phosphatidate biosynthesis I (the dihydroxyacetone pathway)
gomodel:YeastPathways_PWY3O-6407
Phosphatidate biosynthesis I in Saccharomyces cerevisiae S288C acylates glycerone phosphate to 1-acylglycerone 3-phosphate, reduces it to 1-acyl-sn-glycerol 3-phosphate, and acylates that lysophosphatidate to 1,2-diacyl-sn-glycerol 3-phosphate through the SGD GO-CAM dihydroxyacetone pathway.
- Pathway type
- lipid biosynthesis
- Organism scope
Pathway network
24 nodes · 33 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 | |
SCT1 ScerSGD:S000000107 | protein | |
phospholipid biosynthetic processGO:0008654 | biological process | |
coenzyme A(4-)CHEBI:57287 | small molecule | |
SLC1 ScerSGD:S000002210 | protein | |
glycerone phosphate(2-)CHEBI:57642 | small molecule | |
long-chain fatty acyl-CoACHEBI:33184 | lipid | |
NADPH(4-)CHEBI:57783 | small molecule | |
1-acylglycerone 3-phosphateCHEBI:15835 | small molecule | |
NADP(3-)CHEBI:58349 | small molecule | |
cytosolGO:0005829 | cellular component | |
acyl-CoACHEBI:17984 | small molecule | |
hydronCHEBI:15378 | small molecule | |
GPT2 ScerSGD:S000001775 | protein | |
1-acyl-sn-glycerol 3-phosphateCHEBI:16975 | lipid | |
AYR1 ScerSGD:S000001386 | protein | |
1,2-diacyl-sn-glycerol 3-phosphateCHEBI:29089 | lipid | |
endoplasmic reticulum membraneGO:0005789 | cellular component | |
lipid dropletGO:0005811 | cellular component | |
mitochondrial outer membraneGO:0005741 | cellular component | |
endoplasmic reticulumGO:0005783 | cellular component | |
an acyl-CoA + a 1-acyl-sn-glycerol 3-phosphate -> a 1,2-diacyl-sn-glycerol 3-phosphate + coenzyme Agomodel:RXN-1623 | molecular activity | |
glycerone phosphate + a long-chain acyl-CoA -> 1-acyl-dihydroxyacetone-phosphate + coenzyme Agomodel:RXN3O-5279 | molecular activity | |
1-acyl-dihydroxyacetone-phosphate + NADPH -> a 1-acyl-sn-glycerol 3-phosphate + NADP+ + H+gomodel:RXN3O-9800 | molecular activity | |
glycerone-phosphate O-acyltransferase activitygomodel:YeastPathways_PWY3O-6407/6a4c244800000335 | molecular activity |
Mechanistic edges
| Subject | Predicate and description | Object | Evidence |
|---|---|---|---|
SCT1 ScerSGD:S000000107 | enables | glycerone-phosphate O-acyltransferase activitygomodel:YeastPathways_PWY3O-6407/6a4c244800000335 |
|
1-acyl-dihydroxyacetone-phosphate + NADPH -> a 1-acyl-sn-glycerol 3-phosphate + NADP+ + H+gomodel:RXN3O-9800 | part_of | phospholipid biosynthetic processGO:0008654 |
|
an acyl-CoA + a 1-acyl-sn-glycerol 3-phosphate -> a 1,2-diacyl-sn-glycerol 3-phosphate + coenzyme Agomodel:RXN-1623 | has_output | coenzyme A(4-)CHEBI:57287 |
|
glycerone phosphate + a long-chain acyl-CoA -> 1-acyl-dihydroxyacetone-phosphate + coenzyme Agomodel:RXN3O-5279 | has_output | coenzyme A(4-)CHEBI:57287 |
|
glycerone-phosphate O-acyltransferase activitygomodel:YeastPathways_PWY3O-6407/6a4c244800000335 | has_output | coenzyme A(4-)CHEBI:57287 |
|
SLC1 ScerSGD:S000002210 | enables | an acyl-CoA + a 1-acyl-sn-glycerol 3-phosphate -> a 1,2-diacyl-sn-glycerol 3-phosphate + coenzyme Agomodel:RXN-1623 |
|
glycerone-phosphate O-acyltransferase activitygomodel:YeastPathways_PWY3O-6407/6a4c244800000335 | has_input | glycerone phosphate(2-)CHEBI:57642 |
|
glycerone-phosphate O-acyltransferase activitygomodel:YeastPathways_PWY3O-6407/6a4c244800000335 | has_input | long-chain fatty acyl-CoACHEBI:33184 |
|
1-acyl-dihydroxyacetone-phosphate + NADPH -> a 1-acyl-sn-glycerol 3-phosphate + NADP+ + H+gomodel:RXN3O-9800 | has_input | NADPH(4-)CHEBI:57783 |
|
glycerone-phosphate O-acyltransferase activitygomodel:YeastPathways_PWY3O-6407/6a4c244800000335 | has_output | 1-acylglycerone 3-phosphateCHEBI:15835 |
|
1-acyl-dihydroxyacetone-phosphate + NADPH -> a 1-acyl-sn-glycerol 3-phosphate + NADP+ + H+gomodel:RXN3O-9800 | has_output | NADP(3-)CHEBI:58349 |
|
1-acyl-dihydroxyacetone-phosphate + NADPH -> a 1-acyl-sn-glycerol 3-phosphate + NADP+ + H+gomodel:RXN3O-9800 | has_input | 1-acylglycerone 3-phosphateCHEBI:15835 |
|
glycerone-phosphate O-acyltransferase activitygomodel:YeastPathways_PWY3O-6407/6a4c244800000335 | part_of | phospholipid biosynthetic processGO:0008654 |
|
glycerone phosphate + a long-chain acyl-CoA -> 1-acyl-dihydroxyacetone-phosphate + coenzyme Agomodel:RXN3O-5279 | has_input | long-chain fatty acyl-CoACHEBI:33184 |
|
an acyl-CoA + a 1-acyl-sn-glycerol 3-phosphate -> a 1,2-diacyl-sn-glycerol 3-phosphate + coenzyme Agomodel:RXN-1623 | has_input | acyl-CoACHEBI:17984 |
|
1-acyl-dihydroxyacetone-phosphate + NADPH -> a 1-acyl-sn-glycerol 3-phosphate + NADP+ + H+gomodel:RXN3O-9800 | has_output | hydronCHEBI:15378 |
|
GPT2 ScerSGD:S000001775 | enables | glycerone phosphate + a long-chain acyl-CoA -> 1-acyl-dihydroxyacetone-phosphate + coenzyme Agomodel:RXN3O-5279 |
|
an acyl-CoA + a 1-acyl-sn-glycerol 3-phosphate -> a 1,2-diacyl-sn-glycerol 3-phosphate + coenzyme Agomodel:RXN-1623 | has_input | 1-acyl-sn-glycerol 3-phosphateCHEBI:16975 |
|
AYR1 ScerSGD:S000001386 | enables | 1-acyl-dihydroxyacetone-phosphate + NADPH -> a 1-acyl-sn-glycerol 3-phosphate + NADP+ + H+gomodel:RXN3O-9800 |
|
glycerone phosphate + a long-chain acyl-CoA -> 1-acyl-dihydroxyacetone-phosphate + coenzyme Agomodel:RXN3O-5279 | has_input | glycerone phosphate(2-)CHEBI:57642 |
|
an acyl-CoA + a 1-acyl-sn-glycerol 3-phosphate -> a 1,2-diacyl-sn-glycerol 3-phosphate + coenzyme Agomodel:RXN-1623 | part_of | phospholipid biosynthetic processGO:0008654 |
|
glycerone phosphate + a long-chain acyl-CoA -> 1-acyl-dihydroxyacetone-phosphate + coenzyme Agomodel:RXN3O-5279 | has_output | 1-acylglycerone 3-phosphateCHEBI:15835 |
|
glycerone phosphate + a long-chain acyl-CoA -> 1-acyl-dihydroxyacetone-phosphate + coenzyme Agomodel:RXN3O-5279 | part_of | phospholipid biosynthetic processGO:0008654 |
|
1-acyl-dihydroxyacetone-phosphate + NADPH -> a 1-acyl-sn-glycerol 3-phosphate + NADP+ + H+gomodel:RXN3O-9800 | has_output | 1-acyl-sn-glycerol 3-phosphateCHEBI:16975 |
|
an acyl-CoA + a 1-acyl-sn-glycerol 3-phosphate -> a 1,2-diacyl-sn-glycerol 3-phosphate + coenzyme Agomodel:RXN-1623 | has_output | 1,2-diacyl-sn-glycerol 3-phosphateCHEBI:29089 |
|
SCT1 ScerSGD:S000000107 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:14562095); ECO:0000269 (PubMed:19525420) Topology: Multi-pass membrane protein. Source qualification: Localizes to both perinuclear and cortical endoplasmic reticulum | endoplasmic reticulum membraneGO:0005789 |
|
SLC1 ScerSGD:S000002210 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:18154737); ECO:0000269 (PubMed:21820081); ECO:0000269 (PubMed:24868093) | lipid dropletGO:0005811 |
|
GPT2 ScerSGD:S000001775 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:22267742); ECO:0000269 (PubMed:31421179); ECO:0000269 (PubMed:9401016) Source qualification: Localizes to both perinuclear and cortical endoplasmic reticulum | lipid dropletGO:0005811 |
|
GPT2 ScerSGD:S000001775 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:19525420); ECO:0000269 (PubMed:31421179) Topology: Multi-pass membrane protein. Source qualification: Localizes to both perinuclear and cortical endoplasmic reticulum | endoplasmic reticulum membraneGO:0005789 |
|
AYR1 ScerSGD:S000001386 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:10515935); ECO:0000269 (PubMed:10617610); ECO:0000269 (PubMed:21820081); ECO:0000269 (PubMed:24868093) | lipid dropletGO:0005811 |
|
AYR1 ScerSGD:S000001386 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:16407407); ECO:0000269 (PubMed:28916712) | mitochondrial outer membraneGO:0005741 |
|
AYR1 ScerSGD:S000001386 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:14562095); ECO:0000269 (PubMed:28916712) | endoplasmic reticulumGO:0005783 |
|
an acyl-CoA + a 1-acyl-sn-glycerol 3-phosphate -> a 1,2-diacyl-sn-glycerol 3-phosphate + coenzyme Agomodel:RXN-1623 | occurs_in Activity compartment supported by an inspected functional annotation. ECO:0000269 (PubMed:17675291); ECO:0000269 (PubMed:17890783); ECO:0000269 (PubMed:20694142); ECO:0000269 (PubMed:9401016). Alternative isoenzymes may function elsewhere. | lipid dropletGO:0005811 |
|
References
gomodel:YeastPathways_PWY3O-6407SGD GO-CAM phosphatidate biosynthesis I (the dihydroxyacetone pathway) - imported from: Saccharomyces Genome Database (source version: Pinned Noctua JSON archive; model date 2026-07-07; member ./YeastPathways_PWY3O-6407.json)UniProtKB:P32784Reviewed UniProtKB P32784 location annotations (source version: UniProt release 2026_03)UniProtKB:P33333Reviewed UniProtKB P33333 location annotations (source version: UniProt release 2026_03)UniProtKB:P36148Reviewed UniProtKB P36148 location annotations (source version: UniProt release 2026_03)UniProtKB:P40471Reviewed UniProtKB P40471 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 4 activity location assignments and 4 mapped physical proteins against reviewed S288C UniProt release2026_03 location/function/caution batch SHA256 95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d. Added 8 independently supported location edges and quarantined 4 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