HemE is a cytoplasmic uroporphyrinogen decarboxylase. It removes the four acetate carboxyl groups of uroporphyrinogen III without an external cofactor, producing coproporphyrinogen III for the oxygen-dependent HemF or oxygen-independent HemN branch of protoporphyrinogen IX synthesis.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004853 uroporphyrinogen decarboxylase activity | IEA GO_REF:0000120 | ACCEPT | Summary: This is the exact substrate-level activity of HemE. Reason: UniProt assigns EC 4.1.1.37 and describes four decarboxylations yielding coproporphyrinogen III. Supporting Evidence: file:PSEPK/hemE/hemE-uniprot.txt Catalyzes the decarboxylation of four acetate groups of |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | MARK AS OVER ANNOTATED | Summary: Cytoplasm is compatible with HemE biology but is the broader parent of the separately annotated cytosol term. Reason: The more specific cytosol annotation is also present and supported for this soluble enzyme, making cytoplasm redundant as a distinct retained annotation. Supporting Evidence: file:PSEPK/hemE/hemE-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0005829 cytosol | IEA GO_REF:0000118 | ACCEPT | Summary: Cytosol is the more specific informative location for the soluble bacterial HemE enzyme. Reason: The TreeGrafter cytosol call is consistent with UniProt's cytoplasm assignment and avoids retaining both a child term and its broader parent as equivalent annotations. Supporting Evidence: file:PSEPK/hemE/hemE-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0006778 porphyrin-containing compound metabolic process | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: This broad metabolic-process annotation is correct but not core. Reason: HemE does participate in porphyrin-containing compound metabolism, but its substrate-specific decarboxylase activity and biosynthetic process assignments describe the role more informatively. Supporting Evidence: file:PSEPK/hemE/hemE-uniprot.txt biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4. |
| GO:0006779 porphyrin-containing compound biosynthetic process | IEA GO_REF:0000002 | MODIFY | Summary: The biosynthetic assignment is sound and can be made endpoint-specific for KT2440. Reason: In KT2440, HemE supplies coproporphyrinogen III to the HemF/HemN, protoporphyrinogen oxidase, and ferrochelatase reactions that produce heme B, supporting the live endpoint term GO:0006785. Proposed replacements: heme B biosynthetic process Supporting Evidence: file:PSEPK/hemE/hemE-uniprot.txt uroporphyrinogen-III to yield coproporphyrinogen-III. |
| GO:0006783 heme biosynthetic process | IEA GO_REF:0000118 | ACCEPT | Summary: HemE is an obligatory shared enzyme in protoporphyrin-dependent heme-b synthesis. Reason: Coproporphyrinogen III is required for the subsequent HemF/HemN, protoporphyrinogen oxidase, and ferrochelatase reactions. Supporting Evidence: file:PSEPK/hemE/hemE-uniprot.txt PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX |
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Download this section (compressed HTML)Q: Does HemE flux constrain use of the HemF versus HemN late-step route?
Experiment: Quantify tetrapyrrole intermediates after hemE depletion during aerobic growth and oxygen-limited growth.
Hypothesis: HemE supplies coproporphyrinogen III to both late-step alternatives.
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