HemH is the cytoplasmic ferrochelatase that catalyzes the terminal reaction of heme-b biosynthesis. It inserts ferrous iron into protoporphyrin IX to form protoheme (heme b), supplying the cofactor used by respiratory and other hemoproteins.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004325 protoporphyrin ferrochelatase activity | IEA GO_REF:0000120 | ACCEPT | Summary: This term precisely describes the terminal HemH reaction. Reason: UniProt assigns EC 4.98.1.1 and explicitly describes ferrous insertion into protoporphyrin IX. Supporting Evidence: file:PSEPK/hemH/hemH-uniprot.txt Catalyzes the ferrous insertion into protoporphyrin IX. |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: Cytoplasmic localization is explicitly predicted for the KT2440 enzyme. Reason: UniProt assigns HemH to the cytoplasm and does not predict a membrane anchor. Supporting Evidence: file:PSEPK/hemH/hemH-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0006779 porphyrin-containing compound biosynthetic process | IEA GO_REF:0000104 | MODIFY | Summary: The broad porphyrin process is correct but can be replaced by the exact product process. Reason: HemH directly produces heme B, so GO:0006785 is a supported live replacement for this broad porphyrin-biosynthesis annotation. Proposed replacements: heme B biosynthetic process Supporting Evidence: file:PSEPK/hemH/hemH-uniprot.txt biosynthesis; protoheme from protoporphyrin-IX: step 1/1. |
| GO:0006783 heme biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: HemH directly performs the final heme-b biosynthetic step. Reason: Insertion of Fe2+ into protoporphyrin IX creates heme b, so the broader heme-biosynthesis row is correct. GO:0006785 captures the endpoint more specifically in the replacement and core-function records. Supporting Evidence: file:PSEPK/hemH/hemH-uniprot.txt biosynthesis; protoheme from protoporphyrin-IX: step 1/1. |
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Download this section (compressed HTML)Q: Which iron-delivery factors supply ferrous iron to HemH in KT2440?
Experiment: Quantify protoporphyrin IX and heme b after conditional hemH depletion, iron perturbation, and complementation.
Hypothesis: HemH is the terminal ferrochelatase required for heme-b production.
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