hemE

UniProt ID: Q88CV6
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Review Status: COMPLETE
Aliases:
PP_5074
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Gene Description

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.

Existing Annotations Review

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

Core Functions

Decarboxylates the four acetate side chains of uroporphyrinogen III to produce coproporphyrinogen III for protoporphyrinogen IX and heme-b synthesis.

Directly Involved In:
Cellular Locations:
Supporting Evidence:
  • file:PSEPK/hemE/hemE-uniprot.txt
    Catalyzes the decarboxylation of four acetate groups of

References

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Suggested Questions for Experts

Q: Does HemE flux constrain use of the HemF versus HemN late-step route?

Suggested Experiments

Experiment: Quantify tetrapyrrole intermediates after hemE depletion during aerobic growth and oxygen-limited growth.

Hypothesis: HemE supplies coproporphyrinogen III to both late-step alternatives.

Deep Research

OpenScientist

(hemE-deep-research-openscientist.md)

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πŸ“š Additional Documentation

Notes

(hemE-notes.md)

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