Entner-Doudoroff pathway, glucose-6P => glyceraldehyde-3P + pyruvate

KEGG:M00008

Complete phosphorylative Entner–Doudoroff module from beta-D-glucose 6-phosphate to D-glyceraldehyde 3-phosphate and pyruvate, scoped to current E. coli K-12 proteins with experiment-specific strain and construct limits. Five reaction objects cover four sequential positions: alternative NADP- and NAD-dependent oxidations converge on lactone hydrolysis, dehydration and aldol cleavage. The beta identity is the native KEGG convention, not experimentally proven exclusive anomer use. First-step charged forms are explicit acid-base normalizations, and the two donor branches are never summed or assumed to carry equal in vivo flux. R10907 is listed by M00008 even though its inverse MODULE field omits M00008. Edd historical sequence and inferred iron-sulfur details remain qualified; Eda has source-supported homotrimer assembly. The CsrA Results/Fig.7 and Discussion report indirect positive expression effects, despite a negative section heading/current UniProt statement; no direct inhibition edge is inferred. Cofactor assays do not make Mg/Mn obligatory bound cofactors or LDH reporter NADH an Eda reactant. Uptake, precursor phosphorylation, downstream lower glycolysis, ATP production and other Eda substrate activities are outside this exact boundary.

Pathway type

central carbon catabolism

Organism scope

Escherichia coli K-12 NCBITaxon:83333

Read the source YAML

Pathway network

25 nodes · 37 asserted directed edges

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

Reaction / activity
Chemical / cofactor
Protein / complex
Cell / process context
Pathway
Solid arrow: mechanistic relation
Dashed arrow: membership, location or cofactor relation

Show at full size (scroll to explore)

Components and activities

Declared biological components and source reaction directions
Node	Kind or role	Source direction
Escherichia coli K-12 `NCBITaxon:83333`	taxon
pyruvate `CHEBI:15361`	small molecule
water `CHEBI:15377`	small molecule
hydron `CHEBI:15378`	small molecule
tetra-mu3-sulfido-tetrairon `CHEBI:49883`	cofactor
NAD(1-) `CHEBI:57540`	small molecule
2-dehydro-3-deoxy-6-phosphonato-D-gluconate(3-) `CHEBI:57569`	small molecule
NADPH(4-) `CHEBI:57783`	small molecule
NADH(2-) `CHEBI:57945`	small molecule
6-O-phosphonato-D-glucono-1,5-lactone(2-) `CHEBI:57955`	small molecule
beta-D-glucose 6-phosphate(2-) `CHEBI:58247`	small molecule
NADP(3-) `CHEBI:58349`	small molecule
6-phosphonatooxy-D-gluconate `CHEBI:58759`	small molecule
D-glyceraldehyde 3-phosphate(2-) `CHEBI:59776`	small molecule
Glucose-6-phosphate 1-dehydrogenase `UniProtKB:P0AC53`	protein
6-phosphogluconolactonase `UniProtKB:P52697`	protein
Phosphogluconate dehydratase `UniProtKB:P0ADF6`	protein
KHG/KDPG aldolase `UniProtKB:P0A955`	protein
KHG/KDPG aldolase `MetaCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-CPLX`	complex
cytoplasm `GO:0005737`	cellular component
beta-D-glucose-6-phosphate:NADP+ 1-oxoreductase `KEGG:R02736`	reaction	reversible
beta-D-glucose-6-phosphate:NAD+ 1-oxidoreductase `KEGG:R10907`	reaction	reversible
6-phospho-D-glucono-1,5-lactone + H2O => 6-phospho-D-gluconate + H(+) `RHEA:12557`	reaction	left to right
6-phospho-D-gluconate => 2-dehydro-3-deoxy-6-phospho-D-gluconate + H2O `RHEA:17278`	reaction	left to right
2-dehydro-3-deoxy-6-phospho-D-gluconate => D-glyceraldehyde 3-phosphate + pyruvate `RHEA:17090`	reaction	left to right

Mechanistic edges

Mechanistic edges and their cited evidence
Subject	Predicate and description	Object	Evidence
beta-D-glucose-6-phosphate:NADP+ 1-oxoreductase `KEGG:R02736`	part_of Full native module member. Alternative first-position cofactor activity; do not add its flux to the other alternative.	`KEGG:M00008`	KEGG:M00008 Source assertion: The module has four sequential positions and explicitly includes R02736 at position 1. R02736 and R10907 are alternatives at the first position, not serial reactions. Source location `ENTRY; NAME; DEFINITION; ORTHOLOGY`
beta-D-glucose-6-phosphate:NAD+ 1-oxidoreductase `KEGG:R10907`	part_of Full native module member. Alternative first-position cofactor activity; do not add its flux to the other alternative.	`KEGG:M00008`	KEGG:M00008 Source assertion: The module has four sequential positions and explicitly includes R10907 at position 1. R02736 and R10907 are alternatives at the first position, not serial reactions. Source location `ENTRY; NAME; DEFINITION; ORTHOLOGY` KEGG:R10907 Source assertion: The reaction lists M00004 and M00006 in its MODULE field, but not M00008; this inverse-membership inconsistency is retained. M00008 itself explicitly lists R10907. Source location `MODULE`
6-phospho-D-glucono-1,5-lactone + H2O => 6-phospho-D-gluconate + H(+) `RHEA:12557`	part_of Full native module member. No uptake, ATP-generating lower glycolysis or narrower two-step shunt substitution.	`KEGG:M00008`	KEGG:M00008 Source assertion: The module has four sequential positions and explicitly includes R02035 at position 2. R02736 and R10907 are alternatives at the first position, not serial reactions. Source location `ENTRY; NAME; DEFINITION; ORTHOLOGY` KEGG:R02035 Source assertion: The native equation has the selected transformation and a cross-reference to bidirectional Rhea 12559; it does not itself specify the directed identifier. Source location `EQUATION; DBLINKS` RHEA:12557 Source assertion: Rhea master 12556 links bidirectional 12559 and directional 12557; the selected substrates/products orient catabolic module flow. Source location `http://rdf.rhea-db.org/12556 rh:bidirectionalReaction, rh:directionalReaction; RHEA:12557 rh:substrates, rh:products`
6-phospho-D-gluconate => 2-dehydro-3-deoxy-6-phospho-D-gluconate + H2O `RHEA:17278`	part_of Full native module member. No uptake, ATP-generating lower glycolysis or narrower two-step shunt substitution.	`KEGG:M00008`	KEGG:M00008 Source assertion: The module has four sequential positions and explicitly includes R02036 at position 3. R02736 and R10907 are alternatives at the first position, not serial reactions. Source location `ENTRY; NAME; DEFINITION; ORTHOLOGY` KEGG:R02036 Source assertion: The native equation has the selected transformation and a cross-reference to bidirectional Rhea 17280; it does not itself specify the directed identifier. Source location `EQUATION; DBLINKS` RHEA:17278 Source assertion: Rhea master 17277 links bidirectional 17280 and directional 17278; the selected substrates/products orient catabolic module flow. Source location `http://rdf.rhea-db.org/17277 rh:bidirectionalReaction, rh:directionalReaction; RHEA:17278 rh:substrates, rh:products`
2-dehydro-3-deoxy-6-phospho-D-gluconate => D-glyceraldehyde 3-phosphate + pyruvate `RHEA:17090`	part_of Full native module member. No uptake, ATP-generating lower glycolysis or narrower two-step shunt substitution.	`KEGG:M00008`	KEGG:M00008 Source assertion: The module has four sequential positions and explicitly includes R05605 at position 4. R02736 and R10907 are alternatives at the first position, not serial reactions. Source location `ENTRY; NAME; DEFINITION; ORTHOLOGY` KEGG:R05605 Source assertion: The native equation has the selected transformation and a cross-reference to bidirectional Rhea 17092; it does not itself specify the directed identifier. Source location `EQUATION; DBLINKS` RHEA:17090 Source assertion: Rhea master 17089 links bidirectional 17092 and directional 17090; the selected substrates/products orient catabolic module flow. Source location `http://rdf.rhea-db.org/17089 rh:bidirectionalReaction, rh:directionalReaction; RHEA:17090 rh:substrates, rh:products`
NADP(3-) `CHEBI:58349`	consumes Coefficient: 1. This is one alternative source-specific beta-anomer equation, normalized to charged participants; exclusive beta enzyme specificity and equal in vivo donor flux are not claimed.	beta-D-glucose-6-phosphate:NADP+ 1-oxoreductase `KEGG:R02736`	KEGG:R02736 Source assertion: The original beta-specific equation is C01172 + C00006 <=> C01236 + C00005 + C00080. Forward module use is selected; the native equation is reversible. Source location `EQUATION; DEFINITION` KEGG:C00006 Source assertion: The original compound entry and its ATOM/BOND fields fix the native chemical identity. The selected charged ChEBI form preserves connectivity and stereochemistry with explicit acid-base normalization; no neutral/charged exactMatch is asserted. Source location `ENTRY; NAME; FORMULA; ATOM; BOND` CHEBI:58349 Source assertion: The issuing structure, formula and charge specify the selected normalized reaction participant. Its protonation is compared with the original KEGG structure; coefficients balance this complete charged equation. Source location `statements subject=CHEBI:58349; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge`
beta-D-glucose-6-phosphate:NADP+ 1-oxoreductase `KEGG:R02736`	produces Coefficient: 1. This is one alternative source-specific beta-anomer equation, normalized to charged participants; exclusive beta enzyme specificity and equal in vivo donor flux are not claimed.	6-O-phosphonato-D-glucono-1,5-lactone(2-) `CHEBI:57955`	KEGG:R02736 Source assertion: The original beta-specific equation is C01172 + C00006 <=> C01236 + C00005 + C00080. Forward module use is selected; the native equation is reversible. Source location `EQUATION; DEFINITION` KEGG:C01236 Source assertion: The original compound entry and its ATOM/BOND fields fix the native chemical identity. The selected charged ChEBI form preserves connectivity and stereochemistry with explicit acid-base normalization; no neutral/charged exactMatch is asserted. Source location `ENTRY; NAME; FORMULA; ATOM; BOND` CHEBI:57955 Source assertion: The issuing structure, formula and charge specify the selected normalized reaction participant. Its protonation is compared with the original KEGG structure; coefficients balance this complete charged equation. Source location `statements subject=CHEBI:57955; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge`
beta-D-glucose-6-phosphate:NADP+ 1-oxoreductase `KEGG:R02736`	produces Coefficient: 1. This is one alternative source-specific beta-anomer equation, normalized to charged participants; exclusive beta enzyme specificity and equal in vivo donor flux are not claimed.	NADPH(4-) `CHEBI:57783`	KEGG:R02736 Source assertion: The original beta-specific equation is C01172 + C00006 <=> C01236 + C00005 + C00080. Forward module use is selected; the native equation is reversible. Source location `EQUATION; DEFINITION` KEGG:C00005 Source assertion: The original compound entry and its ATOM/BOND fields fix the native chemical identity. The selected charged ChEBI form preserves connectivity and stereochemistry with explicit acid-base normalization; no neutral/charged exactMatch is asserted. Source location `ENTRY; NAME; FORMULA; ATOM; BOND` CHEBI:57783 Source assertion: The issuing structure, formula and charge specify the selected normalized reaction participant. Its protonation is compared with the original KEGG structure; coefficients balance this complete charged equation. Source location `statements subject=CHEBI:57783; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge`
beta-D-glucose-6-phosphate:NADP+ 1-oxoreductase `KEGG:R02736`	produces Coefficient: 1. This is one alternative source-specific beta-anomer equation, normalized to charged participants; exclusive beta enzyme specificity and equal in vivo donor flux are not claimed.	hydron `CHEBI:15378`	KEGG:R02736 Source assertion: The original beta-specific equation is C01172 + C00006 <=> C01236 + C00005 + C00080. Forward module use is selected; the native equation is reversible. Source location `EQUATION; DEFINITION` KEGG:C00080 Source assertion: The original compound entry and its ATOM/BOND fields fix the native chemical identity. The selected charged ChEBI form preserves connectivity and stereochemistry with explicit acid-base normalization; no neutral/charged exactMatch is asserted. Source location `ENTRY; NAME; FORMULA; ATOM; BOND` CHEBI:15378 Source assertion: The issuing structure, formula and charge specify the selected normalized reaction participant. Its protonation is compared with the original KEGG structure; coefficients balance this complete charged equation. Source location `statements subject=CHEBI:15378; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge`
beta-D-glucose 6-phosphate(2-) `CHEBI:58247`	consumes Coefficient: 1. This is one alternative source-specific beta-anomer equation, normalized to charged participants; exclusive beta enzyme specificity and equal in vivo donor flux are not claimed.	beta-D-glucose-6-phosphate:NADP+ 1-oxoreductase `KEGG:R02736`	KEGG:R02736 Source assertion: The original beta-specific equation is C01172 + C00006 <=> C01236 + C00005 + C00080. Forward module use is selected; the native equation is reversible. Source location `EQUATION; DEFINITION` KEGG:C01172 Source assertion: The original compound entry and its ATOM/BOND fields fix the native chemical identity. The selected charged ChEBI form preserves connectivity and stereochemistry with explicit acid-base normalization; no neutral/charged exactMatch is asserted. Source location `ENTRY; NAME; FORMULA; ATOM; BOND` CHEBI:58247 Source assertion: The issuing structure, formula and charge specify the selected normalized reaction participant. Its protonation is compared with the original KEGG structure; coefficients balance this complete charged equation. Source location `statements subject=CHEBI:58247; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge`
beta-D-glucose-6-phosphate:NAD+ 1-oxidoreductase `KEGG:R10907`	produces Coefficient: 1. This is one alternative source-specific beta-anomer equation, normalized to charged participants; exclusive beta enzyme specificity and equal in vivo donor flux are not claimed.	6-O-phosphonato-D-glucono-1,5-lactone(2-) `CHEBI:57955`	KEGG:R10907 Source assertion: The original beta-specific equation is C01172 + C00003 <=> C01236 + C00004 + C00080. Forward module use is selected; the native equation is reversible. Source location `EQUATION; DEFINITION` KEGG:C01236 Source assertion: The original compound entry and its ATOM/BOND fields fix the native chemical identity. The selected charged ChEBI form preserves connectivity and stereochemistry with explicit acid-base normalization; no neutral/charged exactMatch is asserted. Source location `ENTRY; NAME; FORMULA; ATOM; BOND` CHEBI:57955 Source assertion: The issuing structure, formula and charge specify the selected normalized reaction participant. Its protonation is compared with the original KEGG structure; coefficients balance this complete charged equation. Source location `statements subject=CHEBI:57955; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge`
beta-D-glucose-6-phosphate:NAD+ 1-oxidoreductase `KEGG:R10907`	produces Coefficient: 1. This is one alternative source-specific beta-anomer equation, normalized to charged participants; exclusive beta enzyme specificity and equal in vivo donor flux are not claimed.	hydron `CHEBI:15378`	KEGG:R10907 Source assertion: The original beta-specific equation is C01172 + C00003 <=> C01236 + C00004 + C00080. Forward module use is selected; the native equation is reversible. Source location `EQUATION; DEFINITION` KEGG:C00080 Source assertion: The original compound entry and its ATOM/BOND fields fix the native chemical identity. The selected charged ChEBI form preserves connectivity and stereochemistry with explicit acid-base normalization; no neutral/charged exactMatch is asserted. Source location `ENTRY; NAME; FORMULA; ATOM; BOND` CHEBI:15378 Source assertion: The issuing structure, formula and charge specify the selected normalized reaction participant. Its protonation is compared with the original KEGG structure; coefficients balance this complete charged equation. Source location `statements subject=CHEBI:15378; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge`
beta-D-glucose 6-phosphate(2-) `CHEBI:58247`	consumes Coefficient: 1. This is one alternative source-specific beta-anomer equation, normalized to charged participants; exclusive beta enzyme specificity and equal in vivo donor flux are not claimed.	beta-D-glucose-6-phosphate:NAD+ 1-oxidoreductase `KEGG:R10907`	KEGG:R10907 Source assertion: The original beta-specific equation is C01172 + C00003 <=> C01236 + C00004 + C00080. Forward module use is selected; the native equation is reversible. Source location `EQUATION; DEFINITION` KEGG:C01172 Source assertion: The original compound entry and its ATOM/BOND fields fix the native chemical identity. The selected charged ChEBI form preserves connectivity and stereochemistry with explicit acid-base normalization; no neutral/charged exactMatch is asserted. Source location `ENTRY; NAME; FORMULA; ATOM; BOND` CHEBI:58247 Source assertion: The issuing structure, formula and charge specify the selected normalized reaction participant. Its protonation is compared with the original KEGG structure; coefficients balance this complete charged equation. Source location `statements subject=CHEBI:58247; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge`
NAD(1-) `CHEBI:57540`	consumes Coefficient: 1. This is one alternative source-specific beta-anomer equation, normalized to charged participants; exclusive beta enzyme specificity and equal in vivo donor flux are not claimed.	beta-D-glucose-6-phosphate:NAD+ 1-oxidoreductase `KEGG:R10907`	KEGG:R10907 Source assertion: The original beta-specific equation is C01172 + C00003 <=> C01236 + C00004 + C00080. Forward module use is selected; the native equation is reversible. Source location `EQUATION; DEFINITION` KEGG:C00003 Source assertion: The original compound entry and its ATOM/BOND fields fix the native chemical identity. The selected charged ChEBI form preserves connectivity and stereochemistry with explicit acid-base normalization; no neutral/charged exactMatch is asserted. Source location `ENTRY; NAME; FORMULA; ATOM; BOND` CHEBI:57540 Source assertion: The issuing structure, formula and charge specify the selected normalized reaction participant. Its protonation is compared with the original KEGG structure; coefficients balance this complete charged equation. Source location `statements subject=CHEBI:57540; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge`
beta-D-glucose-6-phosphate:NAD+ 1-oxidoreductase `KEGG:R10907`	produces Coefficient: 1. This is one alternative source-specific beta-anomer equation, normalized to charged participants; exclusive beta enzyme specificity and equal in vivo donor flux are not claimed.	NADH(2-) `CHEBI:57945`	KEGG:R10907 Source assertion: The original beta-specific equation is C01172 + C00003 <=> C01236 + C00004 + C00080. Forward module use is selected; the native equation is reversible. Source location `EQUATION; DEFINITION` KEGG:C00004 Source assertion: The original compound entry and its ATOM/BOND fields fix the native chemical identity. The selected charged ChEBI form preserves connectivity and stereochemistry with explicit acid-base normalization; no neutral/charged exactMatch is asserted. Source location `ENTRY; NAME; FORMULA; ATOM; BOND` CHEBI:57945 Source assertion: The issuing structure, formula and charge specify the selected normalized reaction participant. Its protonation is compared with the original KEGG structure; coefficients balance this complete charged equation. Source location `statements subject=CHEBI:57945; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge`
6-O-phosphonato-D-glucono-1,5-lactone(2-) `CHEBI:57955`	consumes Coefficient: 1. Exact directed Rhea participant in the complete module.	6-phospho-D-glucono-1,5-lactone + H2O => 6-phospho-D-gluconate + H(+) `RHEA:12557`	RHEA:12557 Source assertion: The original directional substrates chain contains CHEBI:57955 with coefficient 1. The formula and charge belong to the linked native compound, not an inferred label mapping. Source location `RHEA:12557 rh:substrates -> http://rdf.rhea-db.org/12556_L rh:contains1 -> http://rdf.rhea-db.org/Participant_12556_compound_3399 rh:compound -> http://rdf.rhea-db.org/Compound_3399 rh:accession/formula/charge`
water `CHEBI:15377`	consumes Coefficient: 1. Exact directed Rhea participant in the complete module.	6-phospho-D-glucono-1,5-lactone + H2O => 6-phospho-D-gluconate + H(+) `RHEA:12557`	RHEA:12557 Source assertion: The original directional substrates chain contains CHEBI:15377 with coefficient 1. The formula and charge belong to the linked native compound, not an inferred label mapping. Source location `RHEA:12557 rh:substrates -> http://rdf.rhea-db.org/12556_L rh:contains1 -> http://rdf.rhea-db.org/Participant_12556_compound_1283 rh:compound -> http://rdf.rhea-db.org/Compound_1283 rh:accession/formula/charge`
6-phospho-D-glucono-1,5-lactone + H2O => 6-phospho-D-gluconate + H(+) `RHEA:12557`	produces Coefficient: 1. Exact directed Rhea participant in the complete module.	6-phosphonatooxy-D-gluconate `CHEBI:58759`	RHEA:12557 Source assertion: The original directional products chain contains CHEBI:58759 with coefficient 1. The formula and charge belong to the linked native compound, not an inferred label mapping. Source location `RHEA:12557 rh:products -> http://rdf.rhea-db.org/12556_R rh:contains1 -> http://rdf.rhea-db.org/Participant_12556_compound_4577 rh:compound -> http://rdf.rhea-db.org/Compound_4577 rh:accession/formula/charge`
6-phospho-D-glucono-1,5-lactone + H2O => 6-phospho-D-gluconate + H(+) `RHEA:12557`	produces Coefficient: 1. Exact directed Rhea participant in the complete module.	hydron `CHEBI:15378`	RHEA:12557 Source assertion: The original directional products chain contains CHEBI:15378 with coefficient 1. The formula and charge belong to the linked native compound, not an inferred label mapping. Source location `RHEA:12557 rh:products -> http://rdf.rhea-db.org/12556_R rh:contains1 -> http://rdf.rhea-db.org/Participant_12556_compound_3249 rh:compound -> http://rdf.rhea-db.org/Compound_3249 rh:accession/formula/charge`
6-phosphonatooxy-D-gluconate `CHEBI:58759`	consumes Coefficient: 1. Exact directed Rhea participant in the complete module.	6-phospho-D-gluconate => 2-dehydro-3-deoxy-6-phospho-D-gluconate + H2O `RHEA:17278`	RHEA:17278 Source assertion: The original directional substrates chain contains CHEBI:58759 with coefficient 1. The formula and charge belong to the linked native compound, not an inferred label mapping. Source location `RHEA:17278 rh:substrates -> http://rdf.rhea-db.org/17277_L rh:contains1 -> http://rdf.rhea-db.org/Participant_17277_compound_4577 rh:compound -> http://rdf.rhea-db.org/Compound_4577 rh:accession/formula/charge`
6-phospho-D-gluconate => 2-dehydro-3-deoxy-6-phospho-D-gluconate + H2O `RHEA:17278`	produces Coefficient: 1. Exact directed Rhea participant in the complete module.	2-dehydro-3-deoxy-6-phosphonato-D-gluconate(3-) `CHEBI:57569`	RHEA:17278 Source assertion: The original directional products chain contains CHEBI:57569 with coefficient 1. The formula and charge belong to the linked native compound, not an inferred label mapping. Source location `RHEA:17278 rh:products -> http://rdf.rhea-db.org/17277_R rh:contains1 -> http://rdf.rhea-db.org/Participant_17277_compound_5038 rh:compound -> http://rdf.rhea-db.org/Compound_5038 rh:accession/formula/charge`
6-phospho-D-gluconate => 2-dehydro-3-deoxy-6-phospho-D-gluconate + H2O `RHEA:17278`	produces Coefficient: 1. Exact directed Rhea participant in the complete module.	water `CHEBI:15377`	RHEA:17278 Source assertion: The original directional products chain contains CHEBI:15377 with coefficient 1. The formula and charge belong to the linked native compound, not an inferred label mapping. Source location `RHEA:17278 rh:products -> http://rdf.rhea-db.org/17277_R rh:contains1 -> http://rdf.rhea-db.org/Participant_17277_compound_1283 rh:compound -> http://rdf.rhea-db.org/Compound_1283 rh:accession/formula/charge`
2-dehydro-3-deoxy-6-phosphonato-D-gluconate(3-) `CHEBI:57569`	consumes Coefficient: 1. Exact directed Rhea participant in the complete module.	2-dehydro-3-deoxy-6-phospho-D-gluconate => D-glyceraldehyde 3-phosphate + pyruvate `RHEA:17090`	RHEA:17090 Source assertion: The original directional substrates chain contains CHEBI:57569 with coefficient 1. The formula and charge belong to the linked native compound, not an inferred label mapping. Source location `RHEA:17090 rh:substrates -> http://rdf.rhea-db.org/17089_L rh:contains1 -> http://rdf.rhea-db.org/Participant_17089_compound_5038 rh:compound -> http://rdf.rhea-db.org/Compound_5038 rh:accession/formula/charge`
2-dehydro-3-deoxy-6-phospho-D-gluconate => D-glyceraldehyde 3-phosphate + pyruvate `RHEA:17090`	produces Coefficient: 1. Exact directed Rhea participant in the complete module.	D-glyceraldehyde 3-phosphate(2-) `CHEBI:59776`	RHEA:17090 Source assertion: The original directional products chain contains CHEBI:59776 with coefficient 1. The formula and charge belong to the linked native compound, not an inferred label mapping. Source location `RHEA:17090 rh:products -> http://rdf.rhea-db.org/17089_R rh:contains1 -> http://rdf.rhea-db.org/Participant_17089_compound_6062 rh:compound -> http://rdf.rhea-db.org/Compound_6062 rh:accession/formula/charge`
2-dehydro-3-deoxy-6-phospho-D-gluconate => D-glyceraldehyde 3-phosphate + pyruvate `RHEA:17090`	produces Coefficient: 1. Exact directed Rhea participant in the complete module.	pyruvate `CHEBI:15361`	RHEA:17090 Source assertion: The original directional products chain contains CHEBI:15361 with coefficient 1. The formula and charge belong to the linked native compound, not an inferred label mapping. Source location `RHEA:17090 rh:products -> http://rdf.rhea-db.org/17089_R rh:contains1 -> http://rdf.rhea-db.org/Participant_17089_compound_3719 rh:compound -> http://rdf.rhea-db.org/Compound_3719 rh:accession/formula/charge`
Glucose-6-phosphate 1-dehydrogenase `UniProtKB:P0AC53`	enables Qualified current Zwf gene-product/activity attribution; both cofactor capacities are supported for modified E. coli preparations. Source beta specificity is curated, not experimentally exclusive. No isolated monomer sufficiency, exact historical construct equality or measured NAD-dependent in vivo ED flux is asserted.	beta-D-glucose-6-phosphate:NADP+ 1-oxoreductase `KEGG:R02736`	UniProtKB:P0AC53 Source assertion: The K-12 zwf/b1852 entry has 491 residues and a generic glucose-6-phosphate/NADP catalytic annotation (ECO:0000255/HAMAP). This is not independent proof of exclusive beta use or of the NAD alternative. Source location `/primaryAccession; /genes; /organism; /sequence; /comments/2` PMID:22519976 Source assertion: The purified modified E. coli preparation oxidized glucose 6-phosphate with NADP and with NAD, with markedly different affinities. The thrombin-cleaved construct retains twelve extra N-terminal residues. No exclusive-anomer assay or in vivo ED donor partition is established. Source location `Results: NADP and NAD as co-substrates, Table 1; Experimental procedures: Purification; Discussion, paragraph on twelve extra N-terminal residues` PMID:27010804 Source assertion: The 2016 study retains a wild-type dual-cofactor comparator and engineered mutants. Its TEV construct is expected to retain Gly-His. These are preparation-specific observations, not exact equality to the current native sequence. Source location `//sec[@id="sec005"]/p \| //table-wrap[@id="pone.0152403.t001"]` DOI:10.1371/journal.pone.0152403.s002 Source assertion: S1 Table identifies Escherichia coli P0AC53 among sequences analyzed. This is an accession bridge for sequence analysis, not a complete kinetic construct sequence proof. Source location `xl/worksheets/sheet1.xml row 9, decoded with xl/sharedStrings.xml` KEGG:R02736 Source assertion: KEGG supplies the beta-specific reaction convention. Applying the enzyme activity to this exact anomer-specific source equation is a qualified annotation-level inference, not direct exclusive-anomer characterization. Source location `DEFINITION; EQUATION`
Glucose-6-phosphate 1-dehydrogenase `UniProtKB:P0AC53`	enables Qualified current Zwf gene-product/activity attribution; both cofactor capacities are supported for modified E. coli preparations. Source beta specificity is curated, not experimentally exclusive. No isolated monomer sufficiency, exact historical construct equality or measured NAD-dependent in vivo ED flux is asserted.	beta-D-glucose-6-phosphate:NAD+ 1-oxidoreductase `KEGG:R10907`	UniProtKB:P0AC53 Source assertion: The K-12 zwf/b1852 entry has 491 residues and a generic glucose-6-phosphate/NADP catalytic annotation (ECO:0000255/HAMAP). This is not independent proof of exclusive beta use or of the NAD alternative. Source location `/primaryAccession; /genes; /organism; /sequence; /comments/2` PMID:22519976 Source assertion: The purified modified E. coli preparation oxidized glucose 6-phosphate with NADP and with NAD, with markedly different affinities. The thrombin-cleaved construct retains twelve extra N-terminal residues. No exclusive-anomer assay or in vivo ED donor partition is established. Source location `Results: NADP and NAD as co-substrates, Table 1; Experimental procedures: Purification; Discussion, paragraph on twelve extra N-terminal residues` PMID:27010804 Source assertion: The 2016 study retains a wild-type dual-cofactor comparator and engineered mutants. Its TEV construct is expected to retain Gly-His. These are preparation-specific observations, not exact equality to the current native sequence. Source location `//sec[@id="sec005"]/p \| //table-wrap[@id="pone.0152403.t001"]` DOI:10.1371/journal.pone.0152403.s002 Source assertion: S1 Table identifies Escherichia coli P0AC53 among sequences analyzed. This is an accession bridge for sequence analysis, not a complete kinetic construct sequence proof. Source location `xl/worksheets/sheet1.xml row 9, decoded with xl/sharedStrings.xml` KEGG:R10907 Source assertion: KEGG supplies the beta-specific reaction convention. Applying the enzyme activity to this exact anomer-specific source equation is a qualified annotation-level inference, not direct exclusive-anomer characterization. Source location `DEFINITION; EQUATION`
6-phosphogluconolactonase `UniProtKB:P52697`	enables K-12 Pgl activity supported by deletion/complementation and cell-extract assays; no purified-enzyme assembly or bound metal requirement is inferred.	6-phospho-D-glucono-1,5-lactone + H2O => 6-phospho-D-gluconate + H(+) `RHEA:12557`	UniProtKB:P52697 Source assertion: The K-12 pgl/ybhE product is annotated with Rhea12556 hydrolysis using ECO:0000269/PMID15576773; the current native sequence is 331 residues. Source location `/primaryAccession; /genes; /organism; /sequence; /comments/0; /comments/1` PMID:15576773 Source assertion: Mutations made in DY378 were moved to MG1655. Loss of pgl removed extract lactonase activity, and plasmid complementation restored it; the assay was explicitly not fully quantitative. Source location `//section[@id="sec4"]/p[1] \| //section[@id="sec15"]/p[1]`
Phosphogluconate dehydratase `UniProtKB:P0ADF6`	enables Current Edd gene-product/activity relation with historical 603/602-residue conflict retained. Coupled lysate activity does not identify a purified assembly or make assay Mn/Mg obligatory cofactors.	6-phospho-D-gluconate => 2-dehydro-3-deoxy-6-phospho-D-gluconate + H2O `RHEA:17278`	UniProtKB:P0ADF6 Source assertion: The K-12 edd/b1851 entry annotates Rhea17277 activity with HAMAP and experimental citations. Its current 603-residue sequence has PLR at 252–254, versus historical AC; exact old construct equality is not established. Source location `/primaryAccession; /genes; /organism; /sequence; /comments/1; /features/3` PMID:17962400 Source assertion: The edd ORF was amplified from K-12 DNA and expressed in BL21(DE3); active lysates were used. Mn supplementation during expression is not proof of an obligatory bound Mn cofactor. Source location `//section[@id="sec10"]/p[position()>=1 and position()<=3]`
KHG/KDPG aldolase `MetaCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-CPLX`	catalyzes Source-verified Eda homotrimer cleaves KDPG. Other Eda substrate activities, coupled LDH/NADH reporting, and engineered-substrate specificity are outside this equation.	2-dehydro-3-deoxy-6-phospho-D-gluconate => D-glyceraldehyde 3-phosphate + pyruvate `RHEA:17090`	MetaCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-CPLX Source assertion: The native KHG/KDPG aldolase complex catalyzes KDPGALDOL-RXN via KDPGALDOL-ENZRXN. The same source also describes additional reactions outside this exact module. Source location `/ptools-xml/Protein/catalyzes/Enzymatic-Reaction[@frameid="KDPGALDOL-ENZRXN"]/reaction` UniProtKB:P0A955 Source assertion: The current Eda entry annotates KDPG cleavage to D-glyceraldehyde 3-phosphate and pyruvate with experimental evidence and identifies a homotrimer. Source location `/comments/1; /comments/8` PMID:17962400 Source assertion: KDPG cleavage was assayed through pyruvate production using coupled lactate dehydrogenase. NADH consumption belongs to that reporter and is not part of the aldolase equation. Source location `//section[@id="sec11"]/p[1]`
KHG/KDPG aldolase `MetaCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-CPLX`	has_part Stoichiometry: 3 identical Eda subunits. Native component identity and current protein annotation connect the complex; primary recombinant assembly supports trimerization without an exact donor-strain/construct equality claim.	KHG/KDPG aldolase `UniProtKB:P0A955`	MetaCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-CPLX Source assertion: The native complex contains three copies of KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER. Source location `/ptools-xml/Protein/component` MetaCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER Source assertion: The component object explicitly unifies UniProt P0A955; the curated native species is K-12 MG1655. Source location `/ptools-xml/Protein/dblink[dblink-db="UNIPROT"]; /ptools-xml/Protein/species` UniProtKB:P0A955 Source assertion: The current K-12 entry states Homotrimer with experimental evidence including PMID11274385. Source location `/primaryAccession; /organism; /comments/8` PMID:11274385 Source assertion: The recombinant E. coli enzyme has trimeric subunit assembly. The eda/pKK-223 preparation is described; expression-host and SeMet preparation details do not independently establish a MG1655 donor strain. Source location `//section[@id="sec2"]/p[1] \| //section[@id="sec5"]/p[1]`
Phosphogluconate dehydratase `UniProtKB:P0ADF6`	has_cofactor Qualified [4Fe-4S] annotation. Activity sensitivity/reactivation supports an iron-sulfur interpretation; exact cluster type and one-per-protein count retain their annotation inference tier.	tetra-mu3-sulfido-tetrairon `CHEBI:49883`	UniProtKB:P0ADF6 Source assertion: The entry assigns one [4Fe-4S] cluster using ECO:0000250, ECO:0000255 and curator inference ECO:0000305. The one-cluster note is similarity/HAMAP evidence, not direct Edd cluster stoichiometry measurement. Source location `/comments/2/cofactors/0; /comments/2/note` PMID:17102132 Source assertion: Edd lysate activity was peroxide-sensitive and recoverable with iron/DTT. The explicit [3Fe-4S] EPR signal in this passage belongs to fumarase A; it is not an Edd spectrum. Source location `//[@id="P9"] \| //[@id="P30"]`
KHG/KDPG aldolase `UniProtKB:P0A955`	located_in Annotated Eda location; this does not infer a directly measured compartment for every module component.	cytoplasm `GO:0005737`	UniProtKB:P0A955 Source assertion: The entry assigns cytoplasm as cellular location with ECO:0000305 curator inference. Source location `/comments/10/subcellularLocations/0/location`
beta-D-glucose-6-phosphate:NADP+ 1-oxoreductase `KEGG:R02736`	provides_input_for The shared CHEBI:57955 product/substrate links these positions. The two first-position alternatives independently feed hydrolysis; neither precedes or feeds the other.	6-phospho-D-glucono-1,5-lactone + H2O => 6-phospho-D-gluconate + H(+) `RHEA:12557`	KEGG:M00008 Source assertion: The native definition orders oxidation, lactone hydrolysis, dehydration and aldol cleavage, with both oxidation alternatives in the same first position. Source location `DEFINITION; ORTHOLOGY` KEGG:R02736 Source assertion: The original beta-specific equation is C01172 + C00006 <=> C01236 + C00005 + C00080. Forward module use is selected; the native equation is reversible. Source location `EQUATION; DEFINITION` KEGG:C01236 Source assertion: The original compound entry and its ATOM/BOND fields fix the native chemical identity. The selected charged ChEBI form preserves connectivity and stereochemistry with explicit acid-base normalization; no neutral/charged exactMatch is asserted. Source location `ENTRY; NAME; FORMULA; ATOM; BOND` CHEBI:57955 Source assertion: The issuing structure, formula and charge specify the selected normalized reaction participant. Its protonation is compared with the original KEGG structure; coefficients balance this complete charged equation. Source location `statements subject=CHEBI:57955; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge` RHEA:12557 Source assertion: The original directional substrates chain contains CHEBI:57955 with coefficient 1. The formula and charge belong to the linked native compound, not an inferred label mapping. Source location `RHEA:12557 rh:substrates -> http://rdf.rhea-db.org/12556_L rh:contains1 -> http://rdf.rhea-db.org/Participant_12556_compound_3399 rh:compound -> http://rdf.rhea-db.org/Compound_3399 rh:accession/formula/charge`
beta-D-glucose-6-phosphate:NAD+ 1-oxidoreductase `KEGG:R10907`	provides_input_for The shared CHEBI:57955 product/substrate links these positions. The two first-position alternatives independently feed hydrolysis; neither precedes or feeds the other.	6-phospho-D-glucono-1,5-lactone + H2O => 6-phospho-D-gluconate + H(+) `RHEA:12557`	KEGG:M00008 Source assertion: The native definition orders oxidation, lactone hydrolysis, dehydration and aldol cleavage, with both oxidation alternatives in the same first position. Source location `DEFINITION; ORTHOLOGY` KEGG:R10907 Source assertion: The original beta-specific equation is C01172 + C00003 <=> C01236 + C00004 + C00080. Forward module use is selected; the native equation is reversible. Source location `EQUATION; DEFINITION` KEGG:C01236 Source assertion: The original compound entry and its ATOM/BOND fields fix the native chemical identity. The selected charged ChEBI form preserves connectivity and stereochemistry with explicit acid-base normalization; no neutral/charged exactMatch is asserted. Source location `ENTRY; NAME; FORMULA; ATOM; BOND` CHEBI:57955 Source assertion: The issuing structure, formula and charge specify the selected normalized reaction participant. Its protonation is compared with the original KEGG structure; coefficients balance this complete charged equation. Source location `statements subject=CHEBI:57955; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge` RHEA:12557 Source assertion: The original directional substrates chain contains CHEBI:57955 with coefficient 1. The formula and charge belong to the linked native compound, not an inferred label mapping. Source location `RHEA:12557 rh:substrates -> http://rdf.rhea-db.org/12556_L rh:contains1 -> http://rdf.rhea-db.org/Participant_12556_compound_3399 rh:compound -> http://rdf.rhea-db.org/Compound_3399 rh:accession/formula/charge`
6-phospho-D-glucono-1,5-lactone + H2O => 6-phospho-D-gluconate + H(+) `RHEA:12557`	provides_input_for The shared CHEBI:58759 product/substrate links these positions. The two first-position alternatives independently feed hydrolysis; neither precedes or feeds the other.	6-phospho-D-gluconate => 2-dehydro-3-deoxy-6-phospho-D-gluconate + H2O `RHEA:17278`	KEGG:M00008 Source assertion: The native definition orders oxidation, lactone hydrolysis, dehydration and aldol cleavage, with both oxidation alternatives in the same first position. Source location `DEFINITION; ORTHOLOGY` RHEA:12557 Source assertion: The original directional products chain contains CHEBI:58759 with coefficient 1. The formula and charge belong to the linked native compound, not an inferred label mapping. Source location `RHEA:12557 rh:products -> http://rdf.rhea-db.org/12556_R rh:contains1 -> http://rdf.rhea-db.org/Participant_12556_compound_4577 rh:compound -> http://rdf.rhea-db.org/Compound_4577 rh:accession/formula/charge` RHEA:17278 Source assertion: The original directional substrates chain contains CHEBI:58759 with coefficient 1. The formula and charge belong to the linked native compound, not an inferred label mapping. Source location `RHEA:17278 rh:substrates -> http://rdf.rhea-db.org/17277_L rh:contains1 -> http://rdf.rhea-db.org/Participant_17277_compound_4577 rh:compound -> http://rdf.rhea-db.org/Compound_4577 rh:accession/formula/charge`
6-phospho-D-gluconate => 2-dehydro-3-deoxy-6-phospho-D-gluconate + H2O `RHEA:17278`	provides_input_for The shared CHEBI:57569 product/substrate links these positions. The two first-position alternatives independently feed hydrolysis; neither precedes or feeds the other.	2-dehydro-3-deoxy-6-phospho-D-gluconate => D-glyceraldehyde 3-phosphate + pyruvate `RHEA:17090`	KEGG:M00008 Source assertion: The native definition orders oxidation, lactone hydrolysis, dehydration and aldol cleavage, with both oxidation alternatives in the same first position. Source location `DEFINITION; ORTHOLOGY` RHEA:17278 Source assertion: The original directional products chain contains CHEBI:57569 with coefficient 1. The formula and charge belong to the linked native compound, not an inferred label mapping. Source location `RHEA:17278 rh:products -> http://rdf.rhea-db.org/17277_R rh:contains1 -> http://rdf.rhea-db.org/Participant_17277_compound_5038 rh:compound -> http://rdf.rhea-db.org/Compound_5038 rh:accession/formula/charge` RHEA:17090 Source assertion: The original directional substrates chain contains CHEBI:57569 with coefficient 1. The formula and charge belong to the linked native compound, not an inferred label mapping. Source location `RHEA:17090 rh:substrates -> http://rdf.rhea-db.org/17089_L rh:contains1 -> http://rdf.rhea-db.org/Participant_17089_compound_5038 rh:compound -> http://rdf.rhea-db.org/Compound_5038 rh:accession/formula/charge`

References

KEGG:M00008 Entner-Doudoroff pathway, glucose-6P => glyceraldehyde-3P + pyruvate (source version: Original KEGG REST flat file retrieved 2026-10-11; native ENTRY and complete fields retained)
KEGG:R02736 beta-D-glucose-6-phosphate:NADP+ 1-oxoreductase (source version: Original KEGG REST flat file retrieved 2026-10-11; native ENTRY and complete fields retained)
KEGG:R10907 beta-D-glucose-6-phosphate:NAD+ 1-oxidoreductase (source version: Original KEGG REST flat file retrieved 2026-10-11; native ENTRY and complete fields retained)
KEGG:R02035 6-phospho-D-glucono-1,5-lactone lactonohydrolase (source version: Original KEGG REST flat file retrieved 2026-10-11; native ENTRY and complete fields retained)
KEGG:R02036 6-phospho-D-gluconate hydro-lyase (2-dehydro-3-deoxy-6-phospho-D-gluconate-forming) (source version: Original KEGG REST flat file retrieved 2026-10-11; native ENTRY and complete fields retained)
KEGG:R05605 2-dehydro-3-deoxy-6-phospho-D-gluconate D-glyceraldehyde-3-phosphate-lyase (pyruvate-forming) (source version: Original KEGG REST flat file retrieved 2026-10-11; native ENTRY and complete fields retained)
KEGG:C01172 beta-D-Glucose 6-phosphate (source version: Original KEGG REST flat file retrieved 2026-10-11; native ENTRY and complete fields retained)
KEGG:C01236 D-Glucono-1,5-lactone 6-phosphate; 6-Phospho-D-glucono-1,5-lactone (source version: Original KEGG REST flat file retrieved 2026-10-11; native ENTRY and complete fields retained)
KEGG:C00345 6-Phospho-D-gluconate (source version: Original KEGG REST flat file retrieved 2026-10-11; native ENTRY and complete fields retained)
KEGG:C04442 2-Dehydro-3-deoxy-6-phospho-D-gluconate; 6-Phospho-2-dehydro-3-deoxy-D-gluconate; 2-Keto-3-deoxy-6-phosphogluconate; 2-Dehydro-3-deoxy-D-gluconate 6-phosphate (source version: Original KEGG REST flat file retrieved 2026-10-11; native ENTRY and complete fields retained)
KEGG:C00118 D-Glyceraldehyde 3-phosphate; (2R)-2-Hydroxy-3-(phosphonooxy)-propanal; Glyceraldehyde 3-phosphate (source version: Original KEGG REST flat file retrieved 2026-10-11; native ENTRY and complete fields retained)
KEGG:C00022 Pyruvate; Pyruvic acid; 2-Oxopropanoate; 2-Oxopropanoic acid; Pyroracemic acid (source version: Original KEGG REST flat file retrieved 2026-10-11; native ENTRY and complete fields retained)
KEGG:C00001 H2O; Water (source version: Original KEGG REST flat file retrieved 2026-10-11; native ENTRY and complete fields retained)
KEGG:C00080 H+; Hydron (source version: Original KEGG REST flat file retrieved 2026-10-11; native ENTRY and complete fields retained)
KEGG:C00003 NAD+; NAD; Nicotinamide adenine dinucleotide; DPN; Diphosphopyridine nucleotide; Nadide; beta-NAD+ (source version: Original KEGG REST flat file retrieved 2026-10-11; native ENTRY and complete fields retained)
KEGG:C00004 NADH; DPNH; Reduced nicotinamide adenine dinucleotide (source version: Original KEGG REST flat file retrieved 2026-10-11; native ENTRY and complete fields retained)
KEGG:C00005 NADPH; TPNH; Reduced nicotinamide adenine dinucleotide phosphate (source version: Original KEGG REST flat file retrieved 2026-10-11; native ENTRY and complete fields retained)
KEGG:C00006 NADP+; NADP; Nicotinamide adenine dinucleotide phosphate; beta-Nicotinamide adenine dinucleotide phosphate; TPN; Triphosphopyridine nucleotide; beta-NADP+ (source version: Original KEGG REST flat file retrieved 2026-10-11; native ENTRY and complete fields retained)
CHEBI:57955 6-O-phosphonato-D-glucono-1,5-lactone(2-) (source version: ChEBI 255; digest covers entire original uncompressed Semantic SQL database)
CHEBI:15378 hydron (source version: ChEBI 255; digest covers entire original uncompressed Semantic SQL database)
CHEBI:58247 beta-D-glucose 6-phosphate(2-) (source version: ChEBI 255; digest covers entire original uncompressed Semantic SQL database)
CHEBI:58759 6-phosphonatooxy-D-gluconate (source version: ChEBI 255; digest covers entire original uncompressed Semantic SQL database)
CHEBI:57569 2-dehydro-3-deoxy-6-phosphonato-D-gluconate(3-) (source version: ChEBI 255; digest covers entire original uncompressed Semantic SQL database)
CHEBI:57783 NADPH(4-) (source version: ChEBI 255; digest covers entire original uncompressed Semantic SQL database)
CHEBI:17719 beta-D-glucose 6-phosphate (source version: ChEBI 255; digest covers entire original uncompressed Semantic SQL database)
CHEBI:15361 pyruvate (source version: ChEBI 255; digest covers entire original uncompressed Semantic SQL database)
CHEBI:57540 NAD(1-) (source version: ChEBI 255; digest covers entire original uncompressed Semantic SQL database)
CHEBI:49883 tetra-mu3-sulfido-tetrairon (source version: ChEBI 255; digest covers entire original uncompressed Semantic SQL database)
CHEBI:57945 NADH(2-) (source version: ChEBI 255; digest covers entire original uncompressed Semantic SQL database)
CHEBI:61548 D-glucopyranose 6-phosphate(2-) (source version: ChEBI 255; digest covers entire original uncompressed Semantic SQL database)
CHEBI:59776 D-glyceraldehyde 3-phosphate(2-) (source version: ChEBI 255; digest covers entire original uncompressed Semantic SQL database)
CHEBI:15377 water (source version: ChEBI 255; digest covers entire original uncompressed Semantic SQL database)
CHEBI:58349 NADP(3-) (source version: ChEBI 255; digest covers entire original uncompressed Semantic SQL database)
CHEBI:58225 alpha-D-glucose 6-phosphate(2-) (source version: ChEBI 255; digest covers entire original uncompressed Semantic SQL database)
RHEA:12557 6-phospho-D-glucono-1,5-lactone + H2O => 6-phospho-D-gluconate + H(+) (source version: Rhea 142 complete original compressed RDF; selected directional reaction and coefficient predicates)
RHEA:17278 6-phospho-D-gluconate => 2-dehydro-3-deoxy-6-phospho-D-gluconate + H2O (source version: Rhea 142 complete original compressed RDF; selected directional reaction and coefficient predicates)
RHEA:17090 2-dehydro-3-deoxy-6-phospho-D-gluconate => D-glyceraldehyde 3-phosphate + pyruvate (source version: Rhea 142 complete original compressed RDF; selected directional reaction and coefficient predicates)
UniProtKB:P0AC53 Glucose-6-phosphate 1-dehydrogenase (source version: Original UniProt JSON retrieved 2026-10-11; annotation evidence tiers retained)
UniProtKB:P52697 6-phosphogluconolactonase (source version: Original UniProt JSON retrieved 2026-10-11; annotation evidence tiers retained)
UniProtKB:P0ADF6 Phosphogluconate dehydratase (source version: Original UniProt JSON retrieved 2026-10-11; annotation evidence tiers retained)
UniProtKB:P0A955 KHG/KDPG aldolase (source version: Original UniProt JSON retrieved 2026-10-11; annotation evidence tiers retained)
MetaCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-CPLX MetaCyc native KDPGALDOL-4OH2OXOGLUTARALDOL-CPLX (source version: MetaCyc 27.0 XML original; source-specific curated assembly and component identity)
MetaCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER MetaCyc native KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER (source version: MetaCyc 27.0 XML original; source-specific curated assembly and component identity)
PMID:15576773 Identification of the Escherichia coli K-12 ybhE Gene as pgl, Encoding 6-Phosphogluconolactonase (source version: Original full primary article HTML from PMC; retrieved 2026-10-11)
PMID:17962400 Mutagenesis of the phosphate-binding pocket of KDPG aldolase enhances selectivity for hydrophobic substrates (source version: Original full primary article HTML from PMC; retrieved 2026-10-11)
PMID:17102132 MICROMOLAR INTRACELLULAR HYDROGEN PEROXIDE DISRUPTS METABOLISM BY DAMAGING IRON-SULFUR ENZYMES (source version: Original full primary article HTML from PMC; retrieved 2026-10-11)
PMID:11274385 Covalent intermediate trapped in 2-keto-3-deoxy-6- phosphogluconate (KDPG) aldolase structure at 1.95-Å resolution (source version: Original full primary article HTML from PMC; retrieved 2026-10-11)
PMID:15659677 Multiple Regulators Control Expression of the Entner-Doudoroff Aldolase (Eda) of Escherichia coli (source version: Original full primary article HTML from PMC; retrieved 2026-10-11)
PMID:27010804 Determinants of Cofactor Specificity for the Glucose-6-Phosphate Dehydrogenase from Escherichia coli : Simulation, Kinetics and Evolutionary Studies (source version: Original full 2016 primary JATS; wild-type versus engineered variant scope retained)
DOI:10.1371/journal.pone.0152403.s002 S1 Table. Accession numbers of bacterial G6PDHs (source version: Original supplementary workbook; accession row establishes sequence-analysis scope only)
PMID:22519976 The cofactor preference of glucose-6-phosphate dehydrogenase from Escherichia coli– modeling the physiological production of reduced cofactors (source version: Full official main article inspected through web on 2026-10-11; local HTTP403 body is not full text; no local article digest claimed)

Curation history

2026-10-11T17:37:03Z codex
- CREATE — Add the complete KEGG Entner-Doudoroff pathway
  Add KEGG:M00008 from glucose-6-phosphate through glyceraldehyde-3-phosphate and pyruvate: all four native positions, five reaction objects, nineteen participants, thirty-seven edges and ninety-two evidence blocks. Preserve NADP/NAD first-step alternatives, explicit beta-anomer/protonation and assay-preference limits, exact K-12 proteins versus historical constructs, Eda trimer evidence, Edd cofactor evidence tiers, and conflicting CsrA annotations without an unsupported regulatory edge. Original-source replay and independent whole-record review passed before integration. Root accepted exact target and canonical authority artifacts on prospective Myx commit4362f83; current corpus gates, integration replay and saved scientific review follow. Dossier: research/pathway_additions/2026-10-11-next-218.
Read this curation session