adenosine deoxyribonucleotides de novo biosynthesis II
gomodel:YeastPathways_PWY-7220-1
Adenosine deoxyribonucleotide biosynthesis in Saccharomyces cerevisiae S288C reduces ADP to dADP through the represented ribonucleoside-diphosphate reductase complexes and phosphorylates dADP to dATP through YNK1. The imported formate-dependent ATP-to-dATP branch has no yeast enzyme assignment and is excluded: it describes class III anaerobic ribonucleotide reductase chemistry, whereas the independently characterized yeast system reduces ribonucleoside diphosphates.
- Pathway type
- nucleotide biosynthesis
- Organism scope
Pathway network
24 nodes · 42 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 | |
thioredoxin dithiolCHEBI:15967 | protein | |
ADP(3-)CHEBI:456216 | small molecule | |
dADP(3-)CHEBI:57667 | small molecule | |
thioredoxin disulfideCHEBI:18191 | protein | |
ATP(4-)CHEBI:30616 | small molecule | |
waterCHEBI:15377 | small molecule | |
CPX-1102 ScerSGD:S000217933 | complex | |
CPX-1103 ScerSGD:S000217934 | complex | |
YNK1 ScerSGD:S000001550 | protein | |
cytosolGO:0005829 | cellular component | |
adenosine metabolic processGO:0046085 | biological process | |
dATP(4-)CHEBI:61404 | small molecule | |
iron cationCHEBI:24875 | cofactor | |
Ribonucleoside-diphosphate reductase large chain 1UniProtKB:P21524 | protein | |
Ribonucleoside-diphosphate reductase small chain 1UniProtKB:P09938 | protein | |
Ribonucleoside-diphosphate reductase small chain 2UniProtKB:P49723 | protein | |
cytoplasmGO:0005737 | cellular component | |
Ribonucleoside-diphosphate reductase large chain 2UniProtKB:P21672 | protein | |
mitochondrial intermembrane spaceGO:0005758 | cellular component | |
nucleusGO:0005634 | cellular component | |
magnesium(2+)CHEBI:18420 | cofactor | |
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorgomodel:ADPREDUCT-RXN | molecular activity | |
nucleoside diphosphate kinase activitygomodel:DADPKIN-RXN | molecular activity | |
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorgomodel:YeastPathways_PWY-7220-1/6a2b236300005372 | molecular activity |
Mechanistic edges
| Subject | Predicate and description | Object | Evidence |
|---|---|---|---|
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorgomodel:YeastPathways_PWY-7220-1/6a2b236300005372 | has_input | thioredoxin dithiolCHEBI:15967 |
|
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorgomodel:YeastPathways_PWY-7220-1/6a2b236300005372 | has_input | ADP(3-)CHEBI:456216 |
|
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorgomodel:ADPREDUCT-RXN | has_output | dADP(3-)CHEBI:57667 |
|
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorgomodel:ADPREDUCT-RXN | has_output | thioredoxin disulfideCHEBI:18191 |
|
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorgomodel:ADPREDUCT-RXN | has_output | waterCHEBI:15377 |
|
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorgomodel:YeastPathways_PWY-7220-1/6a2b236300005372 | has_output | dADP(3-)CHEBI:57667 |
|
CPX-1102 ScerSGD:S000217933 | enables | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorgomodel:ADPREDUCT-RXN |
|
CPX-1103 ScerSGD:S000217934 | enables | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorgomodel:YeastPathways_PWY-7220-1/6a2b236300005372 |
|
nucleoside diphosphate kinase activitygomodel:DADPKIN-RXN | has_output | ADP(3-)CHEBI:456216 |
|
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorgomodel:YeastPathways_PWY-7220-1/6a2b236300005372 | has_output | thioredoxin disulfideCHEBI:18191 |
|
YNK1 ScerSGD:S000001550 | enables | nucleoside diphosphate kinase activitygomodel:DADPKIN-RXN |
|
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorgomodel:YeastPathways_PWY-7220-1/6a2b236300005372 | has_output | waterCHEBI:15377 |
|
nucleoside diphosphate kinase activitygomodel:DADPKIN-RXN | has_input | dADP(3-)CHEBI:57667 |
|
nucleoside diphosphate kinase activitygomodel:DADPKIN-RXN | occurs_in | cytosolGO:0005829 |
|
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorgomodel:YeastPathways_PWY-7220-1/6a2b236300005372 | occurs_in | cytosolGO:0005829 |
|
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorgomodel:ADPREDUCT-RXN | occurs_in | cytosolGO:0005829 |
|
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorgomodel:YeastPathways_PWY-7220-1/6a2b236300005372 | part_of | adenosine metabolic processGO:0046085 |
|
nucleoside diphosphate kinase activitygomodel:DADPKIN-RXN | part_of | adenosine metabolic processGO:0046085 |
|
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorgomodel:ADPREDUCT-RXN | part_of | adenosine metabolic processGO:0046085 |
|
nucleoside diphosphate kinase activitygomodel:DADPKIN-RXN | has_input | ATP(4-)CHEBI:30616 |
|
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorgomodel:ADPREDUCT-RXN | has_input | thioredoxin dithiolCHEBI:15967 |
|
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptorgomodel:ADPREDUCT-RXN | has_input | ADP(3-)CHEBI:456216 |
|
nucleoside diphosphate kinase activitygomodel:DADPKIN-RXN | has_output | dATP(4-)CHEBI:61404 |
|
CPX-1102 ScerSGD:S000217933 | has_part ECO:0000353: physical interaction evidence; source stoichiometry minValue: 2, maxValue: 2 | iron cationCHEBI:24875 |
|
CPX-1102 ScerSGD:S000217933 | has_part ECO:0000353: physical interaction evidence; source stoichiometry minValue: 2, maxValue: 2 | Ribonucleoside-diphosphate reductase large chain 1UniProtKB:P21524 |
|
CPX-1102 ScerSGD:S000217933 | has_part ECO:0000353: physical interaction evidence; source stoichiometry minValue: 1, maxValue: 1 | Ribonucleoside-diphosphate reductase small chain 1UniProtKB:P09938 |
|
CPX-1102 ScerSGD:S000217933 | has_part ECO:0000353: physical interaction evidence; source stoichiometry minValue: 1, maxValue: 1 | Ribonucleoside-diphosphate reductase small chain 2UniProtKB:P49723 |
|
CPX-1102 ScerSGD:S000217933 | located_in Complex location from the independent composition source; original GO-CAM activity locations are retained with their own provenance. | cytoplasmGO:0005737 |
|
CPX-1103 ScerSGD:S000217934 | has_part ECO:0005546: inferred by paralogy; source stoichiometry minValue: 2, maxValue: 2 | iron cationCHEBI:24875 |
|
CPX-1103 ScerSGD:S000217934 | has_part ECO:0005546: inferred by paralogy; source stoichiometry minValue: 1, maxValue: 1 | Ribonucleoside-diphosphate reductase large chain 1UniProtKB:P21524 |
|
CPX-1103 ScerSGD:S000217934 | has_part ECO:0005546: inferred by paralogy; source stoichiometry minValue: 1, maxValue: 1 | Ribonucleoside-diphosphate reductase small chain 1UniProtKB:P09938 |
|
CPX-1103 ScerSGD:S000217934 | has_part ECO:0005546: inferred by paralogy; source stoichiometry minValue: 1, maxValue: 1 | Ribonucleoside-diphosphate reductase large chain 2UniProtKB:P21672 |
|
CPX-1103 ScerSGD:S000217934 | has_part ECO:0005546: inferred by paralogy; source stoichiometry minValue: 1, maxValue: 1 | Ribonucleoside-diphosphate reductase small chain 2UniProtKB:P49723 |
|
CPX-1103 ScerSGD:S000217934 | located_in Complex location from the independent composition source; original GO-CAM activity locations are retained with their own provenance. | cytoplasmGO:0005737 |
|
YNK1 ScerSGD:S000001550 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:12472466) Source qualification: Localizes predominantly to the cytoplasm. A small fraction is present in the mitochondrial intermembrane space | cytoplasmGO:0005737 |
|
YNK1 ScerSGD:S000001550 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:12472466); ECO:0000269 (PubMed:16823961); ECO:0000269 (PubMed:22984289) Source qualification: Localizes predominantly to the cytoplasm. A small fraction is present in the mitochondrial intermembrane space | mitochondrial intermembrane spaceGO:0005758 |
|
Ribonucleoside-diphosphate reductase large chain 1UniProtKB:P21524 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:12732713) | cytoplasmGO:0005737 |
|
Ribonucleoside-diphosphate reductase small chain 1UniProtKB:P09938 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:12732713); ECO:0000269 (PubMed:18851834) Source qualification: Found predominantly in the nucleus under normal growth conditions and is redistributed to the cytoplasm in damaged cells in a DNA replication and damage checkpoint-dependent manner. Nuclear localization is mediated by DIF1 | nucleusGO:0005634 |
|
Ribonucleoside-diphosphate reductase small chain 2UniProtKB:P49723 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:12732713); ECO:0000269 (PubMed:18851834) Source qualification: Found predominantly in the nucleus under normal growth conditions and is redistributed to the cytoplasm in damaged cells in a DNA replication and damage checkpoint-dependent manner. Nuclear localization is mediated by DIF1 | nucleusGO:0005634 |
|
Ribonucleoside-diphosphate reductase large chain 2UniProtKB:P21672 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:12732713) | cytoplasmGO:0005737 |
|
YNK1 ScerSGD:S000001550 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000269 (PubMed:5793714) | magnesium(2+)CHEBI:18420 |
|
Ribonucleoside-diphosphate reductase small chain 1UniProtKB:P09938 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: not specified Binds 2 iron ions per subunit. | iron cationCHEBI:24875 |
|
References
gomodel:YeastPathways_PWY-7220-1GO-CAM adenosine deoxyribonucleotides de novo biosynthesis II model YeastPathways_PWY-7220-1 (source version: Pinned Noctua JSON archive; model date 2026-07-02; member ./YeastPathways_PWY-7220-1.json)SGD:S000217933Complex Portal CPX-1102: Ribonucleoside-diphosphate reductase variant 1 (source version: Inspected API snapshot 2026-10-05; release dates 2014-10-16)SGD:S000217934Complex Portal CPX-1103: Ribonucleoside-diphosphate reductase variant 2 (source version: Inspected API snapshot 2026-10-05; release dates 2014-10-16)UniProtKB:P36010Reviewed UniProtKB P36010 location annotations (source version: UniProt release 2026_03)UniProtKB:P21524Reviewed UniProtKB P21524 location annotations (source version: UniProt release 2026_03)UniProtKB:P09938Reviewed UniProtKB P09938 location annotations (source version: UniProt release 2026_03)UniProtKB:P49723Reviewed UniProtKB P49723 location annotations (source version: UniProt release 2026_03)UniProtKB:P21672Reviewed UniProtKB P21672 location annotations (source version: UniProt release 2026_03)PMID:6370695Deoxyribonucleotide biosynthesis in yeast (Saccharomyces cerevisiae). A ribonucleotide reductase system of sufficient activity for DNA synthesis
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. Reviewed exact Complex Portal composition, source evidence grades, and independent physical complex locations.
- Codex; review-complex-composition; Reviewed exact Complex Portal composition, source evidence grades, and independent physical complex locations; reused existing proteins through reviewed UniProt SGD cross-references.
- Codex; edited; Exclude unenabled class III formate-dependent ATP reduction from the yeast graph. Native source inclusion alone does not establish yeast activity; the directly characterized yeast reductase and exact yeast UniProt entries support diphosphate reduction.
- Codex
- EDIT — Audit causal activity compartments and preserve scoped protein location evidence
Reviewed all 4 activity location assignments and 5 mapped physical proteins against reviewed S288C UniProt release2026_03 location/function/caution batch SHA256 95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d. Added 6 independently supported location edges and quarantined 0 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
- Codex
- EDIT — Exclude unenabled class III formate-dependent ATP reduction from the yeast graph. Native source inclusion alone does not establish yeast activity; the directly characterized yeast reductase and exact yeast UniProt entries support diphosphate reduction.
User-authorized full causal graph curation. Exclude unenabled class III formate-dependent ATP reduction from the yeast graph. Native source inclusion alone does not establish yeast activity; the directly characterized yeast reductase and exact yeast UniProt entries support diphosphate reduction. Independent UniProt release2026_03 annotations, Rhea139 and ChEBI255 were inspected; primary literature was checked for the taxon/function distinctions. Exact source pointers and superseded edge assertions are retained in reports/causal_graph_review/gocam-chemical-final-supplement.json. Native schema validation and focused biochemical regression tests were run. Shared final rendering and full gates are performed by the coordinating agent.
- EDIT — Exclude unenabled class III formate-dependent ATP reduction from the yeast graph. Native source inclusion alone does not establish yeast activity; the directly characterized yeast reductase and exact yeast UniProt entries support diphosphate reduction.