sulfoquinovose degradation II
MetaCyc:PWY-7722
The complete five-transformation sulfo-Entner-Doudoroff route from free sulfoquinovose to pyruvate and sulfolactate in Pseudomonas putida strain SQ1 (DSM 100120). Six exact Rhea activities represent the five native members because the final SLA oxidation has alternative NAD- and NADP-dependent forms. All five SQ1 enzymes were reconstituted in vitro and induced during aerobic SQ growth. Current native reaction structures and reviewed Rhea/UniProt assignments retain S-SLA/S-SL; older native protein prose linking R-SLA is superseded, without recasting the SQ1 HPLC-MS assay as an enantiomer-resolved experiment. SQDH has direct tetramer evidence; the other functional protein/activity relations do not assert monomer sufficiency. Metal annotations preserve inference levels, and the aldolase genomic-start difference is explicit. The endpoint retains organic sulfur. SQ-glycoside hydrolysis, mutarotation, unidentified transport/regulatory mechanisms, downstream pyruvate metabolism and partner-organism sulfolactate mineralization are outside this exact native boundary. KT2440 expression datasets do not establish SQ1 applicability.
- Pathway type
- sulfo ED catabolism
- Organism scope
Pathway network
27 nodes · 48 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
- Pathway
- Solid arrow: mechanistic relation
- Dashed arrow: membership, location or cofactor relation
Components and activities
| Node | Kind or role | Source direction |
|---|---|---|
Pseudomonas putidaNCBITaxon:303 | taxon | |
pyruvateCHEBI:15361 | small molecule | |
waterCHEBI:15377 | small molecule | |
hydronCHEBI:15378 | small molecule | |
NAD(1-)CHEBI:57540 | small molecule | |
NADPH(4-)CHEBI:57783 | small molecule | |
NADH(2-)CHEBI:57945 | small molecule | |
NADP(3-)CHEBI:58349 | small molecule | |
(S)-3-sulfonatolactate(2-)CHEBI:61289 | small molecule | |
6-sulfo-D-quinovose(1-)CHEBI:77132 | small molecule | |
6-deoxy-6-sulfoglucono-1,5-lactone(1-)CHEBI:88091 | small molecule | |
6-deoxy-6-sulfo-D-gluconate(2-)CHEBI:88093 | small molecule | |
2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate(2-)CHEBI:88094 | small molecule | |
L-3-sulfolactaldehyde(1-)CHEBI:90109 | small molecule | |
divalent metal cationCHEBI:60240 | cofactor | |
tetra-mu3-sulfido-tetraironCHEBI:49883 | cofactor | |
Sulfoquinovose 1-dehydrogenaseUniProtKB:P0DOV5 | protein | |
6-deoxy-6-sulfogluconolactonaseUniProtKB:P0DOV6 | protein | |
6-deoxy-6-sulfo-D-gluconate dehydrataseUniProtKB:P0DOV7 | protein | |
2-dehydro-3,6-dideoxy-6-sulfogluconate aldolaseUniProtKB:P0DOV8 | protein | |
3-sulfolactaldehyde dehydrogenaseUniProtKB:P0DOV9 | protein | |
6-sulfo-D-quinovose + NAD(+) => 6-deoxy-6-sulfo-D-glucono-1,5-lactone + NADH + H(+)RHEA:47897 | molecular activity | left to right |
6-deoxy-6-sulfo-D-glucono-1,5-lactone + H2O => 6-deoxy-6-sulfo-D-gluconate + H(+)RHEA:47909 | molecular activity | left to right |
6-deoxy-6-sulfo-D-gluconate => 2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate + H2ORHEA:47913 | molecular activity | left to right |
2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate => (2S)-3-sulfolactaldehyde + pyruvateRHEA:47925 | molecular activity | left to right |
(2S)-3-sulfolactaldehyde + NADP(+) + H2O => (2S)-3-sulfolactate + NADPH + 2 H(+)RHEA:47929 | molecular activity | left to right |
(2S)-3-sulfolactaldehyde + NAD(+) + H2O => (2S)-3-sulfolactate + NADH + 2 H(+)RHEA:47933 | molecular activity | left to right |
Mechanistic edges
| Subject | Predicate and description | Object | Evidence |
|---|---|---|---|
6-sulfo-D-quinovose(1-)CHEBI:77132 | consumes | 6-sulfo-D-quinovose + NAD(+) => 6-deoxy-6-sulfo-D-glucono-1,5-lactone + NADH + H(+)RHEA:47897 |
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NAD(1-)CHEBI:57540 | consumes | 6-sulfo-D-quinovose + NAD(+) => 6-deoxy-6-sulfo-D-glucono-1,5-lactone + NADH + H(+)RHEA:47897 |
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6-sulfo-D-quinovose + NAD(+) => 6-deoxy-6-sulfo-D-glucono-1,5-lactone + NADH + H(+)RHEA:47897 | produces | 6-deoxy-6-sulfoglucono-1,5-lactone(1-)CHEBI:88091 |
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6-sulfo-D-quinovose + NAD(+) => 6-deoxy-6-sulfo-D-glucono-1,5-lactone + NADH + H(+)RHEA:47897 | produces | NADH(2-)CHEBI:57945 |
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6-sulfo-D-quinovose + NAD(+) => 6-deoxy-6-sulfo-D-glucono-1,5-lactone + NADH + H(+)RHEA:47897 | produces | hydronCHEBI:15378 |
|
6-deoxy-6-sulfoglucono-1,5-lactone(1-)CHEBI:88091 | consumes | 6-deoxy-6-sulfo-D-glucono-1,5-lactone + H2O => 6-deoxy-6-sulfo-D-gluconate + H(+)RHEA:47909 |
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waterCHEBI:15377 | consumes | 6-deoxy-6-sulfo-D-glucono-1,5-lactone + H2O => 6-deoxy-6-sulfo-D-gluconate + H(+)RHEA:47909 |
|
6-deoxy-6-sulfo-D-glucono-1,5-lactone + H2O => 6-deoxy-6-sulfo-D-gluconate + H(+)RHEA:47909 | produces | 6-deoxy-6-sulfo-D-gluconate(2-)CHEBI:88093 |
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6-deoxy-6-sulfo-D-glucono-1,5-lactone + H2O => 6-deoxy-6-sulfo-D-gluconate + H(+)RHEA:47909 | produces | hydronCHEBI:15378 |
|
6-deoxy-6-sulfo-D-gluconate(2-)CHEBI:88093 | consumes | 6-deoxy-6-sulfo-D-gluconate => 2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate + H2ORHEA:47913 |
|
6-deoxy-6-sulfo-D-gluconate => 2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate + H2ORHEA:47913 | produces | 2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate(2-)CHEBI:88094 |
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6-deoxy-6-sulfo-D-gluconate => 2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate + H2ORHEA:47913 | produces | waterCHEBI:15377 |
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2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate(2-)CHEBI:88094 | consumes | 2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate => (2S)-3-sulfolactaldehyde + pyruvateRHEA:47925 |
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2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate => (2S)-3-sulfolactaldehyde + pyruvateRHEA:47925 | produces | L-3-sulfolactaldehyde(1-)CHEBI:90109 |
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2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate => (2S)-3-sulfolactaldehyde + pyruvateRHEA:47925 | produces | pyruvateCHEBI:15361 |
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L-3-sulfolactaldehyde(1-)CHEBI:90109 | consumes | (2S)-3-sulfolactaldehyde + NADP(+) + H2O => (2S)-3-sulfolactate + NADPH + 2 H(+)RHEA:47929 |
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NADP(3-)CHEBI:58349 | consumes | (2S)-3-sulfolactaldehyde + NADP(+) + H2O => (2S)-3-sulfolactate + NADPH + 2 H(+)RHEA:47929 |
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waterCHEBI:15377 | consumes | (2S)-3-sulfolactaldehyde + NADP(+) + H2O => (2S)-3-sulfolactate + NADPH + 2 H(+)RHEA:47929 |
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(2S)-3-sulfolactaldehyde + NADP(+) + H2O => (2S)-3-sulfolactate + NADPH + 2 H(+)RHEA:47929 | produces | (S)-3-sulfonatolactate(2-)CHEBI:61289 |
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(2S)-3-sulfolactaldehyde + NADP(+) + H2O => (2S)-3-sulfolactate + NADPH + 2 H(+)RHEA:47929 | produces | NADPH(4-)CHEBI:57783 |
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(2S)-3-sulfolactaldehyde + NADP(+) + H2O => (2S)-3-sulfolactate + NADPH + 2 H(+)RHEA:47929 | produces | hydronCHEBI:15378 |
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L-3-sulfolactaldehyde(1-)CHEBI:90109 | consumes | (2S)-3-sulfolactaldehyde + NAD(+) + H2O => (2S)-3-sulfolactate + NADH + 2 H(+)RHEA:47933 |
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NAD(1-)CHEBI:57540 | consumes | (2S)-3-sulfolactaldehyde + NAD(+) + H2O => (2S)-3-sulfolactate + NADH + 2 H(+)RHEA:47933 |
|
waterCHEBI:15377 | consumes | (2S)-3-sulfolactaldehyde + NAD(+) + H2O => (2S)-3-sulfolactate + NADH + 2 H(+)RHEA:47933 |
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(2S)-3-sulfolactaldehyde + NAD(+) + H2O => (2S)-3-sulfolactate + NADH + 2 H(+)RHEA:47933 | produces | (S)-3-sulfonatolactate(2-)CHEBI:61289 |
|
(2S)-3-sulfolactaldehyde + NAD(+) + H2O => (2S)-3-sulfolactate + NADH + 2 H(+)RHEA:47933 | produces | NADH(2-)CHEBI:57945 |
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(2S)-3-sulfolactaldehyde + NAD(+) + H2O => (2S)-3-sulfolactate + NADH + 2 H(+)RHEA:47933 | produces | hydronCHEBI:15378 |
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6-sulfo-D-quinovose + NAD(+) => 6-deoxy-6-sulfo-D-glucono-1,5-lactone + NADH + H(+)RHEA:47897 | part_of | MetaCyc:PWY-7722 |
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6-deoxy-6-sulfo-D-glucono-1,5-lactone + H2O => 6-deoxy-6-sulfo-D-gluconate + H(+)RHEA:47909 | part_of | MetaCyc:PWY-7722 |
|
6-deoxy-6-sulfo-D-gluconate => 2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate + H2ORHEA:47913 | part_of | MetaCyc:PWY-7722 |
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2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate => (2S)-3-sulfolactaldehyde + pyruvateRHEA:47925 | part_of | MetaCyc:PWY-7722 |
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(2S)-3-sulfolactaldehyde + NADP(+) + H2O => (2S)-3-sulfolactate + NADPH + 2 H(+)RHEA:47929 | part_of | MetaCyc:PWY-7722 |
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(2S)-3-sulfolactaldehyde + NAD(+) + H2O => (2S)-3-sulfolactate + NADH + 2 H(+)RHEA:47933 | part_of | MetaCyc:PWY-7722 |
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Sulfoquinovose 1-dehydrogenaseUniProtKB:P0DOV5 | enables Functional protein/activity relation, not monomer sufficiency. The 2025 recombinant SQ1 enzyme is tetrameric in solution and crystals. Minor NADP activity and trace G6P activity are assay-dependent side activities outside the native NAD-dependent step. | 6-sulfo-D-quinovose + NAD(+) => 6-deoxy-6-sulfo-D-glucono-1,5-lactone + NADH + H(+)RHEA:47897 |
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6-deoxy-6-sulfogluconolactonaseUniProtKB:P0DOV6 | enables Functional activity assignment. Divalent-metal binding below is a reviewed similarity inference, not an SQ1 metal-titration measurement. No physical monomer or oligomer state is inferred from the native MONOMER frame name. | 6-deoxy-6-sulfo-D-glucono-1,5-lactone + H2O => 6-deoxy-6-sulfo-D-gluconate + H(+)RHEA:47909 |
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6-deoxy-6-sulfo-D-gluconate dehydrataseUniProtKB:P0DOV7 | enables Functional activity assignment; current reviewed homodimer and one [4Fe-4S] cluster annotations are inferred by similarity to Q1JUQ1, not directly measured SQ1 assembly or cluster occupancy. | 6-deoxy-6-sulfo-D-gluconate => 2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate + H2ORHEA:47913 |
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2-dehydro-3,6-dideoxy-6-sulfogluconate aldolaseUniProtKB:P0DOV8 | enables Functional assignment of the reviewed SQ1 gene product. The 2015 cloned IMG00100 gene uses an upstream start relative to the current GenBank annotation at the same locus. Native prose has stale R-SLA/family annotations; current native reaction and Rhea/UniProt chemistry select S-SLA. No monomer sufficiency is asserted. | 2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate => (2S)-3-sulfolactaldehyde + pyruvateRHEA:47925 |
|
3-sulfolactaldehyde dehydrogenaseUniProtKB:P0DOV9 | enables Alternative NADP- and NAD-dependent final activity, not sequential steps. Current Rhea/UniProt and native reaction sides select S-SLA/S-SL; stale native protein prose links R-SLA. The SQ1 HPLC-MS assay was not an independent enantiomer-resolved characterization. | (2S)-3-sulfolactaldehyde + NADP(+) + H2O => (2S)-3-sulfolactate + NADPH + 2 H(+)RHEA:47929 |
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3-sulfolactaldehyde dehydrogenaseUniProtKB:P0DOV9 | enables Alternative NADP- and NAD-dependent final activity, not sequential steps. Current Rhea/UniProt and native reaction sides select S-SLA/S-SL; stale native protein prose links R-SLA. The SQ1 HPLC-MS assay was not an independent enantiomer-resolved characterization. | (2S)-3-sulfolactaldehyde + NAD(+) + H2O => (2S)-3-sulfolactate + NADH + 2 H(+)RHEA:47933 |
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6-deoxy-6-sulfogluconolactonaseUniProtKB:P0DOV6 | has_cofactor | divalent metal cationCHEBI:60240 |
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6-deoxy-6-sulfo-D-gluconate dehydrataseUniProtKB:P0DOV7 | has_cofactor | tetra-mu3-sulfido-tetraironCHEBI:49883 |
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2-dehydro-3,6-dideoxy-6-sulfogluconate aldolaseUniProtKB:P0DOV8 | has_cofactor | divalent metal cationCHEBI:60240 |
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6-sulfo-D-quinovose + NAD(+) => 6-deoxy-6-sulfo-D-glucono-1,5-lactone + NADH + H(+)RHEA:47897 | provides_input_for | 6-deoxy-6-sulfo-D-glucono-1,5-lactone + H2O => 6-deoxy-6-sulfo-D-gluconate + H(+)RHEA:47909 |
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6-deoxy-6-sulfo-D-glucono-1,5-lactone + H2O => 6-deoxy-6-sulfo-D-gluconate + H(+)RHEA:47909 | provides_input_for | 6-deoxy-6-sulfo-D-gluconate => 2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate + H2ORHEA:47913 |
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6-deoxy-6-sulfo-D-gluconate => 2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate + H2ORHEA:47913 | provides_input_for | 2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate => (2S)-3-sulfolactaldehyde + pyruvateRHEA:47925 |
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2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate => (2S)-3-sulfolactaldehyde + pyruvateRHEA:47925 | provides_input_for | (2S)-3-sulfolactaldehyde + NADP(+) + H2O => (2S)-3-sulfolactate + NADPH + 2 H(+)RHEA:47929 |
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2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate => (2S)-3-sulfolactaldehyde + pyruvateRHEA:47925 | provides_input_for | (2S)-3-sulfolactaldehyde + NAD(+) + H2O => (2S)-3-sulfolactate + NADH + 2 H(+)RHEA:47933 |
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NADH(2-)CHEBI:57945 | inhibits Conditional recombinant-enzyme inhibition; no cellular regulation or new transcription-factor identity is inferred. | Sulfoquinovose 1-dehydrogenaseUniProtKB:P0DOV5 |
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References
MetaCyc:PWY-7722sulfoquinovose degradation II (source version: MetaCyc 22.5 public mirror; full original XML retrieved 2026-10-11)MetaCyc:RXN-17096RXN-17096 (source version: MetaCyc 22.5 public mirror; full original XML retrieved 2026-10-11)MetaCyc:RXN-17095RXN-17095 (source version: MetaCyc 22.5 public mirror; full original XML retrieved 2026-10-11)MetaCyc:RXN-17097RXN-17097 (source version: MetaCyc 22.5 public mirror; full original XML retrieved 2026-10-11)MetaCyc:RXN-17098RXN-17098 (source version: MetaCyc 22.5 public mirror; full original XML retrieved 2026-10-11)MetaCyc:RXN-17101RXN-17101 (source version: MetaCyc 22.5 public mirror; full original XML retrieved 2026-10-11)UniProtKB:P0DOV5Sulfoquinovose 1-dehydrogenase (source version: Complete reviewed entry JSON retrieved 2026-10-11; entry version 25, sequence version 1; last annotation 2026-09-02)UniProtKB:P0DOV66-deoxy-6-sulfogluconolactonase (source version: Complete reviewed entry JSON retrieved 2026-10-11; entry version 21, sequence version 1; last annotation 2026-06-10)UniProtKB:P0DOV76-deoxy-6-sulfo-D-gluconate dehydratase (source version: Complete reviewed entry JSON retrieved 2026-10-11; entry version 26, sequence version 1; last annotation 2026-09-02)UniProtKB:P0DOV82-dehydro-3,6-dideoxy-6-sulfogluconate aldolase (source version: Complete reviewed entry JSON retrieved 2026-10-11; entry version 21, sequence version 1; last annotation 2026-09-02)UniProtKB:P0DOV93-sulfolactaldehyde dehydrogenase (source version: Complete reviewed entry JSON retrieved 2026-10-11; entry version 25, sequence version 1; last annotation 2026-09-02)PMID:26195800Entner-Doudoroff pathway for sulfoquinovose degradation in Pseudomonas putida SQ1. (source version: Original 2015 full primary article including SI methods, tables and figure legends in publisher-deposited PMC HTML; retrieved 2026-10-11)PMID:39840830Structure, kinetics, and mechanism of Pseudomonas putida sulfoquinovose dehydrogenase, the first enzyme in the sulfoglycolytic Entner-Doudoroff pathway. (source version: Original 2025 full primary PMC HTML, including complete construct sequences and Methods; retrieved 2026-10-11)PMID:37886098Molecular basis of sulfolactate synthesis by sulfolactaldehyde dehydrogenase from Rhizobium leguminosarum. (source version: Original 2023 primary full PMC HTML; other-organism scope, inspected as a transfer limit; retrieved 2026-10-11)PMID:41830472Metal-Dependent 2-Keto-3,6-dideoxy-6-sulfo-gluconate (KDSG) Aldolase: Decoding the Key C-C Bond Cleaving Step in Bacterial Sulfoglycolysis. (source version: Original 2026 primary abstract only, through Europe PMC single-PMID core JSON; full article/SI unavailable and deposited structure API requests returned404; retrieved 2026-10-11)NCBIProtein:KHL76360.1SQ1 PpSQ1_00455 protein and genomic CDS annotation (source version: Original accession-version GBSet/GBSeq XML retrieved 2026-10-11; sequence and strain/CDS identity only, automated original functional name not imported)RHEA:478976-sulfo-D-quinovose + NAD(+) => 6-deoxy-6-sulfo-D-glucono-1,5-lactone + NADH + H(+) (source version: Rhea 142, 2026-09-02; digest covers full original compressed RDF gzip)RHEA:479096-deoxy-6-sulfo-D-glucono-1,5-lactone + H2O => 6-deoxy-6-sulfo-D-gluconate + H(+) (source version: Rhea 142, 2026-09-02; digest covers full original compressed RDF gzip)RHEA:479136-deoxy-6-sulfo-D-gluconate => 2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate + H2O (source version: Rhea 142, 2026-09-02; digest covers full original compressed RDF gzip)RHEA:479252-dehydro-3,6-dideoxy-6-sulfo-D-gluconate => (2S)-3-sulfolactaldehyde + pyruvate (source version: Rhea 142, 2026-09-02; digest covers full original compressed RDF gzip)RHEA:47929(2S)-3-sulfolactaldehyde + NADP(+) + H2O => (2S)-3-sulfolactate + NADPH + 2 H(+) (source version: Rhea 142, 2026-09-02; digest covers full original compressed RDF gzip)RHEA:47933(2S)-3-sulfolactaldehyde + NAD(+) + H2O => (2S)-3-sulfolactate + NADH + 2 H(+) (source version: Rhea 142, 2026-09-02; digest covers full original compressed RDF gzip)
Curation history
- codex
- CREATE — Add sulfoquinovose degradation II
Curated all five native sulfo-ED steps with six cofactor-specific Rhea activities, exact SQ1 protein/construct scope and chemical stereochemistry qualifications. Maintained record MetaCyc:PWY-7722; creation bytes SHA256 20a95c209243399b88a90fbecb0d8d310ebfb3094fc6ee4487352fdc2185c596. Original-source projections, replay and identifier decisions are in research/pathway_additions/2026-10-11-next-203/. Duplicate searches included ignored and hidden files. Independent review and full integration gates are separate subsequent checks, not claimed by this creation event.
- CREATE — Add sulfoquinovose degradation II