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hemN-2 hemN-2 hemF hemF hemN hemN
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
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second shell of interactors
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Your Input:
hemN-2Oxygen 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)
hemFCoproporphyrinogen 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)
hemNOxygen 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)
Your Current Organism:
Synechocystis sp. PCC6803
NCBI taxonomy Id: 1148
Other names: Aphanocapsa sp. (strain N-1), Aphanocapsa sp. N-1, S. sp. PCC 6803, Synechocystis sp. (ATCC 27184), Synechocystis sp. (PCC 6803), Synechocystis sp. (strain PCC 6803), Synechocystis sp. ATCC 27184, Synechocystis sp. PCC 6803, Synechocystis sp. PCC 6803 A, Synechocystis sp. PCC 6803 B
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