| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SBO17492.1 | SBO17896.1 | CDIV41_320053 | CDIV41_320459 | Conserved hypothetical protein; Homologs of previously reported genes of unknown function. | NUDIX domain protein. | 0.490 |
| SBO17492.1 | fer | CDIV41_320053 | CDIV41_320263 | Conserved hypothetical protein; Homologs of previously reported genes of unknown function. | Ferredoxin; Function of homologous gene experimentally demonstrated in an other organism; carrier. | 0.637 |
| SBO17492.1 | hemN | CDIV41_320053 | CDIV41_320461 | Conserved hypothetical protein; Homologs of previously reported genes of unknown function. | Coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.648 |
| SBO17896.1 | SBO17492.1 | CDIV41_320459 | CDIV41_320053 | NUDIX domain protein. | Conserved hypothetical protein; Homologs of previously reported genes of unknown function. | 0.490 |
| SBO17896.1 | hemN | CDIV41_320459 | CDIV41_320461 | NUDIX domain protein. | Coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.655 |
| fat | hemN | CDIV41_270193 | CDIV41_320461 | Acyl-ACP thioesterase family protein. | Coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.753 |
| fer | SBO17492.1 | CDIV41_320263 | CDIV41_320053 | Ferredoxin; Function of homologous gene experimentally demonstrated in an other organism; carrier. | Conserved hypothetical protein; Homologs of previously reported genes of unknown function. | 0.637 |
| fer | hemN | CDIV41_320263 | CDIV41_320461 | Ferredoxin; Function of homologous gene experimentally demonstrated in an other organism; carrier. | Coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.713 |
| fer | nifJ | CDIV41_320263 | CDIV41_140119 | Ferredoxin; Function of homologous gene experimentally demonstrated in an other organism; carrier. | Pyruvate-flavodoxin oxidoreductase. | 0.890 |
| hemG | hemH | CDIV41_320644 | CDIV41_140286 | Protoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 0.985 |
| hemG | hemN | CDIV41_320644 | CDIV41_320461 | Protoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. | Coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.937 |
| hemH | hemG | CDIV41_140286 | CDIV41_320644 | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | Protoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. | 0.985 |
| hemH | hemN | CDIV41_140286 | CDIV41_320461 | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | Coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.634 |
| hemN | SBO17492.1 | CDIV41_320461 | CDIV41_320053 | Coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Conserved hypothetical protein; Homologs of previously reported genes of unknown function. | 0.648 |
| hemN | SBO17896.1 | CDIV41_320461 | CDIV41_320459 | Coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | NUDIX domain protein. | 0.655 |
| hemN | fat | CDIV41_320461 | CDIV41_270193 | Coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Acyl-ACP thioesterase family protein. | 0.753 |
| hemN | fer | CDIV41_320461 | CDIV41_320263 | Coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Ferredoxin; Function of homologous gene experimentally demonstrated in an other organism; carrier. | 0.713 |
| hemN | hemG | CDIV41_320461 | CDIV41_320644 | Coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Protoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. | 0.937 |
| hemN | hemH | CDIV41_320461 | CDIV41_140286 | Coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 0.634 |
| hemN | lepA | CDIV41_320461 | CDIV41_320454 | Coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Ribosomal elongation factor, GTPase; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | 0.901 |