sulfoquinovose degradation I

MetaCyc:PWY-7446

The complete four-reaction sulfo-EMP route from free sulfoquinovose to glycerone phosphate and (2S)-3-sulfopropanediol in Escherichia coli K-12. YihS isomerization, YihV phosphorylation, YihT aldol cleavage and YihU NADH-dependent reduction retain all charged reaction sides. Current chemistry selects beta-SQ and (2S)-SLA/(2S)-DHPS; the old native protein prose naming (2R)-SLA is superseded, while the native reaction frames use a stereounspecified SLA class. E. coli YihT activity was detected in the 2014 coupled reconstitution but not in the 2021 purified preparation; that later study used Salmonella enzyme for kinetics. YihS and YihU use source-defined assemblies; YihV and YihT are qualified functional gene-product assertions, not claims of monomer sufficiency. CsqR repression and assay-dependent kinase modulation are included with their experimental conditions. The endpoint retains organic sulfur: glycoside hydrolysis, SQ mutarotation, membrane transport, sulforhamnose side-reaction chemistry, lower glycolysis and partner-organism DHPS mineralization are outside the four-member native boundary.

Pathway type

sulfo EMP catabolism

Organism scope

Escherichia coli K-12 NCBITaxon:83333

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Pathway network

31 nodes · 41 asserted directed edges

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Reaction / activity
Chemical / cofactor
Protein / complex
Pathway
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Components and activities

Declared biological components and source reaction directions
Node	Kind or role	Source direction
Escherichia coli K-12 `NCBITaxon:83333`	taxon
6-sulfo-beta-D-quinovose(1-) `CHEBI:142957`	small molecule
hydron `CHEBI:15378`	small molecule
citrate(3-) `CHEBI:16947`	small molecule
(2S)-3-sulfopropanediol(1-) `CHEBI:176527`	small molecule
magnesium(2+) `CHEBI:18420`	cofactor
6-sulfo-D-rhamnose(1-) `CHEBI:190019`	small molecule
ATP(4-) `CHEBI:30616`	small molecule
ADP(3-) `CHEBI:456216`	small molecule
D-fructofuranose 1,6-bisphosphate(4-) `CHEBI:49299`	small molecule
NAD(1-) `CHEBI:57540`	small molecule
D-fructose 6-phosphate(2-) `CHEBI:57579`	small molecule
glycerone phosphate(2-) `CHEBI:57642`	small molecule
NADH(2-) `CHEBI:57945`	small molecule
phosphonatoenolpyruvate `CHEBI:58702`	small molecule
6-sulfo-D-quinovose(1-) `CHEBI:77132`	small molecule
6-deoxy-6-sulfo-D-fructofuranose(1-) `CHEBI:77133`	small molecule
6-deoxy-6-sulfo-D-fructofuranose 1-phosphate(3-) `CHEBI:77134`	small molecule
3-sulfolactaldehyde(1-) `CHEBI:77135`	small molecule
L-3-sulfolactaldehyde(1-) `CHEBI:90109`	small molecule
Sulfoquinovose isomerase `UniProtKB:P32140`	protein
Sulfofructosephosphate aldolase `UniProtKB:P32141`	protein
3-sulfolactaldehyde reductase `UniProtKB:P0A9V8`	protein
Sulfofructose kinase `UniProtKB:P32143`	protein
HTH-type transcriptional repressor CsqR `UniProtKB:P32144`	protein
sulfoquinovose isomerase `MetaCyc:CPLX0-7683`	complex
3-sulfolactaldehyde reductase `MetaCyc:CPLX0-7794`	complex
6-sulfo-beta-D-quinovose => 6-deoxy-6-sulfo-D-fructose `RHEA:40440`	molecular activity	left to right
6-deoxy-6-sulfo-D-fructose + ATP => 6-deoxy-6-sulfo-D-fructose 1-phosphate + ADP + H(+) `RHEA:40444`	molecular activity	left to right
6-deoxy-6-sulfo-D-fructose 1-phosphate => (2S)-3-sulfolactaldehyde + dihydroxyacetone phosphate `RHEA:40516`	molecular activity	left to right
(2S)-3-sulfolactaldehyde + NADH + H(+) => (2S)-3-sulfopropanediol + NAD(+) `RHEA:40513`	molecular activity	right to left

Mechanistic edges

Mechanistic edges and their cited evidence
Subject	Predicate and description	Object	Evidence
6-sulfo-beta-D-quinovose(1-) `CHEBI:142957`	consumes	6-sulfo-beta-D-quinovose => 6-deoxy-6-sulfo-D-fructose `RHEA:40440`	RHEA:40440 Source assertion: RHEA:40440 assigns CHEBI:142957 to its substrates with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40440']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40439_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40439_compound_15317']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_15317)`
6-sulfo-beta-D-quinovose => 6-deoxy-6-sulfo-D-fructose `RHEA:40440`	produces	6-deoxy-6-sulfo-D-fructofuranose(1-) `CHEBI:77133`	RHEA:40440 Source assertion: RHEA:40440 assigns CHEBI:77133 to its products with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40440']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40439_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40439_compound_9102']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_9102)`
6-deoxy-6-sulfo-D-fructofuranose(1-) `CHEBI:77133`	consumes	6-deoxy-6-sulfo-D-fructose + ATP => 6-deoxy-6-sulfo-D-fructose 1-phosphate + ADP + H(+) `RHEA:40444`	RHEA:40444 Source assertion: RHEA:40444 assigns CHEBI:77133 to its substrates with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40444']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40443_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40443_compound_9102']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_9102)`
ATP(4-) `CHEBI:30616`	consumes	6-deoxy-6-sulfo-D-fructose + ATP => 6-deoxy-6-sulfo-D-fructose 1-phosphate + ADP + H(+) `RHEA:40444`	RHEA:40444 Source assertion: RHEA:40444 assigns CHEBI:30616 to its substrates with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40444']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40443_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40443_compound_6372']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_6372)`
6-deoxy-6-sulfo-D-fructose + ATP => 6-deoxy-6-sulfo-D-fructose 1-phosphate + ADP + H(+) `RHEA:40444`	produces	6-deoxy-6-sulfo-D-fructofuranose 1-phosphate(3-) `CHEBI:77134`	RHEA:40444 Source assertion: RHEA:40444 assigns CHEBI:77134 to its products with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40444']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40443_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40443_compound_9103']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_9103)`
6-deoxy-6-sulfo-D-fructose + ATP => 6-deoxy-6-sulfo-D-fructose 1-phosphate + ADP + H(+) `RHEA:40444`	produces	ADP(3-) `CHEBI:456216`	RHEA:40444 Source assertion: RHEA:40444 assigns CHEBI:456216 to its products with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40444']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40443_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40443_compound_2710']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_2710)`
6-deoxy-6-sulfo-D-fructose + ATP => 6-deoxy-6-sulfo-D-fructose 1-phosphate + ADP + H(+) `RHEA:40444`	produces	hydron `CHEBI:15378`	RHEA:40444 Source assertion: RHEA:40444 assigns CHEBI:15378 to its products with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40444']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40443_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40443_compound_3249']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_3249)`
6-deoxy-6-sulfo-D-fructofuranose 1-phosphate(3-) `CHEBI:77134`	consumes	6-deoxy-6-sulfo-D-fructose 1-phosphate => (2S)-3-sulfolactaldehyde + dihydroxyacetone phosphate `RHEA:40516`	RHEA:40516 Source assertion: RHEA:40516 assigns CHEBI:77134 to its substrates with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40516']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40515_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40515_compound_9103']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_9103)`
6-deoxy-6-sulfo-D-fructose 1-phosphate => (2S)-3-sulfolactaldehyde + dihydroxyacetone phosphate `RHEA:40516`	produces	L-3-sulfolactaldehyde(1-) `CHEBI:90109`	RHEA:40516 Source assertion: RHEA:40516 assigns CHEBI:90109 to its products with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40516']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40515_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40515_compound_12045']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_12045)`
6-deoxy-6-sulfo-D-fructose 1-phosphate => (2S)-3-sulfolactaldehyde + dihydroxyacetone phosphate `RHEA:40516`	produces	glycerone phosphate(2-) `CHEBI:57642`	RHEA:40516 Source assertion: RHEA:40516 assigns CHEBI:57642 to its products with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40516']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40515_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40515_compound_4255']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_4255)`
L-3-sulfolactaldehyde(1-) `CHEBI:90109`	consumes	(2S)-3-sulfolactaldehyde + NADH + H(+) => (2S)-3-sulfopropanediol + NAD(+) `RHEA:40513`	RHEA:40513 Source assertion: RHEA:40513 assigns CHEBI:90109 to its substrates with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40513']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40511_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40511_compound_12045']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_12045)`
NADH(2-) `CHEBI:57945`	consumes	(2S)-3-sulfolactaldehyde + NADH + H(+) => (2S)-3-sulfopropanediol + NAD(+) `RHEA:40513`	RHEA:40513 Source assertion: RHEA:40513 assigns CHEBI:57945 to its substrates with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40513']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40511_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40511_compound_1650']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_1650)`
hydron `CHEBI:15378`	consumes	(2S)-3-sulfolactaldehyde + NADH + H(+) => (2S)-3-sulfopropanediol + NAD(+) `RHEA:40513`	RHEA:40513 Source assertion: RHEA:40513 assigns CHEBI:15378 to its substrates with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40513']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40511_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40511_compound_3249']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_3249)`
(2S)-3-sulfolactaldehyde + NADH + H(+) => (2S)-3-sulfopropanediol + NAD(+) `RHEA:40513`	produces	(2S)-3-sulfopropanediol(1-) `CHEBI:176527`	RHEA:40513 Source assertion: RHEA:40513 assigns CHEBI:176527 to its products with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40513']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40511_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40511_compound_17525']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_17525)`
(2S)-3-sulfolactaldehyde + NADH + H(+) => (2S)-3-sulfopropanediol + NAD(+) `RHEA:40513`	produces	NAD(1-) `CHEBI:57540`	RHEA:40513 Source assertion: RHEA:40513 assigns CHEBI:57540 to its products with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40513']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40511_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40511_compound_3484']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_3484)`
6-sulfo-beta-D-quinovose => 6-deoxy-6-sulfo-D-fructose `RHEA:40440`	part_of	`MetaCyc:PWY-7446`	MetaCyc:PWY-7446 Source assertion: The native pathway lists RXN-15296 as a member. Source location `/ptools-xml/Pathway[@frameid="PWY-7446"]/reaction-list/Reaction[@frameid="RXN-15296"]` MetaCyc:RXN-15296 Source assertion: The native reaction explicitly cross-references RHEA:40440. Source location `/ptools-xml/Reaction[@frameid="RXN-15296"]/dblink[dblink-db="RHEA"]/dblink-oid` RHEA:40440 Source assertion: Rhea family 40439 contains directed reaction 40440, whose physiological side assignment is used here. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/40439"]/rh:directionalReaction[@rdf:resource="http://rdf.rhea-db.org/40440"]; rdf:Description[@rdf:about="http://rdf.rhea-db.org/40440"]/rh:substrates and rh:products` PMID:24463506 Source assertion: K-12 substrains grew aerobically on SQ; MG1655 proteomics and recombinant four-enzyme reconstitution supported the route. BW25113 yihS, yihT and yihV deletions failed to grow on SQ. Source location `Printed pp114-116; Figure 2 and Figure 3; Methods, Bacteria and growth conditions and Heterologous expression and purification`
6-deoxy-6-sulfo-D-fructose + ATP => 6-deoxy-6-sulfo-D-fructose 1-phosphate + ADP + H(+) `RHEA:40444`	part_of	`MetaCyc:PWY-7446`	MetaCyc:PWY-7446 Source assertion: The native pathway lists RXN-15297 as a member. Source location `/ptools-xml/Pathway[@frameid="PWY-7446"]/reaction-list/Reaction[@frameid="RXN-15297"]` MetaCyc:RXN-15297 Source assertion: The native reaction explicitly cross-references RHEA:40444. Source location `/ptools-xml/Reaction[@frameid="RXN-15297"]/dblink[dblink-db="RHEA"]/dblink-oid` RHEA:40444 Source assertion: Rhea family 40443 contains directed reaction 40444, whose physiological side assignment is used here. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/40443"]/rh:directionalReaction[@rdf:resource="http://rdf.rhea-db.org/40444"]; rdf:Description[@rdf:about="http://rdf.rhea-db.org/40444"]/rh:substrates and rh:products`
6-deoxy-6-sulfo-D-fructose 1-phosphate => (2S)-3-sulfolactaldehyde + dihydroxyacetone phosphate `RHEA:40516`	part_of	`MetaCyc:PWY-7446`	MetaCyc:PWY-7446 Source assertion: The native pathway lists RXN-15298 as a member. Source location `/ptools-xml/Pathway[@frameid="PWY-7446"]/reaction-list/Reaction[@frameid="RXN-15298"]` MetaCyc:RXN-15298 Source assertion: The native reaction explicitly cross-references RHEA:40516. Source location `/ptools-xml/Reaction[@frameid="RXN-15298"]/dblink[dblink-db="RHEA"]/dblink-oid` RHEA:40516 Source assertion: Rhea family 40515 contains directed reaction 40516, whose physiological side assignment is used here. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/40515"]/rh:directionalReaction[@rdf:resource="http://rdf.rhea-db.org/40516"]; rdf:Description[@rdf:about="http://rdf.rhea-db.org/40516"]/rh:substrates and rh:products`
(2S)-3-sulfolactaldehyde + NADH + H(+) => (2S)-3-sulfopropanediol + NAD(+) `RHEA:40513`	part_of	`MetaCyc:PWY-7446`	MetaCyc:PWY-7446 Source assertion: The native pathway lists RXN-15299 as a member. Source location `/ptools-xml/Pathway[@frameid="PWY-7446"]/reaction-list/Reaction[@frameid="RXN-15299"]` MetaCyc:RXN-15299 Source assertion: The native reaction explicitly cross-references RHEA:40513. Source location `/ptools-xml/Reaction[@frameid="RXN-15299"]/dblink[dblink-db="RHEA"]/dblink-oid` RHEA:40513 Source assertion: Rhea family 40511 contains directed reaction 40513, whose physiological side assignment is used here. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/40511"]/rh:directionalReaction[@rdf:resource="http://rdf.rhea-db.org/40513"]; rdf:Description[@rdf:about="http://rdf.rhea-db.org/40513"]/rh:substrates and rh:products`
6-sulfo-beta-D-quinovose => 6-deoxy-6-sulfo-D-fructose `RHEA:40440`	provides_input_for The connected reactions share CHEBI:77133; this is material transfer, not a claim that the enzyme reactions are thermodynamically irreversible.	6-deoxy-6-sulfo-D-fructose + ATP => 6-deoxy-6-sulfo-D-fructose 1-phosphate + ADP + H(+) `RHEA:40444`	MetaCyc:PWY-7446 Source assertion: Native reaction ordering places RXN-15296 before RXN-15297. Source location `/ptools-xml/Pathway/reaction-ordering[Reaction/@frameid="RXN-15297"]/predecessor-reactions/Reaction[@frameid="RXN-15296"]` RHEA:40440 Source assertion: RHEA:40440 assigns CHEBI:77133 to its products with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40440']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40439_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40439_compound_9102']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_9102)` RHEA:40444 Source assertion: RHEA:40444 assigns CHEBI:77133 to its substrates with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40444']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40443_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40443_compound_9102']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_9102)`
6-deoxy-6-sulfo-D-fructose + ATP => 6-deoxy-6-sulfo-D-fructose 1-phosphate + ADP + H(+) `RHEA:40444`	provides_input_for The connected reactions share CHEBI:77134; this is material transfer, not a claim that the enzyme reactions are thermodynamically irreversible.	6-deoxy-6-sulfo-D-fructose 1-phosphate => (2S)-3-sulfolactaldehyde + dihydroxyacetone phosphate `RHEA:40516`	MetaCyc:PWY-7446 Source assertion: Native reaction ordering places RXN-15297 before RXN-15298. Source location `/ptools-xml/Pathway/reaction-ordering[Reaction/@frameid="RXN-15298"]/predecessor-reactions/Reaction[@frameid="RXN-15297"]` RHEA:40444 Source assertion: RHEA:40444 assigns CHEBI:77134 to its products with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40444']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40443_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40443_compound_9103']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_9103)` RHEA:40516 Source assertion: RHEA:40516 assigns CHEBI:77134 to its substrates with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40516']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40515_L']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40515_compound_9103']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_9103)`
6-deoxy-6-sulfo-D-fructose 1-phosphate => (2S)-3-sulfolactaldehyde + dihydroxyacetone phosphate `RHEA:40516`	provides_input_for The connected reactions share CHEBI:90109; this is material transfer, not a claim that the enzyme reactions are thermodynamically irreversible.	(2S)-3-sulfolactaldehyde + NADH + H(+) => (2S)-3-sulfopropanediol + NAD(+) `RHEA:40513`	MetaCyc:PWY-7446 Source assertion: Native reaction ordering places RXN-15298 before RXN-15299. Source location `/ptools-xml/Pathway/reaction-ordering[Reaction/@frameid="RXN-15299"]/predecessor-reactions/Reaction[@frameid="RXN-15298"]` RHEA:40516 Source assertion: RHEA:40516 assigns CHEBI:90109 to its products with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40516']/rh:products; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40515_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40515_compound_12045']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_12045)` RHEA:40513 Source assertion: RHEA:40513 assigns CHEBI:90109 to its substrates with coefficient 1. Source location `rdf:Description[@rdf:about='http://rdf.rhea-db.org/40513']/rh:substrates; rdf:Description[@rdf:about='http://rdf.rhea-db.org/40511_R']/rh:contains1[@rdf:resource='http://rdf.rhea-db.org/Participant_40511_compound_12045']; rh:compound/rh:chebi (http://rdf.rhea-db.org/Compound_12045)`
Sulfoquinovose isomerase `UniProtKB:P32140`	part_of Assembly composition is 6 copies; the protein membership edge does not assert independent monomer catalysis.	sulfoquinovose isomerase `MetaCyc:CPLX0-7683`	MetaCyc:CPLX0-7683 Source assertion: The native assembly has 6 copies of EG11845-MONOMER. Source location `/ptools-xml/Protein[@frameid="CPLX0-7683"]/component[Protein/@frameid="EG11845-MONOMER"]/coefficient` MetaCyc:EG11845-MONOMER Source assertion: The native protein maps to UniProt P32140 and belongs to CPLX0-7683. Source location `/ptools-xml/Protein[@frameid="EG11845-MONOMER"]/dblink[dblink-db="UNIPROT"]; component-of` UniProtKB:P32140 Source assertion: ECO:0000255; The reviewed entry annotates a homohexamer, with HAMAP and PMID18328504 evidence. Source location `/comments/5/texts`
3-sulfolactaldehyde reductase `UniProtKB:P0A9V8`	part_of Assembly composition is 4 copies; the protein membership edge does not assert independent monomer catalysis.	3-sulfolactaldehyde reductase `MetaCyc:CPLX0-7794`	MetaCyc:CPLX0-7794 Source assertion: The native assembly has 4 copies of EG11847-MONOMER. Source location `/ptools-xml/Protein[@frameid="CPLX0-7794"]/component[Protein/@frameid="EG11847-MONOMER"]/coefficient` MetaCyc:EG11847-MONOMER Source assertion: The native protein maps to UniProt P0A9V8 and belongs to CPLX0-7794. Source location `/ptools-xml/Protein[@frameid="EG11847-MONOMER"]/dblink[dblink-db="UNIPROT"]; component-of` DOI:10.1021/acscatal.9b04427 Source assertion: E. coli YihU crystallized as a dimer of dimers, and SEC-MALS confirmed a solution tetramer. The active site spans the intimate dimer interface. Source location `Accepted manuscript printed pp7-8, Results and Discussion, YihU forms a dimer of intimate homodimer pairs; Figure 4A`
sulfoquinovose isomerase `MetaCyc:CPLX0-7683`	catalyzes The selected catabolic branch is SQ to SF. SR formation is real but belongs to adjacent side-reaction chemistry; no exclusive one-product or absolute alpha-anomer inactivity is asserted.	6-sulfo-beta-D-quinovose => 6-deoxy-6-sulfo-D-fructose `RHEA:40440`	MetaCyc:CPLX0-7683 Source assertion: The native assembly catalyzes ENZRXN0-7820, linked to RXN-15296. Source location `/ptools-xml/Protein/catalyzes/Enzymatic-Reaction[@frameid="ENZRXN0-7820"]/reaction` UniProtKB:P32140 Source assertion: ECO:0000269; SQ isomerase activity and physiological left-to-right RHEA:40440 are annotated with direct evidence from PMID24463506 and PMID33791429. Source location `/comments/0; /comments/1/reaction and physiologicalReactions` PMID:33791429 Source assertion: E. coli YihS interconverts SQ, SF and SR and strongly prefers beta-SQ. Slow alpha-SQ exchange may reflect mutarotation; low direct alpha activity was not excluded. Source location `//sec[@id="sec2.1"]/p[position() >= 1 and position() <= 4]; Figure 2a-b` PMID:24463506 Source assertion: Purified recombinant b3880 converted SQ into SF in the sequential reconstitution. Source location `Printed pp115-116, Figure 3a-b; Methods, Heterologous expression and purification`
Sulfofructose kinase `UniProtKB:P32143`	enables Functional gene-product support, not monomer sufficiency. No verified external assembly instance is substituted for the source-supported dimeric enzyme.	6-deoxy-6-sulfo-D-fructose + ATP => 6-deoxy-6-sulfo-D-fructose 1-phosphate + ADP + H(+) `RHEA:40444`	UniProtKB:P32143 Source assertion: ECO:0000269; The entry assigns SF kinase activity and RHEA:40444 to YihV with direct 2014/2021 evidence. Source location `/comments/0; /comments/1/reaction and physiologicalReactions` PMID:24463506 Source assertion: Adding purified recombinant b3883 and ATP after b3880 produced SFP and ADP; phosphatase treatment converted SFP back to SF. Source location `Printed p115; Figure 3b-c; Methods, Heterologous expression and purification` PMID:33791429 Source assertion: E. coli YihV forms a dimeric structure with intersubunit active-site contacts. SEC-MALS showed more than 60% dimer and a 13% tetramer subpopulation. Source location `//sec[@id="sec2.3"]/p[3]; Figure 4b-f` DOI:10.1021/acscentsci.0c01285.s001 Source assertion: Figure S9 explicitly identifies the solution assembly experiment as EcYihV; Figure S9B reports dimer, minor tetramer and higher aggregates. Source location `Figure S9 caption, printed S10; Section 2, S29; EcYihV sequence, S30`
Sulfofructosephosphate aldolase `UniProtKB:P32141`	enables E. coli pathway function is supported by the 2014 coupled assay and genetics despite the later preparation-specific negative assay. No Salmonella kinetic constants, solution stoichiometry or Schiff-base residue experiment is transferred as direct E. coli evidence. Current (2S) chemistry supersedes older native protein-comment (2R) wording.	6-deoxy-6-sulfo-D-fructose 1-phosphate => (2S)-3-sulfolactaldehyde + dihydroxyacetone phosphate `RHEA:40516`	UniProtKB:P32141 Source assertion: ECO:0000269; The entry assigns SFP cleavage to (2S)-SLA and DHAP, with direct PMID24463506 and HAMAP MF_01912 evidence. Source location `/comments/0; /comments/1/reaction and physiologicalReactions` PMID:24463506 Source assertion: Adding recombinant b3881 to the coupled b3880/b3883 system generated SLA and DHAP; subsequent NADH/YihU addition drove conversion further. Source location `Printed p116; Figure 3c-e; Methods, Heterologous expression and purification` PMID:33791429 Source assertion: The 2021 study detected no activity with its E. coli YihT preparation under tested conditions, then used Salmonella YihT for positive direct kinetics. Source location `//sec[@id="sec2.4"]/p[1]` DOI:10.1021/acscentsci.0c01285.s001 Source assertion: Figure S19 solution tetramer data are for SeYihT. Figure S20B displays crystallographic tetramers of EcYihT and SeYihT; this does not establish an E. coli solution tetramer experimentally. Source location `Figure S19 caption, S19; Figure S20B caption, S20; EcYihT and SeYihT sequences, S30` MetaCyc:EG11846-MONOMER Source assertion: The old protein comment names (2R)-SLA. This legacy wording is not used as evidence for the selected absolute stereochemistry. Source location `/ptools-xml/Protein/comment` DOI:10.1021/acscatal.9b04427 Source assertion: Figure 1A explicitly depicts the sulfo-EMP aldehyde as S-SLA and its reduction product as S-DHPS. Source location `Accepted manuscript Figure 1A, printed p18 (PDF page20)`
3-sulfolactaldehyde reductase `MetaCyc:CPLX0-7794`	catalyzes The selected reductive flux is right-to-left relative to the Rhea master. NADH is a consumed cosubstrate, not a permanently bound prosthetic group; old relative D/L naming is not used to infer a different absolute stereoisomer.	(2S)-3-sulfolactaldehyde + NADH + H(+) => (2S)-3-sulfopropanediol + NAD(+) `RHEA:40513`	MetaCyc:CPLX0-7794 Source assertion: The native tetramer catalyzes ENZRXN0-7824 linked to RXN-15299. Source location `/ptools-xml/Protein/catalyzes/Enzymatic-Reaction[@frameid="ENZRXN0-7824"]/reaction` UniProtKB:P0A9V8 Source assertion: ECO:0000269; The entry annotates (2S)-SLA reduction by NADH, physiological right-to-left RHEA:40513, with direct PMID24463506 and DOI10.1021/acscatal.9b04427 evidence. Source location `/comments/0; /comments/1/reaction and physiologicalReactions` PMID:24463506 Source assertion: SLA reductase activity was enriched from SQ-grown MG1655 and reconstituted with recombinant b3882; NADH drove SLA to DHPS. In the reverse assay NADP did not replace NAD. Source location `Printed pp115-116; Figure 3d-e; Methods, Enzyme assays and Heterologous expression and purification` DOI:10.1021/acscatal.9b04427 Source assertion: The E. coli YihU ternary structure models S-DHPS; Figure 1A labels S-SLA to S-DHPS. Kinetics used racemic SLA with an assumed active half, described as D-SLA in the text. Source location `Accepted manuscript printed pp6,10-11 and18; Figure 1A and Figure 6A-C`
Sulfofructose kinase `UniProtKB:P32143`	has_cofactor Nucleotide-associated Mg binding and assay support are retained; no metal-removal/rescue test, exclusivity among divalent ions or fixed per-enzyme stoichiometry is claimed.	magnesium(2+) `CHEBI:18420`	PMID:33791429 Source assertion: EcYihV structures contain hydrated Mg with AMPPNP and Mg coordinated to ADP in the SF complex; kinetic assays used MgCl2. Source location `//sec[@id="sec2.3"]/p[position()=1 or position()=4 or position()=6]; Figure 4b-f` DOI:10.1021/acscentsci.0c01285.s001 Source assertion: EcYihV kinetic assays contained 5 mM MgCl2 with ATP. Source location `Section SF kinase (YihV) kinetics, printed S33-S34`
HTH-type transcriptional repressor CsqR `UniProtKB:P32144`	inhibits Transcriptional repression of pathway-enzyme genes, not direct inhibition of the catalytic reactions.	`MetaCyc:PWY-7446`	PMID:30372406 Source assertion: Genomic SELEX, gel shifts and in vivo reporters support CsqR repression of yihUTS, yihV and csqR transcription units in E. coli K-12. Source location `/resultList/result[id="30372406"]/abstractText` UniProtKB:P32144 Source assertion: ECO:0000269; CsqR represses yihUTS, yihV and its own gene and binds their regulatory DNA. Source location `/comments/0`
6-sulfo-D-quinovose(1-) `CHEBI:77132`	inhibits In vitro derepression context; no universal cellular threshold or unique anomer specificity is assigned.	HTH-type transcriptional repressor CsqR `UniProtKB:P32144`	PMID:33791429 Source assertion: SQ disrupts E. coli CsqR-DNA binding in gel-shift and AFM experiments; these assays do not resolve the SQ anomer. Source location `//sec[@id="sec2.2"]/p[position() >= 1 and position() <= 3]`
6-sulfo-D-rhamnose(1-) `CHEBI:190019`	inhibits In vitro derepression context; no universal cellular threshold or unique anomer specificity is assigned.	HTH-type transcriptional repressor CsqR `UniProtKB:P32144`	PMID:33791429 Source assertion: SR relieves CsqR-DNA complexes in gel-shift and AFM experiments, less strongly than SQ; SR did not stabilize the isolated effector-binding domain at 10 mM. Source location `//sec[@id="sec2.2"]/p[position() >= 1 and position() <= 3]`
ADP(3-) `CHEBI:456216`	inhibits Regulatory effects are conditional. Anomer-unspecified SQ/FBP and stereounspecified SLA preserve the assay scope; they are not additional core-reaction intermediates.	Sulfofructose kinase `UniProtKB:P32143`	PMID:33791429 Source assertion: The study reports ADP inhibition of EcYihV under its metabolite-addition assay conditions. Source location `//sec[@id="sec2.3"]/p[1]; Table 1 and Figure 4a` DOI:10.1021/acscentsci.0c01285.s001 Source assertion: Added metabolites were tested at 10 mM in ATP/Mg assays at pH7.5 and 30 degrees C. These are conditional enzyme experiments, not measured intracellular concentrations. Source location `SF kinase (YihV) kinetics, printed S33-S34`
6-sulfo-D-quinovose(1-) `CHEBI:77132`	activates Regulatory effects are conditional. Anomer-unspecified SQ/FBP and stereounspecified SLA preserve the assay scope; they are not additional core-reaction intermediates.	Sulfofructose kinase `UniProtKB:P32143`	PMID:33791429 Source assertion: The study reports SQ activation of EcYihV under its metabolite-addition assay conditions. Source location `//sec[@id="sec2.3"]/p[1]; Table 1 and Figure 4a` DOI:10.1021/acscentsci.0c01285.s001 Source assertion: Added metabolites were tested at 10 mM in ATP/Mg assays at pH7.5 and 30 degrees C. These are conditional enzyme experiments, not measured intracellular concentrations. Source location `SF kinase (YihV) kinetics, printed S33-S34`
3-sulfolactaldehyde(1-) `CHEBI:77135`	activates Regulatory effects are conditional. Anomer-unspecified SQ/FBP and stereounspecified SLA preserve the assay scope; they are not additional core-reaction intermediates.	Sulfofructose kinase `UniProtKB:P32143`	PMID:33791429 Source assertion: The study reports SLA activation of EcYihV under its metabolite-addition assay conditions. Source location `//sec[@id="sec2.3"]/p[1]; Table 1 and Figure 4a` DOI:10.1021/acscentsci.0c01285.s001 Source assertion: Added metabolites were tested at 10 mM in ATP/Mg assays at pH7.5 and 30 degrees C. These are conditional enzyme experiments, not measured intracellular concentrations. Source location `SF kinase (YihV) kinetics, printed S33-S34`
glycerone phosphate(2-) `CHEBI:57642`	activates Regulatory effects are conditional. Anomer-unspecified SQ/FBP and stereounspecified SLA preserve the assay scope; they are not additional core-reaction intermediates.	Sulfofructose kinase `UniProtKB:P32143`	PMID:33791429 Source assertion: The study reports DHAP activation of EcYihV under its metabolite-addition assay conditions. Source location `//sec[@id="sec2.3"]/p[1]; Table 1 and Figure 4a` DOI:10.1021/acscentsci.0c01285.s001 Source assertion: Added metabolites were tested at 10 mM in ATP/Mg assays at pH7.5 and 30 degrees C. These are conditional enzyme experiments, not measured intracellular concentrations. Source location `SF kinase (YihV) kinetics, printed S33-S34`
D-fructose 6-phosphate(2-) `CHEBI:57579`	activates Regulatory effects are conditional. Anomer-unspecified SQ/FBP and stereounspecified SLA preserve the assay scope; they are not additional core-reaction intermediates.	Sulfofructose kinase `UniProtKB:P32143`	PMID:33791429 Source assertion: The study reports F6P activation of EcYihV under its metabolite-addition assay conditions. Source location `//sec[@id="sec2.3"]/p[1]; Table 1 and Figure 4a` DOI:10.1021/acscentsci.0c01285.s001 Source assertion: Added metabolites were tested at 10 mM in ATP/Mg assays at pH7.5 and 30 degrees C. These are conditional enzyme experiments, not measured intracellular concentrations. Source location `SF kinase (YihV) kinetics, printed S33-S34`
D-fructofuranose 1,6-bisphosphate(4-) `CHEBI:49299`	activates Regulatory effects are conditional. Anomer-unspecified SQ/FBP and stereounspecified SLA preserve the assay scope; they are not additional core-reaction intermediates.	Sulfofructose kinase `UniProtKB:P32143`	PMID:33791429 Source assertion: The study reports FBP activation of EcYihV under its metabolite-addition assay conditions. Source location `//sec[@id="sec2.3"]/p[1]; Table 1 and Figure 4a` DOI:10.1021/acscentsci.0c01285.s001 Source assertion: Added metabolites were tested at 10 mM in ATP/Mg assays at pH7.5 and 30 degrees C. These are conditional enzyme experiments, not measured intracellular concentrations. Source location `SF kinase (YihV) kinetics, printed S33-S34`
phosphonatoenolpyruvate `CHEBI:58702`	activates Regulatory effects are conditional. Anomer-unspecified SQ/FBP and stereounspecified SLA preserve the assay scope; they are not additional core-reaction intermediates.	Sulfofructose kinase `UniProtKB:P32143`	PMID:33791429 Source assertion: The study reports PEP activation of EcYihV under its metabolite-addition assay conditions. Source location `//sec[@id="sec2.3"]/p[1]; Table 1 and Figure 4a` DOI:10.1021/acscentsci.0c01285.s001 Source assertion: Added metabolites were tested at 10 mM in ATP/Mg assays at pH7.5 and 30 degrees C. These are conditional enzyme experiments, not measured intracellular concentrations. Source location `SF kinase (YihV) kinetics, printed S33-S34`
citrate(3-) `CHEBI:16947`	activates Regulatory effects are conditional. Anomer-unspecified SQ/FBP and stereounspecified SLA preserve the assay scope; they are not additional core-reaction intermediates.	Sulfofructose kinase `UniProtKB:P32143`	PMID:33791429 Source assertion: The study reports citrate activation of EcYihV under its metabolite-addition assay conditions. Source location `//sec[@id="sec2.3"]/p[1]; Table 1 and Figure 4a` DOI:10.1021/acscentsci.0c01285.s001 Source assertion: Added metabolites were tested at 10 mM in ATP/Mg assays at pH7.5 and 30 degrees C. These are conditional enzyme experiments, not measured intracellular concentrations. Source location `SF kinase (YihV) kinetics, printed S33-S34`
6-deoxy-6-sulfo-D-fructofuranose(1-) `CHEBI:77133`	inhibits A substrate can also inhibit at elevated concentration; this edge is explicitly conditional and does not negate SF consumption by the kinase reaction.	Sulfofructose kinase `UniProtKB:P32143`	PMID:33791429 Source assertion: SF substrate inhibition of EcYihV depended on ATP concentration: estimated Ki about 8 mM at 1 mM ATP and 0.3 mM at 0.1 mM ATP. Source location `//sec[@id="sec2.3"]/p[1]; Table 1`

References

MetaCyc:PWY-7446 sulfoquinovose degradation I (source version: MetaCyc 22.5 public mirror; complete native XML response retrieved 2026-10-11)
MetaCyc:RXN-15296 RXN-15296 (source version: MetaCyc 22.5 public mirror; complete native XML response retrieved 2026-10-11)
MetaCyc:RXN-15297 RXN-15297 (source version: MetaCyc 22.5 public mirror; complete native XML response retrieved 2026-10-11)
MetaCyc:RXN-15298 RXN-15298 (source version: MetaCyc 22.5 public mirror; complete native XML response retrieved 2026-10-11)
MetaCyc:RXN-15299 RXN-15299 (source version: MetaCyc 22.5 public mirror; complete native XML response retrieved 2026-10-11)
MetaCyc:CPLX0-7683 sulfoquinovose isomerase (source version: MetaCyc 22.5 public mirror; complete native XML response retrieved 2026-10-11)
MetaCyc:CPLX0-7794 3-sulfolactaldehyde reductase (source version: MetaCyc 22.5 public mirror; complete native XML response retrieved 2026-10-11)
MetaCyc:EG11845-MONOMER sulfoquinovose isomerase (source version: MetaCyc 22.5 public mirror; complete native XML response retrieved 2026-10-11)
MetaCyc:EG11846-MONOMER 6-deoxy-6-sulfofructose-1-phosphate aldolase (source version: MetaCyc 22.5 public mirror; complete native XML response retrieved 2026-10-11)
MetaCyc:EG11847-MONOMER 3-sulfolactaldehyde reductase (source version: MetaCyc 22.5 public mirror; complete native XML response retrieved 2026-10-11)
UniProtKB:P32140 Sulfoquinovose isomerase (source version: UniProt 2026_03 (02-September-2026); complete original entry JSON retrieved 2026-10-11)
UniProtKB:P32141 Sulfofructosephosphate aldolase (source version: UniProt 2026_03 (02-September-2026); complete original entry JSON retrieved 2026-10-11)
UniProtKB:P0A9V8 3-sulfolactaldehyde reductase (source version: UniProt 2026_03 (02-September-2026); complete original entry JSON retrieved 2026-10-11)
UniProtKB:P32143 Sulfofructose kinase (source version: UniProt 2026_03 (02-September-2026); complete original entry JSON retrieved 2026-10-11)
UniProtKB:P32144 HTH-type transcriptional repressor CsqR (source version: UniProt 2026_03 (02-September-2026); complete original entry JSON retrieved 2026-10-11)
PMID:24463506 Sulphoglycolysis in Escherichia coli K-12 closes a gap in the biogeochemical sulphur cycle. (source version: Original 2014 Nature article with Methods and Extended Data; SHA256 covers complete 15-page institutional PDF)
PMID:33791429 Molecular Basis of Sulfosugar Selectivity in Sulfoglycolysis (source version: Original 2021 full-text JATS XML; complete response retrieved 2026-10-11)
DOI:10.1021/acscentsci.0c01285.s001 Molecular Basis of Sulfosugar Selectivity in Sulfoglycolysis: Supporting Information (source version: Original publisher-deposited supplement, linked by Figshare article 14096259 to DOI 10.1021/acscentsci.0c01285; complete PDF)
DOI:10.1021/acscatal.9b04427 Dynamic Structural Changes Accompany the Production of Dihydroxypropanesulfonate by Sulfolactaldehyde Reductase (source version: 2020 accepted author manuscript, not publisher version of record; SHA256 covers full 27-page institutional PDF including 2 cover pages)
PMID:30372406 Regulatory role of CsqR (YihW) in transcription of the genes for catabolism of the anionic sugar sulfoquinovose (SQ) in Escherichia coli K-12. (source version: Primary abstract inspected through Europe PMC; SHA256 covers the complete single-PMID API JSON response, /resultList/result/0)
RHEA:40440 Rhea 142 directed reaction 40440 and family (source version: Rhea 142, 2026-09-02; SHA256 covers complete official compressed RDF gzip)
RHEA:40444 Rhea 142 directed reaction 40444 and family (source version: Rhea 142, 2026-09-02; SHA256 covers complete official compressed RDF gzip)
RHEA:40516 Rhea 142 directed reaction 40516 and family (source version: Rhea 142, 2026-09-02; SHA256 covers complete official compressed RDF gzip)
RHEA:40513 Rhea 142 directed reaction 40513 and family (source version: Rhea 142, 2026-09-02; SHA256 covers complete official compressed RDF gzip)

Curation history

2026-10-11T08:01:55Z codex
- CREATE — Add sulfoquinovose degradation I
  Curated the full four-step sulfoquinovose-to-DHAP/DHPS route with strain, stereochemistry, regulation and assembly evidence limits. Maintained record MetaCyc:PWY-7446; creation bytes SHA256 ddf84c0b9f8ac95d1f5285f22c229770b754e4290998924f92bedbcec497d394. Original-source projections, replay and identifier decisions are recorded in research/pathway_additions/2026-10-11-next-201/. Duplicate searches included ignored and hidden files. Independent review and full integration gates are subsequent checks, not claimed by this creation event.
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2026-10-11T08:11:01Z codex
- EDIT — Correct sulforhamnose derepression evidence locator
  Expanded the original JATS section 2.2 locator to include paragraph 1 containing the gel-shift result as well as paragraphs 2–3. The source assertion and all graph nodes and edges remain unchanged. Initial finding and input bytes are preserved in the 20261011T080521Z-sulfoquinovose-initial-independent-review bundle and current cohort archive. Corrected maintained bytes SHA256 741fc68daedf7cb7000b7cc5dc94ce5c0029fe9d30ce56d392c51a2aa9ac390c. Author source replay and successor independent review have distinct scopes; final shared gates and deployment are separate checks.
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