node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ABZ97458.1 | ABZ97459.1 | LEPBI_I1348 | LEPBI_I1349 | Putative metalloendopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the peptidase M16 family. | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.967 |
ABZ97458.1 | ABZ97460.1 | LEPBI_I1348 | LEPBI_I1350 | Putative metalloendopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the peptidase M16 family. | Putative metallo-hydrolase/oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.864 |
ABZ97458.1 | ABZ97461.1 | LEPBI_I1348 | LEPBI_I1351 | Putative metalloendopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the peptidase M16 family. | Putative O-methyltransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.875 |
ABZ97458.1 | ABZ99692.1 | LEPBI_I1348 | LEPBI_II0157 | Putative metalloendopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the peptidase M16 family. | Putative 4-coumarate--CoA ligase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.952 |
ABZ97458.1 | ctaC | LEPBI_I1348 | LEPBI_I2684 | Putative metalloendopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the peptidase M16 family. | Cytochrome c oxidase polypeptide II (Cytochrome aa3 subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.975 |
ABZ97458.1 | norC | LEPBI_I1348 | LEPBI_I2955 | Putative metalloendopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the peptidase M16 family. | Nitric oxide reductase, cytochrome c-containing subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.968 |
ABZ97458.1 | nuoC | LEPBI_I1348 | LEPBI_I1298 | Putative metalloendopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the peptidase M16 family. | NADH-quinone oxidoreductase, chain C; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 30 kDa subunit family. | 0.851 |
ABZ97458.1 | nuoE | LEPBI_I1348 | LEPBI_I1300 | Putative metalloendopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the peptidase M16 family. | NADH dehydrogenase I, chain E; NDH-1, chain E; NUO5); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.860 |
ABZ97458.1 | nuoF | LEPBI_I1348 | LEPBI_I1301 | Putative metalloendopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the peptidase M16 family. | NADH-quinone oxidoreductase, chain F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. | 0.909 |
ABZ97458.1 | nuoG | LEPBI_I1348 | LEPBI_I3406 | Putative metalloendopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the peptidase M16 family. | NADH-quinone oxidoreductase chain G; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.891 |
ABZ97459.1 | ABZ97458.1 | LEPBI_I1349 | LEPBI_I1348 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative metalloendopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the peptidase M16 family. | 0.967 |
ABZ97459.1 | ABZ97460.1 | LEPBI_I1349 | LEPBI_I1350 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative metallo-hydrolase/oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.864 |
ABZ97459.1 | ABZ97461.1 | LEPBI_I1349 | LEPBI_I1351 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative O-methyltransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.875 |
ABZ97459.1 | ABZ99692.1 | LEPBI_I1349 | LEPBI_II0157 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative 4-coumarate--CoA ligase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.952 |
ABZ97459.1 | ctaC | LEPBI_I1349 | LEPBI_I2684 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Cytochrome c oxidase polypeptide II (Cytochrome aa3 subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.975 |
ABZ97459.1 | norC | LEPBI_I1349 | LEPBI_I2955 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Nitric oxide reductase, cytochrome c-containing subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.968 |
ABZ97459.1 | nuoC | LEPBI_I1349 | LEPBI_I1298 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone oxidoreductase, chain C; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 30 kDa subunit family. | 0.869 |
ABZ97459.1 | nuoE | LEPBI_I1349 | LEPBI_I1300 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH dehydrogenase I, chain E; NDH-1, chain E; NUO5); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.860 |
ABZ97459.1 | nuoF | LEPBI_I1349 | LEPBI_I1301 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone oxidoreductase, chain F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. | 0.909 |
ABZ97459.1 | nuoG | LEPBI_I1349 | LEPBI_I3406 | Putative metallopeptidase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone oxidoreductase chain G; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.891 |