| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PP_2236 | PP_2238 | PP_2236 | PP_2238 | Putative hydrolase of the alpha/beta superfamily; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Proteinfate : Degradation of proteins, peptides, and glycopeptides. | 0.538 |
| PP_2238 | PP_2236 | PP_2238 | PP_2236 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Proteinfate : Degradation of proteins, peptides, and glycopeptides. | Putative hydrolase of the alpha/beta superfamily; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.538 |
| PP_2238 | PP_4108 | PP_2238 | PP_4108 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Proteinfate : Degradation of proteins, peptides, and glycopeptides. | Putative 4-aminobutyrate aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. | 0.783 |
| PP_2238 | amaC | PP_2238 | PP_3590 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Proteinfate : Degradation of proteins, peptides, and glycopeptides. | D-lysine aminotransferase; Function experimentally demonstrated in the studied strain; enzyme; Aminoacidbiosynthesis : Aromatic amino acid family. | 0.742 |
| PP_2238 | creA | PP_2238 | PP_3667 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Proteinfate : Degradation of proteins, peptides, and glycopeptides. | Creatinase; Function experimentally demonstrated in the studied species; enzyme; Proteinfate : Degradation of proteins, peptides, and glycopeptides. | 0.766 |
| PP_2238 | gdhB | PP_2238 | PP_2080 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Proteinfate : Degradation of proteins, peptides, and glycopeptides. | NAD-specific glutamate dehydrogenase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Energymetabolism : Amino acids and amines. | 0.634 |
| PP_2238 | map | PP_2238 | PP_1590 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Proteinfate : Degradation of proteins, peptides, and glycopeptides. | Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.908 |
| PP_2238 | mdeA | PP_2238 | PP_1308 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Proteinfate : Degradation of proteins, peptides, and glycopeptides. | Methionine gamma-lyase; Function experimentally demonstrated in the studied strain; enzyme; Fattyacidandphospholipidmetabolism : Degradation. | 0.587 |
| PP_2238 | pip | PP_2238 | PP_5028 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Proteinfate : Degradation of proteins, peptides, and glycopeptides. | Proline iminopeptidase; Function of strongly homologous gene; enzyme; Belongs to the peptidase S33 family. | 0.574 |
| PP_2238 | ppx | PP_2238 | PP_5216 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Proteinfate : Degradation of proteins, peptides, and glycopeptides. | Exopolyphosphatase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Centralintermediarymetabolism : Phosphorus compounds; Belongs to the GppA/Ppx family. | 0.540 |
| PP_2238 | puuE | PP_2238 | PP_4286 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Proteinfate : Degradation of proteins, peptides, and glycopeptides. | Allantoinase; Function experimentally demonstrated in the studied genus; enzyme; Fattyacidandphospholipidmetabolism : Degradation. | 0.771 |
| PP_4108 | PP_2238 | PP_4108 | PP_2238 | Putative 4-aminobutyrate aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Proteinfate : Degradation of proteins, peptides, and glycopeptides. | 0.783 |
| PP_4108 | puuE | PP_4108 | PP_4286 | Putative 4-aminobutyrate aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. | Allantoinase; Function experimentally demonstrated in the studied genus; enzyme; Fattyacidandphospholipidmetabolism : Degradation. | 0.762 |
| amaC | PP_2238 | PP_3590 | PP_2238 | D-lysine aminotransferase; Function experimentally demonstrated in the studied strain; enzyme; Aminoacidbiosynthesis : Aromatic amino acid family. | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Proteinfate : Degradation of proteins, peptides, and glycopeptides. | 0.742 |
| amaC | gdhB | PP_3590 | PP_2080 | D-lysine aminotransferase; Function experimentally demonstrated in the studied strain; enzyme; Aminoacidbiosynthesis : Aromatic amino acid family. | NAD-specific glutamate dehydrogenase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Energymetabolism : Amino acids and amines. | 0.514 |
| amaC | map | PP_3590 | PP_1590 | D-lysine aminotransferase; Function experimentally demonstrated in the studied strain; enzyme; Aminoacidbiosynthesis : Aromatic amino acid family. | Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.683 |
| amaC | mdeA | PP_3590 | PP_1308 | D-lysine aminotransferase; Function experimentally demonstrated in the studied strain; enzyme; Aminoacidbiosynthesis : Aromatic amino acid family. | Methionine gamma-lyase; Function experimentally demonstrated in the studied strain; enzyme; Fattyacidandphospholipidmetabolism : Degradation. | 0.944 |
| amaC | pip | PP_3590 | PP_5028 | D-lysine aminotransferase; Function experimentally demonstrated in the studied strain; enzyme; Aminoacidbiosynthesis : Aromatic amino acid family. | Proline iminopeptidase; Function of strongly homologous gene; enzyme; Belongs to the peptidase S33 family. | 0.417 |
| creA | PP_2238 | PP_3667 | PP_2238 | Creatinase; Function experimentally demonstrated in the studied species; enzyme; Proteinfate : Degradation of proteins, peptides, and glycopeptides. | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Proteinfate : Degradation of proteins, peptides, and glycopeptides. | 0.766 |
| creA | map | PP_3667 | PP_1590 | Creatinase; Function experimentally demonstrated in the studied species; enzyme; Proteinfate : Degradation of proteins, peptides, and glycopeptides. | Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.770 |