hemC

UniProt ID: Q88RE5
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Review Status: COMPLETE
Aliases:
PP_0186
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Gene Description

HemC is the cytoplasmic hydroxymethylbilane synthase, also called porphobilinogen deaminase. It uses a covalently bound dipyrromethane cofactor to polymerize four porphobilinogen molecules into the linear tetrapyrrole hydroxymethylbilane, which HemD cyclizes to uroporphyrinogen III.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0004418 hydroxymethylbilane synthase activity
IEA
GO_REF:0000120
ACCEPT
Summary: This is the specific core catalytic function of HemC.
Reason: UniProt assigns EC 2.5.1.61 and describes tetrapolymerization of porphobilinogen into hydroxymethylbilane.
Supporting Evidence:
file:PSEPK/hemC/hemC-uniprot.txt
Tetrapolymerization of the monopyrrole PBG into the
GO:0005737 cytoplasm
IEA
GO_REF:0000120
ACCEPT
Summary: Cytoplasmic localization is consistent with this soluble bacterial enzyme.
Reason: HemC lacks membrane or export features, and the current UniProt cross-reference retains a cytoplasmic assignment.
Supporting Evidence:
file:PSEPK/hemC/hemC-uniprot.txt
GO; GO:0005737; C:cytoplasm;
GO:0006783 heme biosynthetic process
IEA
GO_REF:0000120
ACCEPT
Summary: HemC is an obligatory middle enzyme in the protoporphyrin route to heme b.
Reason: The HemC reaction generates the linear tetrapyrrole precursor required for uroporphyrinogen III and all downstream heme-b intermediates.
Supporting Evidence:
file:PSEPK/hemC/hemC-uniprot.txt
PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
GO:0033014 tetrapyrrole biosynthetic process
IEA
GO_REF:0000002
MODIFY
Summary: The annotation is true but can be made more specific to the immediate product route.
Reason: HemC directly builds hydroxymethylbilane for conversion to uroporphyrinogen III, so GO:0006780 is more informative than the broad tetrapyrrole parent.
Supporting Evidence:
file:PSEPK/hemC/hemC-uniprot.txt
Tetrapolymerization of the monopyrrole PBG into the

Core Functions

Polymerizes four porphobilinogen molecules into hydroxymethylbilane for uroporphyrinogen III and downstream heme-b synthesis.

Supporting Evidence:
  • file:PSEPK/hemC/hemC-uniprot.txt
    Tetrapolymerization of the monopyrrole PBG into the

References

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Suggested Questions for Experts

Q: Is HemC abundance coordinated with the adjacent hemD locus in KT2440?

Suggested Experiments

Experiment: Quantify porphobilinogen and downstream tetrapyrroles after conditional hemC depletion and complementation.

Hypothesis: HemC supplies hydroxymethylbilane for the principal heme-b pathway.

Deep Research

OpenScientist

(hemC-deep-research-openscientist.md)

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Notes

(hemC-notes.md)

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