| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| fadA | fadB | STM3982 | STM3983 | 3-ketoacyl-CoA thiolase; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Involved in the aerobic and anaerobic degradation of long-chain fatty acids (By similarity). | 3-hydroxyacyl-coA dehydrogenase of 4-enzyme FadB protein; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. | 0.999 |
| fadA | hemG | STM3982 | STM3987 | 3-ketoacyl-CoA thiolase; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Involved in the aerobic and anaerobic degradation of long-chain fatty acids (By similarity). | Protoporphyrin oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX using menaquinone as electron acceptor. | 0.498 |
| fadA | pepQ | STM3982 | STM3984 | 3-ketoacyl-CoA thiolase; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Involved in the aerobic and anaerobic degradation of long-chain fatty acids (By similarity). | Proline dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position. | 0.573 |
| fadA | trkH | STM3982 | STM3986 | 3-ketoacyl-CoA thiolase; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Involved in the aerobic and anaerobic degradation of long-chain fatty acids (By similarity). | 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. | 0.541 |
| fadA | yigZ | STM3982 | STM3985 | 3-ketoacyl-CoA thiolase; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Involved in the aerobic and anaerobic degradation of long-chain fatty acids (By similarity). | 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. | 0.564 |
| fadB | fadA | STM3983 | STM3982 | 3-hydroxyacyl-coA dehydrogenase of 4-enzyme FadB protein; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. | 3-ketoacyl-CoA thiolase; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Involved in the aerobic and anaerobic degradation of long-chain fatty acids (By similarity). | 0.999 |
| fadB | hemG | STM3983 | STM3987 | 3-hydroxyacyl-coA dehydrogenase of 4-enzyme FadB protein; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. | Protoporphyrin oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX using menaquinone as electron acceptor. | 0.593 |
| fadB | pepQ | STM3983 | STM3984 | 3-hydroxyacyl-coA dehydrogenase of 4-enzyme FadB protein; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. | Proline dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position. | 0.597 |
| fadB | trkH | STM3983 | STM3986 | 3-hydroxyacyl-coA dehydrogenase of 4-enzyme FadB protein; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. | 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. | 0.518 |
| fadB | yigZ | STM3983 | STM3985 | 3-hydroxyacyl-coA dehydrogenase of 4-enzyme FadB protein; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. | 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. | 0.638 |
| hemG | fadA | STM3987 | STM3982 | Protoporphyrin oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX using menaquinone as electron acceptor. | 3-ketoacyl-CoA thiolase; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Involved in the aerobic and anaerobic degradation of long-chain fatty acids (By similarity). | 0.498 |
| hemG | fadB | STM3987 | STM3983 | Protoporphyrin oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX using menaquinone as electron acceptor. | 3-hydroxyacyl-coA dehydrogenase of 4-enzyme FadB protein; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. | 0.593 |
| 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. | 0.697 |
| 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. | 0.804 |
| 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. | 0.735 |
| 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. | 0.582 |
| 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. | 0.413 |
| 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. | 0.940 |
| 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. | 0.926 |
| 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. | 0.863 |
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