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hemN-2 | Oxygen independent coprophorphyrinogen III oxidase; Involved in the heme and chlorophyll biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX; Belongs to the anaerobic coproporphyrinogen-III oxidase family. (466 aa) | ||||
hemF | Coproporphyrinogen III oxidase; Involved in the heme and chlorophyll biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX. (340 aa) | ||||
hemN | Oxygen independent coprophorphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently (By similarity). Binds 1 [2Fe-2S] cluster. Although this protein has sequence motifs typically found in proteins binding the [4Fe-4S]-AdoMet radical-SAM cluster and S-adenosylmethionine, spectroscopic evidence suggests that a [2Fe-2S] cluster is present; S- adenosylmethionine was not detected. Has no detectable coproporphyrinogen-III oxidase activity. (412 aa) |