3-hydroxypropanoate/4-hydroxybutanate cycle
MetaCyc:PWY-5789
The complete 3-hydroxypropionate/4-hydroxybutyrate carbon-fixation cycle is represented for Metallosphaera sedula TH2 (DSM 5348). Acetyl-CoA and propionyl-CoA carboxylation feed malonyl-CoA and methylmalonyl-CoA, followed by succinyl-CoA reduction and conversion through 4-hydroxybutyryl-CoA, trans-crotonyl-CoA and (S)-3-hydroxybutyryl-CoA to two acetyl-CoA molecules. One acetyl-CoA regenerates the acceptor; succinyl-CoA is also an experimentally supported major biosynthetic exit. The 18 native reaction objects correspond to 16 enzymatic transformations plus auxiliary CO2 hydration: two biotin-carboxylase half-reactions are represented by their independently issued net reaction, giving 17 reaction nodes. Native charged intermediates and all current Rhea side coefficients are retained; the native crotonyl-CoA structure is less specific at one conserved CoA stereocenter. The measured archaeal carboxylase assembly and sequence-verified subunits are distinguished from generic bacterial carrier notation. Later primary work supports Msed_2001 and Msed_1423 as the principal crotonyl-CoA hydratase and hydroxybutyryl-CoA dehydrogenase; measured alternative activities remain qualified. Native and current sequence annotation conflicts, inferred cofactors and cross-species recombinant measurements are explicitly scoped. Recombinant Msed_2001 monomer/octamer and Msed_1424 dimer/pentamer estimates remain unresolved rather than universal assembly claims. The selected autotrophic archaeal strain, rather than its E. coli expression hosts or other carbon-fixation pathways, defines the organism scope.
- Pathway type
- autotrophic carbon fixation
- Organism scope
Pathway network
86 nodes · 164 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 |
|---|---|---|
Metallosphaera sedula DSM 5348NCBITaxon:399549 | taxon | |
waterCHEBI:15377 | small molecule | |
hydronCHEBI:15378 | small molecule | |
3-hydroxypropionateCHEBI:16510 | small molecule | |
carbon dioxideCHEBI:16526 | small molecule | |
4-hydroxybutyrateCHEBI:16724 | small molecule | |
hydrogencarbonateCHEBI:17544 | small molecule | |
ATP(4-)CHEBI:30616 | small molecule | |
diphosphate(3-)CHEBI:33019 | small molecule | |
3-oxopropanoateCHEBI:33190 | small molecule | |
hydrogenphosphateCHEBI:43474 | small molecule | |
acetoacetyl-CoA(4-)CHEBI:57286 | small molecule | |
coenzyme A(4-)CHEBI:57287 | small molecule | |
acetyl-CoA(4-)CHEBI:57288 | small molecule | |
succinyl-CoA(5-)CHEBI:57292 | small molecule | |
(S)-3-hydroxybutanoyl-CoA(4-)CHEBI:57316 | small molecule | |
(R)-methylmalonyl-CoA(5-)CHEBI:57326 | small molecule | |
(S)-methylmalonyl-CoA(5-)CHEBI:57327 | small molecule | |
crotonoyl-CoA(4-)CHEBI:57332 | small molecule | |
acryloyl-CoA(4-)CHEBI:57367 | small molecule | |
malonyl-CoA(5-)CHEBI:57384 | small molecule | |
propionyl-CoA(4-)CHEBI:57392 | small molecule | |
NAD(1-)CHEBI:57540 | small molecule | |
4-oxobutanoateCHEBI:57706 | small molecule | |
NADPH(4-)CHEBI:57783 | small molecule | |
NADH(2-)CHEBI:57945 | small molecule | |
NADP(3-)CHEBI:58349 | small molecule | |
3-hydroxypropanoyl-CoA(4-)CHEBI:58528 | small molecule | |
4-hydroxybutyryl-CoA(4-)CHEBI:58574 | small molecule | |
adenosine 5'-monophosphate(2-)CHEBI:456215 | small molecule | |
ADP(3-)CHEBI:456216 | small molecule | |
cobamamideCHEBI:18408 | cofactor | |
biotinateCHEBI:57586 | cofactor | |
tetra-mu3-sulfido-tetrairon(0)CHEBI:33725 | cofactor | |
FAD(3-)CHEBI:57692 | cofactor | |
magnesium(2+)CHEBI:18420 | cofactor | |
zinc(2+)CHEBI:29105 | cofactor | |
cobalt(2+)CHEBI:48828 | cofactor | |
nickel(2+)CHEBI:49786 | cofactor | |
manganese(2+)CHEBI:29035 | cofactor | |
Biotin carboxylaseUniProtKB:A4YD22 | protein | |
Biotin carboxyl carrier proteinUniProtKB:A4YD23 | protein | |
Acetyl-CoA carboxylase carboxyltransferase subunit alpha / acetyl-CoA carboxylase carboxyltransferase subunit beta / propionyl-CoA carboxylase carboxyltransferase subunitUniProtKB:A4YGI1 | protein | |
Malonyl CoA reductase (NADP)UniProtKB:A4YEN2 | protein | |
3-hydroxypropionate dehydrogenase (NADP(+))UniProtKB:A4YI81 | protein | |
3-hydroxypropionyl-coenzyme A synthetaseUniProtKB:A4YGR1 | protein | |
3-hydroxypropionyl-coenzyme A dehydrataseUniProtKB:A4YI89 | protein | |
Acryloyl-coenzyme A reductaseUniProtKB:A4YGN2 | protein | |
Methylmalonyl-CoA epimeraseUniProtKB:A4YEG2 | protein | |
Methylmalonyl-CoA mutaseUniProtKB:A4YEG1 | protein | |
Cobalamin B12-binding domain proteinUniProtKB:A4YIE3 | protein | |
Msed_1424 succinic semialdehyde reductaseUniProtKB:A4YGN0 | protein | |
4-hydroxybutyrate--CoA ligase 1UniProtKB:A4YDT1 | protein | |
Vinylacetyl-CoA Delta-isomeraseUniProtKB:A4YGC7 | protein | |
3-hydroxyacyl-CoA dehydrogenaseUniProtKB:A4YGM9 | protein | |
Acetyl-CoA acetyltransferaseUniProtKB:A4YEH9 | protein | |
4-hydroxybutyrate--CoA ligase 2UniProtKB:A4YDR9 | protein | |
3-hydroxyacyl-CoA dehydrogenase, NAD-binding proteinUniProtKB:A4YDS4 | protein | |
Enoyl-CoA hydratase/isomeraseUniProtKB:A4YDL1 | protein | |
Short chain enoyl-CoA hydrataseUniProtKB:A4YDQ9 | protein | |
3-hydroxyacyl-CoA dehydrogenaseUniProtKB:A4YDR4 | protein | |
acyl CoA carboxylase holoenzymeMetaCyc:CPLX-7580 | complex | |
acyl CoA carboxylase trimerMetaCyc:CPLX-7575 | complex | |
malonyl-coenzyme A reductase / succinyl-CoA reductaseMetaCyc:CPLX-7577 | complex | |
NADP-dependent malonate semialdehyde reductaseMetaCyc:CPLX-7947 | complex | |
3-hydroxypropionyl-CoA synthetase (AMP-forming)MetaCyc:CPLX-7579 | complex | |
methylmalonyl-CoA epimeraseMetaCyc:CPLX-8530 | complex | |
methylmalonyl-CoA mutaseMetaCyc:CPLX-7576 | complex | |
NADPH-dependent succinate semialdehyde reductaseMetaCyc:CPLX-7948 | complex | |
CO2 + H2O => hydrogencarbonate + H(+)RHEA:10750 | reaction | right to left |
hydrogencarbonate + acetyl-CoA + ATP => malonyl-CoA + ADP + phosphate + H(+)RHEA:11309 | molecular activity | left to right |
malonyl-CoA + NADPH + H(+) => 3-oxopropanoate + NADP(+) + CoARHEA:26448 | molecular activity | right to left |
3-oxopropanoate + NADPH + H(+) => 3-hydroxypropanoate + NADP(+)RHEA:26440 | molecular activity | right to left |
3-hydroxypropanoate + ATP + CoA => 3-hydroxypropanoyl-CoA + AMP + diphosphateRHEA:26535 | molecular activity | left to right |
3-hydroxypropanoyl-CoA => acryloyl-CoA + H2ORHEA:26519 | molecular activity | left to right |
acryloyl-CoA + NADPH + H(+) => propanoyl-CoA + NADP(+)RHEA:26456 | molecular activity | right to left |
propanoyl-CoA + hydrogencarbonate + ATP => (S)-methylmalonyl-CoA + ADP + phosphate + H(+)RHEA:23721 | molecular activity | left to right |
(S)-methylmalonyl-CoA => (R)-methylmalonyl-CoARHEA:20555 | molecular activity | right to left |
(R)-methylmalonyl-CoA => succinyl-CoARHEA:22889 | molecular activity | left to right |
succinyl-CoA + NADPH + H(+) => succinate semialdehyde + NADP(+) + CoARHEA:26452 | molecular activity | right to left |
succinate semialdehyde + NADPH + H(+) => 4-hydroxybutanoate + NADP(+)RHEA:26383 | molecular activity | right to left |
4-hydroxybutanoate + ATP + CoA => 4-hydroxybutanoyl-CoA + AMP + diphosphateRHEA:23129 | molecular activity | left to right |
4-hydroxybutanoyl-CoA => (2E)-butenoyl-CoA + H2ORHEA:26531 | molecular activity | left to right |
(2E)-butenoyl-CoA + H2O => (3S)-3-hydroxybutanoyl-CoARHEA:26560 | molecular activity | right to left |
(3S)-3-hydroxybutanoyl-CoA + NAD(+) => acetoacetyl-CoA + NADH + H(+)RHEA:30800 | molecular activity | left to right |
acetoacetyl-CoA + CoA => 2 acetyl-CoARHEA:21038 | molecular activity | right to left |
Mechanistic edges
| Subject | Predicate and description | Object | Evidence |
|---|---|---|---|
carbon dioxideCHEBI:16526 | consumes | CO2 + H2O => hydrogencarbonate + H(+)RHEA:10750 |
|
waterCHEBI:15377 | consumes | CO2 + H2O => hydrogencarbonate + H(+)RHEA:10750 |
|
CO2 + H2O => hydrogencarbonate + H(+)RHEA:10750 | produces | hydrogencarbonateCHEBI:17544 |
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CO2 + H2O => hydrogencarbonate + H(+)RHEA:10750 | produces | hydronCHEBI:15378 |
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hydrogencarbonateCHEBI:17544 | consumes | hydrogencarbonate + acetyl-CoA + ATP => malonyl-CoA + ADP + phosphate + H(+)RHEA:11309 |
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acetyl-CoA(4-)CHEBI:57288 | consumes | hydrogencarbonate + acetyl-CoA + ATP => malonyl-CoA + ADP + phosphate + H(+)RHEA:11309 |
|
ATP(4-)CHEBI:30616 | consumes | hydrogencarbonate + acetyl-CoA + ATP => malonyl-CoA + ADP + phosphate + H(+)RHEA:11309 |
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hydrogencarbonate + acetyl-CoA + ATP => malonyl-CoA + ADP + phosphate + H(+)RHEA:11309 | produces | malonyl-CoA(5-)CHEBI:57384 |
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hydrogencarbonate + acetyl-CoA + ATP => malonyl-CoA + ADP + phosphate + H(+)RHEA:11309 | produces | ADP(3-)CHEBI:456216 |
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hydrogencarbonate + acetyl-CoA + ATP => malonyl-CoA + ADP + phosphate + H(+)RHEA:11309 | produces | hydrogenphosphateCHEBI:43474 |
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hydrogencarbonate + acetyl-CoA + ATP => malonyl-CoA + ADP + phosphate + H(+)RHEA:11309 | produces | hydronCHEBI:15378 |
|
malonyl-CoA(5-)CHEBI:57384 | consumes | malonyl-CoA + NADPH + H(+) => 3-oxopropanoate + NADP(+) + CoARHEA:26448 |
|
NADPH(4-)CHEBI:57783 | consumes | malonyl-CoA + NADPH + H(+) => 3-oxopropanoate + NADP(+) + CoARHEA:26448 |
|
hydronCHEBI:15378 | consumes | malonyl-CoA + NADPH + H(+) => 3-oxopropanoate + NADP(+) + CoARHEA:26448 |
|
malonyl-CoA + NADPH + H(+) => 3-oxopropanoate + NADP(+) + CoARHEA:26448 | produces | 3-oxopropanoateCHEBI:33190 |
|
malonyl-CoA + NADPH + H(+) => 3-oxopropanoate + NADP(+) + CoARHEA:26448 | produces | NADP(3-)CHEBI:58349 |
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malonyl-CoA + NADPH + H(+) => 3-oxopropanoate + NADP(+) + CoARHEA:26448 | produces | coenzyme A(4-)CHEBI:57287 |
|
3-oxopropanoateCHEBI:33190 | consumes | 3-oxopropanoate + NADPH + H(+) => 3-hydroxypropanoate + NADP(+)RHEA:26440 |
|
NADPH(4-)CHEBI:57783 | consumes | 3-oxopropanoate + NADPH + H(+) => 3-hydroxypropanoate + NADP(+)RHEA:26440 |
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hydronCHEBI:15378 | consumes | 3-oxopropanoate + NADPH + H(+) => 3-hydroxypropanoate + NADP(+)RHEA:26440 |
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3-oxopropanoate + NADPH + H(+) => 3-hydroxypropanoate + NADP(+)RHEA:26440 | produces | 3-hydroxypropionateCHEBI:16510 |
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3-oxopropanoate + NADPH + H(+) => 3-hydroxypropanoate + NADP(+)RHEA:26440 | produces | NADP(3-)CHEBI:58349 |
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3-hydroxypropionateCHEBI:16510 | consumes | 3-hydroxypropanoate + ATP + CoA => 3-hydroxypropanoyl-CoA + AMP + diphosphateRHEA:26535 |
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ATP(4-)CHEBI:30616 | consumes | 3-hydroxypropanoate + ATP + CoA => 3-hydroxypropanoyl-CoA + AMP + diphosphateRHEA:26535 |
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coenzyme A(4-)CHEBI:57287 | consumes | 3-hydroxypropanoate + ATP + CoA => 3-hydroxypropanoyl-CoA + AMP + diphosphateRHEA:26535 |
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3-hydroxypropanoate + ATP + CoA => 3-hydroxypropanoyl-CoA + AMP + diphosphateRHEA:26535 | produces | 3-hydroxypropanoyl-CoA(4-)CHEBI:58528 |
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3-hydroxypropanoate + ATP + CoA => 3-hydroxypropanoyl-CoA + AMP + diphosphateRHEA:26535 | produces | adenosine 5'-monophosphate(2-)CHEBI:456215 |
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3-hydroxypropanoate + ATP + CoA => 3-hydroxypropanoyl-CoA + AMP + diphosphateRHEA:26535 | produces | diphosphate(3-)CHEBI:33019 |
|
3-hydroxypropanoyl-CoA(4-)CHEBI:58528 | consumes | 3-hydroxypropanoyl-CoA => acryloyl-CoA + H2ORHEA:26519 |
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3-hydroxypropanoyl-CoA => acryloyl-CoA + H2ORHEA:26519 | produces | acryloyl-CoA(4-)CHEBI:57367 |
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3-hydroxypropanoyl-CoA => acryloyl-CoA + H2ORHEA:26519 | produces | waterCHEBI:15377 |
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acryloyl-CoA(4-)CHEBI:57367 | consumes | acryloyl-CoA + NADPH + H(+) => propanoyl-CoA + NADP(+)RHEA:26456 |
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NADPH(4-)CHEBI:57783 | consumes | acryloyl-CoA + NADPH + H(+) => propanoyl-CoA + NADP(+)RHEA:26456 |
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hydronCHEBI:15378 | consumes | acryloyl-CoA + NADPH + H(+) => propanoyl-CoA + NADP(+)RHEA:26456 |
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acryloyl-CoA + NADPH + H(+) => propanoyl-CoA + NADP(+)RHEA:26456 | produces | propionyl-CoA(4-)CHEBI:57392 |
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acryloyl-CoA + NADPH + H(+) => propanoyl-CoA + NADP(+)RHEA:26456 | produces | NADP(3-)CHEBI:58349 |
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propionyl-CoA(4-)CHEBI:57392 | consumes | propanoyl-CoA + hydrogencarbonate + ATP => (S)-methylmalonyl-CoA + ADP + phosphate + H(+)RHEA:23721 |
|
hydrogencarbonateCHEBI:17544 | consumes | propanoyl-CoA + hydrogencarbonate + ATP => (S)-methylmalonyl-CoA + ADP + phosphate + H(+)RHEA:23721 |
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ATP(4-)CHEBI:30616 | consumes | propanoyl-CoA + hydrogencarbonate + ATP => (S)-methylmalonyl-CoA + ADP + phosphate + H(+)RHEA:23721 |
|
propanoyl-CoA + hydrogencarbonate + ATP => (S)-methylmalonyl-CoA + ADP + phosphate + H(+)RHEA:23721 | produces | (S)-methylmalonyl-CoA(5-)CHEBI:57327 |
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propanoyl-CoA + hydrogencarbonate + ATP => (S)-methylmalonyl-CoA + ADP + phosphate + H(+)RHEA:23721 | produces | ADP(3-)CHEBI:456216 |
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propanoyl-CoA + hydrogencarbonate + ATP => (S)-methylmalonyl-CoA + ADP + phosphate + H(+)RHEA:23721 | produces | hydrogenphosphateCHEBI:43474 |
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propanoyl-CoA + hydrogencarbonate + ATP => (S)-methylmalonyl-CoA + ADP + phosphate + H(+)RHEA:23721 | produces | hydronCHEBI:15378 |
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(S)-methylmalonyl-CoA(5-)CHEBI:57327 | consumes | (S)-methylmalonyl-CoA => (R)-methylmalonyl-CoARHEA:20555 |
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(S)-methylmalonyl-CoA => (R)-methylmalonyl-CoARHEA:20555 | produces | (R)-methylmalonyl-CoA(5-)CHEBI:57326 |
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(R)-methylmalonyl-CoA(5-)CHEBI:57326 | consumes | (R)-methylmalonyl-CoA => succinyl-CoARHEA:22889 |
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(R)-methylmalonyl-CoA => succinyl-CoARHEA:22889 | produces | succinyl-CoA(5-)CHEBI:57292 |
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succinyl-CoA(5-)CHEBI:57292 | consumes | succinyl-CoA + NADPH + H(+) => succinate semialdehyde + NADP(+) + CoARHEA:26452 |
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NADPH(4-)CHEBI:57783 | consumes | succinyl-CoA + NADPH + H(+) => succinate semialdehyde + NADP(+) + CoARHEA:26452 |
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hydronCHEBI:15378 | consumes | succinyl-CoA + NADPH + H(+) => succinate semialdehyde + NADP(+) + CoARHEA:26452 |
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succinyl-CoA + NADPH + H(+) => succinate semialdehyde + NADP(+) + CoARHEA:26452 | produces | 4-oxobutanoateCHEBI:57706 |
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succinyl-CoA + NADPH + H(+) => succinate semialdehyde + NADP(+) + CoARHEA:26452 | produces | NADP(3-)CHEBI:58349 |
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succinyl-CoA + NADPH + H(+) => succinate semialdehyde + NADP(+) + CoARHEA:26452 | produces | coenzyme A(4-)CHEBI:57287 |
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4-oxobutanoateCHEBI:57706 | consumes | succinate semialdehyde + NADPH + H(+) => 4-hydroxybutanoate + NADP(+)RHEA:26383 |
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NADPH(4-)CHEBI:57783 | consumes | succinate semialdehyde + NADPH + H(+) => 4-hydroxybutanoate + NADP(+)RHEA:26383 |
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hydronCHEBI:15378 | consumes | succinate semialdehyde + NADPH + H(+) => 4-hydroxybutanoate + NADP(+)RHEA:26383 |
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succinate semialdehyde + NADPH + H(+) => 4-hydroxybutanoate + NADP(+)RHEA:26383 | produces | 4-hydroxybutyrateCHEBI:16724 |
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succinate semialdehyde + NADPH + H(+) => 4-hydroxybutanoate + NADP(+)RHEA:26383 | produces | NADP(3-)CHEBI:58349 |
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4-hydroxybutyrateCHEBI:16724 | consumes | 4-hydroxybutanoate + ATP + CoA => 4-hydroxybutanoyl-CoA + AMP + diphosphateRHEA:23129 |
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ATP(4-)CHEBI:30616 | consumes | 4-hydroxybutanoate + ATP + CoA => 4-hydroxybutanoyl-CoA + AMP + diphosphateRHEA:23129 |
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coenzyme A(4-)CHEBI:57287 | consumes | 4-hydroxybutanoate + ATP + CoA => 4-hydroxybutanoyl-CoA + AMP + diphosphateRHEA:23129 |
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4-hydroxybutanoate + ATP + CoA => 4-hydroxybutanoyl-CoA + AMP + diphosphateRHEA:23129 | produces | 4-hydroxybutyryl-CoA(4-)CHEBI:58574 |
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4-hydroxybutanoate + ATP + CoA => 4-hydroxybutanoyl-CoA + AMP + diphosphateRHEA:23129 | produces | adenosine 5'-monophosphate(2-)CHEBI:456215 |
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4-hydroxybutanoate + ATP + CoA => 4-hydroxybutanoyl-CoA + AMP + diphosphateRHEA:23129 | produces | diphosphate(3-)CHEBI:33019 |
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4-hydroxybutyryl-CoA(4-)CHEBI:58574 | consumes | 4-hydroxybutanoyl-CoA => (2E)-butenoyl-CoA + H2ORHEA:26531 |
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4-hydroxybutanoyl-CoA => (2E)-butenoyl-CoA + H2ORHEA:26531 | produces | crotonoyl-CoA(4-)CHEBI:57332 |
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4-hydroxybutanoyl-CoA => (2E)-butenoyl-CoA + H2ORHEA:26531 | produces | waterCHEBI:15377 |
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crotonoyl-CoA(4-)CHEBI:57332 | consumes | (2E)-butenoyl-CoA + H2O => (3S)-3-hydroxybutanoyl-CoARHEA:26560 |
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waterCHEBI:15377 | consumes | (2E)-butenoyl-CoA + H2O => (3S)-3-hydroxybutanoyl-CoARHEA:26560 |
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(2E)-butenoyl-CoA + H2O => (3S)-3-hydroxybutanoyl-CoARHEA:26560 | produces | (S)-3-hydroxybutanoyl-CoA(4-)CHEBI:57316 |
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(S)-3-hydroxybutanoyl-CoA(4-)CHEBI:57316 | consumes | (3S)-3-hydroxybutanoyl-CoA + NAD(+) => acetoacetyl-CoA + NADH + H(+)RHEA:30800 |
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NAD(1-)CHEBI:57540 | consumes | (3S)-3-hydroxybutanoyl-CoA + NAD(+) => acetoacetyl-CoA + NADH + H(+)RHEA:30800 |
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(3S)-3-hydroxybutanoyl-CoA + NAD(+) => acetoacetyl-CoA + NADH + H(+)RHEA:30800 | produces | acetoacetyl-CoA(4-)CHEBI:57286 |
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(3S)-3-hydroxybutanoyl-CoA + NAD(+) => acetoacetyl-CoA + NADH + H(+)RHEA:30800 | produces | NADH(2-)CHEBI:57945 |
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(3S)-3-hydroxybutanoyl-CoA + NAD(+) => acetoacetyl-CoA + NADH + H(+)RHEA:30800 | produces | hydronCHEBI:15378 |
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acetoacetyl-CoA(4-)CHEBI:57286 | consumes | acetoacetyl-CoA + CoA => 2 acetyl-CoARHEA:21038 |
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coenzyme A(4-)CHEBI:57287 | consumes | acetoacetyl-CoA + CoA => 2 acetyl-CoARHEA:21038 |
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acetoacetyl-CoA + CoA => 2 acetyl-CoARHEA:21038 | produces | acetyl-CoA(4-)CHEBI:57288 |
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CO2 + H2O => hydrogencarbonate + H(+)RHEA:10750 | part_of Auxiliary CO2 hydration supplies bicarbonate. The formal reaction is retained without a molecular-activity category or an unsupported enzyme assignment. | MetaCyc:PWY-5789 |
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hydrogencarbonate + acetyl-CoA + ATP => malonyl-CoA + ADP + phosphate + H(+)RHEA:11309 | part_of The two native biotin half-reactions are represented once by their independently issued net equation. This preserves the measured archaeal holoenzyme without asserting the bacterial BCCP-dimer carrier identity or counting the same turnover twice. | MetaCyc:PWY-5789 |
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malonyl-CoA + NADPH + H(+) => 3-oxopropanoate + NADP(+) + CoARHEA:26448 | part_of | MetaCyc:PWY-5789 |
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3-oxopropanoate + NADPH + H(+) => 3-hydroxypropanoate + NADP(+)RHEA:26440 | part_of | MetaCyc:PWY-5789 |
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3-hydroxypropanoate + ATP + CoA => 3-hydroxypropanoyl-CoA + AMP + diphosphateRHEA:26535 | part_of | MetaCyc:PWY-5789 |
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3-hydroxypropanoyl-CoA => acryloyl-CoA + H2ORHEA:26519 | part_of | MetaCyc:PWY-5789 |
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acryloyl-CoA + NADPH + H(+) => propanoyl-CoA + NADP(+)RHEA:26456 | part_of | MetaCyc:PWY-5789 |
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propanoyl-CoA + hydrogencarbonate + ATP => (S)-methylmalonyl-CoA + ADP + phosphate + H(+)RHEA:23721 | part_of | MetaCyc:PWY-5789 |
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(S)-methylmalonyl-CoA => (R)-methylmalonyl-CoARHEA:20555 | part_of | MetaCyc:PWY-5789 |
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(R)-methylmalonyl-CoA => succinyl-CoARHEA:22889 | part_of The selected methylmalonyl-CoA-to-succinyl-CoA direction follows the autotrophic cycle. The purified enzyme also catalyzes the reverse reaction at a higher measured rate. | MetaCyc:PWY-5789 |
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succinyl-CoA + NADPH + H(+) => succinate semialdehyde + NADP(+) + CoARHEA:26452 | part_of | MetaCyc:PWY-5789 |
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succinate semialdehyde + NADPH + H(+) => 4-hydroxybutanoate + NADP(+)RHEA:26383 | part_of | MetaCyc:PWY-5789 |
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4-hydroxybutanoate + ATP + CoA => 4-hydroxybutanoyl-CoA + AMP + diphosphateRHEA:23129 | part_of | MetaCyc:PWY-5789 |
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4-hydroxybutanoyl-CoA => (2E)-butenoyl-CoA + H2ORHEA:26531 | part_of Native crotonyl-CoA leaves one conserved CoA hydroxyl stereocenter unspecified. The independently issued current Rhea/ChEBI structure is more specific; both sources agree on the trans acyl double bond. This is not an exact structural equivalence assertion. | MetaCyc:PWY-5789 |
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(2E)-butenoyl-CoA + H2O => (3S)-3-hydroxybutanoyl-CoARHEA:26560 | part_of Native crotonyl-CoA leaves one conserved CoA hydroxyl stereocenter unspecified. The independently issued current Rhea/ChEBI structure is more specific; both sources agree on the trans acyl double bond. This is not an exact structural equivalence assertion. | MetaCyc:PWY-5789 |
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(3S)-3-hydroxybutanoyl-CoA + NAD(+) => acetoacetyl-CoA + NADH + H(+)RHEA:30800 | part_of | MetaCyc:PWY-5789 |
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acetoacetyl-CoA + CoA => 2 acetyl-CoARHEA:21038 | part_of | MetaCyc:PWY-5789 |
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acyl CoA carboxylase holoenzymeMetaCyc:CPLX-7580 | has_part Four heterotrimeric units are a supported assembly model from native mass and subunit sequencing, not a high-resolution stoichiometric determination. | acyl CoA carboxylase trimerMetaCyc:CPLX-7575 |
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acyl CoA carboxylase trimerMetaCyc:CPLX-7575 | has_part One copy per heterotrimer. Original gene sequences ground the assignment; the native biotin-carrier and biotin-carboxylase UniProt cross-references are reversed and are not followed. | Biotin carboxylaseUniProtKB:A4YD22 |
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acyl CoA carboxylase trimerMetaCyc:CPLX-7575 | has_part One copy per heterotrimer. Original gene sequences ground the assignment; the native biotin-carrier and biotin-carboxylase UniProt cross-references are reversed and are not followed. | Biotin carboxyl carrier proteinUniProtKB:A4YD23 |
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acyl CoA carboxylase trimerMetaCyc:CPLX-7575 | has_part One copy per heterotrimer. Original gene sequences ground the assignment; the native biotin-carrier and biotin-carboxylase UniProt cross-references are reversed and are not followed. | Acetyl-CoA carboxylase carboxyltransferase subunit alpha / acetyl-CoA carboxylase carboxyltransferase subunit beta / propionyl-CoA carboxylase carboxyltransferase subunitUniProtKB:A4YGI1 |
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malonyl-coenzyme A reductase / succinyl-CoA reductaseMetaCyc:CPLX-7577 | has_part Four subunits follow the curated native complex and approximate native mass. The S. tokodaii recombinant preparation bound RNA, making its own oligomeric estimate ambiguous. | Malonyl CoA reductase (NADP)UniProtKB:A4YEN2 |
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NADP-dependent malonate semialdehyde reductaseMetaCyc:CPLX-7947 | has_part | 3-hydroxypropionate dehydrogenase (NADP(+))UniProtKB:A4YI81 |
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3-hydroxypropionyl-CoA synthetase (AMP-forming)MetaCyc:CPLX-7579 | has_part | 3-hydroxypropionyl-coenzyme A synthetaseUniProtKB:A4YGR1 |
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methylmalonyl-CoA epimeraseMetaCyc:CPLX-8530 | has_part | Methylmalonyl-CoA epimeraseUniProtKB:A4YEG2 |
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methylmalonyl-CoA mutaseMetaCyc:CPLX-7576 | has_part Two copies of this subunit in the primary-supported heterotetramer. The ambiguous nested native dimer hierarchy is not multiplied into an alpha4beta4 assembly. | Methylmalonyl-CoA mutaseUniProtKB:A4YEG1 |
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methylmalonyl-CoA mutaseMetaCyc:CPLX-7576 | has_part Two copies of this subunit in the primary-supported heterotetramer. The ambiguous nested native dimer hierarchy is not multiplied into an alpha4beta4 assembly. | Cobalamin B12-binding domain proteinUniProtKB:A4YIE3 |
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NADPH-dependent succinate semialdehyde reductaseMetaCyc:CPLX-7948 | has_part Two copies describe the native-database and 2009 dimer model. A later recombinant preparation was interpreted as pentameric; the discrepancy is unresolved, not evidence for a universal dimer. Direct reductase experiments override the unrelated current UniProt catalytic annotation. | Msed_1424 succinic semialdehyde reductaseUniProtKB:A4YGN0 |
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acyl CoA carboxylase holoenzymeMetaCyc:CPLX-7580 | catalyzes The same experimentally purified holoenzyme catalyzes both acetyl-CoA and propionyl-CoA carboxylation. | hydrogencarbonate + acetyl-CoA + ATP => malonyl-CoA + ADP + phosphate + H(+)RHEA:11309 |
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acyl CoA carboxylase holoenzymeMetaCyc:CPLX-7580 | catalyzes | propanoyl-CoA + hydrogencarbonate + ATP => (S)-methylmalonyl-CoA + ADP + phosphate + H(+)RHEA:23721 |
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malonyl-coenzyme A reductase / succinyl-CoA reductaseMetaCyc:CPLX-7577 | catalyzes The bifunctional native reductase assignment is retained; cross-species recombinant experiments are not presented as measurements of the selected M. sedula construct. | malonyl-CoA + NADPH + H(+) => 3-oxopropanoate + NADP(+) + CoARHEA:26448 |
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malonyl-coenzyme A reductase / succinyl-CoA reductaseMetaCyc:CPLX-7577 | catalyzes The bifunctional native reductase assignment is retained; cross-species recombinant experiments are not presented as measurements of the selected M. sedula construct. | succinyl-CoA + NADPH + H(+) => succinate semialdehyde + NADP(+) + CoARHEA:26452 |
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NADP-dependent malonate semialdehyde reductaseMetaCyc:CPLX-7947 | catalyzes | 3-oxopropanoate + NADPH + H(+) => 3-hydroxypropanoate + NADP(+)RHEA:26440 |
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3-hydroxypropionyl-CoA synthetase (AMP-forming)MetaCyc:CPLX-7579 | catalyzes The native tetramer and its activity are supported separately. Later recombinant HPCS associated with HPCD; this association is retained as experimental context without assigning the larger assembly to the native homotetramer identifier. | 3-hydroxypropanoate + ATP + CoA => 3-hydroxypropanoyl-CoA + AMP + diphosphateRHEA:26535 |
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methylmalonyl-CoA epimeraseMetaCyc:CPLX-8530 | catalyzes | (S)-methylmalonyl-CoA => (R)-methylmalonyl-CoARHEA:20555 |
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methylmalonyl-CoA mutaseMetaCyc:CPLX-7576 | catalyzes | (R)-methylmalonyl-CoA => succinyl-CoARHEA:22889 |
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NADPH-dependent succinate semialdehyde reductaseMetaCyc:CPLX-7948 | catalyzes The experimentally characterized NADPH reductase is used despite the conflicting current UniProt acetylating-dehydrogenase assignment. | succinate semialdehyde + NADPH + H(+) => 4-hydroxybutanoate + NADP(+)RHEA:26383 |
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3-hydroxypropionyl-coenzyme A dehydrataseUniProtKB:A4YI89 | enables Functional activity is supported directly. The earlier recombinant preparation was interpreted as monomeric, whereas the later preparation was interpreted as octameric. The source difference is unresolved and monomer sufficiency is not asserted. | 3-hydroxypropanoyl-CoA => acryloyl-CoA + H2ORHEA:26519 |
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3-hydroxypropionyl-coenzyme A dehydrataseUniProtKB:A4YI89 | enables This newer experimentally supported assignment supersedes the older exclusive Msed_0399 pathway assignment. The percentage is a kinetic/proteomic estimate, not a direct flux or knockout measurement. | (2E)-butenoyl-CoA + H2O => (3S)-3-hydroxybutanoyl-CoARHEA:26560 |
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Acryloyl-coenzyme A reductaseUniProtKB:A4YGN2 | enables Native peptide identification and later recombinant Msed_1426 assays support the activity directly. The 2009 detailed recombinant experiment used S. tokodaii; the later selected-protein preparation required coexpression with Msed_1424, without positive two-hybrid evidence for an ACR/SSR complex. | acryloyl-CoA + NADPH + H(+) => propanoyl-CoA + NADP(+)RHEA:26456 |
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4-hydroxybutyrate--CoA ligase 1UniProtKB:A4YDT1 | enables A measured functional role with no claim of monomer sufficiency or an independently established assembly. | 4-hydroxybutanoate + ATP + CoA => 4-hydroxybutanoyl-CoA + AMP + diphosphateRHEA:23129 |
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Vinylacetyl-CoA Delta-isomeraseUniProtKB:A4YGC7 | enables The protein enables the reaction as a functional role; the apparent tetramer is retained as experimental context. The enzyme was less oxygen-sensitive than the clostridial homolog under the tested conditions. | 4-hydroxybutanoyl-CoA => (2E)-butenoyl-CoA + H2ORHEA:26531 |
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3-hydroxyacyl-CoA dehydrogenaseUniProtKB:A4YGM9 | enables The measured primary reassignment is retained separately from the older native Msed_0399-only assignment; no physical assembly or monomer sufficiency is asserted. | (3S)-3-hydroxybutanoyl-CoA + NAD(+) => acetoacetyl-CoA + NADH + H(+)RHEA:30800 |
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Acetyl-CoA acetyltransferaseUniProtKB:A4YEH9 | enables Functional thiolase role in the complete four-enzyme reconstitution; the selected cleavage equation produces two acetyl-CoA molecules. | acetoacetyl-CoA + CoA => 2 acetyl-CoARHEA:21038 |
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4-hydroxybutyrate--CoA ligase 2UniProtKB:A4YDR9 | enables An experimentally measured alternative activity, with weaker evidence for major cycle flux than Msed_0406; the two proteins are not assigned equal physiological contribution. | 4-hydroxybutanoate + ATP + CoA => 4-hydroxybutanoyl-CoA + AMP + diphosphateRHEA:23129 |
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3-hydroxyacyl-CoA dehydrogenase, NAD-binding proteinUniProtKB:A4YDS4 | enables A retained measured alternative. Later work identifies Msed_2001 and Msed_1423 as the principal hydratase and dehydrogenase, respectively; activity does not establish exclusive physiological responsibility. | (2E)-butenoyl-CoA + H2O => (3S)-3-hydroxybutanoyl-CoARHEA:26560 |
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3-hydroxyacyl-CoA dehydrogenase, NAD-binding proteinUniProtKB:A4YDS4 | enables A retained measured alternative. Later work identifies Msed_2001 and Msed_1423 as the principal hydratase and dehydrogenase, respectively; activity does not establish exclusive physiological responsibility. | (3S)-3-hydroxybutanoyl-CoA + NAD(+) => acetoacetyl-CoA + NADH + H(+)RHEA:30800 |
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Enoyl-CoA hydratase/isomeraseUniProtKB:A4YDL1 | enables Alternative measured hydratase activity, not an equally supported principal cycle enzyme or a defined assembly. Later proteomic/kinetic estimates favor Msed_2001. | (2E)-butenoyl-CoA + H2O => (3S)-3-hydroxybutanoyl-CoARHEA:26560 |
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Short chain enoyl-CoA hydrataseUniProtKB:A4YDQ9 | enables Alternative measured hydratase activity, not an equally supported principal cycle enzyme or a defined assembly. Later proteomic/kinetic estimates favor Msed_2001. | (2E)-butenoyl-CoA + H2O => (3S)-3-hydroxybutanoyl-CoARHEA:26560 |
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3-hydroxyacyl-CoA dehydrogenaseUniProtKB:A4YDR4 | enables Measured alternative activity; genomic context favors beta-oxidation rather than a dominant HP/HB cycle role. No obligatory cycle flux or assembly is asserted. | (3S)-3-hydroxybutanoyl-CoA + NAD(+) => acetoacetyl-CoA + NADH + H(+)RHEA:30800 |
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Biotin carboxyl carrier proteinUniProtKB:A4YD23 | has_cofactor Covalently attached biotin prosthetic group on the carrier subunit, not a free biotin reactant in the net carboxylation equation. | biotinateCHEBI:57586 |
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acyl CoA carboxylase holoenzymeMetaCyc:CPLX-7580 | has_cofactor Direct divalent-ion dependence and MgATP assay support. Other divalent ions partly substitute; this does not specify a permanent bound-magnesium stoichiometry. | magnesium(2+)CHEBI:18420 |
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NADPH-dependent succinate semialdehyde reductaseMetaCyc:CPLX-7948 | has_cofactor Two zinc sites per monomer are inferred from metal content and conserved motifs; adding zinc did not stimulate the already loaded preparation. | zinc(2+)CHEBI:29105 |
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Acryloyl-coenzyme A reductaseUniProtKB:A4YGN2 | has_cofactor The zinc requirement is inferred for the selected M. sedula protein; the detailed recombinant experiment used the S. tokodaii homolog. | zinc(2+)CHEBI:29105 |
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methylmalonyl-CoA epimeraseMetaCyc:CPLX-8530 | has_cofactor One of the experimentally tested alternative activating metals, not evidence that all three bind simultaneously or are equally physiological. | magnesium(2+)CHEBI:18420 |
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methylmalonyl-CoA epimeraseMetaCyc:CPLX-8530 | has_cofactor One of the experimentally tested alternative activating metals, not evidence that all three bind simultaneously or are equally physiological. | cobalt(2+)CHEBI:48828 |
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methylmalonyl-CoA epimeraseMetaCyc:CPLX-8530 | has_cofactor One of the experimentally tested alternative activating metals, not evidence that all three bind simultaneously or are equally physiological. | nickel(2+)CHEBI:49786 |
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methylmalonyl-CoA mutaseMetaCyc:CPLX-7576 | has_cofactor Adenosylcobalamin belongs to the mutase complex, rather than a free cobalt-ion substitution. | cobamamideCHEBI:18408 |
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Vinylacetyl-CoA Delta-isomeraseUniProtKB:A4YGC7 | has_cofactor Curated database cofactor identity; the cluster identifier is not an experimental oxidation-state determination. The cited 2007 discovery paper was not available as inspected full text, and the 2014 activity assay is not treated as direct measurement of cofactor occupancy. | FAD(3-)CHEBI:57692 |
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Vinylacetyl-CoA Delta-isomeraseUniProtKB:A4YGC7 | has_cofactor Curated database cofactor identity; the cluster identifier is not an experimental oxidation-state determination. The cited 2007 discovery paper was not available as inspected full text, and the 2014 activity assay is not treated as direct measurement of cofactor occupancy. | tetra-mu3-sulfido-tetrairon(0)CHEBI:33725 |
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4-hydroxybutyrate--CoA ligase 1UniProtKB:A4YDT1 | has_cofactor Similarity-based alternative divalent cofactor annotation; no selected-protein binding stoichiometry is asserted. | magnesium(2+)CHEBI:18420 |
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4-hydroxybutyrate--CoA ligase 1UniProtKB:A4YDT1 | has_cofactor Similarity-based alternative divalent cofactor annotation; no selected-protein binding stoichiometry is asserted. | manganese(2+)CHEBI:29035 |
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4-hydroxybutyrate--CoA ligase 2UniProtKB:A4YDR9 | has_cofactor Similarity-based alternative divalent cofactor annotation; no selected-protein binding stoichiometry is asserted. | magnesium(2+)CHEBI:18420 |
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4-hydroxybutyrate--CoA ligase 2UniProtKB:A4YDR9 | has_cofactor Similarity-based alternative divalent cofactor annotation; no selected-protein binding stoichiometry is asserted. | manganese(2+)CHEBI:29035 |
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malonyl-CoA(5-)CHEBI:57384 | inhibits In vitro inhibition under the reported MgATP assay conditions. An intracellular regulatory effect at physiological concentrations is not established. | acyl CoA carboxylase holoenzymeMetaCyc:CPLX-7580 |
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succinyl-CoA(5-)CHEBI:57292 | inhibits In vitro inhibition under the reported MgATP assay conditions. An intracellular regulatory effect at physiological concentrations is not established. | acyl CoA carboxylase holoenzymeMetaCyc:CPLX-7580 |
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coenzyme A(4-)CHEBI:57287 | inhibits In vitro inhibition under the reported MgATP assay conditions. An intracellular regulatory effect at physiological concentrations is not established. | acyl CoA carboxylase holoenzymeMetaCyc:CPLX-7580 |
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ADP(3-)CHEBI:456216 | inhibits In vitro inhibition under the reported MgATP assay conditions. An intracellular regulatory effect at physiological concentrations is not established. | acyl CoA carboxylase holoenzymeMetaCyc:CPLX-7580 |
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hydrogencarbonate + acetyl-CoA + ATP => malonyl-CoA + ADP + phosphate + H(+)RHEA:11309 | provides_input_for Shared CHEBI:57384 supplies material continuity in the source-defined cycle; the graph does not assert that this is the only metabolic fate of the intermediate. | malonyl-CoA + NADPH + H(+) => 3-oxopropanoate + NADP(+) + CoARHEA:26448 |
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malonyl-CoA + NADPH + H(+) => 3-oxopropanoate + NADP(+) + CoARHEA:26448 | provides_input_for Shared CHEBI:33190 supplies material continuity in the source-defined cycle; the graph does not assert that this is the only metabolic fate of the intermediate. | 3-oxopropanoate + NADPH + H(+) => 3-hydroxypropanoate + NADP(+)RHEA:26440 |
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3-oxopropanoate + NADPH + H(+) => 3-hydroxypropanoate + NADP(+)RHEA:26440 | provides_input_for Shared CHEBI:16510 supplies material continuity in the source-defined cycle; the graph does not assert that this is the only metabolic fate of the intermediate. | 3-hydroxypropanoate + ATP + CoA => 3-hydroxypropanoyl-CoA + AMP + diphosphateRHEA:26535 |
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3-hydroxypropanoate + ATP + CoA => 3-hydroxypropanoyl-CoA + AMP + diphosphateRHEA:26535 | provides_input_for Shared CHEBI:58528 supplies material continuity in the source-defined cycle; the graph does not assert that this is the only metabolic fate of the intermediate. | 3-hydroxypropanoyl-CoA => acryloyl-CoA + H2ORHEA:26519 |
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3-hydroxypropanoyl-CoA => acryloyl-CoA + H2ORHEA:26519 | provides_input_for Shared CHEBI:57367 supplies material continuity in the source-defined cycle; the graph does not assert that this is the only metabolic fate of the intermediate. | acryloyl-CoA + NADPH + H(+) => propanoyl-CoA + NADP(+)RHEA:26456 |
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acryloyl-CoA + NADPH + H(+) => propanoyl-CoA + NADP(+)RHEA:26456 | provides_input_for Shared CHEBI:57392 supplies material continuity in the source-defined cycle; the graph does not assert that this is the only metabolic fate of the intermediate. | propanoyl-CoA + hydrogencarbonate + ATP => (S)-methylmalonyl-CoA + ADP + phosphate + H(+)RHEA:23721 |
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propanoyl-CoA + hydrogencarbonate + ATP => (S)-methylmalonyl-CoA + ADP + phosphate + H(+)RHEA:23721 | provides_input_for Shared CHEBI:57327 supplies material continuity in the source-defined cycle; the graph does not assert that this is the only metabolic fate of the intermediate. | (S)-methylmalonyl-CoA => (R)-methylmalonyl-CoARHEA:20555 |
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(S)-methylmalonyl-CoA => (R)-methylmalonyl-CoARHEA:20555 | provides_input_for Shared CHEBI:57326 supplies material continuity in the source-defined cycle; the graph does not assert that this is the only metabolic fate of the intermediate. | (R)-methylmalonyl-CoA => succinyl-CoARHEA:22889 |
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(R)-methylmalonyl-CoA => succinyl-CoARHEA:22889 | provides_input_for Shared CHEBI:57292 supplies material continuity in the source-defined cycle; the graph does not assert that this is the only metabolic fate of the intermediate. | succinyl-CoA + NADPH + H(+) => succinate semialdehyde + NADP(+) + CoARHEA:26452 |
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succinyl-CoA + NADPH + H(+) => succinate semialdehyde + NADP(+) + CoARHEA:26452 | provides_input_for Shared CHEBI:57706 supplies material continuity in the source-defined cycle; the graph does not assert that this is the only metabolic fate of the intermediate. | succinate semialdehyde + NADPH + H(+) => 4-hydroxybutanoate + NADP(+)RHEA:26383 |
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succinate semialdehyde + NADPH + H(+) => 4-hydroxybutanoate + NADP(+)RHEA:26383 | provides_input_for Shared CHEBI:16724 supplies material continuity in the source-defined cycle; the graph does not assert that this is the only metabolic fate of the intermediate. | 4-hydroxybutanoate + ATP + CoA => 4-hydroxybutanoyl-CoA + AMP + diphosphateRHEA:23129 |
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4-hydroxybutanoate + ATP + CoA => 4-hydroxybutanoyl-CoA + AMP + diphosphateRHEA:23129 | provides_input_for Shared CHEBI:58574 supplies material continuity in the source-defined cycle; the graph does not assert that this is the only metabolic fate of the intermediate. | 4-hydroxybutanoyl-CoA => (2E)-butenoyl-CoA + H2ORHEA:26531 |
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4-hydroxybutanoyl-CoA => (2E)-butenoyl-CoA + H2ORHEA:26531 | provides_input_for Shared CHEBI:57332 supplies material continuity in the source-defined cycle; the graph does not assert that this is the only metabolic fate of the intermediate. | (2E)-butenoyl-CoA + H2O => (3S)-3-hydroxybutanoyl-CoARHEA:26560 |
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(2E)-butenoyl-CoA + H2O => (3S)-3-hydroxybutanoyl-CoARHEA:26560 | provides_input_for Shared CHEBI:57316 supplies material continuity in the source-defined cycle; the graph does not assert that this is the only metabolic fate of the intermediate. | (3S)-3-hydroxybutanoyl-CoA + NAD(+) => acetoacetyl-CoA + NADH + H(+)RHEA:30800 |
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(3S)-3-hydroxybutanoyl-CoA + NAD(+) => acetoacetyl-CoA + NADH + H(+)RHEA:30800 | provides_input_for Shared CHEBI:57286 supplies material continuity in the source-defined cycle; the graph does not assert that this is the only metabolic fate of the intermediate. | acetoacetyl-CoA + CoA => 2 acetyl-CoARHEA:21038 |
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acetoacetyl-CoA + CoA => 2 acetyl-CoARHEA:21038 | provides_input_for Shared CHEBI:57288 supplies material continuity in the source-defined cycle; the graph does not assert that this is the only metabolic fate of the intermediate. | hydrogencarbonate + acetyl-CoA + ATP => malonyl-CoA + ADP + phosphate + H(+)RHEA:11309 |
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CO2 + H2O => hydrogencarbonate + H(+)RHEA:10750 | provides_input_for Shared CHEBI:17544 supplies material continuity in the source-defined cycle; the graph does not assert that this is the only metabolic fate of the intermediate. | hydrogencarbonate + acetyl-CoA + ATP => malonyl-CoA + ADP + phosphate + H(+)RHEA:11309 |
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CO2 + H2O => hydrogencarbonate + H(+)RHEA:10750 | provides_input_for Shared CHEBI:17544 supplies material continuity in the source-defined cycle; the graph does not assert that this is the only metabolic fate of the intermediate. | propanoyl-CoA + hydrogencarbonate + ATP => (S)-methylmalonyl-CoA + ADP + phosphate + H(+)RHEA:23721 |
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References
MetaCyc:PWY-5789MetaCyc PWY-5789 full native pathway XML (source version: MetaCyc 22.5; original XML)MetaCyc:RXN0-5224MetaCyc RXN0-5224 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:BIOTIN-CARBOXYL-RXNMetaCyc BIOTIN-CARBOXYL-RXN native XML (source version: MetaCyc 22.5; original XML)MetaCyc:RXN0-5055MetaCyc RXN0-5055 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:RXN-8963MetaCyc RXN-8963 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:RXN-8974MetaCyc RXN-8974 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:RXN-9086MetaCyc RXN-9086 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:RXN-6383MetaCyc RXN-6383 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:RXN-9087MetaCyc RXN-9087 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:PROPIONYL-COA-CARBOXY-RXNMetaCyc PROPIONYL-COA-CARBOXY-RXN native XML (source version: MetaCyc 22.5; original XML)MetaCyc:METHYLMALONYL-COA-EPIM-RXNMetaCyc METHYLMALONYL-COA-EPIM-RXN native XML (source version: MetaCyc 22.5; original XML)MetaCyc:METHYLMALONYL-COA-MUT-RXNMetaCyc METHYLMALONYL-COA-MUT-RXN native XML (source version: MetaCyc 22.5; original XML)MetaCyc:RXN-8891MetaCyc RXN-8891 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:RXN-11002MetaCyc RXN-11002 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:RXN-9092MetaCyc RXN-9092 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:RXN-8890MetaCyc RXN-8890 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:RXN-11667MetaCyc RXN-11667 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:RXN-11662MetaCyc RXN-11662 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:ACETYL-COA-ACETYLTRANSFER-RXNMetaCyc ACETYL-COA-ACETYLTRANSFER-RXN native XML (source version: MetaCyc 22.5; original XML)RHEA:10750Rhea 10750 directed reaction (source version: 142 (2026-09-02); complete compressed RDF body)RHEA:11309Rhea 11309 directed reaction (source version: 142 (2026-09-02); complete compressed RDF body)RHEA:26448Rhea 26448 directed reaction (source version: 142 (2026-09-02); complete compressed RDF body)RHEA:26440Rhea 26440 directed reaction (source version: 142 (2026-09-02); complete compressed RDF body)RHEA:26535Rhea 26535 directed reaction (source version: 142 (2026-09-02); complete compressed RDF body)RHEA:26519Rhea 26519 directed reaction (source version: 142 (2026-09-02); complete compressed RDF body)RHEA:26456Rhea 26456 directed reaction (source version: 142 (2026-09-02); complete compressed RDF body)RHEA:23721Rhea 23721 directed reaction (source version: 142 (2026-09-02); complete compressed RDF body)RHEA:20555Rhea 20555 directed reaction (source version: 142 (2026-09-02); complete compressed RDF body)RHEA:22889Rhea 22889 directed reaction (source version: 142 (2026-09-02); complete compressed RDF body)RHEA:26452Rhea 26452 directed reaction (source version: 142 (2026-09-02); complete compressed RDF body)RHEA:26383Rhea 26383 directed reaction (source version: 142 (2026-09-02); complete compressed RDF body)RHEA:23129Rhea 23129 directed reaction (source version: 142 (2026-09-02); complete compressed RDF body)RHEA:26531Rhea 26531 directed reaction (source version: 142 (2026-09-02); complete compressed RDF body)RHEA:26560Rhea 26560 directed reaction (source version: 142 (2026-09-02); complete compressed RDF body)RHEA:30800Rhea 30800 directed reaction (source version: 142 (2026-09-02); complete compressed RDF body)RHEA:21038Rhea 21038 directed reaction (source version: 142 (2026-09-02); complete compressed RDF body)UniProtKB:A4YD22UniProtKB A4YD22 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YD23UniProtKB A4YD23 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YGI1UniProtKB A4YGI1 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YEN2UniProtKB A4YEN2 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YI81UniProtKB A4YI81 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YGR1UniProtKB A4YGR1 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YI89UniProtKB A4YI89 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YGN2UniProtKB A4YGN2 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YEG2UniProtKB A4YEG2 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YEG1UniProtKB A4YEG1 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YIE3UniProtKB A4YIE3 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YGN0UniProtKB A4YGN0 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YDT1UniProtKB A4YDT1 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YGC7UniProtKB A4YGC7 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YGM9UniProtKB A4YGM9 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YEH9UniProtKB A4YEH9 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YDR9UniProtKB A4YDR9 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YDS4UniProtKB A4YDS4 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YDL1UniProtKB A4YDL1 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YDQ9UniProtKB A4YDQ9 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)UniProtKB:A4YDR4UniProtKB A4YDR4 original complete-entry search response (source version: 2026_03 (2026-09-02); hash of retained complete multi-entry query response, selected by primaryAccession)PMID:12581213Characterization of acetyl-CoA/propionyl-CoA carboxylase in Metallosphaera sedula (source version: 2003; retained tool-rendered public publisher full text; hash covers JSON tool representation, NOT original HTML)PMID:19684143Malonic Semialdehyde Reductase, Succinic Semialdehyde Reductase, and Succinyl-Coenzyme A Reductase from Metallosphaera sedula : Enzymes of the Autotrophic 3-Hydroxypropionate/4-Hydroxybutyrate Cycle in Sulfolobales ▿ (source version: Original full-text PMC HTML; acquired 2026-10-11)PMID:194296103-Hydroxypropionyl-Coenzyme A Dehydratase and Acryloyl-Coenzyme A Reductase, Enzymes of the Autotrophic 3-Hydroxypropionate/4-Hydroxybutyrate Cycle in the Sulfolobales ▿ (source version: Original full-text PMC HTML; acquired 2026-10-11)PMID:21169486Labeling and Enzyme Studies of the Central Carbon Metabolism in Metallosphaera sedula ▿ (source version: Original full-text PMC HTML; acquired 2026-10-11)PMID:33472982Convergent Evolution of a Promiscuous 3-Hydroxypropionyl-CoA Dehydratase/Crotonyl-CoA Hydratase in Crenarchaeota and Thaumarchaeota (source version: Original full-text PMC HTML; acquired 2026-10-11)PMID:22752162Epimerase (Msed_0639) and Mutase (Msed_0638 and Msed_2055) Convert ( S )-Methylmalonyl-Coenzyme A (CoA) to Succinyl-CoA in the Metallosphaera sedula 3-Hydroxypropionate/4-Hydroxybutyrate Cycle (source version: Original full-text PMC HTML; acquired 2026-10-11)PMID:23258541Role of 4-Hydroxybutyrate-CoA Synthetase in the CO 2 Fixation Cycle in Thermoacidophilic Archaea * (source version: Original full-text PMC HTML; acquired 2026-10-11)PMID:24532060Conversion of 4-Hydroxybutyrate to Acetyl Coenzyme A and Its Anapleurosis in the Metallosphaera sedula 3-Hydroxypropionate/4-Hydroxybutyrate Carbon Fixation Pathway (source version: Original full-text PMC HTML; acquired 2026-10-11)PMID:32218776Enzymes Catalyzing Crotonyl-CoA Conversion to Acetoacetyl-CoA During the Autotrophic CO2 Fixation in Metallosphaera sedula (source version: Original full-text JATS XML; acquired 2026-10-11)PMID:17041055Malonyl-Coenzyme A Reductase in the Modified 3-Hydroxypropionate Cycle for Autotrophic Carbon Fixation in Archaeal Metallosphaera and Sulfolobus spp. ▿ (source version: Original full-text PMC HTML; acquired 2026-10-11)PMID:181653103-Hydroxypropionyl-Coenzyme A Synthetase from Metallosphaera sedula , an Enzyme Involved in Autotrophic CO 2 Fixation ▿ (source version: Original full-text PMC HTML; acquired 2026-10-11)PMID:21169482Identification of Missing Genes and Enzymes for Autotrophic Carbon Fixation in Crenarchaeota ▿ † (source version: Original full-text PMC HTML; acquired 2026-10-11)PMID:27771364Reaction Kinetic Analysis of the 3-Hydroxypropionate/4-Hydroxybutyrate CO 2 Fixation Cycle in Extremely Thermoacidophilic Archaea (source version: Original full-text PMC HTML; acquired 2026-10-11)NCBIProtein:AAO15571.1Original archaeal carboxylase CDS AAO15571.1 (source version: Original ENA EMBL nucleotide record with CDS translation)NCBIProtein:AAO15572.1Original archaeal carboxylase CDS AAO15572.1 (source version: Original ENA EMBL nucleotide record with CDS translation)NCBIProtein:AAO15573.1Original archaeal carboxylase CDS AAO15573.1 (source version: Original ENA EMBL nucleotide record with CDS translation)MetaCyc:CPLX-7580MetaCyc CPLX-7580 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:CPLX-7575MetaCyc CPLX-7575 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:CPLX-7577MetaCyc CPLX-7577 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:CPLX-7947MetaCyc CPLX-7947 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:CPLX-7579MetaCyc CPLX-7579 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:CPLX-8530MetaCyc CPLX-8530 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:CPLX-7576MetaCyc CPLX-7576 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:CPLX-7948MetaCyc CPLX-7948 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:MONOMER-13717MetaCyc MONOMER-13717 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:MONOMER-13716MetaCyc MONOMER-13716 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:MONOMER-13718MetaCyc MONOMER-13718 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:MONOMER-13726MetaCyc MONOMER-13726 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:MONOMER-13727MetaCyc MONOMER-13727 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:MONOMER-13728MetaCyc MONOMER-13728 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:MONOMER-13731MetaCyc MONOMER-13731 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:MONOMER-13732MetaCyc MONOMER-13732 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:MONOMER-13733MetaCyc MONOMER-13733 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:MONOMER-13734MetaCyc MONOMER-13734 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:ENZRXN-14657MetaCyc ENZRXN-14657 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:ENZRXN-14658MetaCyc ENZRXN-14658 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:ENZRXN-14667MetaCyc ENZRXN-14667 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:ENZRXN-14674MetaCyc ENZRXN-14674 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:ENZRXN-14668MetaCyc ENZRXN-14668 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:ENZRXN-14669MetaCyc ENZRXN-14669 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:ENZRXN-14672MetaCyc ENZRXN-14672 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:ENZRXN-14673MetaCyc ENZRXN-14673 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:ENZRXN-14675MetaCyc ENZRXN-14675 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:ENZRXN-14670MetaCyc ENZRXN-14670 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:ENZRXN-14676MetaCyc ENZRXN-14676 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:ENZRXN-14678MetaCyc ENZRXN-14678 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:ENZRXN-14681MetaCyc ENZRXN-14681 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:ENZRXN-14679MetaCyc ENZRXN-14679 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:ENZRXN-14680MetaCyc ENZRXN-14680 native XML (source version: MetaCyc 22.5; original XML)MetaCyc:BIOTINMetaCyc BIOTIN native XML (source version: MetaCyc 22.5; original XML)MetaCyc:FADMetaCyc FAD native XML (source version: MetaCyc 22.5; original XML)MetaCyc:CPD-7MetaCyc CPD-7 native XML (source version: MetaCyc 22.5; original XML)
Curation history
- codex
- CREATE — Add 3-hydroxypropanoate/4-hydroxybutanate cycle
Curated the complete Metallosphaera sedula hydroxypropionate/hydroxybutyrate cycle with 17 directed activities accounting for all 18 native objects; original sequence evidence corrects swapped native subunit cross-references and conflicting assembly and activity annotations remain explicit. Maintained record MetaCyc:PWY-5789; creation bytes SHA256 4064577a2f20c35cefbc838b5065f053c4cfe175ef113b6b782d3f712cfcd823. Original-source projections, replay and identifier decisions are in research/pathway_additions/2026-10-11-next-206/. 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 3-hydroxypropanoate/4-hydroxybutanate cycle
- codex
- EDIT — Correct HP/HB primary title and three source locators
Replaced the contaminated PMID32218776 title with the exact original JATS front title and pointed three terminal-module assertions to their named-activity/reconstitution Results paragraphs. All other parsed record fields, including all reaction, protein and strain qualifications, remain unchanged. Exact prior/final bytes and source checks are retained in research/pathway_additions/2026-10-11-next-206/hphb-provenance-fix.json and review-correction-audit.json. Final record SHA256 6a85a549351ff95acd904261afac28bfe5712e553efbd41b3e4bd40ebbcb080a. Initial review bundles and inspected input archives are preserved. This event records the supported edit and author checks; independent successor disposition and final coordinated repository gates are subsequent checks.
- EDIT — Correct HP/HB primary title and three source locators