threonine degradation
gomodel:YeastPathways_THREOCAT2-PWY
Threonine degradation in Saccharomyces cerevisiae S288C includes CHA1-enabled threonine deamination to 2-oxobutanoate and the GLY1 threonine aldolase route to glycine and acetaldehyde. The broader native outline contains unassigned or neighbouring reactions; KBL is absent and threonine dehydrogenase is uncertain in yeast. An unsupported reverse cystathionine-condensation branch is excluded.
- Pathway type
- amino acid degradation
- Organism scope
Pathway network
14 nodes · 16 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-threonine zwitterionCHEBI:57926 | small molecule | |
cytosolGO:0005829 | cellular component | |
L-threonine catabolic processGO:0006567 | biological process | |
2-oxobutanoateCHEBI:16763 | lipid | |
ammoniaCHEBI:16134 | small molecule | |
CHA1 ScerSGD:S000000569 | protein | |
waterCHEBI:15377 | small molecule | |
Low specificity L-threonine aldolaseUniProtKB:P37303 | protein | |
acetaldehydeCHEBI:15343 | small molecule | |
glycine zwitterionCHEBI:57305 | small molecule | |
mitochondrionGO:0005739 | cellular component | |
pyridoxal 5'-phosphate(2-)CHEBI:597326 | cofactor | |
threonine deaminase activitygomodel:THREDEHYD2-RXN | molecular activity | |
threonine aldolase activityGO:0004793 | molecular activity |
Mechanistic edges
| Subject | Predicate and description | Object | Evidence |
|---|---|---|---|
threonine deaminase activitygomodel:THREDEHYD2-RXN | has_input | L-threonine zwitterionCHEBI:57926 |
|
threonine deaminase activitygomodel:THREDEHYD2-RXN | part_of | L-threonine catabolic processGO:0006567 |
|
threonine deaminase activitygomodel:THREDEHYD2-RXN | has_output | ammoniaCHEBI:16134 |
|
CHA1 ScerSGD:S000000569 | enables | threonine deaminase activitygomodel:THREDEHYD2-RXN |
|
threonine deaminase activitygomodel:THREDEHYD2-RXN | has_output | waterCHEBI:15377 |
|
threonine deaminase activitygomodel:THREDEHYD2-RXN | has_output | 2-oxobutanoateCHEBI:16763 |
|
threonine deaminase activitygomodel:THREDEHYD2-RXN | has_input | waterCHEBI:15377 |
|
Low specificity L-threonine aldolaseUniProtKB:P37303 | enables | threonine aldolase activityGO:0004793 |
|
threonine aldolase activityGO:0004793 | has_input | L-threonine zwitterionCHEBI:57926 |
|
threonine aldolase activityGO:0004793 | has_output | acetaldehydeCHEBI:15343 |
|
threonine aldolase activityGO:0004793 | has_output | glycine zwitterionCHEBI:57305 |
|
Low specificity L-threonine aldolaseUniProtKB:P37303 | located_in | cytosolGO:0005829 |
|
threonine aldolase activityGO:0004793 | part_of | L-threonine catabolic processGO:0006567 |
|
CHA1 ScerSGD:S000000569 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:14562095); ECO:0000269 (PubMed:16823961) | mitochondrionGO:0005739 |
|
CHA1 ScerSGD:S000000569 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000250 | pyridoxal 5'-phosphate(2-)CHEBI:597326 |
|
Low specificity L-threonine aldolaseUniProtKB:P37303 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: not specified | pyridoxal 5'-phosphate(2-)CHEBI:597326 |
|
References
gomodel:YeastPathways_THREOCAT2-PWYGO-CAM threonine degradation model YeastPathways_THREOCAT2-PWY (source version: Pinned Noctua JSON archive; model date 2024-07-30; member ./YeastPathways_THREOCAT2-PWY.json)UniProtKB:P37303UniProt reviewed GLY1 (P37303), Saccharomyces cerevisiae S288C (source version: Entry 198; annotation update 2026-06-10)UniProtKB:P25379Reviewed UniProtKB P25379 location annotations (source version: UniProt release 2026_03)UniProtKB:P31373Reviewed UniProtKB P31373 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; review-catalytic-function; Reconciled native GO-CAM chemistry with independently reviewed enzyme specificity, direction, physiological scope and source cautions; superseded facts remain in the function review ledger.
- Codex
- EDIT — Audit causal activity compartments and preserve scoped protein location evidence
Reviewed all 3 activity location assignments and 3 mapped physical proteins against reviewed S288C UniProt release2026_03 location/function/caution batch SHA256 95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d. Added 2 independently supported location edges and quarantined 1 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