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- * Coproporphyrinogen III oxidase signature *
- ********************************************
-
- 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.
-
- -Consensus pattern: K-K-W-C-D-[DE]-[FY](3)-[LIVM]-x-H-R-x-E-x-R-G-[LIVM]-G-G-
- [LIVM]-F-F-D-D
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Note: an anaerobic form of coproporphyrinogen III oxidase from Rhodobacter
- sphaeroides has been sequenced [4]. It does not belong to this family.
-
- -Last update: June 1994 / First entry.
-
- [ 1] Xu K., Elliott T.
- J. Bacteriol. 175:4990-4999(1993).
- [ 2] Kohno H., Furukawa T., Yoshinaga T., Tokunaga R., Taketani S.
- J. Biol. Chem. 268:21359-21363(1993).
- [ 3] Camadro J.M., Chambon H., Jolles J., Labbe P.
- Eur. J. Biochem. 156:579-587(1986).
- [ 4] Coomber S.A., Jones R.M., Jordan P.M., Hunter C.N.
- Mol. Microbiol. 6:3159-3169(1992).
-