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PROSITE documentation PDOC00783
Coproporphyrinogen III oxidase signature


Description

Coproporphyrinogen III oxidase (EC 1.3.3.3) (coproporphyrinogenase) [1,2] catalyzes the oxidative decarboxylation of coproporphyrinogen III into protoporphyrinogen IX, a common step in the pathway for the biosynthesis of porphyrins such as heme, chlorophyll or cobalamin.

Coproporphyrinogen III oxidase is an enzyme that requires iron for its activity. A cysteine seems to be important for the catalytic mechanism [3]. Sequences from a variety of eukaryotic and prokaryotic sources show that this enzyme has been evolutionarily conserved. As a signature pattern we selected a highly conserved region in the central part of the sequence; this region contains the only conserved cysteine and is rich in charged amino acids.

Note:

Some bacteria possess an anaerobic form of coproporphyrinogen III oxidase [4] which does not belong to this family.

Last update:

April 2006 / Pattern revised.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

COPROGEN_OXIDASE, PS01021; Coproporphyrinogen III oxidase signature  (PATTERN)


References

1AuthorsXu K. Elliott T.
TitleAn oxygen-dependent coproporphyrinogen oxidase encoded by the hemF gene of Salmonella typhimurium.
SourceJ. Bacteriol. 175:4990-4999(1993).
PubMed ID8349542

2AuthorsKohno H. Furukawa T. Yoshinaga T. Tokunaga R. Taketani S.
TitleCoproporphyrinogen oxidase. Purification, molecular cloning, and induction of mRNA during erythroid differentiation.
SourceJ. Biol. Chem. 268:21359-21363(1993).
PubMed ID8407975

3AuthorsCamadro J.M. Chambon H. Jolles J. Labbe P.
TitlePurification and properties of coproporphyrinogen oxidase from the yeast Saccharomyces cerevisiae.
SourceEur. J. Biochem. 156:579-587(1986).
PubMed ID3516695

4AuthorsXu K. Elliott T.
TitleCloning, DNA sequence, and complementation analysis of the Salmonella typhimurium hemN gene encoding a putative oxygen-independent coproporphyrinogen III oxidase.
SourceJ. Bacteriol. 176:3196-3203(1994).
PubMed ID8195073



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