L-proline degradation
gomodel:YeastPathways_PROUT-PWY
L-proline degradation in Saccharomyces cerevisiae S288C oxidizes L-proline to (S)-1-pyrroline-5-carboxylate, hydrates that intermediate to L-glutamic 5-semialdehyde, and oxidizes it to L-glutamate.
- Pathway type
- amino acid degradation
- Organism scope
Pathway network
20 nodes · 25 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
- Cell / process context
- Solid arrow: mechanistic relation
- Dashed arrow: membership, location or cofactor relation
Components and activities
| Node | Kind or role | Source direction |
|---|---|---|
Saccharomyces cerevisiae S288CNCBITaxon:559292 | taxon | |
L-proline catabolic processGO:0006562 | biological process | |
NADH(2-)CHEBI:57945 | small molecule | |
hydronCHEBI:15378 | small molecule | |
cytosolGO:0005829 | cellular component | |
PUT1 ScerSGD:S000004132 | protein | |
hydroquinoneCHEBI:17594 | small molecule | |
(S)-1-pyrroline-5-carboxylateCHEBI:17388 | small molecule | |
waterCHEBI:15377 | small molecule | |
L-proline zwitterionCHEBI:60039 | small molecule | |
PUT2 ScerSGD:S000001079 | protein | |
quinoneCHEBI:36141 | small molecule | |
L-glutamic 5-semialdehyde zwitterionCHEBI:58066 | small molecule | |
NAD(1-)CHEBI:57540 | small molecule | |
L-glutamate(1-)CHEBI:29985 | small molecule | |
mitochondrial matrixGO:0005759 | cellular component | |
mitochondrial inner membraneGO:0005743 | cellular component | |
FAD(3-)CHEBI:57692 | cofactor | |
L-glutamate gamma-semialdehyde dehydrogenase (NAD+) activitygomodel:RXN-14116 | molecular activity | |
proline dehydrogenase activitygomodel:RXN-14903 | molecular activity | |
(S)-1-pyrroline-5-carboxylate + H+ + H2O <-> L-glutamate-5-semialdehydegomodel:SPONTPRO-RXN | molecular activity |
Mechanistic edges
| Subject | Predicate and description | Object | Evidence |
|---|---|---|---|
(S)-1-pyrroline-5-carboxylate + H+ + H2O <-> L-glutamate-5-semialdehydegomodel:SPONTPRO-RXN | part_of | L-proline catabolic processGO:0006562 |
|
L-glutamate gamma-semialdehyde dehydrogenase (NAD+) activitygomodel:RXN-14116 | has_output | NADH(2-)CHEBI:57945 |
|
L-glutamate gamma-semialdehyde dehydrogenase (NAD+) activitygomodel:RXN-14116 | has_output | hydronCHEBI:15378 |
|
PUT1 ScerSGD:S000004132 | enables | proline dehydrogenase activitygomodel:RXN-14903 |
|
(S)-1-pyrroline-5-carboxylate + H+ + H2O <-> L-glutamate-5-semialdehydegomodel:SPONTPRO-RXN | has_input | hydronCHEBI:15378 |
|
proline dehydrogenase activitygomodel:RXN-14903 | has_output | hydroquinoneCHEBI:17594 |
|
(S)-1-pyrroline-5-carboxylate + H+ + H2O <-> L-glutamate-5-semialdehydegomodel:SPONTPRO-RXN | has_input | (S)-1-pyrroline-5-carboxylateCHEBI:17388 |
|
L-glutamate gamma-semialdehyde dehydrogenase (NAD+) activitygomodel:RXN-14116 | has_input | waterCHEBI:15377 |
|
(S)-1-pyrroline-5-carboxylate + H+ + H2O <-> L-glutamate-5-semialdehydegomodel:SPONTPRO-RXN | has_input | waterCHEBI:15377 |
|
L-glutamate gamma-semialdehyde dehydrogenase (NAD+) activitygomodel:RXN-14116 | part_of | L-proline catabolic processGO:0006562 |
|
(S)-1-pyrroline-5-carboxylate + H+ + H2O <-> L-glutamate-5-semialdehydegomodel:SPONTPRO-RXN | occurs_in | cytosolGO:0005829 |
|
proline dehydrogenase activitygomodel:RXN-14903 | has_output | hydronCHEBI:15378 |
|
proline dehydrogenase activitygomodel:RXN-14903 | has_input | L-proline zwitterionCHEBI:60039 |
|
proline dehydrogenase activitygomodel:RXN-14903 | causally_upstream_of | L-glutamate gamma-semialdehyde dehydrogenase (NAD+) activitygomodel:RXN-14116 |
|
PUT2 ScerSGD:S000001079 | enables | L-glutamate gamma-semialdehyde dehydrogenase (NAD+) activitygomodel:RXN-14116 |
|
proline dehydrogenase activitygomodel:RXN-14903 | has_input | quinoneCHEBI:36141 |
|
(S)-1-pyrroline-5-carboxylate + H+ + H2O <-> L-glutamate-5-semialdehydegomodel:SPONTPRO-RXN | has_output | L-glutamic 5-semialdehyde zwitterionCHEBI:58066 |
|
L-glutamate gamma-semialdehyde dehydrogenase (NAD+) activitygomodel:RXN-14116 | has_input | NAD(1-)CHEBI:57540 |
|
proline dehydrogenase activitygomodel:RXN-14903 | has_output | (S)-1-pyrroline-5-carboxylateCHEBI:17388 |
|
L-glutamate gamma-semialdehyde dehydrogenase (NAD+) activitygomodel:RXN-14116 | has_output | L-glutamate(1-)CHEBI:29985 |
|
L-glutamate gamma-semialdehyde dehydrogenase (NAD+) activitygomodel:RXN-14116 | has_input | L-glutamic 5-semialdehyde zwitterionCHEBI:58066 |
|
proline dehydrogenase activitygomodel:RXN-14903 | part_of | L-proline catabolic processGO:0006562 |
|
PUT1 ScerSGD:S000004132 | located_in Physical protein location from reviewed UniProt. evidence code not specified by source | mitochondrial matrixGO:0005759 |
|
PUT2 ScerSGD:S000001079 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:11502169) | mitochondrial inner membraneGO:0005743 |
|
PUT1 ScerSGD:S000004132 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: not specified | FAD(3-)CHEBI:57692 |
|
References
gomodel:YeastPathways_PROUT-PWYGO-CAM L-proline degradation model YeastPathways_PROUT-PWY (source version: Pinned Noctua JSON archive; model date 2026-07-23; member ./YeastPathways_PROUT-PWY.json)UniProtKB:P09368Reviewed UniProtKB P09368 location annotations (source version: UniProt release 2026_03)UniProtKB:P07275Reviewed UniProtKB P07275 location annotations (source version: UniProt release 2026_03)
Curation history
- Codex; review-causal-graph; Reviewed every native GO-CAM fact; preserved precise input/output, causal, location, membership and complex-part relations with traceable structured source evidence. Kept distinct generic physical instances and recorded source-scope exclusions in the cohort review ledger.
- Codex
- EDIT — Audit causal activity compartments and preserve scoped protein location evidence
Reviewed all 3 activity location assignments and 2 mapped physical proteins against reviewed S288C UniProt release2026_03 location/function/caution batch SHA256 95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d. Added 2 independently supported location edges and quarantined 2 generic cytosol source assertions. Mapped physical protein locations via exact SGD cross-references; retained source ECO grades, molecular form and conditional notes. Physical protein location alone never generates activity location. Explicitly inspected functional assertions support bounded activity projections. Every original activity location and exclusion is recorded in reports/causal_graph_review/gocam-location-review.json. No independent location annotation is treated as an evidence gap, not a negative result. Cytoplasm is not narrowed to cytosol. Microsome fractions are not projected as in-vivo organelles. Semantic validation passed all85 records;4 independent source-role acceptance tests passed.
- EDIT — Audit causal activity compartments and preserve scoped protein location evidence