phosphatidate biosynthesis II (the glycerol-3-phosphate pathway)
gomodel:YeastPathways_PWY3O-6499
Phosphatidate biosynthesis II in Saccharomyces cerevisiae S288C forms sn-glycerol 3-phosphate, acylates 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 glycerol-3-phosphate pathway.
- Pathway type
- lipid biosynthesis
- Organism scope
Pathway network
27 nodes · 43 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 | |
GPD2 ScerSGD:S000005420 | protein | |
phospholipid biosynthetic processGO:0008654 | biological process | |
coenzyme A(4-)CHEBI:57287 | small molecule | |
glycerone phosphate(2-)CHEBI:57642 | small molecule | |
long-chain fatty acyl-CoACHEBI:33184 | lipid | |
1,2-diacyl-sn-glycerol 3-phosphateCHEBI:29089 | lipid | |
1-acyl-sn-glycerol 3-phosphateCHEBI:16975 | lipid | |
cytosolGO:0005829 | cellular component | |
GPT2 ScerSGD:S000001775 | protein | |
GPD1 ScerSGD:S000002180 | protein | |
sn-glycerol 3-phosphate(2-)CHEBI:57597 | small molecule | |
acyl-CoACHEBI:17984 | small molecule | |
hydronCHEBI:15378 | small molecule | |
NAD(1-)CHEBI:57540 | small molecule | |
NADH(2-)CHEBI:57945 | small molecule | |
SLC1 ScerSGD:S000002210 | protein | |
endoplasmic reticulum membraneGO:0005789 | cellular component | |
cytoplasmGO:0005737 | cellular component | |
mitochondrionGO:0005739 | cellular component | |
lipid dropletGO:0005811 | cellular component | |
peroxisomeGO:0005777 | cellular component | |
sn-glycerol 3-phosphate + NAD+ <- glycerone phosphate + NADH + H+gomodel:1.1.1.8-RXN | molecular activity | |
sn-glycerol 3-phosphate + a long-chain acyl-CoA -> a 1-acyl-sn-glycerol 3-phosphate + coenzyme Agomodel:GLYCEROL-3-P-ACYLTRANSFER-RXN | molecular activity | |
an acyl-CoA + a 1-acyl-sn-glycerol 3-phosphate -> a 1,2-diacyl-sn-glycerol 3-phosphate + coenzyme Agomodel:RXN-1623 | molecular activity | |
glycerol-3-phosphate dehydrogenase [NAD(P)+] activitygomodel:YeastPathways_PWY3O-6499/6a4c244800001520 | molecular activity | |
glycerol-3-phosphate O-acyltransferase activitygomodel:YeastPathways_PWY3O-6499/6a4c244800001536 | molecular activity |
Mechanistic edges
| Subject | Predicate and description | Object | Evidence |
|---|---|---|---|
SCT1 ScerSGD:S000000107 | enables | glycerol-3-phosphate O-acyltransferase activitygomodel:YeastPathways_PWY3O-6499/6a4c244800001536 |
|
GPD2 ScerSGD:S000005420 | enables | glycerol-3-phosphate dehydrogenase [NAD(P)+] activitygomodel:YeastPathways_PWY3O-6499/6a4c244800001520 |
|
sn-glycerol 3-phosphate + NAD+ <- glycerone phosphate + NADH + H+gomodel:1.1.1.8-RXN | part_of | phospholipid biosynthetic processGO:0008654 |
|
sn-glycerol 3-phosphate + a long-chain acyl-CoA -> a 1-acyl-sn-glycerol 3-phosphate + coenzyme Agomodel:GLYCEROL-3-P-ACYLTRANSFER-RXN | has_output | coenzyme A(4-)CHEBI:57287 |
|
sn-glycerol 3-phosphate + NAD+ <- glycerone phosphate + NADH + H+gomodel:1.1.1.8-RXN | has_input | glycerone phosphate(2-)CHEBI:57642 |
|
glycerol-3-phosphate O-acyltransferase activitygomodel:YeastPathways_PWY3O-6499/6a4c244800001536 | 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_output | 1,2-diacyl-sn-glycerol 3-phosphateCHEBI:29089 |
|
glycerol-3-phosphate O-acyltransferase activitygomodel:YeastPathways_PWY3O-6499/6a4c244800001536 | has_output | coenzyme A(4-)CHEBI:57287 |
|
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 |
|
glycerol-3-phosphate dehydrogenase [NAD(P)+] activitygomodel:YeastPathways_PWY3O-6499/6a4c244800001520 | part_of | phospholipid biosynthetic processGO:0008654 |
|
sn-glycerol 3-phosphate + a long-chain acyl-CoA -> a 1-acyl-sn-glycerol 3-phosphate + coenzyme Agomodel:GLYCEROL-3-P-ACYLTRANSFER-RXN | 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 | coenzyme A(4-)CHEBI:57287 |
|
glycerol-3-phosphate dehydrogenase [NAD(P)+] activitygomodel:YeastPathways_PWY3O-6499/6a4c244800001520 | has_input | glycerone phosphate(2-)CHEBI:57642 |
|
GPT2 ScerSGD:S000001775 | enables | sn-glycerol 3-phosphate + a long-chain acyl-CoA -> a 1-acyl-sn-glycerol 3-phosphate + coenzyme Agomodel:GLYCEROL-3-P-ACYLTRANSFER-RXN |
|
GPD1 ScerSGD:S000002180 | enables | sn-glycerol 3-phosphate + NAD+ <- glycerone phosphate + NADH + H+gomodel:1.1.1.8-RXN |
|
sn-glycerol 3-phosphate + a long-chain acyl-CoA -> a 1-acyl-sn-glycerol 3-phosphate + coenzyme Agomodel:GLYCEROL-3-P-ACYLTRANSFER-RXN | has_input | sn-glycerol 3-phosphate(2-)CHEBI:57597 |
|
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 |
|
glycerol-3-phosphate O-acyltransferase activitygomodel:YeastPathways_PWY3O-6499/6a4c244800001536 | 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_input | acyl-CoACHEBI:17984 |
|
glycerol-3-phosphate O-acyltransferase activitygomodel:YeastPathways_PWY3O-6499/6a4c244800001536 | has_output | 1-acyl-sn-glycerol 3-phosphateCHEBI:16975 |
|
sn-glycerol 3-phosphate + NAD+ <- glycerone phosphate + NADH + H+gomodel:1.1.1.8-RXN | has_input | hydronCHEBI:15378 |
|
glycerol-3-phosphate dehydrogenase [NAD(P)+] activitygomodel:YeastPathways_PWY3O-6499/6a4c244800001520 | has_output | sn-glycerol 3-phosphate(2-)CHEBI:57597 |
|
sn-glycerol 3-phosphate + NAD+ <- glycerone phosphate + NADH + H+gomodel:1.1.1.8-RXN | has_output | NAD(1-)CHEBI:57540 |
|
sn-glycerol 3-phosphate + a long-chain acyl-CoA -> a 1-acyl-sn-glycerol 3-phosphate + coenzyme Agomodel:GLYCEROL-3-P-ACYLTRANSFER-RXN | has_input | long-chain fatty acyl-CoACHEBI:33184 |
|
glycerol-3-phosphate dehydrogenase [NAD(P)+] activitygomodel:YeastPathways_PWY3O-6499/6a4c244800001520 | has_output | NAD(1-)CHEBI:57540 |
|
sn-glycerol 3-phosphate + NAD+ <- glycerone phosphate + NADH + H+gomodel:1.1.1.8-RXN | has_input | NADH(2-)CHEBI:57945 |
|
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 |
|
glycerol-3-phosphate dehydrogenase [NAD(P)+] activitygomodel:YeastPathways_PWY3O-6499/6a4c244800001520 | has_input | hydronCHEBI:15378 |
|
sn-glycerol 3-phosphate + NAD+ <- glycerone phosphate + NADH + H+gomodel:1.1.1.8-RXN | occurs_in | cytosolGO:0005829 |
|
glycerol-3-phosphate dehydrogenase [NAD(P)+] activitygomodel:YeastPathways_PWY3O-6499/6a4c244800001520 | has_input | NADH(2-)CHEBI:57945 |
|
sn-glycerol 3-phosphate + NAD+ <- glycerone phosphate + NADH + H+gomodel:1.1.1.8-RXN | has_output | sn-glycerol 3-phosphate(2-)CHEBI:57597 |
|
glycerol-3-phosphate O-acyltransferase activitygomodel:YeastPathways_PWY3O-6499/6a4c244800001536 | has_input | sn-glycerol 3-phosphate(2-)CHEBI:57597 |
|
glycerol-3-phosphate dehydrogenase [NAD(P)+] activitygomodel:YeastPathways_PWY3O-6499/6a4c244800001520 | occurs_in | cytosolGO:0005829 |
|
sn-glycerol 3-phosphate + a long-chain acyl-CoA -> a 1-acyl-sn-glycerol 3-phosphate + coenzyme Agomodel:GLYCEROL-3-P-ACYLTRANSFER-RXN | part_of | phospholipid biosynthetic processGO:0008654 |
|
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 |
|
GPD2 ScerSGD:S000005420 | located_in Physical protein location from reviewed UniProt. evidence code not specified by source | cytoplasmGO:0005737 |
|
GPD2 ScerSGD:S000005420 | located_in Physical protein location from reviewed UniProt. evidence code not specified by source | mitochondrionGO:0005739 |
|
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 |
|
GPD1 ScerSGD:S000002180 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:15210723) | cytoplasmGO:0005737 |
|
GPD1 ScerSGD:S000002180 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:14562095); ECO:0000269 (PubMed:15210723) | peroxisomeGO:0005777 |
|
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 |
|
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-6499SGD GO-CAM phosphatidate biosynthesis II (the glycerol-3-phosphate pathway) - imported from: Saccharomyces Genome Database (source version: Pinned Noctua JSON archive; model date 2026-07-13; member ./YeastPathways_PWY3O-6499.json)UniProtKB:P32784Reviewed UniProtKB P32784 location annotations (source version: UniProt release 2026_03)UniProtKB:P41911Reviewed UniProtKB P41911 location annotations (source version: UniProt release 2026_03)UniProtKB:P36148Reviewed UniProtKB P36148 location annotations (source version: UniProt release 2026_03)UniProtKB:Q00055Reviewed UniProtKB Q00055 location annotations (source version: UniProt release 2026_03)UniProtKB:P33333Reviewed UniProtKB P33333 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 5 activity location assignments and 5 mapped physical proteins against reviewed S288C UniProt release2026_03 location/function/caution batch SHA256 95f72dcc644358c480e0e59f996cf88533558b5fa4256460a030e0a1eaf9678d. Added 9 independently supported location edges and quarantined 3 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