periplasmic NAD degradation
gomodel:YeastPathways_PERIPLASMA-NAD-DEGRADATION
Periplasmic NAD degradation in Saccharomyces cerevisiae S288C hydrolyzes NAD to AMP and NMN, then dephosphorylates AMP to adenosine and hydrogenphosphate.
- Pathway type
- cofactor degradation
- Organism scope
Pathway network
18 nodes · 19 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 | |
adenosineCHEBI:16335 | small molecule | |
cytosolGO:0005829 | cellular component | |
adenosine 5'-monophosphate(2-)CHEBI:456215 | small molecule | |
waterCHEBI:15377 | small molecule | |
NPY1 ScerSGD:S000003035 | protein | |
NAD+ catabolic processGO:0019677 | biological process | |
NMN(-)CHEBI:14649 | small molecule | |
NAD(1-)CHEBI:57540 | small molecule | |
hydronCHEBI:15378 | small molecule | |
SMN1 ScerSGD:S000001245 | protein | |
hydrogenphosphateCHEBI:43474 | small molecule | |
peroxisomeGO:0005777 | cellular component | |
extracellular regionGO:0005576 | cellular component | |
vacuoleGO:0005773 | cellular component | |
magnesium(2+)CHEBI:18420 | cofactor | |
zinc(2+)CHEBI:29105 | cofactor | |
AMP + H2O -> adenosine + phosphategomodel:AMP-DEPHOSPHORYLATION-RXN | molecular activity | |
NADH pyrophosphatase activitygomodel:NADPYROPHOSPHAT-RXN | molecular activity |
Mechanistic edges
| Subject | Predicate and description | Object | Evidence |
|---|---|---|---|
AMP + H2O -> adenosine + phosphategomodel:AMP-DEPHOSPHORYLATION-RXN | has_output | adenosineCHEBI:16335 |
|
NADH pyrophosphatase activitygomodel:NADPYROPHOSPHAT-RXN | has_output | adenosine 5'-monophosphate(2-)CHEBI:456215 |
|
AMP + H2O -> adenosine + phosphategomodel:AMP-DEPHOSPHORYLATION-RXN | has_input | waterCHEBI:15377 |
|
NPY1 ScerSGD:S000003035 | enables | NADH pyrophosphatase activitygomodel:NADPYROPHOSPHAT-RXN |
|
NADH pyrophosphatase activitygomodel:NADPYROPHOSPHAT-RXN | part_of | NAD+ catabolic processGO:0019677 |
|
NADH pyrophosphatase activitygomodel:NADPYROPHOSPHAT-RXN | has_output | NMN(-)CHEBI:14649 |
|
AMP + H2O -> adenosine + phosphategomodel:AMP-DEPHOSPHORYLATION-RXN | part_of | NAD+ catabolic processGO:0019677 |
|
NADH pyrophosphatase activitygomodel:NADPYROPHOSPHAT-RXN | has_input | NAD(1-)CHEBI:57540 |
|
NADH pyrophosphatase activitygomodel:NADPYROPHOSPHAT-RXN | has_output | hydronCHEBI:15378 |
|
SMN1 ScerSGD:S000001245 | enables | AMP + H2O -> adenosine + phosphategomodel:AMP-DEPHOSPHORYLATION-RXN |
|
AMP + H2O -> adenosine + phosphategomodel:AMP-DEPHOSPHORYLATION-RXN | has_input | adenosine 5'-monophosphate(2-)CHEBI:456215 |
|
NADH pyrophosphatase activitygomodel:NADPYROPHOSPHAT-RXN | has_input | waterCHEBI:15377 |
|
AMP + H2O -> adenosine + phosphategomodel:AMP-DEPHOSPHORYLATION-RXN | has_output | hydrogenphosphateCHEBI:43474 |
|
NPY1 ScerSGD:S000003035 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:11361135) | peroxisomeGO:0005777 |
|
SMN1 ScerSGD:S000001245 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:35123996) | extracellular regionGO:0005576 |
|
SMN1 ScerSGD:S000001245 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:14562095) | vacuoleGO:0005773 |
|
NPY1 ScerSGD:S000003035 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000250 (UniProtKB:Q9DCN1) Binds 3 Mg(2+) ions per subunit. UniProt note evidence: ECO:0000250 (UniProtKB:Q9DCN1) | magnesium(2+)CHEBI:18420 |
|
NPY1 ScerSGD:S000003035 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000250 (UniProtKB:Q9DCN1) Binds 1 zinc ion per subunit. UniProt note evidence: ECO:0000250 (UniProtKB:Q9DCN1) | zinc(2+)CHEBI:29105 |
|
SMN1 ScerSGD:S000001245 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000250 (UniProtKB:P21589) | zinc(2+)CHEBI:29105 |
|
References
gomodel:YeastPathways_PERIPLASMA-NAD-DEGRADATIONGO-CAM periplasmic NAD degradation model YeastPathways_PERIPLASMA-NAD-DEGRADATION (source version: Pinned Noctua JSON archive; model date 2026-07-14; member ./YeastPathways_PERIPLASMA-NAD-DEGRADATION.json)UniProtKB:P53164Reviewed UniProtKB P53164 location annotations (source version: UniProt release 2026_03)UniProtKB:P38887Reviewed UniProtKB P38887 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 2 activity location assignments and 2 mapped physical proteins against reviewed S288C UniProt release2026_03 location/function/caution batch SHA256 95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d. Added 3 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