quinate degradation I

MetaCyc:QUINATEDEG-PWY

The three-step MetaCyc 27.0 quinate degradation I definition converts L-quinate through 3-dehydroquinate and 3-dehydroshikimate to protocatechuate. The initial oxidation retains the source-defined quinone/quinol classes; PQQ is an enzyme cofactor, not a net reaction substrate. The shared dehydroquinate dehydration is reversible although the pathway selects catabolic forward flux. Enzyme evidence is qualified by organism, preparation and construct; the record does not assert a purified three-enzyme reconstitution in one strain.

Pathway type
aromatic compound catabolism
Organism scope

Read the source YAML

Pathway network

29 nodes · 37 asserted directed edges

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

Pathway network: quinate degradation I 29 nodes · 37 asserted directed edges. Every arrow links to its evidence table row; nodes link to their component details. Isolated declared components are retained. MetaCyc:QUINATEDEG-PWY — part_of → NCBITaxon:62977; Native pathway species context; individual enzyme evidence retains its strain and preparation scope.; Evidence: MetaCyc:QUINATEDEG-PWYpart of MetaCyc:QUINATEDEG-PWY — part_of → NCBITaxon:442; Native pathway species context; individual enzyme evidence retains its strain and preparation scope.; Evidence: MetaCyc:QUINATEDEG-PWYpart of MetaCyc:1.1.99.25-RXN — part_of → MetaCyc:QUINATEDEG-PWY; One of the three explicit native pathway members; the native reaction direction is preserved.; Evidence: MetaCyc:QUINATEDEG-PWYpart of CHEBI:29751 — consumes → MetaCyc:1.1.99.25-RXN; Selected catabolic pathway orientation.; Evidence: MetaCyc:1.1.99.25-RXN, MetaCyc:QUINATEconsumes MetaCyc:Quinones — consumes → MetaCyc:1.1.99.25-RXN; Selected catabolic pathway orientation. Native generic quinone class; this does not establish specificity for every class member or a measured physiological quinone.; Evidence: MetaCyc:1.1.99.25-RXNconsumes MetaCyc:1.1.99.25-RXN — produces → CHEBI:32364; Selected catabolic pathway orientation.; Evidence: MetaCyc:1.1.99.25-RXN, MetaCyc:DEHYDROQUINATEproduces MetaCyc:1.1.99.25-RXN — produces → MetaCyc:Reduced-Quinones; Selected catabolic pathway orientation. Native generic quinone class; this does not establish specificity for every class member or a measured physiological quinone.; Evidence: MetaCyc:1.1.99.25-RXNproduces RHEA:21099 — part_of → MetaCyc:QUINATEDEG-PWY; One of the three explicit native pathway members; the native reaction direction is preserved.; Evidence: MetaCyc:QUINATEDEG-PWYpart of CHEBI:32364 — consumes → RHEA:21099; Selected catabolic pathway orientation. The reaction itself is reversible; this edge does not restrict reverse chemistry.; Evidence: MetaCyc:3-DEHYDROQUINATE-DEHYDRATASE-RXN, MetaCyc:DEHYDROQUINATE, RHEA:21099consumes RHEA:21099 — produces → CHEBI:15377; Selected catabolic pathway orientation. The reaction itself is reversible; this edge does not restrict reverse chemistry.; Evidence: MetaCyc:3-DEHYDROQUINATE-DEHYDRATASE-RXN, MetaCyc:WATER, RHEA:21099produces RHEA:21099 — produces → CHEBI:16630; Selected catabolic pathway orientation. The reaction itself is reversible; this edge does not restrict reverse chemistry.; Evidence: MetaCyc:3-DEHYDROQUINATE-DEHYDRATASE-RXN, MetaCyc:3-DEHYDRO-SHIKIMATE, RHEA:21099produces RHEA:24849 — part_of → MetaCyc:QUINATEDEG-PWY; One of the three explicit native pathway members; the native reaction direction is preserved.; Evidence: MetaCyc:QUINATEDEG-PWYpart of CHEBI:16630 — consumes → RHEA:24849; Selected catabolic pathway orientation.; Evidence: MetaCyc:DHSHIKIMATE-DEHYDRO-RXN, MetaCyc:3-DEHYDRO-SHIKIMATE, RHEA:24849consumes RHEA:24849 — produces → CHEBI:36241; Selected catabolic pathway orientation.; Evidence: MetaCyc:DHSHIKIMATE-DEHYDRO-RXN, MetaCyc:3-4-DIHYDROXYBENZOATE, RHEA:24849produces RHEA:24849 — produces → CHEBI:15377; Selected catabolic pathway orientation.; Evidence: MetaCyc:DHSHIKIMATE-DEHYDRO-RXN, MetaCyc:WATER, RHEA:24849produces RHEA:21099 — precedes → RHEA:24849; Native pathway reaction ordering selects forward catabolic progression.; Evidence: MetaCyc:QUINATEDEG-PWYprecedes MetaCyc:1.1.99.25-RXN — precedes → RHEA:21099; Native pathway reaction ordering selects forward catabolic progression.; Evidence: MetaCyc:QUINATEDEG-PWYprecedes MetaCyc:MONOMER-0 — catalyzes → RHEA:21099; subject molecular state: Native IFO3244 detergent-purified pDQD assembly. Estimated 191 kDa and 16 kDa subunit support a proposed 12-subunit assembly; no engineered construct. N-terminal comparison does not establish whole-sequence identity to 621H.; Evidence PMID:18540103: pDQD was highly purified; Native IFO3244 pDQD catalyzes DHQ dehydration. PMID: 18540103 measures a 191 kDa native mass and 16 kDa SDS subunit, suggesting 12 subunits; the source molecular-weight field 189 kDa is not copied. Exact 621H sequence identity is not assumed.; Evidence: MetaCyc:ENZRXN-02catalyzes UniProtKB:Q59086 — catalyzes → MetaCyc:1.1.99.25-RXN; Native ADP1 QuiA activity is supported by genetic and cell-extract results in PMID: 8002591. The source groups this as quinone-dependent oxidation; this does not establish use of every quinone or transfer purified Acinetobacter SA1/AC3 measurements to ADP1.; Evidence: MetaCyc:ENZRXN-29, MetaCyc:MONOMER-28catalyzes MetaCyc:MONOMER-1 — catalyzes → RHEA:24849; subject molecular state: Native IFO3244 partially purified cytoplasmic enzyme fraction; DHS-dehydratase activity eluted separately from DQD on DEAE-Sephadex A-50. Exact protein sequence, termini and oligomeric state are unresolved.; Evidence PMID:14586099: DSA dehydratase was separated from DQD; Native IFO3244 DHS-dehydratase activity was separated from DQD and detected with a coupled qualitative protocatechuate assay. No gene, sequence or purified homogeneous protein identity is claimed.; Evidence: MetaCyc:ENZRXN-3catalyzes UniProtKB:Q59087 — catalyzes → RHEA:21099; Native ADP1 induced thermolabile QuiB activity and deletion phenotypes support catabolic DHQ dehydration (PMID: 7592351). The old recombinant 290-aa annotation and proposed leader localization are not assumed identical to the corrected 272-aa canonical sequence.; Evidence: MetaCyc:ENZRXN-35, MetaCyc:MONOMER-33catalyzes UniProtKB:Q43922 — catalyzes → RHEA:24849; subject experimental construct: ADP1 genomic quiC expressed in E. coli DH5α(pZR564), a 2.0 kb HindIII insert; crude-extract assay. No protein tag reported or expressed termini measured. Text/Table 1 disagree on pBSK versus pBKS vector label.; Evidence PMID:7592351: pZR564 contains the open reading frame; DHS dehydration is supported by cloned quiC activity and native genetic phenotypes. The native protein comment incorrectly labels the assay as DHQ dehydration; no numeric activity is copied.; Evidence: MetaCyc:ENZRXN-38, MetaCyc:MONOMER-37catalyzes MetaCyc:MONOMER-67 — catalyzes → MetaCyc:1.1.99.25-RXN; subject molecular state: Native IFO3244 membrane holo-QDH preparation; SDS bands approximately 65 and 21 kDa may reflect proteolysis of one polypeptide. Exact cleavage and whole-protein sequence are unresolved.; Evidence PMID:15598527: could be the result of proteolysis of single polypeptide; The native source assigns IFO3244 QDH to the generic quinone oxidation reaction. The inspected primary abstract supports purified holo-QDH; the full-body acceptor panel remains unread, so universal quinone specificity is not asserted.; Evidence: MetaCyc:ENZRXN-68catalyzes MetaCyc:MONOMER-0 — part_of → NCBITaxon:442; Source protein taxon context; assays and preparations remain strain-qualified on catalytic edges. This is not a claim that every isolate of the species expresses the full pathway.; Evidence: MetaCyc:MONOMER-0part of MetaCyc:MONOMER-1 — part_of → NCBITaxon:442; Source protein taxon context; assays and preparations remain strain-qualified on catalytic edges. This is not a claim that every isolate of the species expresses the full pathway.; Evidence: MetaCyc:MONOMER-1part of UniProtKB:Q59086 — part_of → NCBITaxon:62977; Source protein taxon context; assays and preparations remain strain-qualified on catalytic edges. This is not a claim that every isolate of the species expresses the full pathway.; Evidence: MetaCyc:MONOMER-28, MetaCyc:MONOMER-28part of UniProtKB:Q59087 — part_of → NCBITaxon:62977; Source protein taxon context; assays and preparations remain strain-qualified on catalytic edges. This is not a claim that every isolate of the species expresses the full pathway.; Evidence: MetaCyc:MONOMER-33, MetaCyc:MONOMER-33part of UniProtKB:Q43922 — part_of → NCBITaxon:62977; Source protein taxon context; assays and preparations remain strain-qualified on catalytic edges. This is not a claim that every isolate of the species expresses the full pathway.; Evidence: MetaCyc:MONOMER-37, MetaCyc:MONOMER-37part of MetaCyc:MONOMER-67 — part_of → NCBITaxon:442; Source protein taxon context; assays and preparations remain strain-qualified on catalytic edges. This is not a claim that every isolate of the species expresses the full pathway.; Evidence: MetaCyc:MONOMER-67part of MetaCyc:MONOMER-15328 — part_of → NCBITaxon:442; Source protein taxon context; assays and preparations remain strain-qualified on catalytic edges. This is not a claim that every isolate of the species expresses the full pathway.; Evidence: MetaCyc:MONOMER-15328part of UniProtKB:Q59086 — located_in → GO:0016020; Broad membrane annotation; independently curated UniProt location is ECO:0000305, not direct ADP1 topology measurement. Predicted transmembrane regions in PMID: 8002591 are sequence-based.; Evidence: MetaCyc:MONOMER-28, UniProtKB:Q59086, MetaCyc:MONOMER-28located in MetaCyc:MONOMER-67 — located_in → GO:0016020; Native source and inspected PMID: 15598527 abstract describe membrane-bound IFO3244 QDH. This broad location does not establish exact membrane orientation or an obligate respiratory assembly.; Evidence: MetaCyc:MONOMER-67located in MetaCyc:MONOMER-0 — located_in → GO:0016020; General membrane association is supported by fractionation and detergent solubilization. The precise periplasmic/plasma-membrane-side topology in the native source is not promoted: PMID: 18540103 explicitly lacked RSO/ISO topology tests.; Evidence: PMID:18540103located in MetaCyc:MONOMER-0 — has_part → MetaCyc:MONOMER-15328; object molecular state: Native IFO3244 approximately 16 kDa pDQD subunit. Figure 2C and prose differ at one N-terminal residue; the comparison uses 621H GOX0437. Exact full sequence and cleavage boundaries remain unresolved.; Evidence MetaCyc:MONOMER-0: The native MONOMER-0 complex lists MONOMER-15328 with coefficient 12 and describes the complex as a homododecamer. (/ptools-xml/Protein[@frameid="MONOMER-0"]/component|comment); Evidence PMID:18540103: N-terminal amino acid sequences; The native source encodes 12 identical subunits; the primary mass comparison supports a suggested homododecamer, not an independently solved assembly. Membership does not assign catalytic activity to isolated subunits.; Evidence: MetaCyc:MONOMER-0has part UniProtKB:Q59086 — has_cofactor → CHEBI:58442; PQQ is a prosthetic cofactor, distinct from the net electron-accepting quinone. This ADP1 assertion is a native/current UniProt annotation; Acinetobacter SA1/AC3 or LMD79.41 biochemical results are not transferred as direct ADP1 tests.; Evidence: MetaCyc:ENZRXN-29, UniProtKB:Q59086, MetaCyc:MONOMER-28has cofactor MetaCyc:MONOMER-1 — located_in → GO:0005737; Recovery in the cytoplasmic fraction is reported in the native source and inspected PMID: 14586099 methods. Fractionation supports this context without asserting exclusive localization of all enzyme molecules.; Evidence: MetaCyc:ENZRXN-3located in MetaCyc:MONOMER-67 — has_cofactor → CHEBI:58442; subject molecular state: Native IFO3244 purified holo-QDH preparation; exact proteolytic cleavage state is unresolved.; Evidence MetaCyc:MONOMER-67: The native QDH protein comment describes a purified holoenzyme with 65/21 kDa SDS bands suggested to arise by proteolysis. (/ptools-xml/Protein[@frameid="MONOMER-67"]/comment); PQQ is bound as a prosthetic group; it is not consumed as the quinone electron acceptor. The full 2004 body remains unread.; Evidence: PMID:15598527has cofactor (-)-quinate; CHEBI:29751; Declared type: small_molecule small molecule (-)-quinate 3-dehydroquinate; CHEBI:32364; Declared type: small_molecule small molecule 3-dehydroquinate 3-dehydroshikimate; CHEBI:16630; Declared type: small_molecule small molecule 3-dehydroshikimate 3,4-dihydroxybenzoate; CHEBI:36241; Declared type: small_molecule small molecule 3,4-dihydroxybenzoate water; CHEBI:15377; Declared type: small_molecule small molecule water a quinone; MetaCyc:Quinones; Declared type: chemical_entity chemical entity a quinone a quinol; MetaCyc:Reduced-Quinones; Declared type: chemical_entity chemical entity a quinol periplasmic dehydroquinate dehydratase; MetaCyc:MONOMER-0; Declared type: complex complex periplasmic dehydroquinate dehydratase dehydroshikimate dehydratase; MetaCyc:MONOMER-1; Declared type: protein protein dehydroshikimate dehydratase Quinate/shikimate dehydrogenase (quinone); UniProtKB:Q59086; Declared type: protein protein Quinate/shikimate dehydrogenase (quinone) Catabolic 3-dehydroquinate dehydratase; UniProtKB:Q59087; Declared type: protein protein Catabolic 3-dehydroquinate dehydratase 3-dehydroshikimate dehydratase; UniProtKB:Q43922; Declared type: protein protein 3-dehydroshikimate dehydratase quinate dehydrogenase; MetaCyc:MONOMER-67; Declared type: protein protein quinate dehydrogenase periplasmic dehydroquinate dehydratase; MetaCyc:MONOMER-15328; Declared type: protein protein periplasmic dehydroquinate dehydratase pyrroloquinoline quinone(3-); CHEBI:58442; Declared type: cofactor cofactor pyrroloquinoline quinone(3-) membrane; GO:0016020; Declared type: cellular_component cellular component membrane cytoplasm; GO:0005737; Declared type: cellular_component cellular component cytoplasm quinate oxidation with a quinone; MetaCyc:1.1.99.25-RXN; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity quinate oxidation with a quinone 3-dehydroquinate <=> 3-dehydroshikimate + H2O; RHEA:21099; Declared type: molecular_activity; Source reaction direction: reversible molecular activity 3-dehydroquinate <=> 3-dehydroshikimate + H2O 3-dehydroshikimate => 3,4-dihydroxybenzoate + H2O; RHEA:24849; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity 3-dehydroshikimate => 3,4-dihydroxybenzoate + H2O Acinetobacter baylyi ADP1; NCBITaxon:62977; Declared type: taxon taxon Acinetobacter baylyi ADP1 Gluconobacter oxydans; NCBITaxon:442; Declared type: taxon taxon Gluconobacter oxydans quinate degradation I; MetaCyc:QUINATEDEG-PWY; Declared type: pathway pathway quinate degradation I periplasmic dehydroquinate dehydratase; MetaCyc:MONOMER-0; Declared type: complex; molecular state: Native IFO3244 detergent-purified pDQD assembly. Estimated 191 kDa and 16 kDa subunit support a proposed 12-subunit assembly; no engineered construct. N-terminal comparison does not establish whole-sequence identity to 621H.; Evidence PMID:18540103: pDQD was highly purified molecular state periplasmic dehydroquinate dehydratase [molecular state: Native IFO3244 detergent-purified pDQD assembly. Estimated 191 kDa and 16 kDa subunit support a…] dehydroshikimate dehydratase; MetaCyc:MONOMER-1; Declared type: protein; molecular state: Native IFO3244 partially purified cytoplasmic enzyme fraction; DHS-dehydratase activity eluted separately from DQD on DEAE-Sephadex A-50. Exact protein sequence, termini and oligomeric state are unresolved.; Evidence PMID:14586099: DSA dehydratase was separated from DQD molecular state dehydroshikimate dehydratase [molecular state: Native IFO3244 partially purified cytoplasmic enzyme fraction; DHS-dehydratase activity eluted…] 3-dehydroshikimate dehydratase; UniProtKB:Q43922; Declared type: protein; experimental construct: ADP1 genomic quiC expressed in E. coli DH5α(pZR564), a 2.0 kb HindIII insert; crude-extract assay. No protein tag reported or expressed termini measured. Text/Table 1 disagree on pBSK versus pBKS vector label.; Evidence PMID:7592351: pZR564 contains the open reading frame experimental construct 3-dehydroshikimate dehydratase [experimental construct: ADP1 genomic quiC expressed in E. coli DH5α(pZR564), a 2.0 kb HindIII insert; crude- extract assay.…] quinate dehydrogenase; MetaCyc:MONOMER-67; Declared type: protein; molecular state: Native IFO3244 membrane holo-QDH preparation; SDS bands approximately 65 and 21 kDa may reflect proteolysis of one polypeptide. Exact cleavage and whole-protein sequence are unresolved.; Evidence PMID:15598527: could be the result of proteolysis of single polypeptide molecular state quinate dehydrogenase [molecular state: Native IFO3244 membrane holo-QDH preparation; SDS bands approximately 65 and 21 kDa may reflect…] periplasmic dehydroquinate dehydratase; MetaCyc:MONOMER-15328; Declared type: protein; molecular state: Native IFO3244 approximately 16 kDa pDQD subunit. Figure 2C and prose differ at one N-terminal residue; the comparison uses 621H GOX0437. Exact full sequence and cleavage boundaries remain unresolved.; Evidence MetaCyc:MONOMER-0: The native MONOMER-0 complex lists MONOMER-15328 with coefficient 12 and describes the complex as a homododecamer. (/ptools-xml/Protein[@frameid="MONOMER-0"]/component|comment); Evidence PMID:18540103: N-terminal amino acid sequences molecular state periplasmic dehydroquinate dehydratase [molecular state: Native IFO3244 approximately 16 kDa pDQD subunit. Figure 2C and prose differ at one N-terminal…] quinate dehydrogenase; MetaCyc:MONOMER-67; Declared type: protein; molecular state: Native IFO3244 purified holo-QDH preparation; exact proteolytic cleavage state is unresolved.; Evidence MetaCyc:MONOMER-67: The native QDH protein comment describes a purified holoenzyme with 65/21 kDa SDS bands suggested to arise by proteolysis. (/ptools-xml/Protein[@frameid="MONOMER-67"]/comment) molecular state quinate dehydrogenase [molecular state: Native IFO3244 purified holo-QDH preparation; exact proteolytic cleavage state is unresolved.]

Components and activities

Declared biological components and source reaction directions
NodeKind or roleSource direction
Acinetobacter baylyi ADP1
NCBITaxon:62977		taxon
Gluconobacter oxydans
NCBITaxon:442		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
a quinone
MetaCyc:Quinones		chemical entity
a quinol
MetaCyc:Reduced-Quinones		chemical entity
periplasmic dehydroquinate dehydratase
MetaCyc:MONOMER-0		complex
dehydroshikimate dehydratase
MetaCyc:MONOMER-1		protein
Quinate/shikimate dehydrogenase (quinone)
UniProtKB:Q59086		protein
Catabolic 3-dehydroquinate dehydratase
UniProtKB:Q59087		protein
3-dehydroshikimate dehydratase
UniProtKB:Q43922		protein
quinate dehydrogenase
MetaCyc:MONOMER-67		protein
periplasmic dehydroquinate dehydratase
MetaCyc:MONOMER-15328		protein
pyrroloquinoline quinone(3-)
CHEBI:58442		cofactor
membrane
GO:0016020		cellular component
cytoplasm
GO:0005737		cellular component
quinate oxidation with a quinone
MetaCyc:1.1.99.25-RXN		molecular activityleft to right
3-dehydroquinate <=> 3-dehydroshikimate + H2O
RHEA:21099		molecular activityreversible
3-dehydroshikimate => 3,4-dihydroxybenzoate + H2O
RHEA:24849		molecular activityleft to right

Mechanistic edges

Mechanistic edges and their cited evidence
SubjectPredicate and descriptionObjectEvidence
MetaCyc:QUINATEDEG-PWYpart_of

Native pathway species context; individual enzyme evidence retains its strain and preparation scope.

Acinetobacter baylyi ADP1
NCBITaxon:62977
  • MetaCyc:QUINATEDEG-PWY

    Source assertion: The pathway species slot lists TAX-62977; native pathway evidence includes mutant-phenotype and direct-assay annotations.

    Source location/ptools-xml/Pathway[@frameid="QUINATEDEG-PWY"]/species/Organism[@frameid="TAX-62977"]
MetaCyc:QUINATEDEG-PWYpart_of

Native pathway species context; individual enzyme evidence retains its strain and preparation scope.

Gluconobacter oxydans
NCBITaxon:442
  • MetaCyc:QUINATEDEG-PWY

    Source assertion: The pathway species slot lists TAX-442; native pathway evidence includes mutant-phenotype and direct-assay annotations.

    Source location/ptools-xml/Pathway[@frameid="QUINATEDEG-PWY"]/species/Organism[@frameid="TAX-442"]
quinate oxidation with a quinone
MetaCyc:1.1.99.25-RXN		part_of

One of the three explicit native pathway members; the native reaction direction is preserved.

MetaCyc:QUINATEDEG-PWY
  • MetaCyc:QUINATEDEG-PWY

    Source assertion: The reaction-list includes 1.1.99.25-RXN and the selected pathway layout is L2R.

    Source location/ptools-xml/Pathway[@frameid="QUINATEDEG-PWY"]/reaction-list|reaction-layout[Reaction/@frameid="1.1.99.25-RXN"]
(-)-quinate
CHEBI:29751		consumes

Selected catabolic pathway orientation.

quinate oxidation with a quinone
MetaCyc:1.1.99.25-RXN
  • MetaCyc:1.1.99.25-RXN

    Source assertion: The native left side contains QUINATE. No explicit coefficient is supplied.

    Source location/ptools-xml/Reaction[@frameid="1.1.99.25-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
a quinone
MetaCyc:Quinones		consumes

Selected catabolic pathway orientation. Native generic quinone class; this does not establish specificity for every class member or a measured physiological quinone.

quinate oxidation with a quinone
MetaCyc:1.1.99.25-RXN
  • MetaCyc:1.1.99.25-RXN

    Source assertion: The native left side contains Quinones. No explicit coefficient is supplied.

    Source location/ptools-xml/Reaction[@frameid="1.1.99.25-RXN"]/left/Compound[@frameid="Quinones"]
quinate oxidation with a quinone
MetaCyc:1.1.99.25-RXN		produces

Selected catabolic pathway orientation.

3-dehydroquinate
CHEBI:32364
  • MetaCyc:1.1.99.25-RXN

    Source assertion: The native right side contains DEHYDROQUINATE. No explicit coefficient is supplied.

    Source location/ptools-xml/Reaction[@frameid="1.1.99.25-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 a quinone
MetaCyc:1.1.99.25-RXN		produces

Selected catabolic pathway orientation. Native generic quinone class; this does not establish specificity for every class member or a measured physiological quinone.

a quinol
MetaCyc:Reduced-Quinones
  • MetaCyc:1.1.99.25-RXN

    Source assertion: The native right side contains Reduced-Quinones. No explicit coefficient is supplied.

    Source location/ptools-xml/Reaction[@frameid="1.1.99.25-RXN"]/right/Compound[@frameid="Reduced-Quinones"]
3-dehydroquinate <=> 3-dehydroshikimate + H2O
RHEA:21099		part_of

One of the three explicit native pathway members; the native reaction direction is preserved.

MetaCyc:QUINATEDEG-PWY
  • MetaCyc:QUINATEDEG-PWY

    Source assertion: The reaction-list includes 3-DEHYDROQUINATE-DEHYDRATASE-RXN and the selected pathway layout is L2R.

    Source location/ptools-xml/Pathway[@frameid="QUINATEDEG-PWY"]/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 locationhttp://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 locationhttp://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 locationhttp://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:QUINATEDEG-PWY
  • MetaCyc:QUINATEDEG-PWY

    Source assertion: The reaction-list includes DHSHIKIMATE-DEHYDRO-RXN and the selected pathway layout is L2R.

    Source location/ptools-xml/Pathway[@frameid="QUINATEDEG-PWY"]/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 locationhttp://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 locationhttp://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 locationhttp://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
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:QUINATEDEG-PWY

    Source assertion: 3-DEHYDROQUINATE-DEHYDRATASE-RXN is a predecessor of DHSHIKIMATE-DEHYDRO-RXN.

    Source location/ptools-xml/Pathway[@frameid="QUINATEDEG-PWY"]/reaction-ordering[Reaction/@frameid="DHSHIKIMATE-DEHYDRO-RXN"]/predecessor-reactions
quinate oxidation with a quinone
MetaCyc:1.1.99.25-RXN		precedes

Native pathway reaction ordering selects forward catabolic progression.

3-dehydroquinate <=> 3-dehydroshikimate + H2O
RHEA:21099
  • MetaCyc:QUINATEDEG-PWY

    Source assertion: 1.1.99.25-RXN is a predecessor of 3-DEHYDROQUINATE-DEHYDRATASE-RXN.

    Source location/ptools-xml/Pathway[@frameid="QUINATEDEG-PWY"]/reaction-ordering[Reaction/@frameid="3-DEHYDROQUINATE-DEHYDRATASE-RXN"]/predecessor-reactions
periplasmic dehydroquinate dehydratase
MetaCyc:MONOMER-0

molecular state: Native IFO3244 detergent-purified pDQD assembly. Estimated 191 kDa and 16 kDa subunit support a proposed 12-subunit assembly; no engineered construct. N-terminal comparison does not establish whole-sequence identity to 621H.

Qualification evidence
catalyzes

Native IFO3244 pDQD catalyzes DHQ dehydration. PMID: 18540103 measures a 191 kDa native mass and 16 kDa SDS subunit, suggesting 12 subunits; the source molecular-weight field 189 kDa is not copied. Exact 621H sequence identity is not assumed.

3-dehydroquinate <=> 3-dehydroshikimate + H2O
RHEA:21099
  • MetaCyc:ENZRXN-02

    Source assertion: ENZRXN-02 explicitly joins enzyme MONOMER-0 to reaction 3-DEHYDROQUINATE-DEHYDRATASE-RXN; native evidence: EV-EXP-IDA-PURIFIED-PROTEIN-NH.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid="ENZRXN-02"]/enzyme|reaction|evidence
Quinate/shikimate dehydrogenase (quinone)
UniProtKB:Q59086		catalyzes

Native ADP1 QuiA activity is supported by genetic and cell-extract results in PMID: 8002591. The source groups this as quinone-dependent oxidation; this does not establish use of every quinone or transfer purified Acinetobacter SA1/AC3 measurements to ADP1.

quinate oxidation with a quinone
MetaCyc:1.1.99.25-RXN
  • MetaCyc:ENZRXN-29

    Source assertion: ENZRXN-29 explicitly joins enzyme MONOMER-28 to reaction 1.1.99.25-RXN; native evidence: EV-EXP-IDA-PURIFIED-PROTEIN, EV-EXP-IDA-UNPURIFIED-PROTEIN.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid="ENZRXN-29"]/enzyme|reaction|evidence
  • MetaCyc:MONOMER-28

    Source assertion: The native protein MONOMER-28 carries a UniProt cross-reference to Q59086.

    Source location/ptools-xml/Protein[@frameid="MONOMER-28"]/dblink[dblink-db="UNIPROT"]
dehydroshikimate dehydratase
MetaCyc:MONOMER-1

molecular state: Native IFO3244 partially purified cytoplasmic enzyme fraction; DHS-dehydratase activity eluted separately from DQD on DEAE-Sephadex A-50. Exact protein sequence, termini and oligomeric state are unresolved.

Qualification evidence
catalyzes

Native IFO3244 DHS-dehydratase activity was separated from DQD and detected with a coupled qualitative protocatechuate assay. No gene, sequence or purified homogeneous protein identity is claimed.

3-dehydroshikimate => 3,4-dihydroxybenzoate + H2O
RHEA:24849
  • MetaCyc:ENZRXN-3

    Source assertion: ENZRXN-3 explicitly joins enzyme MONOMER-1 to reaction DHSHIKIMATE-DEHYDRO-RXN; native evidence: EV-EXP-IDA-PART-PURIFIED-PROTEIN.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid="ENZRXN-3"]/enzyme|reaction|evidence
Catabolic 3-dehydroquinate dehydratase
UniProtKB:Q59087		catalyzes

Native ADP1 induced thermolabile QuiB activity and deletion phenotypes support catabolic DHQ dehydration (PMID: 7592351). The old recombinant 290-aa annotation and proposed leader localization are not assumed identical to the corrected 272-aa canonical sequence.

3-dehydroquinate <=> 3-dehydroshikimate + H2O
RHEA:21099
  • MetaCyc:ENZRXN-35

    Source assertion: ENZRXN-35 explicitly joins enzyme MONOMER-33 to reaction 3-DEHYDROQUINATE-DEHYDRATASE-RXN; native evidence: EV-EXP-IDA-UNPURIFIED-PROTEIN.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid="ENZRXN-35"]/enzyme|reaction|evidence
  • MetaCyc:MONOMER-33

    Source assertion: The native protein MONOMER-33 carries a UniProt cross-reference to Q59087.

    Source location/ptools-xml/Protein[@frameid="MONOMER-33"]/dblink[dblink-db="UNIPROT"]
3-dehydroshikimate dehydratase
UniProtKB:Q43922

experimental construct: ADP1 genomic quiC expressed in E. coli DH5α(pZR564), a 2.0 kb HindIII insert; crude-extract assay. No protein tag reported or expressed termini measured. Text/Table 1 disagree on pBSK versus pBKS vector label.

Qualification evidence
catalyzes

DHS dehydration is supported by cloned quiC activity and native genetic phenotypes. The native protein comment incorrectly labels the assay as DHQ dehydration; no numeric activity is copied.

3-dehydroshikimate => 3,4-dihydroxybenzoate + H2O
RHEA:24849
  • MetaCyc:ENZRXN-38

    Source assertion: ENZRXN-38 explicitly joins enzyme MONOMER-37 to reaction DHSHIKIMATE-DEHYDRO-RXN; native evidence: EV-EXP-IDA-UNPURIFIED-PROTEIN.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid="ENZRXN-38"]/enzyme|reaction|evidence
  • MetaCyc:MONOMER-37

    Source assertion: The native protein MONOMER-37 carries a UniProt cross-reference to Q43922.

    Source location/ptools-xml/Protein[@frameid="MONOMER-37"]/dblink[dblink-db="UNIPROT"]
quinate dehydrogenase
MetaCyc:MONOMER-67

molecular state: Native IFO3244 membrane holo-QDH preparation; SDS bands approximately 65 and 21 kDa may reflect proteolysis of one polypeptide. Exact cleavage and whole-protein sequence are unresolved.

Qualification evidence
  • PMID:15598527
    could be the result of proteolysis of single polypeptide
catalyzes

The native source assigns IFO3244 QDH to the generic quinone oxidation reaction. The inspected primary abstract supports purified holo-QDH; the full-body acceptor panel remains unread, so universal quinone specificity is not asserted.

quinate oxidation with a quinone
MetaCyc:1.1.99.25-RXN
  • MetaCyc:ENZRXN-68

    Source assertion: ENZRXN-68 explicitly joins enzyme MONOMER-67 to reaction 1.1.99.25-RXN; native evidence: EV-EXP-IDA-PURIFIED-PROTEIN.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid="ENZRXN-68"]/enzyme|reaction|evidence
periplasmic dehydroquinate dehydratase
MetaCyc:MONOMER-0		part_of

Source protein taxon context; assays and preparations remain strain-qualified on catalytic edges. This is not a claim that every isolate of the species expresses the full pathway.

Gluconobacter oxydans
NCBITaxon:442
  • MetaCyc:MONOMER-0

    Source assertion: The native MONOMER-0 species slot identifies TAX-442; this is source protein context, not proof of full pathway reconstruction in a single strain.

    Source location/ptools-xml/Protein[@frameid="MONOMER-0"]/species
dehydroshikimate dehydratase
MetaCyc:MONOMER-1		part_of

Source protein taxon context; assays and preparations remain strain-qualified on catalytic edges. This is not a claim that every isolate of the species expresses the full pathway.

Gluconobacter oxydans
NCBITaxon:442
  • MetaCyc:MONOMER-1

    Source assertion: The native MONOMER-1 species slot identifies TAX-442; this is source protein context, not proof of full pathway reconstruction in a single strain.

    Source location/ptools-xml/Protein[@frameid="MONOMER-1"]/species
Quinate/shikimate dehydrogenase (quinone)
UniProtKB:Q59086		part_of

Source protein taxon context; assays and preparations remain strain-qualified on catalytic edges. This is not a claim that every isolate of the species expresses the full pathway.

Acinetobacter baylyi ADP1
NCBITaxon:62977
  • MetaCyc:MONOMER-28

    Source assertion: The native MONOMER-28 species slot identifies TAX-62977; this is source protein context, not proof of full pathway reconstruction in a single strain.

    Source location/ptools-xml/Protein[@frameid="MONOMER-28"]/species
  • MetaCyc:MONOMER-28

    Source assertion: The native protein MONOMER-28 carries a UniProt cross-reference to Q59086.

    Source location/ptools-xml/Protein[@frameid="MONOMER-28"]/dblink[dblink-db="UNIPROT"]
Catabolic 3-dehydroquinate dehydratase
UniProtKB:Q59087		part_of

Source protein taxon context; assays and preparations remain strain-qualified on catalytic edges. This is not a claim that every isolate of the species expresses the full pathway.

Acinetobacter baylyi ADP1
NCBITaxon:62977
  • MetaCyc:MONOMER-33

    Source assertion: The native MONOMER-33 species slot identifies TAX-62977; this is source protein context, not proof of full pathway reconstruction in a single strain.

    Source location/ptools-xml/Protein[@frameid="MONOMER-33"]/species
  • MetaCyc:MONOMER-33

    Source assertion: The native protein MONOMER-33 carries a UniProt cross-reference to Q59087.

    Source location/ptools-xml/Protein[@frameid="MONOMER-33"]/dblink[dblink-db="UNIPROT"]
3-dehydroshikimate dehydratase
UniProtKB:Q43922		part_of

Source protein taxon context; assays and preparations remain strain-qualified on catalytic edges. This is not a claim that every isolate of the species expresses the full pathway.

Acinetobacter baylyi ADP1
NCBITaxon:62977
  • MetaCyc:MONOMER-37

    Source assertion: The native MONOMER-37 species slot identifies TAX-62977; this is source protein context, not proof of full pathway reconstruction in a single strain.

    Source location/ptools-xml/Protein[@frameid="MONOMER-37"]/species
  • MetaCyc:MONOMER-37

    Source assertion: The native protein MONOMER-37 carries a UniProt cross-reference to Q43922.

    Source location/ptools-xml/Protein[@frameid="MONOMER-37"]/dblink[dblink-db="UNIPROT"]
quinate dehydrogenase
MetaCyc:MONOMER-67		part_of

Source protein taxon context; assays and preparations remain strain-qualified on catalytic edges. This is not a claim that every isolate of the species expresses the full pathway.

Gluconobacter oxydans
NCBITaxon:442
  • MetaCyc:MONOMER-67

    Source assertion: The native MONOMER-67 species slot identifies TAX-442; this is source protein context, not proof of full pathway reconstruction in a single strain.

    Source location/ptools-xml/Protein[@frameid="MONOMER-67"]/species
periplasmic dehydroquinate dehydratase
MetaCyc:MONOMER-15328		part_of

Source protein taxon context; assays and preparations remain strain-qualified on catalytic edges. This is not a claim that every isolate of the species expresses the full pathway.

Gluconobacter oxydans
NCBITaxon:442
  • MetaCyc:MONOMER-15328

    Source assertion: The native MONOMER-15328 species slot identifies TAX-442; this is source protein context, not proof of full pathway reconstruction in a single strain.

    Source location/ptools-xml/Protein[@frameid="MONOMER-15328"]/species
Quinate/shikimate dehydrogenase (quinone)
UniProtKB:Q59086		located_in

Broad membrane annotation; independently curated UniProt location is ECO:0000305, not direct ADP1 topology measurement. Predicted transmembrane regions in PMID: 8002591 are sequence-based.

membrane
GO:0016020
  • MetaCyc:MONOMER-28

    Source assertion: The native protein has location CCO-MEMBRANE and cellular-component annotation GO:0016020.

    Source location/ptools-xml/Protein[@frameid="MONOMER-28"]/location|has-go-term
  • UniProtKB:Q59086

    Source assertion: Q59086 SUBCELLULAR LOCATION annotates cell membrane and multi-pass membrane protein with ECO:0000305.

    Source location$.comments[5].subcellularLocations[0]
  • MetaCyc:MONOMER-28

    Source assertion: The native protein MONOMER-28 carries a UniProt cross-reference to Q59086.

    Source location/ptools-xml/Protein[@frameid="MONOMER-28"]/dblink[dblink-db="UNIPROT"]
quinate dehydrogenase
MetaCyc:MONOMER-67		located_in

Native source and inspected PMID: 15598527 abstract describe membrane-bound IFO3244 QDH. This broad location does not establish exact membrane orientation or an obligate respiratory assembly.

membrane
GO:0016020
  • MetaCyc:MONOMER-67

    Source assertion: The native protein has location CCO-MEMBRANE and cellular-component annotation GO:0016020.

    Source location/ptools-xml/Protein[@frameid="MONOMER-67"]/location|has-go-term
periplasmic dehydroquinate dehydratase
MetaCyc:MONOMER-0		located_in

General membrane association is supported by fractionation and detergent solubilization. The precise periplasmic/plasma-membrane-side topology in the native source is not promoted: PMID: 18540103 explicitly lacked RSO/ISO topology tests.

membrane
GO:0016020
periplasmic dehydroquinate dehydratase
MetaCyc:MONOMER-0		has_part

The native source encodes 12 identical subunits; the primary mass comparison supports a suggested homododecamer, not an independently solved assembly. Membership does not assign catalytic activity to isolated subunits.

periplasmic dehydroquinate dehydratase
MetaCyc:MONOMER-15328

molecular state: Native IFO3244 approximately 16 kDa pDQD subunit. Figure 2C and prose differ at one N-terminal residue; the comparison uses 621H GOX0437. Exact full sequence and cleavage boundaries remain unresolved.

Qualification evidence
  • MetaCyc:MONOMER-0

    Source assertion: The native MONOMER-0 complex lists MONOMER-15328 with coefficient 12 and describes the complex as a homododecamer.

    Source location/ptools-xml/Protein[@frameid="MONOMER-0"]/component|comment
  • PMID:18540103
    N-terminal amino acid sequences
  • MetaCyc:MONOMER-0

    Source assertion: The native protein-complex object MONOMER-0 contains 12 copies of MONOMER-15328; membership does not independently assert catalysis by an isolated subunit.

    Source location/ptools-xml/Protein[@frameid="MONOMER-0"]/parent|component
Quinate/shikimate dehydrogenase (quinone)
UniProtKB:Q59086		has_cofactor

PQQ is a prosthetic cofactor, distinct from the net electron-accepting quinone. This ADP1 assertion is a native/current UniProt annotation; Acinetobacter SA1/AC3 or LMD79.41 biochemical results are not transferred as direct ADP1 tests.

pyrroloquinoline quinone(3-)
CHEBI:58442
  • MetaCyc:ENZRXN-29

    Source assertion: ENZRXN-29 associates the QuiA native enzyme MONOMER-28 with PQQ as a cofactor.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid="ENZRXN-29"]/enzyme|cofactor
  • UniProtKB:Q59086

    Source assertion: Q59086 COFACTOR comment identifies pyrroloquinoline quinone with ChEBI:58442.

    Source location$.comments[3].cofactors[0]
  • MetaCyc:MONOMER-28

    Source assertion: The native protein MONOMER-28 carries a UniProt cross-reference to Q59086.

    Source location/ptools-xml/Protein[@frameid="MONOMER-28"]/dblink[dblink-db="UNIPROT"]
dehydroshikimate dehydratase
MetaCyc:MONOMER-1		located_in

Recovery in the cytoplasmic fraction is reported in the native source and inspected PMID: 14586099 methods. Fractionation supports this context without asserting exclusive localization of all enzyme molecules.

cytoplasm
GO:0005737
  • MetaCyc:ENZRXN-3

    Source assertion: The native activity comment reports partial purification of Gluconobacter oxydans dehydroshikimate dehydratase from the cytoplasmic fraction.

    Source location/ptools-xml/Enzymatic-Reaction[@frameid="ENZRXN-3"]/comment
quinate dehydrogenase
MetaCyc:MONOMER-67

molecular state: Native IFO3244 purified holo-QDH preparation; exact proteolytic cleavage state is unresolved.

Qualification evidence
  • MetaCyc:MONOMER-67

    Source assertion: The native QDH protein comment describes a purified holoenzyme with 65/21 kDa SDS bands suggested to arise by proteolysis.

    Source location/ptools-xml/Protein[@frameid="MONOMER-67"]/comment
has_cofactor

PQQ is bound as a prosthetic group; it is not consumed as the quinone electron acceptor. The full 2004 body remains unread.

pyrroloquinoline quinone(3-)
CHEBI:58442
  • PMID:15598527
    containing pyrroloquinoline quinone (PQQ) as the prosthetic group

References

Curation history