| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PP_0738 | PP_0742 | PP_0738 | PP_0742 | Homologs of previously reported genes of unknown function. | Conserved exported protein of unknown function; Catalyzes the oxidation of the 1,2-dihydro- and 1,6- dihydro- isomeric forms of beta-NAD(P) back to beta-NAD(P)+. May serve to protect primary metabolism dehydrogenases from inhibition by the 1,2-dihydro- and 1,6-dihydro-beta-NAD(P) isomers; Belongs to the bacterial renalase family. | 0.523 |
| PP_0738 | yfcH | PP_0738 | PP_0743 | Homologs of previously reported genes of unknown function. | Conserved protein with NAD(P)-binding Rossmann-fold domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Cellularprocesses : Cell division. | 0.497 |
| PP_0742 | PP_0738 | PP_0742 | PP_0738 | Conserved exported protein of unknown function; Catalyzes the oxidation of the 1,2-dihydro- and 1,6- dihydro- isomeric forms of beta-NAD(P) back to beta-NAD(P)+. May serve to protect primary metabolism dehydrogenases from inhibition by the 1,2-dihydro- and 1,6-dihydro-beta-NAD(P) isomers; Belongs to the bacterial renalase family. | Homologs of previously reported genes of unknown function. | 0.523 |
| PP_0742 | hemH | PP_0742 | PP_0744 | Conserved exported protein of unknown function; Catalyzes the oxidation of the 1,2-dihydro- and 1,6- dihydro- isomeric forms of beta-NAD(P) back to beta-NAD(P)+. May serve to protect primary metabolism dehydrogenases from inhibition by the 1,2-dihydro- and 1,6-dihydro-beta-NAD(P) isomers; Belongs to the bacterial renalase family. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 0.627 |
| PP_0742 | yfcH | PP_0742 | PP_0743 | Conserved exported protein of unknown function; Catalyzes the oxidation of the 1,2-dihydro- and 1,6- dihydro- isomeric forms of beta-NAD(P) back to beta-NAD(P)+. May serve to protect primary metabolism dehydrogenases from inhibition by the 1,2-dihydro- and 1,6-dihydro-beta-NAD(P) isomers; Belongs to the bacterial renalase family. | Conserved protein with NAD(P)-binding Rossmann-fold domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Cellularprocesses : Cell division. | 0.578 |
| PP_1392 | PP_2323 | PP_1392 | PP_2323 | Putative NAD-binding protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Homologs of previously reported genes of unknown function. | 0.543 |
| PP_1392 | PP_3629 | PP_1392 | PP_3629 | Putative NAD-binding protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Homologs of previously reported genes of unknown function. | 0.400 |
| PP_1392 | arcA | PP_1392 | PP_1001 | Putative NAD-binding protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Arginine deiminase; Function experimentally demonstrated in the studied species; enzyme; Fattyacidandphospholipidmetabolism : Degradation. | 0.481 |
| PP_1392 | yfcH | PP_1392 | PP_0743 | Putative NAD-binding protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Conserved protein with NAD(P)-binding Rossmann-fold domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Cellularprocesses : Cell division. | 0.545 |
| PP_1392 | yqhD | PP_1392 | PP_2492 | Putative NAD-binding protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Alcohol dehydrogenase, NAD(P)-dependent; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Central intermediary metabolism. | 0.511 |
| PP_2323 | PP_1392 | PP_2323 | PP_1392 | Homologs of previously reported genes of unknown function. | Putative NAD-binding protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.543 |
| PP_2323 | yfcH | PP_2323 | PP_0743 | Homologs of previously reported genes of unknown function. | Conserved protein with NAD(P)-binding Rossmann-fold domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Cellularprocesses : Cell division. | 0.598 |
| PP_2323 | yqhD | PP_2323 | PP_2492 | Homologs of previously reported genes of unknown function. | Alcohol dehydrogenase, NAD(P)-dependent; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Central intermediary metabolism. | 0.531 |
| PP_3629 | PP_1392 | PP_3629 | PP_1392 | Homologs of previously reported genes of unknown function. | Putative NAD-binding protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.400 |
| PP_3629 | yfcH | PP_3629 | PP_0743 | Homologs of previously reported genes of unknown function. | Conserved protein with NAD(P)-binding Rossmann-fold domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Cellularprocesses : Cell division. | 0.534 |
| PP_5037 | yfcH | PP_5037 | PP_0743 | Lipocalin family lipoprotein; Involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Displays a binding preference for lysophospholipids. | Conserved protein with NAD(P)-binding Rossmann-fold domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Cellularprocesses : Cell division. | 0.900 |
| arcA | PP_1392 | PP_1001 | PP_1392 | Arginine deiminase; Function experimentally demonstrated in the studied species; enzyme; Fattyacidandphospholipidmetabolism : Degradation. | Putative NAD-binding protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.481 |
| arcA | yfcH | PP_1001 | PP_0743 | Arginine deiminase; Function experimentally demonstrated in the studied species; enzyme; Fattyacidandphospholipidmetabolism : Degradation. | Conserved protein with NAD(P)-binding Rossmann-fold domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Cellularprocesses : Cell division. | 0.529 |
| arcA | yqhD | PP_1001 | PP_2492 | Arginine deiminase; Function experimentally demonstrated in the studied species; enzyme; Fattyacidandphospholipidmetabolism : Degradation. | Alcohol dehydrogenase, NAD(P)-dependent; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Central intermediary metabolism. | 0.527 |
| hemH | PP_0742 | PP_0744 | PP_0742 | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | Conserved exported protein of unknown function; Catalyzes the oxidation of the 1,2-dihydro- and 1,6- dihydro- isomeric forms of beta-NAD(P) back to beta-NAD(P)+. May serve to protect primary metabolism dehydrogenases from inhibition by the 1,2-dihydro- and 1,6-dihydro-beta-NAD(P) isomers; Belongs to the bacterial renalase family. | 0.627 |