| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| hemG | pepQ | STM3987 | STM3984 | Protoporphyrin oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX using menaquinone as electron acceptor. | Proline dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position. | 0.698 |
| hemG | trkH | STM3987 | STM3986 | Protoporphyrin oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX using menaquinone as electron acceptor. | Trk family potassium transport protein; Low-affinity potassium transport system. Interacts with Trk system potassium uptake protein TrkA and requires TrkE for transport activity (By similarity); Belongs to the TrkH potassium transport family. | 0.822 |
| hemG | yigZ | STM3987 | STM3985 | Protoporphyrin oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX using menaquinone as electron acceptor. | Putative cytoplasmic protein; Similar to E. coli orf, hypothetical protein (AAC76851.1); Blastp hit to AAC76851.1 (205 aa), 91% identity in aa 2 - 205. | 0.764 |
| map | pepN | STM0215 | STM1057 | 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. | Similar to E. coli aminopeptidase N (AAC74018.1); Blastp hit to AAC74018.1 (870 aa), 94% identity in aa 1 - 870. | 0.427 |
| map | pepQ | STM0215 | STM3984 | 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. | Proline dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position. | 0.858 |
| map | pepT | STM0215 | STM1227 | 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. | Putative peptidase T; Cleaves the N-terminal amino acid of tripeptides. Hydrolyzes tripeptides containing N-terminal methionine, leucine, or phenylalanine. Displays little or no activity against dipeptides, N- blocked or C-blocked tripeptides, and tetrapeptides. Belongs to the peptidase M20B family. | 0.562 |
| pepA | pepD | STM4477 | STM0316 | Aminopeptidase A; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides. | Similar to E. coli aminoacyl-histidine dipeptidase (peptidase D) (AAC73341.1); Blastp hit to AAC73341.1 (485 aa), 92% identity in aa 1 - 485. | 0.926 |
| pepA | pepN | STM4477 | STM1057 | Aminopeptidase A; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides. | Similar to E. coli aminopeptidase N (AAC74018.1); Blastp hit to AAC74018.1 (870 aa), 94% identity in aa 1 - 870. | 0.931 |
| pepA | pepQ | STM4477 | STM3984 | Aminopeptidase A; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides. | Proline dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position. | 0.782 |
| pepA | pepT | STM4477 | STM1227 | Aminopeptidase A; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides. | Putative peptidase T; Cleaves the N-terminal amino acid of tripeptides. Hydrolyzes tripeptides containing N-terminal methionine, leucine, or phenylalanine. Displays little or no activity against dipeptides, N- blocked or C-blocked tripeptides, and tetrapeptides. Belongs to the peptidase M20B family. | 0.588 |
| pepD | pepA | STM0316 | STM4477 | Similar to E. coli aminoacyl-histidine dipeptidase (peptidase D) (AAC73341.1); Blastp hit to AAC73341.1 (485 aa), 92% identity in aa 1 - 485. | Aminopeptidase A; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides. | 0.926 |
| pepD | pepN | STM0316 | STM1057 | Similar to E. coli aminoacyl-histidine dipeptidase (peptidase D) (AAC73341.1); Blastp hit to AAC73341.1 (485 aa), 92% identity in aa 1 - 485. | Similar to E. coli aminopeptidase N (AAC74018.1); Blastp hit to AAC74018.1 (870 aa), 94% identity in aa 1 - 870. | 0.986 |
| pepD | pepQ | STM0316 | STM3984 | Similar to E. coli aminoacyl-histidine dipeptidase (peptidase D) (AAC73341.1); Blastp hit to AAC73341.1 (485 aa), 92% identity in aa 1 - 485. | Proline dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position. | 0.673 |
| pepD | pepT | STM0316 | STM1227 | Similar to E. coli aminoacyl-histidine dipeptidase (peptidase D) (AAC73341.1); Blastp hit to AAC73341.1 (485 aa), 92% identity in aa 1 - 485. | Putative peptidase T; Cleaves the N-terminal amino acid of tripeptides. Hydrolyzes tripeptides containing N-terminal methionine, leucine, or phenylalanine. Displays little or no activity against dipeptides, N- blocked or C-blocked tripeptides, and tetrapeptides. Belongs to the peptidase M20B family. | 0.402 |
| pepN | map | STM1057 | STM0215 | Similar to E. coli aminopeptidase N (AAC74018.1); Blastp hit to AAC74018.1 (870 aa), 94% identity in aa 1 - 870. | 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. | 0.427 |
| pepN | pepA | STM1057 | STM4477 | Similar to E. coli aminopeptidase N (AAC74018.1); Blastp hit to AAC74018.1 (870 aa), 94% identity in aa 1 - 870. | Aminopeptidase A; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides. | 0.931 |
| pepN | pepD | STM1057 | STM0316 | Similar to E. coli aminopeptidase N (AAC74018.1); Blastp hit to AAC74018.1 (870 aa), 94% identity in aa 1 - 870. | Similar to E. coli aminoacyl-histidine dipeptidase (peptidase D) (AAC73341.1); Blastp hit to AAC73341.1 (485 aa), 92% identity in aa 1 - 485. | 0.986 |
| pepN | pepQ | STM1057 | STM3984 | Similar to E. coli aminopeptidase N (AAC74018.1); Blastp hit to AAC74018.1 (870 aa), 94% identity in aa 1 - 870. | Proline dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position. | 0.890 |
| pepN | pepT | STM1057 | STM1227 | Similar to E. coli aminopeptidase N (AAC74018.1); Blastp hit to AAC74018.1 (870 aa), 94% identity in aa 1 - 870. | Putative peptidase T; Cleaves the N-terminal amino acid of tripeptides. Hydrolyzes tripeptides containing N-terminal methionine, leucine, or phenylalanine. Displays little or no activity against dipeptides, N- blocked or C-blocked tripeptides, and tetrapeptides. Belongs to the peptidase M20B family. | 0.869 |
| pepQ | hemG | STM3984 | STM3987 | Proline dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position. | Protoporphyrin oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX using menaquinone as electron acceptor. | 0.698 |