pentose phosphate pathway (non-oxidative branch) I

MetaCyc:NONOXIPENT-PWY

The non-oxidative branch of the pentose phosphate pathway reversibly interconverts D-ribulose 5-phosphate, aldehydo-D-ribose 5-phosphate, and D-xylulose 5-phosphate with D-sedoheptulose 7-phosphate, D-erythrose 4-phosphate, beta-D-fructose 6-phosphate, and D-glyceraldehyde 3-phosphate through isomerase, epimerase, transketolase, and transaldolase reactions.

Pathway type

central carbon metabolism

Organism scope

Escherichia coli NCBITaxon:562

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Pathway network

31 nodes · 49 asserted directed edges

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Chemical / cofactor
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Solid arrow: mechanistic relation
Dashed arrow: membership, location or cofactor relation

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Components and activities

Declared biological components and source reaction directions
Node	Kind or role	Source direction
Escherichia coli `NCBITaxon:562`	taxon
ribose-5-phosphate isomerase `EC:5.3.1.6`	molecular activity
ribulose-phosphate 3-epimerase `EC:5.1.3.1`	molecular activity
transketolase `EC:2.2.1.1`	molecular activity
transaldolase `EC:2.2.1.2`	molecular activity
D-ribulose 5-phosphate `CHEBI:58121`	small molecule
aldehydo-D-ribose 5-phosphate `CHEBI:58273`	small molecule
D-xylulose 5-phosphate `CHEBI:57737`	small molecule
D-sedoheptulose 7-phosphate `CHEBI:57483`	small molecule
D-glyceraldehyde 3-phosphate `CHEBI:59776`	small molecule
D-erythrose 4-phosphate `CHEBI:16897`	small molecule
beta-D-fructose 6-phosphate `CHEBI:57634`	small molecule
Ribose-5-phosphate isomerase A `UniProtKB:P0A7Z0`	protein
Transaldolase A `UniProtKB:P0A867`	protein
cytoplasm `GO:0005737`	cellular component
Transaldolase B `UniProtKB:P0A870`	protein
Ribulose-phosphate 3-epimerase `UniProtKB:P0AG07`	protein
cobalt(2+) `CHEBI:48828`	cofactor
iron(2+) `CHEBI:29033`	cofactor
manganese(2+) `CHEBI:29035`	cofactor
zinc(2+) `CHEBI:29105`	cofactor
Transketolase 1 `UniProtKB:P27302`	protein
magnesium(2+) `CHEBI:18420`	cofactor
calcium(2+) `CHEBI:29108`	cofactor
thiamine(1+) diphosphate(3-) `CHEBI:58937`	cofactor
Transketolase 2 `UniProtKB:P33570`	protein
Ribose-5-phosphate isomerase B `UniProtKB:P37351`	protein
ribose-5-phosphate isomerase reaction `RHEA:14659`	reaction	right to left
ribulose-phosphate 3-epimerase reaction `RHEA:13678`	reaction	left to right
transketolase sedoheptulose-7-phosphate reaction `RHEA:10510`	reaction	right to left
transaldolase reaction `RHEA:17054`	reaction	left to right
transketolase fructose-6-phosphate reaction `RHEA:27627`	reaction	left to right

Mechanistic edges

Mechanistic edges and their cited evidence
Subject	Predicate and description	Object	Evidence
D-ribulose 5-phosphate `CHEBI:58121`	consumes	ribose-5-phosphate isomerase reaction `RHEA:14659`	RHEA:14659 Source assertion: Rhea lists CHEBI:58121 on the substrates side of RHEA:14659 in this directed reaction. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/14659']/rh:substrates; rh:contains/rh:compound/rh:accession`
ribose-5-phosphate isomerase reaction `RHEA:14659`	produces	aldehydo-D-ribose 5-phosphate `CHEBI:58273`	RHEA:14659 Source assertion: Rhea lists CHEBI:58273 on the products side of RHEA:14659 in this directed reaction. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/14659']/rh:products; rh:contains/rh:compound/rh:accession`
D-ribulose 5-phosphate `CHEBI:58121`	consumes	ribulose-phosphate 3-epimerase reaction `RHEA:13678`	RHEA:13678 Source assertion: Rhea lists CHEBI:58121 on the substrates side of RHEA:13678 in this directed reaction. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/13678']/rh:substrates; rh:contains/rh:compound/rh:accession`
ribulose-phosphate 3-epimerase reaction `RHEA:13678`	produces	D-xylulose 5-phosphate `CHEBI:57737`	RHEA:13678 Source assertion: Rhea lists CHEBI:57737 on the products side of RHEA:13678 in this directed reaction. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/13678']/rh:products; rh:contains/rh:compound/rh:accession`
D-xylulose 5-phosphate `CHEBI:57737`	consumes	transketolase sedoheptulose-7-phosphate reaction `RHEA:10510`	RHEA:10510 Source assertion: Rhea lists CHEBI:57737 on the substrates side of RHEA:10510 in this directed reaction. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/10510']/rh:substrates; rh:contains/rh:compound/rh:accession`
aldehydo-D-ribose 5-phosphate `CHEBI:58273`	consumes	transketolase sedoheptulose-7-phosphate reaction `RHEA:10510`	RHEA:10510 Source assertion: Rhea lists CHEBI:58273 on the substrates side of RHEA:10510 in this directed reaction. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/10510']/rh:substrates; rh:contains/rh:compound/rh:accession`
transketolase sedoheptulose-7-phosphate reaction `RHEA:10510`	produces	D-sedoheptulose 7-phosphate `CHEBI:57483`	RHEA:10510 Source assertion: Rhea lists CHEBI:57483 on the products side of RHEA:10510 in this directed reaction. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/10510']/rh:products; rh:contains/rh:compound/rh:accession`
transketolase sedoheptulose-7-phosphate reaction `RHEA:10510`	produces	D-glyceraldehyde 3-phosphate `CHEBI:59776`	RHEA:10510 Source assertion: Rhea lists CHEBI:59776 on the products side of RHEA:10510 in this directed reaction. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/10510']/rh:products; rh:contains/rh:compound/rh:accession`
D-sedoheptulose 7-phosphate `CHEBI:57483`	consumes	transaldolase reaction `RHEA:17054`	RHEA:17054 Source assertion: Rhea lists CHEBI:57483 on the substrates side of RHEA:17054 in this directed reaction. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/17054']/rh:substrates; rh:contains/rh:compound/rh:accession`
D-glyceraldehyde 3-phosphate `CHEBI:59776`	consumes	transaldolase reaction `RHEA:17054`	RHEA:17054 Source assertion: Rhea lists CHEBI:59776 on the substrates side of RHEA:17054 in this directed reaction. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/17054']/rh:substrates; rh:contains/rh:compound/rh:accession`
transaldolase reaction `RHEA:17054`	produces	D-erythrose 4-phosphate `CHEBI:16897`	RHEA:17054 Source assertion: Rhea lists CHEBI:16897 on the products side of RHEA:17054 in this directed reaction. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/17054']/rh:products; rh:contains/rh:compound/rh:accession`
transaldolase reaction `RHEA:17054`	produces	beta-D-fructose 6-phosphate `CHEBI:57634`	RHEA:17054 Source assertion: Rhea lists CHEBI:57634 on the products side of RHEA:17054 in this directed reaction. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/17054']/rh:products; rh:contains/rh:compound/rh:accession`
D-erythrose 4-phosphate `CHEBI:16897`	consumes	transketolase fructose-6-phosphate reaction `RHEA:27627`	RHEA:27627 Source assertion: Rhea lists CHEBI:16897 on the substrates side of RHEA:27627 in this directed reaction. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/27627']/rh:substrates; rh:contains/rh:compound/rh:accession`
D-xylulose 5-phosphate `CHEBI:57737`	consumes	transketolase fructose-6-phosphate reaction `RHEA:27627`	RHEA:27627 Source assertion: Rhea lists CHEBI:57737 on the substrates side of RHEA:27627 in this directed reaction. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/27627']/rh:substrates; rh:contains/rh:compound/rh:accession`
transketolase fructose-6-phosphate reaction `RHEA:27627`	produces	beta-D-fructose 6-phosphate `CHEBI:57634`	RHEA:27627 Source assertion: Rhea lists CHEBI:57634 on the products side of RHEA:27627 in this directed reaction. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/27627']/rh:products; rh:contains/rh:compound/rh:accession`
transketolase fructose-6-phosphate reaction `RHEA:27627`	produces	D-glyceraldehyde 3-phosphate `CHEBI:59776`	RHEA:27627 Source assertion: Rhea lists CHEBI:59776 on the products side of RHEA:27627 in this directed reaction. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/27627']/rh:products; rh:contains/rh:compound/rh:accession`
ribose-5-phosphate isomerase `EC:5.3.1.6`	catalyzes	ribose-5-phosphate isomerase reaction `RHEA:14659`	RHEA:14657 Source assertion: Rhea associates EC:5.3.1.6 with the reaction family containing RHEA:14659. Source location `rh:ec`
ribulose-phosphate 3-epimerase `EC:5.1.3.1`	catalyzes	ribulose-phosphate 3-epimerase reaction `RHEA:13678`	RHEA:13677 Source assertion: Rhea associates EC:5.1.3.1 with the reaction family containing RHEA:13678. Source location `rh:ec`
transketolase `EC:2.2.1.1`	catalyzes	transketolase sedoheptulose-7-phosphate reaction `RHEA:10510`	RHEA:10508 Source assertion: Rhea associates EC:2.2.1.1 with the reaction family containing RHEA:10510. Source location `rh:ec`
transaldolase `EC:2.2.1.2`	catalyzes	transaldolase reaction `RHEA:17054`	RHEA:17053 Source assertion: Rhea associates EC:2.2.1.2 with the reaction family containing RHEA:17054. Source location `rh:ec`
transketolase `EC:2.2.1.1`	catalyzes	transketolase fructose-6-phosphate reaction `RHEA:27627`	RHEA:27626 Source assertion: Rhea associates EC:2.2.1.1 with the reaction family containing RHEA:27627. Source location `rh:ec`
transketolase sedoheptulose-7-phosphate reaction `RHEA:10510`	precedes	transaldolase reaction `RHEA:17054`	MetaCyc:NONOXIPENT-PWY Source assertion: MetaCyc pathway ordering places RHEA:10510 before RHEA:17054 in this pathway. Shared intermediate: CHEBI:57483, CHEBI:59776. Source location `Pathway/reaction-ordering and reaction-layout; Rhea-to-MetaCyc cross-references`
ribulose-phosphate 3-epimerase reaction `RHEA:13678`	precedes	transketolase sedoheptulose-7-phosphate reaction `RHEA:10510`	MetaCyc:NONOXIPENT-PWY Source assertion: MetaCyc pathway ordering places RHEA:13678 before RHEA:10510 in this pathway. Shared intermediate: CHEBI:57737. Source location `Pathway/reaction-ordering and reaction-layout; Rhea-to-MetaCyc cross-references`
ribulose-phosphate 3-epimerase reaction `RHEA:13678`	precedes	transketolase fructose-6-phosphate reaction `RHEA:27627`	MetaCyc:NONOXIPENT-PWY Source assertion: MetaCyc pathway ordering places RHEA:13678 before RHEA:27627 in this pathway. Shared intermediate: CHEBI:57737. Source location `Pathway/reaction-ordering and reaction-layout; Rhea-to-MetaCyc cross-references`
ribose-5-phosphate isomerase reaction `RHEA:14659`	precedes	transketolase sedoheptulose-7-phosphate reaction `RHEA:10510`	MetaCyc:NONOXIPENT-PWY Source assertion: MetaCyc pathway ordering places RHEA:14659 before RHEA:10510 in this pathway. Shared intermediate: CHEBI:58273. Source location `Pathway/reaction-ordering and reaction-layout; Rhea-to-MetaCyc cross-references`
transaldolase reaction `RHEA:17054`	precedes	transketolase fructose-6-phosphate reaction `RHEA:27627`	MetaCyc:NONOXIPENT-PWY Source assertion: MetaCyc pathway ordering places RHEA:17054 before RHEA:27627 in this pathway. Shared intermediate: CHEBI:16897. Source location `Pathway/reaction-ordering and reaction-layout; Rhea-to-MetaCyc cross-references`
Ribose-5-phosphate isomerase A `UniProtKB:P0A7Z0`	enables	ribose-5-phosphate isomerase reaction `RHEA:14659`	UniProtKB:P0A7Z0 Source assertion: UniProt annotates UniProtKB:P0A7Z0 with catalytic activity for the reaction family of RHEA:14659. Annotation evidence: ECO:0000255, ECO:0000269; organism taxon: NCBITaxon:83333. Source location `comments[commentType='CATALYTIC ACTIVITY'].reaction.reactionCrossReferences`
Transaldolase A `UniProtKB:P0A867`	enables	transaldolase reaction `RHEA:17054`	UniProtKB:P0A867 Source assertion: UniProt annotates UniProtKB:P0A867 with catalytic activity for the reaction family of RHEA:17054. Annotation evidence: ECO:0000255; organism taxon: NCBITaxon:83333. Source location `comments[commentType='CATALYTIC ACTIVITY'].reaction.reactionCrossReferences`
Transaldolase A `UniProtKB:P0A867`	located_in	cytoplasm `GO:0005737`	UniProtKB:P0A867 Source assertion: UniProt locates UniProtKB:P0A867 in Cytoplasm (SL-0086, mapped by UniProt to GO:0005737). Annotation evidence: ECO:0000305. Source location `comments[commentType='SUBCELLULAR LOCATION'].subcellularLocations; UniProt location vocabulary GO mapping`
Transaldolase B `UniProtKB:P0A870`	enables	transaldolase reaction `RHEA:17054`	UniProtKB:P0A870 Source assertion: UniProt annotates UniProtKB:P0A870 with catalytic activity for the reaction family of RHEA:17054. Annotation evidence: ECO:0000269; organism taxon: NCBITaxon:83333. Source location `comments[commentType='CATALYTIC ACTIVITY'].reaction.reactionCrossReferences`
Transaldolase B `UniProtKB:P0A870`	located_in	cytoplasm `GO:0005737`	UniProtKB:P0A870 Source assertion: UniProt locates UniProtKB:P0A870 in Cytoplasm (SL-0086, mapped by UniProt to GO:0005737). Annotation evidence: ECO:0000305. Source location `comments[commentType='SUBCELLULAR LOCATION'].subcellularLocations; UniProt location vocabulary GO mapping`
Ribulose-phosphate 3-epimerase `UniProtKB:P0AG07`	enables	ribulose-phosphate 3-epimerase reaction `RHEA:13678`	UniProtKB:P0AG07 Source assertion: UniProt annotates UniProtKB:P0AG07 with catalytic activity for the reaction family of RHEA:13678. Annotation evidence: ECO:0000255, ECO:0000269; organism taxon: NCBITaxon:83333. Source location `comments[commentType='CATALYTIC ACTIVITY'].reaction.reactionCrossReferences`
Ribulose-phosphate 3-epimerase `UniProtKB:P0AG07`	has_cofactor	cobalt(2+) `CHEBI:48828`	UniProtKB:P0AG07 Source assertion: UniProt lists CHEBI:48828 as a cofactor of UniProtKB:P0AG07 (evidence: ECO:0000269). Binds 1 divalent metal cation per subunit. Active with Co(2+), Fe(2+), Mn(2+) and Zn(2+). Source location `comments[commentType='COFACTOR'].cofactors and note`
Ribulose-phosphate 3-epimerase `UniProtKB:P0AG07`	has_cofactor	iron(2+) `CHEBI:29033`	UniProtKB:P0AG07 Source assertion: UniProt lists CHEBI:29033 as a cofactor of UniProtKB:P0AG07 (evidence: ECO:0000269). Binds 1 divalent metal cation per subunit. Active with Co(2+), Fe(2+), Mn(2+) and Zn(2+). Source location `comments[commentType='COFACTOR'].cofactors and note`
Ribulose-phosphate 3-epimerase `UniProtKB:P0AG07`	has_cofactor	manganese(2+) `CHEBI:29035`	UniProtKB:P0AG07 Source assertion: UniProt lists CHEBI:29035 as a cofactor of UniProtKB:P0AG07 (evidence: ECO:0000269). Binds 1 divalent metal cation per subunit. Active with Co(2+), Fe(2+), Mn(2+) and Zn(2+). Source location `comments[commentType='COFACTOR'].cofactors and note`
Ribulose-phosphate 3-epimerase `UniProtKB:P0AG07`	has_cofactor	zinc(2+) `CHEBI:29105`	UniProtKB:P0AG07 Source assertion: UniProt lists CHEBI:29105 as a cofactor of UniProtKB:P0AG07 (evidence: ECO:0000269). Binds 1 divalent metal cation per subunit. Active with Co(2+), Fe(2+), Mn(2+) and Zn(2+). Source location `comments[commentType='COFACTOR'].cofactors and note`
Transketolase 1 `UniProtKB:P27302`	enables	transketolase sedoheptulose-7-phosphate reaction `RHEA:10510`	UniProtKB:P27302 Source assertion: UniProt annotates UniProtKB:P27302 with catalytic activity for the reaction family of RHEA:10510. Annotation evidence: ECO:0000269; organism taxon: NCBITaxon:83333. Source location `comments[commentType='CATALYTIC ACTIVITY'].reaction.reactionCrossReferences`
Transketolase 1 `UniProtKB:P27302`	has_cofactor	magnesium(2+) `CHEBI:18420`	UniProtKB:P27302 Source assertion: UniProt lists CHEBI:18420 as a cofactor of UniProtKB:P27302 (evidence: ECO:0000269). Binds 1 Mg(2+) ion per subunit (PubMed:7607225, Ref.14). Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+) (PubMed:7607225). Source location `comments[commentType='COFACTOR'].cofactors and note`
Transketolase 1 `UniProtKB:P27302`	has_cofactor	calcium(2+) `CHEBI:29108`	UniProtKB:P27302 Source assertion: UniProt lists CHEBI:29108 as a cofactor of UniProtKB:P27302 (evidence: ECO:0000269). Binds 1 Mg(2+) ion per subunit (PubMed:7607225, Ref.14). Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+) (PubMed:7607225). Source location `comments[commentType='COFACTOR'].cofactors and note`
Transketolase 1 `UniProtKB:P27302`	has_cofactor	manganese(2+) `CHEBI:29035`	UniProtKB:P27302 Source assertion: UniProt lists CHEBI:29035 as a cofactor of UniProtKB:P27302 (evidence: ECO:0000269). Binds 1 Mg(2+) ion per subunit (PubMed:7607225, Ref.14). Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+) (PubMed:7607225). Source location `comments[commentType='COFACTOR'].cofactors and note`
Transketolase 1 `UniProtKB:P27302`	has_cofactor	cobalt(2+) `CHEBI:48828`	UniProtKB:P27302 Source assertion: UniProt lists CHEBI:48828 as a cofactor of UniProtKB:P27302 (evidence: ECO:0000269). Binds 1 Mg(2+) ion per subunit (PubMed:7607225, Ref.14). Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+) (PubMed:7607225). Source location `comments[commentType='COFACTOR'].cofactors and note`
Transketolase 1 `UniProtKB:P27302`	has_cofactor	thiamine(1+) diphosphate(3-) `CHEBI:58937`	UniProtKB:P27302 Source assertion: UniProt lists CHEBI:58937 as a cofactor of UniProtKB:P27302 (evidence: ECO:0000269). Binds 1 thiamine pyrophosphate per subunit. During the reaction, the substrate forms a covalent intermediate with the cofactor. Source location `comments[commentType='COFACTOR'].cofactors and note`
Transketolase 2 `UniProtKB:P33570`	enables	transketolase sedoheptulose-7-phosphate reaction `RHEA:10510`	UniProtKB:P33570 Source assertion: UniProt annotates UniProtKB:P33570 with catalytic activity for the reaction family of RHEA:10510. Annotation evidence: ECO:0000269; organism taxon: NCBITaxon:83333. Source location `comments[commentType='CATALYTIC ACTIVITY'].reaction.reactionCrossReferences`
Transketolase 2 `UniProtKB:P33570`	has_cofactor	magnesium(2+) `CHEBI:18420`	UniProtKB:P33570 Source assertion: UniProt lists CHEBI:18420 as a cofactor of UniProtKB:P33570 (evidence: ECO:0000250). Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+). Source location `comments[commentType='COFACTOR'].cofactors and note`
Transketolase 2 `UniProtKB:P33570`	has_cofactor	calcium(2+) `CHEBI:29108`	UniProtKB:P33570 Source assertion: UniProt lists CHEBI:29108 as a cofactor of UniProtKB:P33570 (evidence: ECO:0000250). Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+). Source location `comments[commentType='COFACTOR'].cofactors and note`
Transketolase 2 `UniProtKB:P33570`	has_cofactor	manganese(2+) `CHEBI:29035`	UniProtKB:P33570 Source assertion: UniProt lists CHEBI:29035 as a cofactor of UniProtKB:P33570 (evidence: ECO:0000250). Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+). Source location `comments[commentType='COFACTOR'].cofactors and note`
Transketolase 2 `UniProtKB:P33570`	has_cofactor	cobalt(2+) `CHEBI:48828`	UniProtKB:P33570 Source assertion: UniProt lists CHEBI:48828 as a cofactor of UniProtKB:P33570 (evidence: ECO:0000250). Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+). Source location `comments[commentType='COFACTOR'].cofactors and note`
Transketolase 2 `UniProtKB:P33570`	has_cofactor	thiamine(1+) diphosphate(3-) `CHEBI:58937`	UniProtKB:P33570 Source assertion: UniProt lists CHEBI:58937 as a cofactor of UniProtKB:P33570 (evidence: ECO:0000250). Binds 1 thiamine pyrophosphate per subunit. Source location `comments[commentType='COFACTOR'].cofactors and note`
Ribose-5-phosphate isomerase B `UniProtKB:P37351`	enables	ribose-5-phosphate isomerase reaction `RHEA:14659`	UniProtKB:P37351 Source assertion: UniProt annotates UniProtKB:P37351 with catalytic activity for the reaction family of RHEA:14659. Annotation evidence: ECO:0000269; organism taxon: NCBITaxon:83333. Source location `comments[commentType='CATALYTIC ACTIVITY'].reaction.reactionCrossReferences`

References

MetaCyc:NONOXIPENT-PWY MetaCyc pentose phosphate pathway (non-oxidative branch) I (source version: 22.5)
RHEA:14657 Rhea ribose-5-phosphate isomerase reaction (source version: 139)
RHEA:14660 Rhea bidirectional ribose-5-phosphate isomerase reaction (source version: 139)
RHEA:13677 Rhea ribulose-phosphate 3-epimerase reaction (source version: 139)
RHEA:13680 Rhea bidirectional ribulose-phosphate 3-epimerase reaction (source version: 139)
RHEA:10508 Rhea transketolase sedoheptulose-7-phosphate reaction (source version: 139)
RHEA:10511 Rhea bidirectional transketolase sedoheptulose-7-phosphate reaction (source version: 139)
RHEA:17053 Rhea transaldolase reaction (source version: 139)
RHEA:17056 Rhea bidirectional transaldolase reaction (source version: 139)
RHEA:27626 Rhea transketolase fructose-6-phosphate reaction (source version: 139)
RHEA:27629 Rhea bidirectional transketolase fructose-6-phosphate reaction (source version: 139)
RHEA:14659 RHEA:14659 authority record (source version: 139)
RHEA:13678 RHEA:13678 authority record (source version: 139)
RHEA:10510 RHEA:10510 authority record (source version: 139)
RHEA:17054 RHEA:17054 authority record (source version: 139)
RHEA:27627 RHEA:27627 authority record (source version: 139)
UniProtKB:P0A7Z0 UniProtKB:P0A7Z0 authority record (source version: 2026_03)
UniProtKB:P0A867 UniProtKB:P0A867 authority record (source version: 2026_03)
UniProtKB:P0A870 UniProtKB:P0A870 authority record (source version: 2026_03)
UniProtKB:P0AG07 UniProtKB:P0AG07 authority record (source version: 2026_03)
UniProtKB:P27302 UniProtKB:P27302 authority record (source version: 2026_03)
UniProtKB:P33570 UniProtKB:P33570 authority record (source version: 2026_03)
UniProtKB:P37351 UniProtKB:P37351 authority record (source version: 2026_03)

Curation history

2026-10-05T06:25:52Z codex
- EDIT — Review causal chemistry and add sourced molecular context
  Reviewed the entire record against MetaCyc 22.5 native pathway XML (including nested pathways), Rhea 139 explicit sides and directions, ENZYME 02-Sep-2026, PubMed records, and reviewed UniProt 2026_03 annotations within the record's taxon scope. Replaced generated structured-source quotations with source_assertion and source_locator. Typed molecular activities and participants. Reaction count 5 to 5; 5 directed-ID corrections; 7 protein annotations, 14 cofactor annotations and 2 sourced locations. All Rhea reaction substrate/product sets checked against independent Rhea authority; native pathway leaf coverage and source exceptions recorded in reports/causal_graph_review/metacyc-review.json. Full source URLs, versions and byte hashes are in metacyc-sources.json. All 50 MetaCyc records passed native schema validation; six targeted chemistry/evidence regression tests passed. Missing protein or cofactor annotations are not treated as biological absence; qualifications and exclusions are preserved in the ledger.
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