methylthiopropanoate degradation I (cleavage)

MetaCyc:PWY-6048

The complete three-reaction MetaCyc route converts 3-(methylthio)propionate (MMPA) to methanethiol, acetaldehyde and carbon dioxide in Ruegeria pomeroyi DSS-3. DmdB2 activates MMPA with ATP and CoA; DmdC1 oxidizes the thioester to trans-methylthioacryloyl-CoA; DmdD-dependent hydration and hydrolysis complete cleavage. The terminal net reaction includes spontaneous methanethiol elimination and expected spontaneous decarboxylation. Generic electron-transfer flavoprotein redox states retain the MetaCyc/Rhea database convention: the physiological partner remains unidentified, and direct DmdC1 assays used artificial acceptors. DmdB2 and DmdC1 are experimentally supported homodimers and DmdD a homohexamer; protein enables edges represent their functional roles without asserting monomer sufficiency. DmdB magnesium dependence and DmdC inferred FAD cofactor are distinguished from the whole carrier. DMSP-dependent DmdB2 inhibition and its conditional relief by MMPA are supported in vitro. The route starts after DMSP demethylation and stops before acetaldehyde oxidation or methanethiol assimilation; it does not assert these adjacent pathways or flux in every environmental condition.

Pathway type
organosulfur catabolism
Organism scope

Read the source YAML

Pathway network

24 nodes · 29 asserted directed edges

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

Pathway network: methylthiopropanoate degradation I (cleavage) 24 nodes · 29 asserted directed edges. Every arrow links to its evidence table row; nodes link to their component details. Isolated declared components are retained. CHEBI:49016 — consumes → RHEA:43053; Evidence: RHEA:43053consumes CHEBI:30616 — consumes → RHEA:43053; Evidence: RHEA:43053consumes CHEBI:57287 — consumes → RHEA:43053; Evidence: RHEA:43053consumes RHEA:43053 — produces → CHEBI:82815; Evidence: RHEA:43053produces RHEA:43053 — produces → CHEBI:456215; Evidence: RHEA:43053produces RHEA:43053 — produces → CHEBI:33019; Evidence: RHEA:43053produces CHEBI:82815 — consumes → RHEA:52613; Evidence: RHEA:52613consumes RHEA-COMP:10685 — consumes → RHEA:52613; This whole generic carrier state is the curated database acceptor-class convention, not a specific DSS-3 protein. Primary assays establish MMPA-CoA oxidation with artificial acceptors; the physiological flavoprotein partner remains unresolved. Carrier-bound FAD is not a substitute node for the carrier.; Evidence: RHEA:52613, MetaCyc:RXN-12572, UniProtKB:Q5LLW7consumes CHEBI:15378 — consumes → RHEA:52613; Evidence: RHEA:52613consumes RHEA:52613 — produces → CHEBI:84994; Evidence: RHEA:52613produces RHEA:52613 — produces → RHEA-COMP:10686; This whole generic carrier state is the curated database acceptor-class convention, not a specific DSS-3 protein. Primary assays establish MMPA-CoA oxidation with artificial acceptors; the physiological flavoprotein partner remains unresolved. Carrier-bound FAD is not a substitute node for the carrier.; Evidence: RHEA:52613, MetaCyc:RXN-12572, UniProtKB:Q5LLW7produces CHEBI:84994 — consumes → RHEA:45145; This is a side of the single terminal net reaction. DmdD catalyzes hydration and hydrolysis; methanethiol elimination and subsequent decarboxylation are spontaneous or expected spontaneous steps within that net conversion.; Evidence: RHEA:45145consumes CHEBI:15377 — consumes → RHEA:45145; This is a side of the single terminal net reaction. DmdD catalyzes hydration and hydrolysis; methanethiol elimination and subsequent decarboxylation are spontaneous or expected spontaneous steps within that net conversion.; Evidence: RHEA:45145consumes RHEA:45145 — produces → CHEBI:16007; This is a side of the single terminal net reaction. DmdD catalyzes hydration and hydrolysis; methanethiol elimination and subsequent decarboxylation are spontaneous or expected spontaneous steps within that net conversion.; Evidence: RHEA:45145produces RHEA:45145 — produces → CHEBI:15343; This is a side of the single terminal net reaction. DmdD catalyzes hydration and hydrolysis; methanethiol elimination and subsequent decarboxylation are spontaneous or expected spontaneous steps within that net conversion.; Evidence: RHEA:45145produces RHEA:45145 — produces → CHEBI:16526; This is a side of the single terminal net reaction. DmdD catalyzes hydration and hydrolysis; methanethiol elimination and subsequent decarboxylation are spontaneous or expected spontaneous steps within that net conversion.; Evidence: RHEA:45145produces RHEA:45145 — produces → CHEBI:57287; This is a side of the single terminal net reaction. DmdD catalyzes hydration and hydrolysis; methanethiol elimination and subsequent decarboxylation are spontaneous or expected spontaneous steps within that net conversion.; Evidence: RHEA:45145produces UniProtKB:Q5LRT0 — enables → RHEA:43053; DmdB2 (SPO2045) enables MMPA activation as a functional gene-product role. Purified recombinant DSS-3 enzyme was a homodimer by gel filtration; this edge does not assert monomer sufficiency. DmdB1 is a separately characterized isozyme outside this native catalyst projection.; Evidence: MetaCyc:ENZRXN-19462, MetaCyc:MONOMER-16783, UniProtKB:Q5LRT0, PMID:21562561, PMID:24443527, UniProtKB:Q5LRT0enables UniProtKB:Q5LLW7 — enables → RHEA:52613; DmdC1 (SPO3804) enables the oxidation in its experimentally supported homodimeric context. Current Rhea specifies a generic ETF acceptor class; this role does not claim that the exact carrier was tested. The 2022 study used recombinant DSS-3 enzyme and artificial electron acceptors.; Evidence: MetaCyc:ENZRXN-19463, MetaCyc:MONOMER-16784, UniProtKB:Q5LLW7, PMID:21562561, PMID:34818101, UniProtKB:Q5LLW7enables UniProtKB:Q5LLW6 — enables → RHEA:45145; DmdD (SPO3805) enables the observed net cleavage as a homohexamer (dimer of trimers), not an isolated monomer. The net equation includes spontaneous methanethiol elimination after hydration and expected spontaneous malonate-semialdehyde decarboxylation. It is not duplicated by component reaction nodes.; Evidence: MetaCyc:ENZRXN-19464, MetaCyc:MONOMER-16785, UniProtKB:Q5LLW6, PMID:21562561, PMID:23704947, UniProtKB:Q5LLW6enables UniProtKB:Q5LRT0 — has_cofactor → CHEBI:18420; Magnesium dependence is reported for ligase activity. The sources do not establish an independent protein-binding stoichiometry or separate MgATP and free-ion mechanisms.; Evidence: UniProtKB:Q5LRT0, PMID:24443527has cofactor UniProtKB:Q5LLW7 — has_cofactor → CHEBI:57692; The enzyme-bound FAD assignment is similarity-scoped and distinct from the generic whole ETF substrate. Free FAD did not act as the sole electron acceptor in the DSS-3 DmdC1 assay; cross-species DmdC activity with free FAD is not transferred here.; Evidence: UniProtKB:Q5LLW7has cofactor CHEBI:16457 — inhibits → UniProtKB:Q5LRT0; The physiological regulatory model is proposed from measured in vitro inhibition and cellular DMSP context; no direct regulator binding or universal in vivo flux assertion is made.; Evidence: PMID:24443527, UniProtKB:Q5LRT0inhibits CHEBI:49016 — activates → UniProtKB:Q5LRT0; Conditional relief of DMSP inhibition, not unqualified stimulation in the absence of inhibitor. MMPA is also the substrate of the activation reaction.; Evidence: PMID:24443527, UniProtKB:Q5LRT0activates RHEA:43053 — part_of → MetaCyc:PWY-6048; Evidence: MetaCyc:PWY-6048, MetaCyc:RXN-12571, RHEA:43053, MetaCyc:RXN-12571part of RHEA:52613 — part_of → MetaCyc:PWY-6048; Evidence: MetaCyc:PWY-6048, MetaCyc:RXN-12572, RHEA:52613, UniProtKB:Q5LLW7part of RHEA:45145 — part_of → MetaCyc:PWY-6048; The selected terminal Rhea net includes all four native component transformations and is represented once.; Evidence: MetaCyc:PWY-6048, MetaCyc:RXN-12573, RHEA:45145, MetaCyc:RXN-12573part of RHEA:43053 — provides_input_for → RHEA:52613; The shared chemical is CHEBI:82815; this is material continuity, not an assumed regulatory relation.; Evidence: MetaCyc:PWY-6048, RHEA:43053, RHEA:52613provides input for RHEA:52613 — provides_input_for → RHEA:45145; The shared chemical is CHEBI:84994; this is material continuity, not an assumed regulatory relation.; Evidence: MetaCyc:PWY-6048, RHEA:52613, RHEA:45145provides input for 3-(methylthio)propionate; CHEBI:49016; Declared type: small_molecule small molecule 3-(methylthio)propionate ATP(4-); CHEBI:30616; Declared type: small_molecule small molecule ATP(4-) coenzyme A(4-); CHEBI:57287; Declared type: small_molecule small molecule coenzyme A(4-) 3-(methylthio)propanoyl-CoA(4-); CHEBI:82815; Declared type: small_molecule small molecule 3-(methylthio)propanoyl- CoA(4-) adenosine 5'-monophosphate(2-); CHEBI:456215; Declared type: small_molecule small molecule adenosine 5'-monophosphate(2-) diphosphate(3-); CHEBI:33019; Declared type: small_molecule small molecule diphosphate(3-) oxidized [electron-transfer flavoprotein]; RHEA-COMP:10685; Declared type: protein protein oxidized [electron-transfer flavoprotein] hydron; CHEBI:15378; Declared type: small_molecule small molecule hydron 3-(methylthio)acryloyl-CoA(4-); CHEBI:84994; Declared type: small_molecule small molecule 3-(methylthio)acryloyl- CoA(4-) reduced [electron-transfer flavoprotein]; RHEA-COMP:10686; Declared type: protein protein reduced [electron-transfer flavoprotein] water; CHEBI:15377; Declared type: small_molecule small molecule water methanethiol; CHEBI:16007; Declared type: small_molecule small molecule methanethiol acetaldehyde; CHEBI:15343; Declared type: small_molecule small molecule acetaldehyde carbon dioxide; CHEBI:16526; Declared type: small_molecule small molecule carbon dioxide magnesium(2+); CHEBI:18420; Declared type: cofactor cofactor magnesium(2+) FAD(3-); CHEBI:57692; Declared type: cofactor cofactor FAD(3-) S,S-dimethyl-beta-propiothetin; CHEBI:16457; Declared type: small_molecule small molecule S,S-dimethyl-beta- propiothetin 3-methylmercaptopropionyl-CoA ligase; UniProtKB:Q5LRT0; Declared type: protein protein 3-methylmercaptopropionyl- CoA ligase 3-methylmercaptopropionyl-CoA dehydrogenase; UniProtKB:Q5LLW7; Declared type: protein protein 3-methylmercaptopropionyl- CoA dehydrogenase Methylthioacryloyl-CoA hydratase; UniProtKB:Q5LLW6; Declared type: protein protein Methylthioacryloyl-CoA hydratase 3-(methylsulfanyl)propanoate + ATP + CoA => 3-(methylsulfanyl)propanoyl-CoA + AMP + diphosphate; RHEA:43053; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity 3-(methylsulfanyl)propanoate + ATP + CoA => 3-(methylsulfanyl)propanoyl- CoA + AMP + diphosphate 3-(methylsulfanyl)propanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) => 3-(methylsulfanyl)acryloyl-CoA + reduced [electron-transfer flavoprotein]; RHEA:52613; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity 3-(methylsulfanyl)propanoyl- CoA + oxidized [electron- transfer flavoprotein] + H(+) => 3-(methylsulfanyl)acryloyl- CoA + reduced [electron- transfer flavoprotein] 3-(methylsulfanyl)acryloyl-CoA + 2 H2O => methanethiol + acetaldehyde + CO2 + CoA; RHEA:45145; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity 3-(methylsulfanyl)acryloyl- CoA + 2 H2O => methanethiol + acetaldehyde + CO2 + CoA methylthiopropanoate degradation I (cleavage); MetaCyc:PWY-6048; Declared type: pathway pathway methylthiopropanoate degradation I (cleavage)

Components and activities

Declared biological components and source reaction directions
NodeKind or roleSource direction
Ruegeria pomeroyi DSS-3
NCBITaxon:246200
taxon
3-(methylthio)propionate
CHEBI:49016
small molecule
ATP(4-)
CHEBI:30616
small molecule
coenzyme A(4-)
CHEBI:57287
small molecule
3-(methylthio)propanoyl-CoA(4-)
CHEBI:82815
small molecule
adenosine 5'-monophosphate(2-)
CHEBI:456215
small molecule
diphosphate(3-)
CHEBI:33019
small molecule
oxidized [electron-transfer flavoprotein]
RHEA-COMP:10685
protein
hydron
CHEBI:15378
small molecule
3-(methylthio)acryloyl-CoA(4-)
CHEBI:84994
small molecule
reduced [electron-transfer flavoprotein]
RHEA-COMP:10686
protein
water
CHEBI:15377
small molecule
methanethiol
CHEBI:16007
small molecule
acetaldehyde
CHEBI:15343
small molecule
carbon dioxide
CHEBI:16526
small molecule
magnesium(2+)
CHEBI:18420
cofactor
FAD(3-)
CHEBI:57692
cofactor
S,S-dimethyl-beta-propiothetin
CHEBI:16457
small molecule
3-methylmercaptopropionyl-CoA ligase
UniProtKB:Q5LRT0
protein
3-methylmercaptopropionyl-CoA dehydrogenase
UniProtKB:Q5LLW7
protein
Methylthioacryloyl-CoA hydratase
UniProtKB:Q5LLW6
protein
3-(methylsulfanyl)propanoate + ATP + CoA => 3-(methylsulfanyl)propanoyl-CoA + AMP + diphosphate
RHEA:43053
molecular activityleft to right
3-(methylsulfanyl)propanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) => 3-(methylsulfanyl)acryloyl-CoA + reduced [electron-transfer flavoprotein]
RHEA:52613
molecular activityleft to right
3-(methylsulfanyl)acryloyl-CoA + 2 H2O => methanethiol + acetaldehyde + CO2 + CoA
RHEA:45145
molecular activityleft to right

Mechanistic edges

Mechanistic edges and their cited evidence
SubjectPredicate and descriptionObjectEvidence
3-(methylthio)propionate
CHEBI:49016
consumes

3-(methylsulfanyl)propanoate + ATP + CoA => 3-(methylsulfanyl)propanoyl-CoA + AMP + diphosphate
RHEA:43053
  • RHEA:43053

    Source assertion: Rhea places CHEBI:49016 on the substrates side of directed RHEA:43053, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/43053/rh:substrates; http://rdf.rhea-db.org/43052_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_43052_compound_6054/rh:compound -> http://rdf.rhea-db.org/Compound_6054/rh:chebi
ATP(4-)
CHEBI:30616
consumes

3-(methylsulfanyl)propanoate + ATP + CoA => 3-(methylsulfanyl)propanoyl-CoA + AMP + diphosphate
RHEA:43053
  • RHEA:43053

    Source assertion: Rhea places CHEBI:30616 on the substrates side of directed RHEA:43053, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/43053/rh:substrates; http://rdf.rhea-db.org/43052_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_43052_compound_6372/rh:compound -> http://rdf.rhea-db.org/Compound_6372/rh:chebi
coenzyme A(4-)
CHEBI:57287
consumes

3-(methylsulfanyl)propanoate + ATP + CoA => 3-(methylsulfanyl)propanoyl-CoA + AMP + diphosphate
RHEA:43053
  • RHEA:43053

    Source assertion: Rhea places CHEBI:57287 on the substrates side of directed RHEA:43053, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/43053/rh:substrates; http://rdf.rhea-db.org/43052_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_43052_compound_1264/rh:compound -> http://rdf.rhea-db.org/Compound_1264/rh:chebi
3-(methylsulfanyl)propanoate + ATP + CoA => 3-(methylsulfanyl)propanoyl-CoA + AMP + diphosphate
RHEA:43053
produces

3-(methylthio)propanoyl-CoA(4-)
CHEBI:82815
  • RHEA:43053

    Source assertion: Rhea places CHEBI:82815 on the products side of directed RHEA:43053, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/43053/rh:products; http://rdf.rhea-db.org/43052_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_43052_compound_10325/rh:compound -> http://rdf.rhea-db.org/Compound_10325/rh:chebi
3-(methylsulfanyl)propanoate + ATP + CoA => 3-(methylsulfanyl)propanoyl-CoA + AMP + diphosphate
RHEA:43053
produces

adenosine 5'-monophosphate(2-)
CHEBI:456215
  • RHEA:43053

    Source assertion: Rhea places CHEBI:456215 on the products side of directed RHEA:43053, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/43053/rh:products; http://rdf.rhea-db.org/43052_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_43052_compound_2590/rh:compound -> http://rdf.rhea-db.org/Compound_2590/rh:chebi
3-(methylsulfanyl)propanoate + ATP + CoA => 3-(methylsulfanyl)propanoyl-CoA + AMP + diphosphate
RHEA:43053
produces

diphosphate(3-)
CHEBI:33019
  • RHEA:43053

    Source assertion: Rhea places CHEBI:33019 on the products side of directed RHEA:43053, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/43053/rh:products; http://rdf.rhea-db.org/43052_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_43052_compound_2106/rh:compound -> http://rdf.rhea-db.org/Compound_2106/rh:chebi
3-(methylthio)propanoyl-CoA(4-)
CHEBI:82815
consumes

3-(methylsulfanyl)propanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) => 3-(methylsulfanyl)acryloyl-CoA + reduced [electron-transfer flavoprotein]
RHEA:52613
  • RHEA:52613

    Source assertion: Rhea places CHEBI:82815 on the substrates side of directed RHEA:52613, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/52613/rh:substrates; http://rdf.rhea-db.org/52612_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_52612_compound_10325/rh:compound -> http://rdf.rhea-db.org/Compound_10325/rh:chebi
oxidized [electron-transfer flavoprotein]
RHEA-COMP:10685
consumes

This whole generic carrier state is the curated database acceptor-class convention, not a specific DSS-3 protein. Primary assays establish MMPA-CoA oxidation with artificial acceptors; the physiological flavoprotein partner remains unresolved. Carrier-bound FAD is not a substitute node for the carrier.

3-(methylsulfanyl)propanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) => 3-(methylsulfanyl)acryloyl-CoA + reduced [electron-transfer flavoprotein]
RHEA:52613
  • RHEA:52613

    Source assertion: Rhea places RHEA-COMP:10685 on the substrates side of directed RHEA:52613, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/52613/rh:substrates; http://rdf.rhea-db.org/52612_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_52612_compound_10685/rh:compound -> http://rdf.rhea-db.org/Compound_10685/rh:id, rh:name, rdfs:subClassOf
  • MetaCyc:RXN-12572

    Source assertion: The native reaction explicitly places the generic protein class ETF-Oxidized on its left side; it does not identify a strain-specific ETF protein.

    Source locationReaction[@frameid="RXN-12572"]/left/Protein[@frameid="ETF-Oxidized"]
  • UniProtKB:Q5LLW7

    Source assertion: The reviewed catalytic-activity entry cross-references RHEA:52612 and both generic ETF components. Its attached 2011 citation does not experimentally identify the physiological carrier.

    Source locationcomments[1].reaction.reactionCrossReferences; comments[1].reaction.evidences
hydron
CHEBI:15378
consumes

3-(methylsulfanyl)propanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) => 3-(methylsulfanyl)acryloyl-CoA + reduced [electron-transfer flavoprotein]
RHEA:52613
  • RHEA:52613

    Source assertion: Rhea places CHEBI:15378 on the substrates side of directed RHEA:52613, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/52613/rh:substrates; http://rdf.rhea-db.org/52612_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_52612_compound_3249/rh:compound -> http://rdf.rhea-db.org/Compound_3249/rh:chebi
3-(methylsulfanyl)propanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) => 3-(methylsulfanyl)acryloyl-CoA + reduced [electron-transfer flavoprotein]
RHEA:52613
produces

3-(methylthio)acryloyl-CoA(4-)
CHEBI:84994
  • RHEA:52613

    Source assertion: Rhea places CHEBI:84994 on the products side of directed RHEA:52613, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/52613/rh:products; http://rdf.rhea-db.org/52612_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_52612_compound_11096/rh:compound -> http://rdf.rhea-db.org/Compound_11096/rh:chebi
3-(methylsulfanyl)propanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) => 3-(methylsulfanyl)acryloyl-CoA + reduced [electron-transfer flavoprotein]
RHEA:52613
produces

This whole generic carrier state is the curated database acceptor-class convention, not a specific DSS-3 protein. Primary assays establish MMPA-CoA oxidation with artificial acceptors; the physiological flavoprotein partner remains unresolved. Carrier-bound FAD is not a substitute node for the carrier.

reduced [electron-transfer flavoprotein]
RHEA-COMP:10686
  • RHEA:52613

    Source assertion: Rhea places RHEA-COMP:10686 on the products side of directed RHEA:52613, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/52613/rh:products; http://rdf.rhea-db.org/52612_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_52612_compound_10686/rh:compound -> http://rdf.rhea-db.org/Compound_10686/rh:id, rh:name, rdfs:subClassOf
  • MetaCyc:RXN-12572

    Source assertion: The native reaction explicitly places the generic protein class ETF-Reduced on its right side; it does not identify a strain-specific ETF protein.

    Source locationReaction[@frameid="RXN-12572"]/right/Protein[@frameid="ETF-Reduced"]
  • UniProtKB:Q5LLW7

    Source assertion: The reviewed catalytic-activity entry cross-references RHEA:52612 and both generic ETF components. Its attached 2011 citation does not experimentally identify the physiological carrier.

    Source locationcomments[1].reaction.reactionCrossReferences; comments[1].reaction.evidences
3-(methylthio)acryloyl-CoA(4-)
CHEBI:84994
consumes

This is a side of the single terminal net reaction. DmdD catalyzes hydration and hydrolysis; methanethiol elimination and subsequent decarboxylation are spontaneous or expected spontaneous steps within that net conversion.

3-(methylsulfanyl)acryloyl-CoA + 2 H2O => methanethiol + acetaldehyde + CO2 + CoA
RHEA:45145
  • RHEA:45145

    Source assertion: Rhea places CHEBI:84994 on the substrates side of directed RHEA:45145, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/45145/rh:substrates; http://rdf.rhea-db.org/45144_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_45144_compound_11096/rh:compound -> http://rdf.rhea-db.org/Compound_11096/rh:chebi
water
CHEBI:15377
consumes

This is a side of the single terminal net reaction. DmdD catalyzes hydration and hydrolysis; methanethiol elimination and subsequent decarboxylation are spontaneous or expected spontaneous steps within that net conversion.

3-(methylsulfanyl)acryloyl-CoA + 2 H2O => methanethiol + acetaldehyde + CO2 + CoA
RHEA:45145
  • RHEA:45145

    Source assertion: Rhea places CHEBI:15377 on the substrates side of directed RHEA:45145, with coefficient 2.

    Source locationhttp://rdf.rhea-db.org/45145/rh:substrates; http://rdf.rhea-db.org/45144_L/rh:contains2 -> http://rdf.rhea-db.org/Participant_45144_compound_1283/rh:compound -> http://rdf.rhea-db.org/Compound_1283/rh:chebi
3-(methylsulfanyl)acryloyl-CoA + 2 H2O => methanethiol + acetaldehyde + CO2 + CoA
RHEA:45145
produces

This is a side of the single terminal net reaction. DmdD catalyzes hydration and hydrolysis; methanethiol elimination and subsequent decarboxylation are spontaneous or expected spontaneous steps within that net conversion.

methanethiol
CHEBI:16007
  • RHEA:45145

    Source assertion: Rhea places CHEBI:16007 on the products side of directed RHEA:45145, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/45145/rh:products; http://rdf.rhea-db.org/45144_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_45144_compound_2831/rh:compound -> http://rdf.rhea-db.org/Compound_2831/rh:chebi
3-(methylsulfanyl)acryloyl-CoA + 2 H2O => methanethiol + acetaldehyde + CO2 + CoA
RHEA:45145
produces

This is a side of the single terminal net reaction. DmdD catalyzes hydration and hydrolysis; methanethiol elimination and subsequent decarboxylation are spontaneous or expected spontaneous steps within that net conversion.

acetaldehyde
CHEBI:15343
  • RHEA:45145

    Source assertion: Rhea places CHEBI:15343 on the products side of directed RHEA:45145, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/45145/rh:products; http://rdf.rhea-db.org/45144_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_45144_compound_3952/rh:compound -> http://rdf.rhea-db.org/Compound_3952/rh:chebi
3-(methylsulfanyl)acryloyl-CoA + 2 H2O => methanethiol + acetaldehyde + CO2 + CoA
RHEA:45145
produces

This is a side of the single terminal net reaction. DmdD catalyzes hydration and hydrolysis; methanethiol elimination and subsequent decarboxylation are spontaneous or expected spontaneous steps within that net conversion.

carbon dioxide
CHEBI:16526
  • RHEA:45145

    Source assertion: Rhea places CHEBI:16526 on the products side of directed RHEA:45145, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/45145/rh:products; http://rdf.rhea-db.org/45144_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_45144_compound_4391/rh:compound -> http://rdf.rhea-db.org/Compound_4391/rh:chebi
3-(methylsulfanyl)acryloyl-CoA + 2 H2O => methanethiol + acetaldehyde + CO2 + CoA
RHEA:45145
produces

This is a side of the single terminal net reaction. DmdD catalyzes hydration and hydrolysis; methanethiol elimination and subsequent decarboxylation are spontaneous or expected spontaneous steps within that net conversion.

coenzyme A(4-)
CHEBI:57287
  • RHEA:45145

    Source assertion: Rhea places CHEBI:57287 on the products side of directed RHEA:45145, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/45145/rh:products; http://rdf.rhea-db.org/45144_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_45144_compound_1264/rh:compound -> http://rdf.rhea-db.org/Compound_1264/rh:chebi
3-methylmercaptopropionyl-CoA ligase
UniProtKB:Q5LRT0
enables

DmdB2 (SPO2045) enables MMPA activation as a functional gene-product role. Purified recombinant DSS-3 enzyme was a homodimer by gel filtration; this edge does not assert monomer sufficiency. DmdB1 is a separately characterized isozyme outside this native catalyst projection.

3-(methylsulfanyl)propanoate + ATP + CoA => 3-(methylsulfanyl)propanoyl-CoA + AMP + diphosphate
RHEA:43053
  • MetaCyc:ENZRXN-19462

    Source assertion: The native enzymatic-reaction object assigns MONOMER-16783 to RXN-12571.

    Source locationEnzymatic-Reaction[@frameid="ENZRXN-19462"]/enzyme/Protein; reaction/Reaction
  • MetaCyc:MONOMER-16783

    Source assertion: The native protein frame cross-references UniProt Q5LRT0; this establishes the gene-product identity, not a monomeric active assembly.

    Source locationProtein[@frameid="MONOMER-16783"]/dblink[dblink-db="UNIPROT"]/dblink-oid
  • UniProtKB:Q5LRT0

    Source assertion: The reviewed catalytic-activity annotation assigns RHEA:43052 with experimental evidence ECO:0000269. The selected forward direction is independently read from Rhea.

    Source locationcomments[1].reaction.reactionCrossReferences; comments[1].reaction.evidences
  • PMID:21562561

    Source assertion: Partially purified native MMPA-CoA ligase identified SPO2045; recombinant expression confirmed activity, with ATP consumption and AMP production.

    Source locationPrinted p.208, MMPA-CoA ligase purification and recombinant expression paragraphs; Figure 1 p.209
  • PMID:24443527

    Source assertion: SPO2045 is RPO_DmdB2. Purified recombinant DmdB2 has MMPA-CoA ligase activity and a native gel-filtration mass consistent with a dimer.

    Source locationFigure 2 caption; Results, DmdBs are dimers with MMPA-CoA ligase activity, section sec3-1; Table 1
  • UniProtKB:Q5LRT0

    Source assertion: The reviewed entry identifies Ruegeria pomeroyi strain ATCC 700808 / DSM 15171 / DSS-3 and taxon 246200.

    Source locationorganism.scientificName; organism.taxonId; genes
3-methylmercaptopropionyl-CoA dehydrogenase
UniProtKB:Q5LLW7
enables

DmdC1 (SPO3804) enables the oxidation in its experimentally supported homodimeric context. Current Rhea specifies a generic ETF acceptor class; this role does not claim that the exact carrier was tested. The 2022 study used recombinant DSS-3 enzyme and artificial electron acceptors.

3-(methylsulfanyl)propanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) => 3-(methylsulfanyl)acryloyl-CoA + reduced [electron-transfer flavoprotein]
RHEA:52613
  • MetaCyc:ENZRXN-19463

    Source assertion: The native enzymatic-reaction object assigns MONOMER-16784 to RXN-12572.

    Source locationEnzymatic-Reaction[@frameid="ENZRXN-19463"]/enzyme/Protein; reaction/Reaction
  • MetaCyc:MONOMER-16784

    Source assertion: The native protein frame cross-references UniProt Q5LLW7; this establishes the gene-product identity, not a monomeric active assembly.

    Source locationProtein[@frameid="MONOMER-16784"]/dblink[dblink-db="UNIPROT"]/dblink-oid
  • UniProtKB:Q5LLW7

    Source assertion: The reviewed catalytic-activity annotation assigns RHEA:52612 with experimental evidence ECO:0000269. The selected forward direction is independently read from Rhea.

    Source locationcomments[1].reaction.reactionCrossReferences; comments[1].reaction.evidences
  • PMID:21562561

    Source assertion: Recombinant SPO3804 catalyzed MMPA-CoA oxidation. The dmdC mutant could not grow on MMPA, and SPO3804 complementation restored growth. Artificial electron acceptors supported the assay.

    Source locationPrinted pp.208-209, MMPA-CoA dehydrogenation, recombinant expression and dmdC disruption/complementation paragraphs
  • PMID:34818101

    Source assertion: The cloned DSS-3 SPO3804 enzyme forms a homodimer. Oxidation required PMS plus DCPIP or INT; free FAD, FMN and NADP+ alone did not support activity. An uncharacterized in vivo flavoprotein is inferred.

    Source locationResults, Properties of RPO_DmdC1 dehydrogenase, section s2-3 paragraphs 1-2; Materials and Methods, Plasmid construction and expression of recombinant protein, section s3-1
  • UniProtKB:Q5LLW7

    Source assertion: The reviewed entry identifies Ruegeria pomeroyi strain ATCC 700808 / DSM 15171 / DSS-3 and taxon 246200.

    Source locationorganism.scientificName; organism.taxonId; genes
Methylthioacryloyl-CoA hydratase
UniProtKB:Q5LLW6
enables

DmdD (SPO3805) enables the observed net cleavage as a homohexamer (dimer of trimers), not an isolated monomer. The net equation includes spontaneous methanethiol elimination after hydration and expected spontaneous malonate-semialdehyde decarboxylation. It is not duplicated by component reaction nodes.

3-(methylsulfanyl)acryloyl-CoA + 2 H2O => methanethiol + acetaldehyde + CO2 + CoA
RHEA:45145
  • MetaCyc:ENZRXN-19464

    Source assertion: The native enzymatic-reaction object assigns MONOMER-16785 to RXN-12573.

    Source locationEnzymatic-Reaction[@frameid="ENZRXN-19464"]/enzyme/Protein; reaction/Reaction
  • MetaCyc:MONOMER-16785

    Source assertion: The native protein frame cross-references UniProt Q5LLW6; this establishes the gene-product identity, not a monomeric active assembly.

    Source locationProtein[@frameid="MONOMER-16785"]/dblink[dblink-db="UNIPROT"]/dblink-oid
  • UniProtKB:Q5LLW6

    Source assertion: The reviewed catalytic-activity annotation assigns RHEA:45144 with experimental evidence ECO:0000269. The selected forward direction is independently read from Rhea.

    Source locationcomments[1].reaction.reactionCrossReferences; comments[1].reaction.evidences
  • PMID:21562561

    Source assertion: Purified DmdD/SPO3805 and recombinant expression establish MTA-CoA cleavage; stoichiometric CoA and methanethiol and approximately 90% theoretical acetaldehyde were obtained. Lost carbon was presumed to be CO2.

    Source locationPrinted pp.208-209, DmdD purification and product-identification paragraphs; Figure 1
  • PMID:23704947

    Source assertion: DmdD is a homohexamer with two trimers and intersubunit active sites. The mechanism assigns enzymatic hydration and thioester hydrolysis; methanethiol release is spontaneous and final decarboxylation is expected spontaneous.

    Source locationResults and Discussion, The hexamer of DmdD (s2b), and Catalytic mechanism of DmdD (s2g); Figure 6
  • UniProtKB:Q5LLW6

    Source assertion: The reviewed entry identifies Ruegeria pomeroyi strain ATCC 700808 / DSM 15171 / DSS-3 and taxon 246200.

    Source locationorganism.scientificName; organism.taxonId; genes
3-methylmercaptopropionyl-CoA ligase
UniProtKB:Q5LRT0
has_cofactor

Magnesium dependence is reported for ligase activity. The sources do not establish an independent protein-binding stoichiometry or separate MgATP and free-ion mechanisms.

magnesium(2+)
CHEBI:18420
  • UniProtKB:Q5LRT0

    Source assertion: The Mg(2+) cofactor annotation is inferred by similarity, ECO:0000250 from Q5SKN9.

    Source locationcomments[2].cofactors[0].cofactorCrossReference; comments[2].cofactors[0].evidences
  • PMID:24443527

    Source assertion: The primary DmdB study explicitly states that Mg2+ was required for activity; divalent cations were consequently not tested in the salt-response experiment.

    Source locationResults, DmdBs show various activities in the presence of salts, section sec3-2 paragraph 1
3-methylmercaptopropionyl-CoA dehydrogenase
UniProtKB:Q5LLW7
has_cofactor

The enzyme-bound FAD assignment is similarity-scoped and distinct from the generic whole ETF substrate. Free FAD did not act as the sole electron acceptor in the DSS-3 DmdC1 assay; cross-species DmdC activity with free FAD is not transferred here.

FAD(3-)
CHEBI:57692
  • UniProtKB:Q5LLW7

    Source assertion: FAD cofactor assignment is ECO:0000250, inferred by similarity to A3SI50; it is not a directly measured DSS-3 occupancy or stoichiometry.

    Source locationcomments[2].cofactors[0].cofactorCrossReference; comments[2].cofactors[0].evidences
S,S-dimethyl-beta-propiothetin
CHEBI:16457
inhibits

The physiological regulatory model is proposed from measured in vitro inhibition and cellular DMSP context; no direct regulator binding or universal in vivo flux assertion is made.

3-methylmercaptopropionyl-CoA ligase
UniProtKB:Q5LRT0
  • PMID:24443527

    Source assertion: DMSP strongly inhibits RPO_DmdB2, with the plotted concentration response measured using purified recombinant enzyme. This is an in vitro enzyme effect, not a transcription-factor claim.

    Source locationResults, DMSP inhibition of marine DmdBs, section sec3-5; Figure 3
  • UniProtKB:Q5LRT0

    Source assertion: The DmdB2 activity-regulation annotation states inhibition by DMSP, with experimental evidence ECO:0000269 from PMID:24443527.

    Source locationcomments[3].texts[0]
3-(methylthio)propionate
CHEBI:49016
activates

Conditional relief of DMSP inhibition, not unqualified stimulation in the absence of inhibitor. MMPA is also the substrate of the activation reaction.

3-methylmercaptopropionyl-CoA ligase
UniProtKB:Q5LRT0
  • PMID:24443527

    Source assertion: MMPA above 2 mM relieves DMSP inhibition of RPO_DmdB2; about 80% activity is regained at 8 mM MMPA. ADP relief belongs to DmdB1 and is not transferred to DmdB2.

    Source locationResults, ADP and MMPA relieved inhibition by DMSP in R. pomeroyi DSS-3, section sec3-6 paragraph 1; Figure 5B
  • UniProtKB:Q5LRT0

    Source assertion: The DmdB2 annotation records MMPA-dependent relief of DMSP inhibition, with ECO:0000269 from PMID:24443527.

    Source locationcomments[3].texts[0]
3-(methylsulfanyl)propanoate + ATP + CoA => 3-(methylsulfanyl)propanoyl-CoA + AMP + diphosphate
RHEA:43053
part_of

MetaCyc:PWY-6048
  • MetaCyc:PWY-6048

    Source assertion: The exact native pathway reaction-list includes RXN-12571. This is one of three complete native members.

    Source locationPathway[@frameid="PWY-6048"]/reaction-list/Reaction
  • MetaCyc:RXN-12571

    Source assertion: The native reaction is physiologically left-to-right and assigns ENZRXN-19462 as its enzymatic reaction.

    Source locationReaction[@frameid="RXN-12571"]/reaction-direction; enzymatic-reaction/Enzymatic-Reaction
  • RHEA:43053

    Source assertion: Rhea master 43052 explicitly links directed reaction 43053 through rh:directionalReaction.

    Source locationhttp://rdf.rhea-db.org/43052/rh:directionalReaction -> http://rdf.rhea-db.org/43053
  • MetaCyc:RXN-12571

    Source assertion: The native reaction directly cross-references RHEA:43053.

    Source locationReaction[@frameid="RXN-12571"]/dblink[dblink-db="RHEA"]/dblink-oid
3-(methylsulfanyl)propanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) => 3-(methylsulfanyl)acryloyl-CoA + reduced [electron-transfer flavoprotein]
RHEA:52613
part_of

MetaCyc:PWY-6048
  • MetaCyc:PWY-6048

    Source assertion: The exact native pathway reaction-list includes RXN-12572. This is one of three complete native members.

    Source locationPathway[@frameid="PWY-6048"]/reaction-list/Reaction
  • MetaCyc:RXN-12572

    Source assertion: The native reaction is physiologically left-to-right and assigns ENZRXN-19463 as its enzymatic reaction.

    Source locationReaction[@frameid="RXN-12572"]/reaction-direction; enzymatic-reaction/Enzymatic-Reaction
  • RHEA:52613

    Source assertion: Rhea master 52612 explicitly links directed reaction 52613 through rh:directionalReaction.

    Source locationhttp://rdf.rhea-db.org/52612/rh:directionalReaction -> http://rdf.rhea-db.org/52613
  • UniProtKB:Q5LLW7

    Source assertion: The native protein crosswalk resolves the reviewed DmdC entry, whose current catalytic-activity annotation links RHEA:52612. The older native reaction itself does not carry this Rhea cross-reference.

    Source locationprimaryAccession; comments[1].reaction.reactionCrossReferences
3-(methylsulfanyl)acryloyl-CoA + 2 H2O => methanethiol + acetaldehyde + CO2 + CoA
RHEA:45145
part_of

The selected terminal Rhea net includes all four native component transformations and is represented once.

MetaCyc:PWY-6048
  • MetaCyc:PWY-6048

    Source assertion: The exact native pathway reaction-list includes RXN-12573. This is one of three complete native members.

    Source locationPathway[@frameid="PWY-6048"]/reaction-list/Reaction
  • MetaCyc:RXN-12573

    Source assertion: The native reaction is physiologically left-to-right and assigns ENZRXN-19464 as its enzymatic reaction.

    Source locationReaction[@frameid="RXN-12573"]/reaction-direction; enzymatic-reaction/Enzymatic-Reaction
  • RHEA:45145

    Source assertion: Rhea master 45144 explicitly links directed reaction 45145 through rh:directionalReaction.

    Source locationhttp://rdf.rhea-db.org/45144/rh:directionalReaction -> http://rdf.rhea-db.org/45145
  • MetaCyc:RXN-12573

    Source assertion: The native reaction directly cross-references RHEA:45145.

    Source locationReaction[@frameid="RXN-12573"]/dblink[dblink-db="RHEA"]/dblink-oid
3-(methylsulfanyl)propanoate + ATP + CoA => 3-(methylsulfanyl)propanoyl-CoA + AMP + diphosphate
RHEA:43053
provides_input_for

The shared chemical is CHEBI:82815; this is material continuity, not an assumed regulatory relation.

3-(methylsulfanyl)propanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) => 3-(methylsulfanyl)acryloyl-CoA + reduced [electron-transfer flavoprotein]
RHEA:52613
  • MetaCyc:PWY-6048

    Source assertion: The native reaction-list contains all three activation, oxidation and cleavage transformations. Exact ChEBI intermediate continuity is established separately from both current Rhea sides.

    Source locationPathway[@frameid="PWY-6048"]/reaction-list/Reaction
  • RHEA:43053

    Source assertion: Rhea places CHEBI:82815 on the products side of directed RHEA:43053, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/43053/rh:products; http://rdf.rhea-db.org/43052_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_43052_compound_10325/rh:compound -> http://rdf.rhea-db.org/Compound_10325/rh:chebi
  • RHEA:52613

    Source assertion: Rhea places CHEBI:82815 on the substrates side of directed RHEA:52613, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/52613/rh:substrates; http://rdf.rhea-db.org/52612_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_52612_compound_10325/rh:compound -> http://rdf.rhea-db.org/Compound_10325/rh:chebi
3-(methylsulfanyl)propanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) => 3-(methylsulfanyl)acryloyl-CoA + reduced [electron-transfer flavoprotein]
RHEA:52613
provides_input_for

The shared chemical is CHEBI:84994; this is material continuity, not an assumed regulatory relation.

3-(methylsulfanyl)acryloyl-CoA + 2 H2O => methanethiol + acetaldehyde + CO2 + CoA
RHEA:45145
  • MetaCyc:PWY-6048

    Source assertion: The native reaction-list contains all three activation, oxidation and cleavage transformations. Exact ChEBI intermediate continuity is established separately from both current Rhea sides.

    Source locationPathway[@frameid="PWY-6048"]/reaction-list/Reaction
  • RHEA:52613

    Source assertion: Rhea places CHEBI:84994 on the products side of directed RHEA:52613, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/52613/rh:products; http://rdf.rhea-db.org/52612_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_52612_compound_11096/rh:compound -> http://rdf.rhea-db.org/Compound_11096/rh:chebi
  • RHEA:45145

    Source assertion: Rhea places CHEBI:84994 on the substrates side of directed RHEA:45145, with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/45145/rh:substrates; http://rdf.rhea-db.org/45144_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_45144_compound_11096/rh:compound -> http://rdf.rhea-db.org/Compound_11096/rh:chebi

References

Curation history