| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PP_0913 | PP_1083 | PP_0913 | PP_1083 | Homologs of previously reported genes of unknown function. | (2Fe-2S)-binding protein. | 0.696 |
| PP_1083 | PP_0913 | PP_1083 | PP_0913 | (2Fe-2S)-binding protein. | Homologs of previously reported genes of unknown function. | 0.696 |
| PP_1083 | PP_4856 | PP_1083 | PP_4856 | (2Fe-2S)-binding protein. | Ferritin, Dps family protein. | 0.613 |
| PP_1083 | bfr-I | PP_1083 | PP_0482 | (2Fe-2S)-binding protein. | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 0.930 |
| PP_1083 | bfr-II | PP_1083 | PP_1082 | (2Fe-2S)-binding protein. | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 0.992 |
| PP_1083 | efp | PP_1083 | PP_1858 | (2Fe-2S)-binding protein. | Elongation factor P; Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. | 0.488 |
| PP_1083 | fpr-I | PP_1083 | PP_1638 | (2Fe-2S)-binding protein. | ferredoxin--NADP(+) reductase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.564 |
| PP_1083 | iscR | PP_1083 | PP_0841 | (2Fe-2S)-binding protein. | DNA-binding transcriptional dual regulator 2Fe-2S cluster IscR; Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins. | 0.549 |
| PP_1083 | pyrC | PP_1083 | PP_1086 | (2Fe-2S)-binding protein. | Dihydroorotase; Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. | 0.488 |
| PP_1083 | rnt | PP_1083 | PP_1085 | (2Fe-2S)-binding protein. | Ribonuclease T; Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis. | 0.488 |
| PP_1083 | tsaA | PP_1083 | PP_1084 | (2Fe-2S)-binding protein. | Putative peroxiredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.583 |
| PP_4856 | PP_1083 | PP_4856 | PP_1083 | Ferritin, Dps family protein. | (2Fe-2S)-binding protein. | 0.613 |
| PP_4856 | bfr-I | PP_4856 | PP_0482 | Ferritin, Dps family protein. | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 0.931 |
| PP_4856 | bfr-II | PP_4856 | PP_1082 | Ferritin, Dps family protein. | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 0.941 |
| bfr-I | PP_1083 | PP_0482 | PP_1083 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | (2Fe-2S)-binding protein. | 0.930 |
| bfr-I | PP_4856 | PP_0482 | PP_4856 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | Ferritin, Dps family protein. | 0.931 |
| bfr-I | bfr-II | PP_0482 | PP_1082 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 0.963 |
| bfr-II | PP_1083 | PP_1082 | PP_1083 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | (2Fe-2S)-binding protein. | 0.992 |
| bfr-II | PP_4856 | PP_1082 | PP_4856 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | Ferritin, Dps family protein. | 0.941 |
| bfr-II | bfr-I | PP_1082 | PP_0482 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 0.963 |