.1`	protein
hypothetical protein cgR_0493 [Corynebacterium glutamicum R] `NCBIProtein:BAF53460.1`	protein
Corynebacterium glutamicum R QsuC `UniProtKB:A4QB64`	protein
Corynebacterium glutamicum R QsuD `UniProtKB:A4QB65`	protein
Aspergillus nidulans QutE `UniProtKB:P05147`	protein
Neurospora crassa Qa2 `UniProtKB:P05195`	protein
Neurospora crassa Qa4 `UniProtKB:P07046`	protein
Aspergillus nidulans QutA `UniProtKB:P10563`	protein
Neurospora crassa Qa3 `UniProtKB:P11635`	protein
Neurospora crassa qa-y quinate permease `UniProtKB:P11636`	protein
Neurospora crassa Qa1S `UniProtKB:P11637`	protein
Neurospora crassa Qa1F `UniProtKB:P11638`	protein
Aspergillus nidulans QutD `UniProtKB:P15325`	protein
Aspergillus nidulans QutB `UniProtKB:P25415`	protein
Amycolatopsis methanolica AroQ subunit `UniProtKB:P46380`	protein
Aspergillus nidulans QutC `UniProtKB:Q00774`	protein
Aspergillus nidulans QutR `UniProtKB:Q00784`	protein
Corynebacterium glutamicum ATCC 13032 QsuD subunit `UniProtKB:Q9X5C9`	protein
quinate oxidation with NAD(P)+ `MetaCyc:QUINATE-5-DEHYDROGENASE-RXN`	molecular activity	left to right
3-dehydroquinate <=> 3-dehydroshikimate + H2O `RHEA:21099`	molecular activity	reversible
3-dehydroshikimate => 3,4-dihydroxybenzoate + H2O `RHEA:24849`	molecular activity	left to right
L-quinate + NAD(+) => 3-dehydroquinate + NADH + H(+) `RHEA:22365`	molecular activity	left to right

Mechanistic edges

Mechanistic edges and their cited evidence
Subject	Predicate and description	Object	Evidence
`MetaCyc:PWY-6416`	part_of Native pathway species context; individual enzyme evidence retains its strain and preparation scope.	Corynebacterium glutamicum R `NCBITaxon:340322`	MetaCyc:PWY-6416 Source assertion: The pathway species slot lists TAX-340322. This is the curated database organism association; its shared evidence blocks are not treated as direct confirmation of this NAD(P) route. Source location `/ptools-xml/Pathway[@frameid="PWY-6416"]/species/Organism[@frameid="TAX-340322"]`
`MetaCyc:PWY-6416`	part_of Native pathway species context; individual enzyme evidence retains its strain and preparation scope.	Corynebacterium glutamicum `NCBITaxon:1718`	MetaCyc:PWY-6416 Source assertion: The pathway species slot lists TAX-1718. This is the curated database organism association; its shared evidence blocks are not treated as direct confirmation of this NAD(P) route. Source location `/ptools-xml/Pathway[@frameid="PWY-6416"]/species/Organism[@frameid="TAX-1718"]`
`MetaCyc:PWY-6416`	part_of Native pathway species context; individual enzyme evidence retains its strain and preparation scope.	Amycolatopsis methanolica `NCBITaxon:1814`	MetaCyc:PWY-6416 Source assertion: The pathway species slot lists TAX-1814. This is the curated database organism association; its shared evidence blocks are not treated as direct confirmation of this NAD(P) route. Source location `/ptools-xml/Pathway[@frameid="PWY-6416"]/species/Organism[@frameid="TAX-1814"]`
`MetaCyc:PWY-6416`	part_of Native pathway species context; individual enzyme evidence retains its strain and preparation scope.	Aspergillus nidulans `NCBITaxon:162425`	MetaCyc:PWY-6416 Source assertion: The pathway species slot lists TAX-162425. This is the curated database organism association; its shared evidence blocks are not treated as direct confirmation of this NAD(P) route. Source location `/ptools-xml/Pathway[@frameid="PWY-6416"]/species/Organism[@frameid="TAX-162425"]`
`MetaCyc:PWY-6416`	part_of Native pathway species context; individual enzyme evidence retains its strain and preparation scope.	Neurospora crassa `NCBITaxon:5141`	MetaCyc:PWY-6416 Source assertion: The pathway species slot lists TAX-5141. This is the curated database organism association; its shared evidence blocks are not treated as direct confirmation of this NAD(P) route. Source location `/ptools-xml/Pathway[@frameid="PWY-6416"]/species/Organism[@frameid="TAX-5141"]`
quinate oxidation with NAD(P)+ `MetaCyc:QUINATE-5-DEHYDROGENASE-RXN`	part_of One of the three explicit native pathway members; the native reaction direction is preserved.	`MetaCyc:PWY-6416`	MetaCyc:PWY-6416 Source assertion: The reaction-list includes QUINATE-5-DEHYDROGENASE-RXN and the selected pathway layout is L2R. Source location `/ptools-xml/Pathway[@frameid="PWY-6416"]/reaction-list\|reaction-layout[Reaction/@frameid="QUINATE-5-DEHYDROGENASE-RXN"]`
(-)-quinate `CHEBI:29751`	consumes Selected catabolic pathway orientation.	quinate oxidation with NAD(P)+ `MetaCyc:QUINATE-5-DEHYDROGENASE-RXN`	MetaCyc:QUINATE-5-DEHYDROGENASE-RXN Source assertion: The native left side contains QUINATE. No explicit coefficient is supplied. Source location `/ptools-xml/Reaction[@frameid="QUINATE-5-DEHYDROGENASE-RXN"]/left/Compound[@frameid="QUINATE"]` MetaCyc:QUINATE Source assertion: The native compound links CHEBI:29751; its complete InChI agrees with the selected ChEBI molecular identity. Source location `/ptools-xml/Compound[@frameid="QUINATE"] /dblink[dblink-db="CHEBI"]\|inchi`
NAD(P)+ `MetaCyc:NAD-P-OR-NOP`	consumes Selected catabolic pathway orientation. Native NAD(P) class; this does not establish equal NAD and NADP acceptance by every enzyme or interchangeable nucleotide specificity.	quinate oxidation with NAD(P)+ `MetaCyc:QUINATE-5-DEHYDROGENASE-RXN`	MetaCyc:QUINATE-5-DEHYDROGENASE-RXN Source assertion: The native left side contains NAD-P-OR-NOP. No explicit coefficient is supplied. Source location `/ptools-xml/Reaction[@frameid="QUINATE-5-DEHYDROGENASE-RXN"]/left/Compound[@frameid="NAD-P-OR-NOP"]`
quinate oxidation with NAD(P)+ `MetaCyc:QUINATE-5-DEHYDROGENASE-RXN`	produces Selected catabolic pathway orientation.	3-dehydroquinate `CHEBI:32364`	MetaCyc:QUINATE-5-DEHYDROGENASE-RXN Source assertion: The native right side contains DEHYDROQUINATE. No explicit coefficient is supplied. Source location `/ptools-xml/Reaction[@frameid="QUINATE-5-DEHYDROGENASE-RXN"]/right/Compound[@frameid="DEHYDROQUINATE"]` MetaCyc:DEHYDROQUINATE Source assertion: The native compound links CHEBI:32364; its complete InChI agrees with the selected ChEBI molecular identity. Source location `/ptools-xml/Compound[@frameid="DEHYDROQUINATE"] /dblink[dblink-db="CHEBI"]\|inchi`
quinate oxidation with NAD(P)+ `MetaCyc:QUINATE-5-DEHYDROGENASE-RXN`	produces Selected catabolic pathway orientation. Native NAD(P) class; this does not establish equal NAD and NADP acceptance by every enzyme or interchangeable nucleotide specificity.	NAD(P)H `MetaCyc:NADH-P-OR-NOP`	MetaCyc:QUINATE-5-DEHYDROGENASE-RXN Source assertion: The native right side contains NADH-P-OR-NOP. No explicit coefficient is supplied. Source location `/ptools-xml/Reaction[@frameid="QUINATE-5-DEHYDROGENASE-RXN"]/right/Compound[@frameid="NADH-P-OR-NOP"]`
quinate oxidation with NAD(P)+ `MetaCyc:QUINATE-5-DEHYDROGENASE-RXN`	produces Selected catabolic pathway orientation.	hydron `CHEBI:15378`	MetaCyc:QUINATE-5-DEHYDROGENASE-RXN Source assertion: The native right side contains PROTON. No explicit coefficient is supplied. Source location `/ptools-xml/Reaction[@frameid="QUINATE-5-DEHYDROGENASE-RXN"]/right/Compound[@frameid="PROTON"]` MetaCyc:PROTON Source assertion: The native compound links CHEBI:15378; its complete InChI agrees with the selected ChEBI molecular identity. Source location `/ptools-xml/Compound[@frameid="PROTON"] /dblink[dblink-db="CHEBI"]\|inchi`
3-dehydroquinate <=> 3-dehydroshikimate + H2O `RHEA:21099`	part_of One of the three explicit native pathway members; the native reaction direction is preserved.	`MetaCyc:PWY-6416`	MetaCyc:PWY-6416 Source assertion: The reaction-list includes 3-DEHYDROQUINATE-DEHYDRATASE-RXN and the selected pathway layout is L2R. Source location `/ptools-xml/Pathway[@frameid="PWY-6416"]/reaction-list\|reaction-layout[Reaction/@frameid="3-DEHYDROQUINATE-DEHYDRATASE-RXN"]`
3-dehydroquinate `CHEBI:32364`	consumes Selected catabolic pathway orientation. The reaction itself is reversible; this edge does not restrict reverse chemistry.	3-dehydroquinate <=> 3-dehydroshikimate + H2O `RHEA:21099`	MetaCyc:3-DEHYDROQUINATE-DEHYDRATASE-RXN Source assertion: The native left side contains DEHYDROQUINATE. No explicit coefficient is supplied. Source location `/ptools-xml/Reaction[@frameid="3-DEHYDROQUINATE-DEHYDRATASE-RXN"]/left/Compound[@frameid="DEHYDROQUINATE"]` MetaCyc:DEHYDROQUINATE Source assertion: The native compound links CHEBI:32364; its complete InChI agrees with the selected ChEBI molecular identity. Source location `/ptools-xml/Compound[@frameid="DEHYDROQUINATE"] /dblink[dblink-db="CHEBI"]\|inchi` RHEA:21099 Source assertion: RHEA:21099 left side contains CHEBI:32364 with coefficient 1. Source location `http://rdf.rhea-db.org/21096_L rh:contains1 http://rdf.rhea-db.org/Participant_21096_compound_1486; http://rdf.rhea-db.org/Participant_21096_compound_1486 rh:compound http://rdf.rhea-db.org/Compound_1486`
3-dehydroquinate <=> 3-dehydroshikimate + H2O `RHEA:21099`	produces Selected catabolic pathway orientation. The reaction itself is reversible; this edge does not restrict reverse chemistry.	water `CHEBI:15377`	MetaCyc:3-DEHYDROQUINATE-DEHYDRATASE-RXN Source assertion: The native right side contains WATER. No explicit coefficient is supplied. Source location `/ptools-xml/Reaction[@frameid="3-DEHYDROQUINATE-DEHYDRATASE-RXN"]/right/Compound[@frameid="WATER"]` MetaCyc:WATER Source assertion: The native compound links CHEBI:15377; its complete InChI agrees with the selected ChEBI molecular identity. Source location `/ptools-xml/Compound[@frameid="WATER"] /dblink[dblink-db="CHEBI"]\|inchi` RHEA:21099 Source assertion: RHEA:21099 right side contains CHEBI:15377 with coefficient 1. Source location `http://rdf.rhea-db.org/21096_R rh:contains1 http://rdf.rhea-db.org/Participant_21096_compound_1283; http://rdf.rhea-db.org/Participant_21096_compound_1283 rh:compound http://rdf.rhea-db.org/Compound_1283`
3-dehydroquinate <=> 3-dehydroshikimate + H2O `RHEA:21099`	produces Selected catabolic pathway orientation. The reaction itself is reversible; this edge does not restrict reverse chemistry.	3-dehydroshikimate `CHEBI:16630`	MetaCyc:3-DEHYDROQUINATE-DEHYDRATASE-RXN Source assertion: The native right side contains 3-DEHYDRO-SHIKIMATE. No explicit coefficient is supplied. Source location `/ptools-xml/Reaction[@frameid="3-DEHYDROQUINATE-DEHYDRATASE-RXN"]/right/Compound[@frameid="3-DEHYDRO-SHIKIMATE"]` MetaCyc:3-DEHYDRO-SHIKIMATE Source assertion: The native compound links CHEBI:16630; its complete InChI agrees with the selected ChEBI molecular identity. Source location `/ptools-xml/Compound[@frameid="3-DEHYDRO-SHIKIMATE"] /dblink[dblink-db="CHEBI"]\|inchi` RHEA:21099 Source assertion: RHEA:21099 right side contains CHEBI:16630 with coefficient 1. Source location `http://rdf.rhea-db.org/21096_R rh:contains1 http://rdf.rhea-db.org/Participant_21096_compound_3489; http://rdf.rhea-db.org/Participant_21096_compound_3489 rh:compound http://rdf.rhea-db.org/Compound_3489`
3-dehydroshikimate => 3,4-dihydroxybenzoate + H2O `RHEA:24849`	part_of One of the three explicit native pathway members; the native reaction direction is preserved.	`MetaCyc:PWY-6416`	MetaCyc:PWY-6416 Source assertion: The reaction-list includes DHSHIKIMATE-DEHYDRO-RXN and the selected pathway layout is L2R. Source location `/ptools-xml/Pathway[@frameid="PWY-6416"]/reaction-list\|reaction-layout[Reaction/@frameid="DHSHIKIMATE-DEHYDRO-RXN"]`
3-dehydroshikimate `CHEBI:16630`	consumes Selected catabolic pathway orientation.	3-dehydroshikimate => 3,4-dihydroxybenzoate + H2O `RHEA:24849`	MetaCyc:DHSHIKIMATE-DEHYDRO-RXN Source assertion: The native left side contains 3-DEHYDRO-SHIKIMATE. No explicit coefficient is supplied. Source location `/ptools-xml/Reaction[@frameid="DHSHIKIMATE-DEHYDRO-RXN"]/left/Compound[@frameid="3-DEHYDRO-SHIKIMATE"]` MetaCyc:3-DEHYDRO-SHIKIMATE Source assertion: The native compound links CHEBI:16630; its complete InChI agrees with the selected ChEBI molecular identity. Source location `/ptools-xml/Compound[@frameid="3-DEHYDRO-SHIKIMATE"] /dblink[dblink-db="CHEBI"]\|inchi` RHEA:24849 Source assertion: RHEA:24849 left side contains CHEBI:16630 with coefficient 1. Source location `http://rdf.rhea-db.org/24848_L rh:contains1 http://rdf.rhea-db.org/Participant_24848_compound_3489; http://rdf.rhea-db.org/Participant_24848_compound_3489 rh:compound http://rdf.rhea-db.org/Compound_3489`
3-dehydroshikimate => 3,4-dihydroxybenzoate + H2O `RHEA:24849`	produces Selected catabolic pathway orientation.	3,4-dihydroxybenzoate `CHEBI:36241`	MetaCyc:DHSHIKIMATE-DEHYDRO-RXN Source assertion: The native right side contains 3-4-DIHYDROXYBENZOATE. No explicit coefficient is supplied. Source location `/ptools-xml/Reaction[@frameid="DHSHIKIMATE-DEHYDRO-RXN"]/right/Compound[@frameid="3-4-DIHYDROXYBENZOATE"]` MetaCyc:3-4-DIHYDROXYBENZOATE Source assertion: The native compound links CHEBI:36241; its complete InChI agrees with the selected ChEBI molecular identity. Source location `/ptools-xml/Compound[@frameid="3-4-DIHYDROXYBENZOATE"] /dblink[dblink-db="CHEBI"]\|inchi` RHEA:24849 Source assertion: RHEA:24849 right side contains CHEBI:36241 with coefficient 1. Source location `http://rdf.rhea-db.org/24848_R rh:contains1 http://rdf.rhea-db.org/Participant_24848_compound_3099; http://rdf.rhea-db.org/Participant_24848_compound_3099 rh:compound http://rdf.rhea-db.org/Compound_3099`
3-dehydroshikimate => 3,4-dihydroxybenzoate + H2O `RHEA:24849`	produces Selected catabolic pathway orientation.	water `CHEBI:15377`	MetaCyc:DHSHIKIMATE-DEHYDRO-RXN Source assertion: The native right side contains WATER. No explicit coefficient is supplied. Source location `/ptools-xml/Reaction[@frameid="DHSHIKIMATE-DEHYDRO-RXN"]/right/Compound[@frameid="WATER"]` MetaCyc:WATER Source assertion: The native compound links CHEBI:15377; its complete InChI agrees with the selected ChEBI molecular identity. Source location `/ptools-xml/Compound[@frameid="WATER"] /dblink[dblink-db="CHEBI"]\|inchi` RHEA:24849 Source assertion: RHEA:24849 right side contains CHEBI:15377 with coefficient 1. Source location `http://rdf.rhea-db.org/24848_R rh:contains1 http://rdf.rhea-db.org/Participant_24848_compound_1283; http://rdf.rhea-db.org/Participant_24848_compound_1283 rh:compound http://rdf.rhea-db.org/Compound_1283`
quinate oxidation with NAD(P)+ `MetaCyc:QUINATE-5-DEHYDROGENASE-RXN`	precedes Native pathway reaction ordering selects forward catabolic progression.	3-dehydroquinate <=> 3-dehydroshikimate + H2O `RHEA:21099`	MetaCyc:PWY-6416 Source assertion: QUINATE-5-DEHYDROGENASE-RXN is a predecessor of 3-DEHYDROQUINATE-DEHYDRATASE-RXN. Source location `/ptools-xml/Pathway[@frameid="PWY-6416"]/reaction-ordering[Reaction/@frameid="3-DEHYDROQUINATE-DEHYDRATASE-RXN"]/predecessor-reactions`
3-dehydroquinate <=> 3-dehydroshikimate + H2O `RHEA:21099`	precedes Native pathway reaction ordering selects forward catabolic progression.	3-dehydroshikimate => 3,4-dihydroxybenzoate + H2O `RHEA:24849`	MetaCyc:PWY-6416 Source assertion: 3-DEHYDROQUINATE-DEHYDRATASE-RXN is a predecessor of DHSHIKIMATE-DEHYDRO-RXN. Source location `/ptools-xml/Pathway[@frameid="PWY-6416"]/reaction-ordering[Reaction/@frameid="DHSHIKIMATE-DEHYDRO-RXN"]/predecessor-reactions`
(-)-quinate `CHEBI:29751`	consumes NAD-specific realization of the first oxidation step; distinct from the broad native NAD(P) class reaction.	L-quinate + NAD(+) => 3-dehydroquinate + NADH + H(+) `RHEA:22365`	MetaCyc:RXN-20483 Source assertion: RXN-20483 left side contains QUINATE; its physiological direction is left to right. Source location `/ptools-xml/Reaction[@frameid="RXN-20483"]/left/Compound[@frameid="QUINATE"]; /reaction-direction` RHEA:22365 Source assertion: RHEA:22365 left side contains CHEBI:29751 with coefficient 1. Source location `http://rdf.rhea-db.org/22364_L rh:contains1 http://rdf.rhea-db.org/Participant_22364_compound_3808; http://rdf.rhea-db.org/Participant_22364_compound_3808 rh:compound http://rdf.rhea-db.org/Compound_3808`
NAD(1-) `CHEBI:57540`	consumes NAD-specific realization of the first oxidation step; distinct from the broad native NAD(P) class reaction.	L-quinate + NAD(+) => 3-dehydroquinate + NADH + H(+) `RHEA:22365`	MetaCyc:RXN-20483 Source assertion: RXN-20483 left side contains NAD; its physiological direction is left to right. Source location `/ptools-xml/Reaction[@frameid="RXN-20483"]/left/Compound[@frameid="NAD"]; /reaction-direction` RHEA:22365 Source assertion: RHEA:22365 left side contains CHEBI:57540 with coefficient 1. Source location `http://rdf.rhea-db.org/22364_L rh:contains1 http://rdf.rhea-db.org/Participant_22364_compound_3484; http://rdf.rhea-db.org/Participant_22364_compound_3484 rh:compound http://rdf.rhea-db.org/Compound_3484`
L-quinate + NAD(+) => 3-dehydroquinate + NADH + H(+) `RHEA:22365`	produces NAD-specific realization of the first oxidation step; distinct from the broad native NAD(P) class reaction.	3-dehydroquinate `CHEBI:32364`	MetaCyc:RXN-20483 Source assertion: RXN-20483 right side contains DEHYDROQUINATE; its physiological direction is left to right. Source location `/ptools-xml/Reaction[@frameid="RXN-20483"]/right/Compound[@frameid="DEHYDROQUINATE"]; /reaction-direction` RHEA:22365 Source assertion: RHEA:22365 right side contains CHEBI:32364 with coefficient 1. Source location `http://rdf.rhea-db.org/22364_R rh:contains1 http://rdf.rhea-db.org/Participant_22364_compound_1486; http://rdf.rhea-db.org/Participant_22364_compound_1486 rh:compound http://rdf.rhea-db.org/Compound_1486`
L-quinate + NAD(+) => 3-dehydroquinate + NADH + H(+) `RHEA:22365`	produces NAD-specific realization of the first oxidation step; distinct from the broad native NAD(P) class reaction.	NADH(2-) `CHEBI:57945`	MetaCyc:RXN-20483 Source assertion: RXN-20483 right side contains NADH; its physiological direction is left to right. Source location `/ptools-xml/Reaction[@frameid="RXN-20483"]/right/Compound[@frameid="NADH"]; /reaction-direction` RHEA:22365 Source assertion: RHEA:22365 right side contains CHEBI:57945 with coefficient 1. Source location `http://rdf.rhea-db.org/22364_R rh:contains1 http://rdf.rhea-db.org/Participant_22364_compound_1650; http://rdf.rhea-db.org/Participant_22364_compound_1650 rh:compound http://rdf.rhea-db.org/Compound_1650`
L-quinate + NAD(+) => 3-dehydroquinate + NADH + H(+) `RHEA:22365`	produces NAD-specific realization of the first oxidation step; distinct from the broad native NAD(P) class reaction.	hydron `CHEBI:15378`	MetaCyc:RXN-20483 Source assertion: RXN-20483 right side contains PROTON; its physiological direction is left to right. Source location `/ptools-xml/Reaction[@frameid="RXN-20483"]/right/Compound[@frameid="PROTON"]; /reaction-direction` RHEA:22365 Source assertion: RHEA:22365 right side contains CHEBI:15378 with coefficient 1. Source location `http://rdf.rhea-db.org/22364_R rh:contains1 http://rdf.rhea-db.org/Participant_22364_compound_3249; http://rdf.rhea-db.org/Participant_22364_compound_3249 rh:compound http://rdf.rhea-db.org/Compound_3249`
Amycolatopsis methanolica AroQ subunit `UniProtKB:P46380`	part_of The experimentally purified A. methanolica enzyme is a homododecamer; one participant represents its repeated subunit identity.	3-dehydroquinate dehydratase `MetaCyc:CPLX-7980`	MetaCyc:CPLX-7980 Source assertion: Native complex CPLX-7980 contains 12 copies of MONOMER-15327; MONOMER-15327 independently maps to UniProtKB:P46380. Source location `/ptools-xml/Protein[@frameid="CPLX-7980"]/component` MetaCyc:MONOMER-15327 Source assertion: MONOMER-15327 has a direct UNIPROT unification dblink to P46380 and belongs to CPLX-7980. Source location `/ptools-xml/Protein[@frameid="MONOMER-15327"]/dblink[dblink-db="UNIPROT"]; /component-of`
3-dehydroquinate dehydratase `MetaCyc:CPLX-7980`	catalyzes Dual-role AroQ catalyzes dehydroquinate dehydration in quinate catabolism; its separate biosynthetic role does not expand this pathway.	3-dehydroquinate <=> 3-dehydroshikimate + H2O `RHEA:21099`	MetaCyc:ENZRXN-17378 Source assertion: ENZRXN-17378 assigns CPLX-7980 to 3-DEHYDROQUINATE-DEHYDRATASE-RXN with EV-EXP-IDA-PURIFIED-PROTEIN-NH and PMID1479361. Source location `/ptools-xml/Enzymatic-Reaction[@frameid="ENZRXN-17378"]`
Corynebacterium glutamicum ATCC 13032 QsuD subunit `UniProtKB:Q9X5C9`	part_of QsuD homodimer composition is separate from catalytic attribution; the monomer is not asserted to catalyze independently.	quinate/shikimate dehydrogenase `MetaCyc:CPLX-7981`	MetaCyc:CPLX-7981 Source assertion: CPLX-7981 contains two MONOMER-15330 subunits; MONOMER-15330 maps to UniProtKB:Q9X5C9, whose issuing entry is ATCC 13032. Source location `/ptools-xml/Protein[@frameid="CPLX-7981"]/component` MetaCyc:MONOMER-15330 Source assertion: MONOMER-15330 has a direct UNIPROT unification dblink to Q9X5C9 and belongs to CPLX-7981. Source location `/ptools-xml/Protein[@frameid="MONOMER-15330"]/dblink[dblink-db="UNIPROT"]; /component-of`
quinate/shikimate dehydrogenase `MetaCyc:CPLX-7981` experimental construct: Recombinant ATCC 13032 QsuD homodimer preparation. Native evidence specifies heterologously expressed purified protein; the associated 2NLO structural sample carries a 19-residue N-terminal extension with His6. Cleavage state across all kinetic preparations was not independently verified. Qualification evidence MetaCyc:ENZRXN-17380 Source assertion: The native activity links CPLX-7981 to NAD-specific RXN-20483, supported by heterologously expressed purified protein (PMID18566515) and mutant phenotype (PMID19376919); these sources involve distinct strain scopes. Source location `/ptools-xml/Enzymatic-Reaction[@frameid="ENZRXN-17380"]` DOI:10.2210/pdb2nlo/pdb Source assertion: 2NLO entity1 is an N-tagged wild-type Cgl0424 sample from ATCC13032, expressed in BL21(DE3) from pETNHis. Its 302-residue sequence is exactly a 19-residue His6-containing prefix followed by Q9X5C9. Source location `$.entity_poly.pdbx_seq_one_letter_code_can; $.entity_src_gen[0]; $.rcsb_polymer_entity.pdbx_mutation; QsuD-construct-identity.json`	catalyzes Recombinant ATCC 13032 QsuD supports the exact NAD-specific reaction RXN-20483/RHEA:22365. NADP turnover is much lower, not absent; the broader formal NAD(P) pathway member remains separately represented.	L-quinate + NAD(+) => 3-dehydroquinate + NADH + H(+) `RHEA:22365`	MetaCyc:ENZRXN-17380 Source assertion: The native activity links CPLX-7981 to NAD-specific RXN-20483, supported by heterologously expressed purified protein (PMID18566515) and mutant phenotype (PMID19376919); these sources involve distinct strain scopes. Source location `/ptools-xml/Enzymatic-Reaction[@frameid="ENZRXN-17380"]` MetaCyc:RXN-20483 Source assertion: RXN-20483 consumes quinate and NAD, producing dehydroquinate, NADH and a proton; native direction is PHYSIOL-LEFT-TO-RIGHT. Source location `/ptools-xml/Reaction[@frameid="RXN-20483"]/left; /right; /reaction-direction` MetaCyc:CPLX-7981 Source assertion: CPLX-7981 reports that replacing NAD+ with NADP+ reduces turnover by more than 300-fold; this supports preference, not complete absence of NADP activity. Source location `/ptools-xml/Protein[@frameid="CPLX-7981"]/comment`
Aspergillus nidulans QutB `UniProtKB:P25415` experimental construct: N-terminal metal-chelating-domain QutB fusion expressed from pRSETB/pRF2 in E. coli BL21(DE3), as described in Methods/Results; Table 2 labels the preparation GST-fusion. Qualification evidence PMID:8257437 metal-chelating domain on the N-terminal end of the quinate dehydrogenase enzyme.	catalyzes The recombinant A. nidulans QutB preparation was assayed with NAD+ (primary Table 2), supporting this NAD-specific realization. The native ENZRXN-17384 assignment to the broader NAD(P) pathway member is retained as source context and does not establish NADP activity.	L-quinate + NAD(+) => 3-dehydroquinate + NADH + H(+) `RHEA:22365`	MetaCyc:ENZRXN-17384 Source assertion: ENZRXN-17384 links MONOMER-15333/QutB to QUINATE-5-DEHYDROGENASE-RXN with heterologously expressed purified-protein evidence PMID8257437. Source location `/ptools-xml/Enzymatic-Reaction[@frameid="ENZRXN-17384"]` PMID:8257437 The purified quinate dehydrogenase is bifunctional PMID:8257437 NAD+ Source location `Table 2, quinate dehydrogenase fusion protein, NAD+ substrate row; superscript normalized`
Neurospora crassa Qa4 `UniProtKB:P07046`	catalyzes Native-host purified N. crassa Qa4 catalyzes DHS dehydration to protocatechuate. Metal-dependent activity and thermal stabilization require their own primary-assay edges.	3-dehydroshikimate => 3,4-dihydroxybenzoate + H2O `RHEA:24849`	MetaCyc:ENZRXN-17379 Source assertion: ENZRXN-17379 links MONOMER-15329/Qa4 to DHSHIKIMATE-DEHYDRO-RXN with EV-EXP-IDA-PURIFIED-PROTEIN-NH and PMID149131. Source location `/ptools-xml/Enzymatic-Reaction[@frameid="ENZRXN-17379"]`
hypothetical protein cgR_0493 [Corynebacterium glutamicum R] `NCBIProtein:BAF53460.1`	enables QsuB catalytic role in strain R is inferred from the 2009 operon, homology and induction context; no purified R-strain assay is asserted. The later ATCC13869 assay is a distinct protein context.	3-dehydroshikimate => 3,4-dihydroxybenzoate + H2O `RHEA:24849`	MetaCyc:MONOMER-15334 Source assertion: Native MONOMER-15334 explicitly states qsuB product was not characterized and infers DHS dehydratase activity from operon context, N-terminal similarity and induction. G-11737 is cgR_0493. Source location `/ptools-xml/Protein[@frameid="MONOMER-15334"]/comment; /gene` MetaCyc:G-11737 Source assertion: G-11737 qsuB has accession-1 cgR_0493 and product MONOMER-15334; the original R-genome protein for this exact locus is BAF53460.1. Source location `/ptools-xml/Gene[@frameid="G-11737"]/accession-1; /product; NCBIProtein:BAF53460.1 CDS/locus_tag`
Corynebacterium glutamicum R QsuC `UniProtKB:A4QB64`	enables QsuC activity in strain R is inferred from operon, sequence similarity and induction; native IGI annotation is not promoted to a purified-enzyme experiment.	3-dehydroquinate <=> 3-dehydroshikimate + H2O `RHEA:21099`	MetaCyc:MONOMER-15335 Source assertion: Native MONOMER-15335 explicitly states qsuC product was not characterized and infers DHQ dehydratase activity from operon context, 60% sequence similarity and induction. Source location `/ptools-xml/Protein[@frameid="MONOMER-15335"]/comment`
chorismate(2-) `CHEBI:29748`	activates Chorismate directly modifies QsuR promoter footprint in vitro (2mM screen; concentration dependence); genetic pathway perturbations support induction mechanism. Do not infer quinate/shikimate direct ligand binding.	hypothetical protein cgR_0491 [Corynebacterium glutamicum R] `NCBIProtein:BAF53458.1` experimental construct: N-terminal hexahistidine-tagged QsuR; pCRF206 derived from pColdI, expressed in E.coliBL21 Qualification evidence PMID:24674055 QsuR with an N-terminal hexahistidine tag	PMID:24674055 Chorismate is a direct effector of QsuR
hypothetical protein cgR_0491 [Corynebacterium glutamicum R] `NCBIProtein:BAF53458.1`	activates C.glutamicum R QsuR activates qsuB/qsuC transcription as part of qsuABCD;2009shikimate-grown deletion/complementation. Residual induction means QsuR is not exclusive regulator.	qsuB `MetaCyc:G-11737`	PMID:19376919 QsuR acts as an activator of the qsuABCD genes.
hypothetical protein cgR_0491 [Corynebacterium glutamicum R] `NCBIProtein:BAF53458.1`	activates C.glutamicum R QsuR activates qsuB/qsuC transcription as part of qsuABCD;2009shikimate-grown deletion/complementation. Residual induction means QsuR is not exclusive regulator.	qsuC `MetaCyc:G-11738`	PMID:19376919 QsuR acts as an activator of the qsuABCD genes.
4-hydroxyphenylpyruvate dioxygenase [Corynebacterium glutamicum] `NCBIProtein:ANU32720.1` experimental construct: C-terminal His6-tagged full-length QsuB from C.glutamicum2256/ATCC13869; pET22b-qsuB expressed in E.coliBL21(DE3). Tag placement is inferred from inspected P4 tail and CDS alignment, not merely vector name. No separately deposited complete assay-clone sequence was inspected. Qualification evidence PMID:32822353 His-tag Source location `Results QsuB purification; S1Table P3/P4 and primer/CDS check ground C-terminal placement`	catalyzes ATCC13869 full-length His-tagged QsuB DHS-to-PCA reaction; spectrophotometry plus supplementary HPLC product comparison. Sourcegene matches issuing ATCC13869 CDS and P3/P4/P5 primer boundaries.	3-dehydroshikimate => 3,4-dihydroxybenzoate + H2O `RHEA:24849`	PMID:32822353 conversion of DHS to 3,4-DHBA
4-hydroxyphenylpyruvate dioxygenase [Corynebacterium glutamicum] `NCBIProtein:ANU32720.1` experimental construct: C-terminal His6-tagged full-length QsuB from C.glutamicum2256/ATCC13869; pET22b-qsuB expressed in E.coliBL21(DE3). Tag placement is inferred from inspected P4 tail and CDS alignment, not merely vector name. No separately deposited complete assay-clone sequence was inspected. Qualification evidence PMID:32822353 His-tag Source location `Results QsuB purification; S1Table P3/P4 and primer/CDS check ground C-terminal placement`	has_cofactor In vitro alternative metal support: Co>Mg>Mn, 10mM metal screen; pH7.5. This is not evidence of unique physiological metal requirement.	cobalt(2+) `CHEBI:48828`	PMID:32822353 Co2+, Mg2+, Mn2+ Source location `Abstract; Results Fig5A metal assay; XML superscript normalized`
4-hydroxyphenylpyruvate dioxygenase [Corynebacterium glutamicum] `NCBIProtein:ANU32720.1` experimental construct: C-terminal His6-tagged full-length QsuB from C.glutamicum2256/ATCC13869; pET22b-qsuB expressed in E.coliBL21(DE3). Tag placement is inferred from inspected P4 tail and CDS alignment, not merely vector name. No separately deposited complete assay-clone sequence was inspected. Qualification evidence PMID:32822353 His-tag Source location `Results QsuB purification; S1Table P3/P4 and primer/CDS check ground C-terminal placement`	has_cofactor In vitro alternative metal support: Co>Mg>Mn, 10mM metal screen; pH7.5. This is not evidence of unique physiological metal requirement.	magnesium(2+) `CHEBI:18420`	PMID:32822353 Co2+, Mg2+, Mn2+ Source location `Abstract; Results Fig5A metal assay; XML superscript normalized`
4-hydroxyphenylpyruvate dioxygenase [Corynebacterium glutamicum] `NCBIProtein:ANU32720.1` experimental construct: C-terminal His6-tagged full-length QsuB from C.glutamicum2256/ATCC13869; pET22b-qsuB expressed in E.coliBL21(DE3). Tag placement is inferred from inspected P4 tail and CDS alignment, not merely vector name. No separately deposited complete assay-clone sequence was inspected. Qualification evidence PMID:32822353 His-tag Source location `Results QsuB purification; S1Table P3/P4 and primer/CDS check ground C-terminal placement`	has_cofactor In vitro alternative metal support: Co>Mg>Mn, 10mM metal screen; pH7.5. This is not evidence of unique physiological metal requirement.	manganese(2+) `CHEBI:29035`	PMID:32822353 Co2+, Mg2+, Mn2+ Source location `Abstract; Results Fig5A metal assay; XML superscript normalized`
3,4-dihydroxybenzoate `CHEBI:36241`	inhibits PCA (3,4-DHBA) causes mixed inhibition of full-length C-terminalHis6 QsuB in vitro. The Methods and Fig7caption report different inhibitor concentrations; no numeric range is adopted. Truncated N-QsuB shows a different inhibition pattern.	4-hydroxyphenylpyruvate dioxygenase [Corynebacterium glutamicum] `NCBIProtein:ANU32720.1` experimental construct: C-terminal His6-tagged full-length QsuB from C.glutamicum2256/ATCC13869; pET22b-qsuB expressed in E.coliBL21(DE3). Tag placement is inferred from inspected P4 tail and CDS alignment, not merely vector name. No separately deposited complete assay-clone sequence was inspected. Qualification evidence PMID:32822353 His-tag Source location `Results QsuB purification; S1Table P3/P4 and primer/CDS check ground C-terminal placement`	PMID:32822353 inhibited by 3,4-DHBA Source location `Results kinetic analysis; Figure 7 and caption (full-length QsuB)`
Neurospora crassa Qa4 `UniProtKB:P07046`	has_cofactor Purified N.crassa Qa4 maximal activity in certain divalent cations including Mg; Mg also stabilizes heat sensitivity. Abstract-only scope, not unique obligatory cofactor.	magnesium(2+) `CHEBI:18420`	PMID:149131 maximal catalytic activity only when assayed in the presence of certain divalent cations, e.g. magnesium.
Neurospora crassa Qa1F `UniProtKB:P11638`	activates 74A-derived genetic and transcript assays support Qa1F positive transcriptional control; qa3 and qa1F measured. No assertion of direct physical binding from this study.	qa-3 `Entrez:3875774`	PMID:2943985 positively controls, at the transcriptional level Source location `Printed3598 conclusion; specific transcript data3596`
Neurospora crassa Qa1F `UniProtKB:P11638`	activates 74A-derived genetic and transcript assays support Qa1F positive transcriptional control; qa3 and qa1F measured. No assertion of direct physical binding from this study.	qa-1F `Entrez:3875756`	PMID:2943985 positively controls, at the transcriptional level Source location `Printed3598 conclusion; specific transcript data3596`
Neurospora crassa Qa1S `UniProtKB:P11637`	inhibits Qa1S negative control of qa1F transcription in historical74A-derived mutants; Results3596 and conclusion3598. Functional repression does not demonstrate direct Qa1S–Qa1F protein binding.	qa-1F `Entrez:3875756`	PMID:2943985 negative control by the qa-1S gene.
Neurospora crassa qa-y quinate permease `UniProtKB:P11636`	enables qa-y deletion growth phenotype supports quinic-acid permease. Enables pathway substrate entry; this predicate does not claim catalytic conversion or direct transport kinetics.	`MetaCyc:PWY-6416`	PMID:1533844 this gene encodes a quinic acid permease.
Aspergillus nidulans QutD `UniProtKB:P15325`	enables qutD loss blocks growth and induction atpH6.5, rescued atpH3.5; primary abstract calls permease hypothesis. Does not establish universal low-pH passive uptake.	`MetaCyc:PWY-6416`	PMID:2835177 a permease required for transport of quinate ion into mycelium at pH 6.5.
Neurospora crassa Qa2 `UniProtKB:P05195`	catalyzes Curated activity for N.crassa reference protein. Native host and1993heterologous contexts are distinct; do not ingest misassigned QutB Km values in this entry.	3-dehydroquinate <=> 3-dehydroshikimate + H2O `RHEA:21099`	UniProtKB:P05195 Source assertion: P05195 qa-2 catalytic-activity annotation gives DHQ→DHS+water; physiological left-to-right RHEA21097 with ECO0000269 PMID126226/8257437. Source location `$.comments[?(@.commentType=="CATALYTIC ACTIVITY")]; $.organism; $.genes`
Neurospora crassa Qa3 `UniProtKB:P11635`	catalyzes N.crassa Qa3 first-step NAD activity; exact NAD specialization distinct from broad native NAD(P) member.	L-quinate + NAD(+) => 3-dehydroquinate + NADH + H(+) `RHEA:22365`	UniProtKB:P11635 Source assertion: P11635 qa-3 has NAD-dependent quinate dehydrogenase activity RHEA22364 and physiological left-to-right RHEA22365, ECO0000269 PMID151647. Source location `$.comments[?(@.commentType=="CATALYTIC ACTIVITY")]; $.organism; $.genes`
Aspergillus nidulans QutE `UniProtKB:P05147`	catalyzes Curated catalytic assignment, with catalytic field based on rule and separate experimental function citations; not a newly inspected direct enzyme assay.	3-dehydroquinate <=> 3-dehydroshikimate + H2O `RHEA:21099`	UniProtKB:P05147 Source assertion: P05147 qutE catalytic activity is DHQ→DHS+water, RHEA21096, supported there by HAMAP MF03136/ECO0000255; experimental function/kinetics cite1554351/8870678. Source location `$.comments[?(@.commentType=="CATALYTIC ACTIVITY")]; $.organism; $.genes`
Aspergillus nidulans QutA `UniProtKB:P10563`	activates A.nidulans QutA functional activation of pathway transcription; this source has no per-text evidence code. No new direct binding experiment claimed.	`MetaCyc:PWY-6416`	UniProtKB:P10563 Source assertion: P10563 FUNCTION assigns transcriptional activation of genes for quinate metabolism by binding a16bp sequence ahead of each qut gene. Source location `$.comments[?(@.commentType=="FUNCTION")]; $.organism; $.genes`
Aspergillus nidulans QutR `UniProtKB:Q00784`	inhibits A.nidulans QutR functional repression. Direct physical inhibition/binding edge omitted because2000construct details were not inspected.	`MetaCyc:PWY-6416`	UniProtKB:Q00784 Source assertion: Q00784 FUNCTION assigns negative transcriptional regulation of quinate-utilization genes, ECO0000269 PMIDs10926843/8294040/8611179; direct QutA binding is described as a possible mechanism. Source location `$.comments[?(@.commentType=="FUNCTION")]; $.organism; $.genes`
Neurospora crassa Qa1F `UniProtKB:P11638`	activates Qa1F positive qa2 transcriptional control; genomic identity independently grounded. Broad cluster evidence, not specific new protein-binding assay.	qa-2 `Entrez:3875772`	UniProtKB:P11638 Source assertion: P11638 FUNCTION assigns activation of qa cluster gene expression (PMIDs123642,2525625,6198093,6458044), with qa2 a structural cluster gene. Source location `$.comments[?(@.commentType=="FUNCTION")]; $.organism; $.genes`
Neurospora crassa Qa1S `UniProtKB:P11637`	inhibits Qa1S repression of qa2 expression supported by deletion phenotype; abstract-level primary corroboration, no direct binding claim.	qa-2 `Entrez:3875772`	UniProtKB:P11637 Source assertion: P11637 DISRUPTION PHENOTYPE reports constitutive qa-2,qa-1F,qa-x expression after disruption, ECO0000269 PMID1533844. Source location `$.comments[?(@.commentType=="DISRUPTION PHENOTYPE")]; $.organism; $.genes`
Aspergillus nidulans QutC `UniProtKB:Q00774` experimental construct: A.nidulans QutC overproduced in E.coli and purified; abstract only. Precise tag, cleavage state and cloning boundaries were not inspected; no claim native untagged enzyme was assayed. Qualification evidence PMID:8670107 overproduced Source location `Primaryabstract QutC production sentence`	catalyzes Purified A.nidulans DHS dehydratase substrate kinetics; recombinant E.coli assay in1996primaryabstract.	3-dehydroshikimate => 3,4-dihydroxybenzoate + H2O `RHEA:24849`	PMID:8670107 purified DHS dehydratase Source location `Primaryabstract, purified DHSdehydratase paragraph`
Aspergillus nidulans QutC `UniProtKB:Q00774` experimental construct: A.nidulans QutC overproduced in E.coli and purified; abstract only. Precise tag, cleavage state and cloning boundaries were not inspected; no claim native untagged enzyme was assayed. Qualification evidence PMID:8670107 overproduced Source location `Primaryabstract QutC production sentence`	has_cofactor Mg/Mn/Zn alternatives satisfy bivalent-ion requirement in vitro; no unique physiological preference.	magnesium(2+) `CHEBI:18420`	PMID:8670107 Mg(2+), Mn(2+) or Zn(2+) Source location `Primaryabstract, purified DHSdehydratase paragraph`
Aspergillus nidulans QutC `UniProtKB:Q00774` experimental construct: A.nidulans QutC overproduced in E.coli and purified; abstract only. Precise tag, cleavage state and cloning boundaries were not inspected; no claim native untagged enzyme was assayed. Qualification evidence PMID:8670107 overproduced Source location `Primaryabstract QutC production sentence`	has_cofactor Mg/Mn/Zn alternatives satisfy bivalent-ion requirement in vitro; no unique physiological preference.	manganese(2+) `CHEBI:29035`	PMID:8670107 Mg(2+), Mn(2+) or Zn(2+) Source location `Primaryabstract, purified DHSdehydratase paragraph`
Aspergillus nidulans QutC `UniProtKB:Q00774` experimental construct: A.nidulans QutC overproduced in E.coli and purified; abstract only. Precise tag, cleavage state and cloning boundaries were not inspected; no claim native untagged enzyme was assayed. Qualification evidence PMID:8670107 overproduced Source location `Primaryabstract QutC production sentence`	has_cofactor Mg/Mn/Zn alternatives satisfy bivalent-ion requirement in vitro; no unique physiological preference.	zinc(2+) `CHEBI:29105`	PMID:8670107 Mg(2+), Mn(2+) or Zn(2+) Source location `Primaryabstract, purified DHSdehydratase paragraph`
Corynebacterium glutamicum R QsuD `UniProtKB:A4QB65`	enables C.glutamicum R qsuD disruption abolishes quinate/shikimate growth and complementation restores it; native genetic dependence supports the NAD-linked firststep. This is not a purified R-strain enzyme kinetics assay.	L-quinate + NAD(+) => 3-dehydroquinate + NADH + H(+) `RHEA:22365`	PMID:19376919 completely suppressed growth Source location `Abstract; Results qsuD growth Fig2`

References

MetaCyc:PWY-6416 MetaCyc native object PWY-6416 (source version: MetaCyc 27.0)
MetaCyc:QUINATE-5-DEHYDROGENASE-RXN MetaCyc native object QUINATE-5-DEHYDROGENASE-RXN (source version: MetaCyc 27.0)
MetaCyc:QUINATE MetaCyc native object QUINATE (source version: MetaCyc 27.0)
MetaCyc:DEHYDROQUINATE MetaCyc native object DEHYDROQUINATE (source version: MetaCyc 27.0)
MetaCyc:PROTON MetaCyc native object PROTON (source version: MetaCyc 27.0)
MetaCyc:3-DEHYDROQUINATE-DEHYDRATASE-RXN MetaCyc native object 3-DEHYDROQUINATE-DEHYDRATASE-RXN (source version: MetaCyc 27.0)
RHEA:21099 Rhea equation RHEA:21099 (source version: Rhea 142)
MetaCyc:WATER MetaCyc native object WATER (source version: MetaCyc 27.0)
MetaCyc:3-DEHYDRO-SHIKIMATE MetaCyc native object 3-DEHYDRO-SHIKIMATE (source version: MetaCyc 27.0)
MetaCyc:DHSHIKIMATE-DEHYDRO-RXN MetaCyc native object DHSHIKIMATE-DEHYDRO-RXN (source version: MetaCyc 27.0)
RHEA:24849 Rhea equation RHEA:24849 (source version: Rhea 142)
MetaCyc:3-4-DIHYDROXYBENZOATE MetaCyc native object 3-4-DIHYDROXYBENZOATE (source version: MetaCyc 27.0)
MetaCyc:RXN-20483 MetaCyc native object RXN-20483 (source version: MetaCyc 27.0)
RHEA:22365 Rhea equation RHEA:22365 (source version: Rhea 142)
MetaCyc:CPLX-7980 MetaCyc CPLX-7980 complete native object (source version: 27.0)
MetaCyc:ENZRXN-17378 MetaCyc ENZRXN-17378 complete native object (source version: 27.0)
MetaCyc:CPLX-7981 MetaCyc CPLX-7981 complete native object (source version: 27.0)
MetaCyc:ENZRXN-17380 MetaCyc ENZRXN-17380 complete native object (source version: 27.0)
PMID:8257437 Characterization of the 3-dehydroquinase domain of the pentafunctional AROM protein, and the quinate dehydrogenase from Aspergillus nidulans, and the overproduction of the type II 3-dehydroquinase from neurospora crassa. (source version: full_text_selected_pages; retrieved2026-10-14; PMC primary abstract/scan-index HTML plus hash-bound scan pages in original-bindings)
MetaCyc:ENZRXN-17384 MetaCyc ENZRXN-17384 complete native object (source version: 27.0)
MetaCyc:ENZRXN-17379 MetaCyc ENZRXN-17379 complete native object (source version: 27.0)
MetaCyc:MONOMER-15334 MetaCyc MONOMER-15334 complete native object (source version: 27.0)
MetaCyc:MONOMER-15335 MetaCyc MONOMER-15335 complete native object (source version: 27.0)
DOI:10.2210/pdb2nlo/pdb PDB2NLO polymer entity1 structural sample metadata (source version: RCSB JSON acquired 2026-10-14)
MetaCyc:MONOMER-15327 MetaCyc MONOMER-15327 complete native object (source version: 27.0)
MetaCyc:MONOMER-15330 MetaCyc MONOMER-15330 complete native object (source version: 27.0)
MetaCyc:G-11737 MetaCyc G-11737 complete native object (source version: 27.0)
PMID:149131 Purification and characterization of 3-dehydroshikimate dehydratase, an enzyme in the inducible quinic acid catabolic pathway of Neurospora crassa. (source version: abstract_only; retrieved2026-10-14; primary publication abstract in EuropePMC core record; no fulltext claim)
PMID:1533844 Use of gene replacement transformation to elucidate gene function in the qa gene cluster of Neurospora crassa. (source version: abstract_only; retrieved2026-10-14; PMC primary abstract/scan-index HTML plus hash-bound scan pages in original-bindings)
PMID:19376919 Regulation of expression of genes involved in quinate and shikimate utilization in Corynebacterium glutamicum. (source version: full_text; retrieved2026-10-14; PMC primary abstract/scan-index HTML plus hash-bound scan pages in original-bindings)
PMID:24674055 Chorismate-dependent transcriptional regulation of quinate/shikimate utilization genes by LysR-type transcriptional regulator QsuR in Corynebacterium glutamicum: carbon flow control at metabolic branch point. (source version: full_text_web_transcript; retrieved2026-10-14)
PMID:2835177 Identification and isolation of a putative permease gene in the quinic acid utilization (QUT) gene cluster of Aspergillus nidulans. (source version: abstract_only; retrieved2026-10-14; primary publication abstract in EuropePMC core record; no fulltext claim)
PMID:2943985 Autogenous regulation of the positive regulatory qa-1F gene in Neurospora crassa. (source version: full_text_selected_pages; retrieved2026-10-14; PMC primary abstract/scan-index HTML plus hash-bound scan pages in original-bindings)
PMID:8670107 Control of metabolic flux through the quinate pathway in Aspergillus nidulans. (source version: abstract_only; retrieved2026-10-14; PMC primary abstract/scan-index HTML plus hash-bound scan pages in original-bindings)
PMID:32822353 Characterization of the Corynebacterium glutamicum dehydroshikimate dehydratase QsuB and its potential for microbial production of protocatechuic acid. (source version: full_text; retrieved2026-10-14)
UniProtKB:P05195 UniProt P05195 structured protein entry (source version: {'firstPublicDate': '1987-08-13', 'lastAnnotationUpdateDate': '2026-09-02', 'lastSequenceUpdateDate': '1989-10-01', 'entryVersion': 146, 'sequenceVersion': 2})
UniProtKB:P11635 UniProt P11635 structured protein entry (source version: {'firstPublicDate': '1989-10-01', 'lastAnnotationUpdateDate': '2026-09-02', 'lastSequenceUpdateDate': '2007-12-04', 'entryVersion': 143, 'sequenceVersion': 2})
UniProtKB:P05147 UniProt P05147 structured protein entry (source version: {'firstPublicDate': '1987-08-13', 'lastAnnotationUpdateDate': '2026-09-02', 'lastSequenceUpdateDate': '2007-05-01', 'entryVersion': 139, 'sequenceVersion': 3})
UniProtKB:P10563 UniProt P10563 structured protein entry (source version: {'firstPublicDate': '1989-07-01', 'lastAnnotationUpdateDate': '2026-09-02', 'lastSequenceUpdateDate': '2007-05-01', 'entryVersion': 143, 'sequenceVersion': 2})
UniProtKB:Q00784 UniProt Q00784 structured protein entry (source version: {'firstPublicDate': '2010-11-30', 'lastAnnotationUpdateDate': '2026-09-02', 'lastSequenceUpdateDate': '1999-01-01', 'entryVersion': 142, 'sequenceVersion': 2})
UniProtKB:P11638 UniProt P11638 structured protein entry (source version: {'firstPublicDate': '1989-10-01', 'lastAnnotationUpdateDate': '2026-09-02', 'lastSequenceUpdateDate': '2004-03-01', 'entryVersion': 153, 'sequenceVersion': 2})
UniProtKB:P11637 UniProt P11637 structured protein entry (source version: {'firstPublicDate': '1989-10-01', 'lastAnnotationUpdateDate': '2026-09-02', 'lastSequenceUpdateDate': '2014-03-19', 'entryVersion': 144, 'sequenceVersion': 3})

Curation history

2026-10-14T19:07:41Z codex
- CREATE — Add quinate degradation II with scoped enzyme and regulatory evidence
  Curated MetaCyc:PWY-6416 after whole-repository duplicate searches including ignored and hidden files. Retained three formal native reactions and a separate NAD-specific realization, species/strain distinctions, experimental construct qualifiers, and source conflicts. Source projections, molecular-identity checks, primary readings and authority provenance are retained under research/pathway_additions/2026-10-14-next-257/quinate-ii. This author event records the addition; independent review and final validation are separate observations.
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2026-10-14T19:17:49Z codex
- EDIT — Address independent quinate review findings and identifier labels
  Applied five findings from initial scientific review 20261014T191557Z-quinate-ii-initial-scientific-review and integration review 20261014T191459Z-quinate-ii-integration-initial, tracked in issues 545, 546 and 547. Retargeted tagged QutB catalysis to the exact NAD-specific reaction, added the nearest QsuD NADP-specificity evidence, limited all five QsuB sequence statements to inspected evidence, corrected its inhibition locator, and restored four issuing MetaCyc participant labels. Preserved all node identities, 60 edges, reaction sides and references. Initial reviews remain immutable; independent successor observations and final gates determine acceptance.
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