| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PP_1661 | PP_1832 | PP_1661 | PP_1832 | Putative Dehydrogenase subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Putative Oxidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.839 |
| PP_1831 | PP_1832 | PP_1831 | PP_1832 | Putative Membrane protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Putative Oxidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.838 |
| PP_1832 | PP_1661 | PP_1832 | PP_1661 | Putative Oxidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Putative Dehydrogenase subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.839 |
| PP_1832 | PP_1831 | PP_1832 | PP_1831 | Putative Oxidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Putative Membrane protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.838 |
| PP_1832 | amaC | PP_1832 | PP_3590 | Putative Oxidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | D-lysine aminotransferase; Function experimentally demonstrated in the studied strain; enzyme; Aminoacidbiosynthesis : Aromatic amino acid family. | 0.912 |
| PP_1832 | cumA | PP_1832 | PP_1034 | Putative Oxidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Multicopper oxidase; Function experimentally demonstrated in the studied species; enzyme. | 0.839 |
| PP_1832 | mcoA | PP_1832 | PP_3184 | Putative Oxidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Mn(II) copper oxidase A; Function experimentally demonstrated in the studied species; enzyme; Biologicalprocesses : Scavenge (Catabolism). | 0.834 |
| PP_1832 | metH | PP_1832 | PP_2375 | Putative Oxidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Cobalamin-dependent methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | 0.730 |
| PP_1832 | mnxG | PP_1832 | PP_3490 | Putative Oxidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Manganese-oxidizing multicopper oxidase; Function experimentally demonstrated in the studied species; enzyme; Biologicalprocesses : Scavenge (Catabolism). | 0.839 |
| PP_1832 | mtnA | PP_1832 | PP_1766 | Putative Oxidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Methylthioribose-1-phosphate isomerase; Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). | 0.860 |
| PP_1832 | nicD | PP_1832 | PP_3943 | Putative Oxidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | N-formylmaleamate deformylase; Deformylase that catalyzes the conversion of N-formylmaleamic acid to maleamate in the aerobic nicotinate degradation pathway. | 0.737 |
| PP_1832 | tyrB | PP_1832 | PP_1972 | Putative Oxidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Aromatic-amino-acid aminotransferase; Function experimentally demonstrated in the studied strain; enzyme; Aminoacidbiosynthesis : Aspartate family. | 0.912 |
| amaC | PP_1832 | PP_3590 | PP_1832 | D-lysine aminotransferase; Function experimentally demonstrated in the studied strain; enzyme; Aminoacidbiosynthesis : Aromatic amino acid family. | Putative Oxidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.912 |
| amaC | metH | PP_3590 | PP_2375 | D-lysine aminotransferase; Function experimentally demonstrated in the studied strain; enzyme; Aminoacidbiosynthesis : Aromatic amino acid family. | Cobalamin-dependent methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | 0.918 |
| amaC | tyrB | PP_3590 | PP_1972 | D-lysine aminotransferase; Function experimentally demonstrated in the studied strain; enzyme; Aminoacidbiosynthesis : Aromatic amino acid family. | Aromatic-amino-acid aminotransferase; Function experimentally demonstrated in the studied strain; enzyme; Aminoacidbiosynthesis : Aspartate family. | 0.906 |
| cumA | PP_1832 | PP_1034 | PP_1832 | Multicopper oxidase; Function experimentally demonstrated in the studied species; enzyme. | Putative Oxidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.839 |
| cumA | mcoA | PP_1034 | PP_3184 | Multicopper oxidase; Function experimentally demonstrated in the studied species; enzyme. | Mn(II) copper oxidase A; Function experimentally demonstrated in the studied species; enzyme; Biologicalprocesses : Scavenge (Catabolism). | 0.914 |
| cumA | mnxG | PP_1034 | PP_3490 | Multicopper oxidase; Function experimentally demonstrated in the studied species; enzyme. | Manganese-oxidizing multicopper oxidase; Function experimentally demonstrated in the studied species; enzyme; Biologicalprocesses : Scavenge (Catabolism). | 0.930 |
| mcoA | PP_1832 | PP_3184 | PP_1832 | Mn(II) copper oxidase A; Function experimentally demonstrated in the studied species; enzyme; Biologicalprocesses : Scavenge (Catabolism). | Putative Oxidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.834 |
| mcoA | cumA | PP_3184 | PP_1034 | Mn(II) copper oxidase A; Function experimentally demonstrated in the studied species; enzyme; Biologicalprocesses : Scavenge (Catabolism). | Multicopper oxidase; Function experimentally demonstrated in the studied species; enzyme. | 0.914 |