dolichyl phosphate D-mannose biosynthesis
gomodel:YeastPathways_PWY3O-123
Dolichyl phosphate D-mannose biosynthesis in Saccharomyces cerevisiae S288C converts beta-D-fructofuranose 6-phosphate to alpha-D-mannose 1-phosphate, forms GDP-alpha-D-mannose, and transfers D-mannose to dolichyl phosphate to produce dolichyl D-mannosyl phosphate.
- Pathway type
- glycan biosynthesis
- Organism scope
Pathway network
26 nodes · 35 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 | |
PSA1 ScerSGD:S000002213 | protein | |
mannose metabolic processGO:0006013 | biological process | |
GDP-alpha-D-mannose(2-)CHEBI:57527 | small molecule | |
GDP(3-)CHEBI:58189 | small molecule | |
cytosolGO:0005829 | cellular component | |
hydronCHEBI:15378 | small molecule | |
beta-D-fructofuranose 6-phosphate(2-)CHEBI:57634 | small molecule | |
alpha-D-mannose 1-phosphate(2-)CHEBI:58409 | small molecule | |
dolichyl phosphateCHEBI:16214 | lipid | |
dolichyl D-mannosyl phosphateCHEBI:15809 | lipid | |
D-mannopyranose 6-phosphateCHEBI:48066 | small molecule | |
DPM1 ScerSGD:S000006387 | protein | |
SEC53 ScerSGD:S000001849 | protein | |
PMI40 ScerSGD:S000000805 | protein | |
cytoplasmGO:0005737 | cellular component | |
endoplasmic reticulum membraneGO:0005789 | cellular component | |
diphosphate(3-)CHEBI:33019 | small molecule | |
GTP(4-)CHEBI:37565 | small molecule | |
magnesium(2+)CHEBI:18420 | cofactor | |
manganese(2+)CHEBI:29035 | cofactor | |
calcium(2+)CHEBI:29108 | cofactor | |
zinc(2+)CHEBI:29105 | cofactor | |
dolichyl-phosphate beta-D-mannosyltransferase activitygomodel:2.4.1.83-RXN | molecular activity | |
alpha-D-mannose 1-phosphate + GTP + H(+) => GDP-alpha-D-mannose + diphosphateRHEA:15230 | molecular activity | left to right |
mannose-6-phosphate isomerase activitygomodel:MANNPISOM-RXN | molecular activity | |
phosphomannomutase activitygomodel:PHOSMANMUT-RXN | molecular activity |
Mechanistic edges
| Subject | Predicate and description | Object | Evidence |
|---|---|---|---|
PSA1 ScerSGD:S000002213 | enables | alpha-D-mannose 1-phosphate + GTP + H(+) => GDP-alpha-D-mannose + diphosphateRHEA:15230 |
|
dolichyl-phosphate beta-D-mannosyltransferase activitygomodel:2.4.1.83-RXN | part_of | mannose metabolic processGO:0006013 |
|
alpha-D-mannose 1-phosphate + GTP + H(+) => GDP-alpha-D-mannose + diphosphateRHEA:15230 | provides_input_for | dolichyl-phosphate beta-D-mannosyltransferase activitygomodel:2.4.1.83-RXN |
|
alpha-D-mannose 1-phosphate + GTP + H(+) => GDP-alpha-D-mannose + diphosphateRHEA:15230 | has_output | GDP-alpha-D-mannose(2-)CHEBI:57527 |
|
dolichyl-phosphate beta-D-mannosyltransferase activitygomodel:2.4.1.83-RXN | has_input | GDP-alpha-D-mannose(2-)CHEBI:57527 |
|
dolichyl-phosphate beta-D-mannosyltransferase activitygomodel:2.4.1.83-RXN | has_output | GDP(3-)CHEBI:58189 |
|
alpha-D-mannose 1-phosphate + GTP + H(+) => GDP-alpha-D-mannose + diphosphateRHEA:15230 | occurs_in | cytosolGO:0005829 |
|
mannose-6-phosphate isomerase activitygomodel:MANNPISOM-RXN | occurs_in | cytosolGO:0005829 |
|
alpha-D-mannose 1-phosphate + GTP + H(+) => GDP-alpha-D-mannose + diphosphateRHEA:15230 | has_input | hydronCHEBI:15378 |
|
mannose-6-phosphate isomerase activitygomodel:MANNPISOM-RXN | provides_input_for | phosphomannomutase activitygomodel:PHOSMANMUT-RXN |
|
mannose-6-phosphate isomerase activitygomodel:MANNPISOM-RXN | has_input | beta-D-fructofuranose 6-phosphate(2-)CHEBI:57634 |
|
alpha-D-mannose 1-phosphate + GTP + H(+) => GDP-alpha-D-mannose + diphosphateRHEA:15230 | has_input | alpha-D-mannose 1-phosphate(2-)CHEBI:58409 |
|
dolichyl-phosphate beta-D-mannosyltransferase activitygomodel:2.4.1.83-RXN | has_input | dolichyl phosphateCHEBI:16214 |
|
dolichyl-phosphate beta-D-mannosyltransferase activitygomodel:2.4.1.83-RXN | has_output | dolichyl D-mannosyl phosphateCHEBI:15809 |
|
alpha-D-mannose 1-phosphate + GTP + H(+) => GDP-alpha-D-mannose + diphosphateRHEA:15230 | has_output | diphosphate(3-)CHEBI:33019 |
|
phosphomannomutase activitygomodel:PHOSMANMUT-RXN | provides_input_for | alpha-D-mannose 1-phosphate + GTP + H(+) => GDP-alpha-D-mannose + diphosphateRHEA:15230 |
|
mannose-6-phosphate isomerase activitygomodel:MANNPISOM-RXN | part_of | mannose metabolic processGO:0006013 |
|
mannose-6-phosphate isomerase activitygomodel:MANNPISOM-RXN | has_output | D-mannopyranose 6-phosphateCHEBI:48066 |
|
alpha-D-mannose 1-phosphate + GTP + H(+) => GDP-alpha-D-mannose + diphosphateRHEA:15230 | has_input | GTP(4-)CHEBI:37565 |
|
phosphomannomutase activitygomodel:PHOSMANMUT-RXN | occurs_in | cytosolGO:0005829 |
|
phosphomannomutase activitygomodel:PHOSMANMUT-RXN | has_output | alpha-D-mannose 1-phosphate(2-)CHEBI:58409 |
|
DPM1 ScerSGD:S000006387 | enables | dolichyl-phosphate beta-D-mannosyltransferase activitygomodel:2.4.1.83-RXN |
|
phosphomannomutase activitygomodel:PHOSMANMUT-RXN | has_input | D-mannopyranose 6-phosphateCHEBI:48066 |
|
SEC53 ScerSGD:S000001849 | enables | phosphomannomutase activitygomodel:PHOSMANMUT-RXN |
|
PMI40 ScerSGD:S000000805 | enables | mannose-6-phosphate isomerase activitygomodel:MANNPISOM-RXN |
|
phosphomannomutase activitygomodel:PHOSMANMUT-RXN | part_of | mannose metabolic processGO:0006013 |
|
alpha-D-mannose 1-phosphate + GTP + H(+) => GDP-alpha-D-mannose + diphosphateRHEA:15230 | part_of | mannose metabolic processGO:0006013 |
|
PSA1 ScerSGD:S000002213 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:9195935) | cytoplasmGO:0005737 |
|
DPM1 ScerSGD:S000006387 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:14562095); ECO:0000269 (PubMed:15657391) Topology: Single-pass type IV membrane protein. Orientation: Cytoplasmic side. | endoplasmic reticulum membraneGO:0005789 |
|
SEC53 ScerSGD:S000001849 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:3905826) | cytoplasmGO:0005737 |
|
PMI40 ScerSGD:S000000805 | located_in Physical protein location from reviewed UniProt. evidence code not specified by source | cytoplasmGO:0005737 |
|
DPM1 ScerSGD:S000006387 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000250 (UniProtKB:Q8U4M3) Binds 1 divalent metal cation. UniProt note evidence: ECO:0000250 (UniProtKB:Q8U4M3) | magnesium(2+)CHEBI:18420 |
|
DPM1 ScerSGD:S000006387 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000250 (UniProtKB:Q8U4M3) Binds 1 divalent metal cation. UniProt note evidence: ECO:0000250 (UniProtKB:Q8U4M3) | manganese(2+)CHEBI:29035 |
|
DPM1 ScerSGD:S000006387 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: ECO:0000250 (UniProtKB:Q8U4M3) Binds 1 divalent metal cation. UniProt note evidence: ECO:0000250 (UniProtKB:Q8U4M3) | calcium(2+)CHEBI:29108 |
|
PMI40 ScerSGD:S000000805 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: not specified Binds 1 zinc ion per subunit. | zinc(2+)CHEBI:29105 |
|
References
gomodel:YeastPathways_PWY3O-123SGD GO-CAM dolichyl phosphate D-mannose biosynthesis pathway PWY3O-123 (source version: Pinned Noctua JSON archive; model date 2026-08-03; member ./YeastPathways_PWY3O-123.json)UniProtKB:P41940Reviewed UniProtKB P41940 location annotations (source version: UniProt release 2026_03)UniProtKB:P14020Reviewed UniProtKB P14020 location annotations (source version: UniProt release 2026_03)UniProtKB:P07283Reviewed UniProtKB P07283 location annotations (source version: UniProt release 2026_03)UniProtKB:P29952Reviewed UniProtKB P29952 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; edited; Correct PSA1 guanylyl donor and leaving group; pathway intermediate GDP-mannose retained.
- 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 4 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
- Codex
- EDIT — Correct PSA1 guanylyl donor and leaving group; pathway intermediate GDP-mannose retained.
User-authorized full causal graph curation. Correct PSA1 guanylyl donor and leaving group; pathway intermediate GDP-mannose retained. 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-corrections.json. Native schema validation and focused biochemical regression tests were run. Shared final rendering and full gates are performed by the coordinating agent.
- EDIT — Correct PSA1 guanylyl donor and leaving group; pathway intermediate GDP-mannose retained.