| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PP_0103 | PP_0111 | PP_0103 | PP_0111 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Electron transport protein SCO1/SenC. | 0.765 |
| PP_0103 | PP_1646 | PP_0103 | PP_1646 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Putative Thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.611 |
| PP_0103 | PP_2379 | PP_0103 | PP_2379 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Putative cytochrome oxidase biogenesis protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor; Energymetabolism : Electron transport. | 0.758 |
| PP_0103 | PP_4236 | PP_0103 | PP_4236 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Putative Thiol:disulfide interchange protein dsbE; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.585 |
| PP_0111 | PP_0103 | PP_0111 | PP_0103 | Electron transport protein SCO1/SenC. | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.765 |
| PP_0111 | PP_1646 | PP_0111 | PP_1646 | Electron transport protein SCO1/SenC. | Putative Thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.731 |
| PP_0111 | PP_4236 | PP_0111 | PP_4236 | Electron transport protein SCO1/SenC. | Putative Thiol:disulfide interchange protein dsbE; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.578 |
| PP_1643 | PP_1644 | PP_1643 | PP_1644 | Homologs of previously reported genes of unknown function. | NAD(P)H dehydrogenase (quinone); Belongs to the WrbA family. | 0.870 |
| PP_1643 | PP_1646 | PP_1643 | PP_1646 | Homologs of previously reported genes of unknown function. | Putative Thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.592 |
| PP_1643 | yfgD | PP_1643 | PP_1645 | Homologs of previously reported genes of unknown function. | Putative enzyme; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Cellularprocesses : Detoxification. | 0.873 |
| PP_1644 | PP_1643 | PP_1644 | PP_1643 | NAD(P)H dehydrogenase (quinone); Belongs to the WrbA family. | Homologs of previously reported genes of unknown function. | 0.870 |
| PP_1644 | PP_1646 | PP_1644 | PP_1646 | NAD(P)H dehydrogenase (quinone); Belongs to the WrbA family. | Putative Thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.597 |
| PP_1644 | yfgD | PP_1644 | PP_1645 | NAD(P)H dehydrogenase (quinone); Belongs to the WrbA family. | Putative enzyme; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Cellularprocesses : Detoxification. | 0.904 |
| PP_1646 | PP_0103 | PP_1646 | PP_0103 | Putative Thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.611 |
| PP_1646 | PP_0111 | PP_1646 | PP_0111 | Putative Thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Electron transport protein SCO1/SenC. | 0.731 |
| PP_1646 | PP_1643 | PP_1646 | PP_1643 | Putative Thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Homologs of previously reported genes of unknown function. | 0.592 |
| PP_1646 | PP_1644 | PP_1646 | PP_1644 | Putative Thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | NAD(P)H dehydrogenase (quinone); Belongs to the WrbA family. | 0.597 |
| PP_1646 | PP_2379 | PP_1646 | PP_2379 | Putative Thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Putative cytochrome oxidase biogenesis protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor; Energymetabolism : Electron transport. | 0.665 |
| PP_1646 | PP_4236 | PP_1646 | PP_4236 | Putative Thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Putative Thiol:disulfide interchange protein dsbE; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.687 |
| PP_1646 | dsbD-I | PP_1646 | PP_0561 | Putative Thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Thiol/disulfide interchange protein 1; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily. | 0.675 |