heme b biosynthesis I (aerobic)
gomodel:YeastPathways_HEME-BIOSYNTHESIS-II
Aerobic heme b biosynthesis in Saccharomyces cerevisiae S288C decarboxylates uroporphyrinogen III to coproporphyrinogen III, oxidizes it through protoporphyrinogen to protoporphyrin, and inserts iron into protoporphyrin to produce ferroheme b.
- Pathway type
- cofactor biosynthesis
- Organism scope
Pathway network
25 nodes · 36 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 | |
cytosolGO:0005829 | cellular component | |
carbon dioxideCHEBI:16526 | small molecule | |
heme biosynthetic processGO:0006783 | biological process | |
coproporphyrinogen III(4-)CHEBI:57309 | small molecule | |
waterCHEBI:15377 | small molecule | |
hydronCHEBI:15378 | small molecule | |
HEM13 ScerSGD:S000002451 | protein | |
dioxygenCHEBI:15379 | small molecule | |
HEM15 ScerSGD:S000005702 | protein | |
protoporphyrinogen(2-)CHEBI:57307 | small molecule | |
HEM12 ScerSGD:S000002454 | protein | |
protoporphyrin(2-)CHEBI:57306 | small molecule | |
HEM14 ScerSGD:S000000816 | protein | |
hydrogen peroxideCHEBI:16240 | small molecule | |
ferroheme bCHEBI:17627 | small molecule | |
mitochondrial inner membraneGO:0005743 | cellular component | |
iron(2+)CHEBI:29033 | small molecule | |
uroporphyrinogen III(8-)CHEBI:57308 | small molecule | |
cytoplasmGO:0005737 | cellular component | |
nucleusGO:0005634 | cellular component | |
FAD(3-)CHEBI:57692 | cofactor | |
protoporphyrin ferrochelatase activitygomodel:PROTOHEMEFERROCHELAT-RXN | molecular activity | |
protoporphyrinogen oxidase activity, oxygen as acceptorgomodel:PROTOPORGENOXI-RXN | molecular activity | |
coproporphyrinogen oxidase activitygomodel:RXN0-1461 | molecular activity | |
uroporphyrinogen decarboxylase activitygomodel:UROGENDECARBOX-RXN | molecular activity |
Mechanistic edges
| Subject | Predicate and description | Object | Evidence |
|---|---|---|---|
uroporphyrinogen decarboxylase activitygomodel:UROGENDECARBOX-RXN | occurs_in | cytosolGO:0005829 |
|
uroporphyrinogen decarboxylase activitygomodel:UROGENDECARBOX-RXN | has_output | carbon dioxideCHEBI:16526 |
|
protoporphyrin ferrochelatase activitygomodel:PROTOHEMEFERROCHELAT-RXN | part_of | heme biosynthetic processGO:0006783 |
|
coproporphyrinogen oxidase activitygomodel:RXN0-1461 | has_input | coproporphyrinogen III(4-)CHEBI:57309 |
|
coproporphyrinogen oxidase activitygomodel:RXN0-1461 | has_output | waterCHEBI:15377 |
|
coproporphyrinogen oxidase activitygomodel:RXN0-1461 | has_input | hydronCHEBI:15378 |
|
HEM13 ScerSGD:S000002451 | enables | coproporphyrinogen oxidase activitygomodel:RXN0-1461 |
|
protoporphyrin ferrochelatase activitygomodel:PROTOHEMEFERROCHELAT-RXN | has_output | hydronCHEBI:15378 |
|
uroporphyrinogen decarboxylase activitygomodel:UROGENDECARBOX-RXN | has_input | hydronCHEBI:15378 |
|
protoporphyrinogen oxidase activity, oxygen as acceptorgomodel:PROTOPORGENOXI-RXN | has_input | dioxygenCHEBI:15379 |
|
HEM15 ScerSGD:S000005702 | enables | protoporphyrin ferrochelatase activitygomodel:PROTOHEMEFERROCHELAT-RXN |
|
coproporphyrinogen oxidase activitygomodel:RXN0-1461 | has_output | carbon dioxideCHEBI:16526 |
|
protoporphyrinogen oxidase activity, oxygen as acceptorgomodel:PROTOPORGENOXI-RXN | has_input | protoporphyrinogen(2-)CHEBI:57307 |
|
HEM12 ScerSGD:S000002454 | enables | uroporphyrinogen decarboxylase activitygomodel:UROGENDECARBOX-RXN |
|
protoporphyrinogen oxidase activity, oxygen as acceptorgomodel:PROTOPORGENOXI-RXN | has_output | protoporphyrin(2-)CHEBI:57306 |
|
HEM14 ScerSGD:S000000816 | enables | protoporphyrinogen oxidase activity, oxygen as acceptorgomodel:PROTOPORGENOXI-RXN |
|
coproporphyrinogen oxidase activitygomodel:RXN0-1461 | has_input | dioxygenCHEBI:15379 |
|
protoporphyrinogen oxidase activity, oxygen as acceptorgomodel:PROTOPORGENOXI-RXN | has_output | hydrogen peroxideCHEBI:16240 |
|
protoporphyrinogen oxidase activity, oxygen as acceptorgomodel:PROTOPORGENOXI-RXN | part_of | heme biosynthetic processGO:0006783 |
|
protoporphyrin ferrochelatase activitygomodel:PROTOHEMEFERROCHELAT-RXN | has_output | ferroheme bCHEBI:17627 |
|
uroporphyrinogen decarboxylase activitygomodel:UROGENDECARBOX-RXN | has_output | coproporphyrinogen III(4-)CHEBI:57309 |
|
protoporphyrin ferrochelatase activitygomodel:PROTOHEMEFERROCHELAT-RXN | occurs_in | mitochondrial inner membraneGO:0005743 |
|
protoporphyrin ferrochelatase activitygomodel:PROTOHEMEFERROCHELAT-RXN | has_input | iron(2+)CHEBI:29033 |
|
coproporphyrinogen oxidase activitygomodel:RXN0-1461 | has_output | protoporphyrinogen(2-)CHEBI:57307 |
|
coproporphyrinogen oxidase activitygomodel:RXN0-1461 | part_of | heme biosynthetic processGO:0006783 |
|
uroporphyrinogen decarboxylase activitygomodel:UROGENDECARBOX-RXN | has_input | uroporphyrinogen III(8-)CHEBI:57308 |
|
protoporphyrinogen oxidase activity, oxygen as acceptorgomodel:PROTOPORGENOXI-RXN | occurs_in | mitochondrial inner membraneGO:0005743 |
|
protoporphyrin ferrochelatase activitygomodel:PROTOHEMEFERROCHELAT-RXN | has_input | protoporphyrin(2-)CHEBI:57306 |
|
uroporphyrinogen decarboxylase activitygomodel:UROGENDECARBOX-RXN | part_of | heme biosynthetic processGO:0006783 |
|
coproporphyrinogen oxidase activitygomodel:RXN0-1461 | occurs_in | cytosolGO:0005829 |
|
HEM13 ScerSGD:S000002451 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:14562095); ECO:0000269 (PubMed:3516695) | cytoplasmGO:0005737 |
|
HEM15 ScerSGD:S000005702 | located_in Physical protein location from reviewed UniProt. evidence code not specified by source Topology: Peripheral membrane protein. Orientation: Matrix side. Source qualification: It is bound to the mitochondrial inner membrane in eukaryotic cells with its active site on the matrix side of the membrane | mitochondrial inner membraneGO:0005743 |
|
HEM12 ScerSGD:S000002454 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:14562095) | nucleusGO:0005634 |
|
HEM12 ScerSGD:S000002454 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:14562095); ECO:0000269 (PubMed:2180703) | cytoplasmGO:0005737 |
|
HEM14 ScerSGD:S000000816 | located_in Physical protein location from reviewed UniProt. ECO:0000269 (PubMed:7798202) Source qualification: Bound to the mitochondrial inner membrane with its active site facing the cytosolic side | mitochondrial inner membraneGO:0005743 |
|
HEM14 ScerSGD:S000000816 | has_cofactor UniProtKB reviewed (Swiss-Prot) annotation. UniProt evidence: not specified Binds 1 FAD per subunit. UniProt note evidence: ECO:0000250 (UniProtKB:P32397) | FAD(3-)CHEBI:57692 |
|
References
gomodel:YeastPathways_HEME-BIOSYNTHESIS-IIGO-CAM heme b biosynthesis I aerobic model YeastPathways_HEME-BIOSYNTHESIS-II (source version: Pinned Noctua JSON archive; model date 2023-12-13; member ./YeastPathways_HEME-BIOSYNTHESIS-II.json)UniProtKB:P11353Reviewed UniProtKB P11353 location annotations (source version: UniProt release 2026_03)UniProtKB:P16622Reviewed UniProtKB P16622 location annotations (source version: UniProt release 2026_03)UniProtKB:P32347Reviewed UniProtKB P32347 location annotations (source version: UniProt release 2026_03)UniProtKB:P40012Reviewed UniProtKB P40012 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 5 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