| 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. | 0.773 |
| 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. | 0.662 |
| 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. | 0.766 |
| 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. | 0.707 |
| 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). | 0.773 |
| 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. | 0.754 |
| 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. | 0.618 |
| PP_0235 | PP_1646 | PP_0235 | PP_1646 | Peroxidase. | Putative Thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.642 |
| PP_0235 | PP_2700 | PP_0235 | PP_2700 | Peroxidase. | AhpC/TSA family protein; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. Prx5 subfamily. | 0.726 |
| PP_0235 | PP_4236 | PP_0235 | PP_4236 | Peroxidase. | Putative Thiol:disulfide interchange protein dsbE; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.637 |
| 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). | 0.662 |
| 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. | 0.754 |
| PP_1646 | PP_0235 | PP_1646 | PP_0235 | Putative Thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Peroxidase. | 0.642 |
| 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. | 0.694 |
| PP_1646 | PP_2700 | PP_1646 | PP_2700 | Putative Thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | AhpC/TSA family protein; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. Prx5 subfamily. | 0.652 |
| 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. | 0.688 |
| 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. | 0.671 |
| PP_1646 | dsbD-II | PP_1646 | PP_4235 | Putative Thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Thiol/disulfide interchange protein 2; 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. | 0.653 |
| PP_1646 | msrA | PP_1646 | PP_0336 | Putative Thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Peptide methionine sulfoxide reductase MsrA; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.751 |
| PP_1646 | nrdA | PP_1646 | PP_1179 | Putative Thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Ribonucleoside-diphosphate reductase subunit alpha; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. | 0.763 |