| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CEL31690.1 | ctaC | SRM1_05059 | SRM1_00136 | Hypothetical protein. | Cytochrome c oxidase subunit 2 precursor; 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). | 0.877 |
| CEL31690.1 | fdx_2 | SRM1_05059 | SRM1_05444 | Hypothetical protein. | Ferredoxin. | 0.930 |
| CEL31690.1 | nuoC | SRM1_05059 | SRM1_03447 | Hypothetical protein. | NADH-quinone oxidoreductase subunit C/D; 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; In the N-terminal section; belongs to the complex I 30 kDa subunit family. | 0.999 |
| CEL31690.1 | nuoE | SRM1_05059 | SRM1_03448 | Hypothetical protein. | NADH-quinone oxidoreductase subunit E. | 0.937 |
| CEL31690.1 | nuoF | SRM1_05059 | SRM1_03449 | Hypothetical protein. | NADH-quinone oxidoreductase subunit 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. | 0.969 |
| CEL31690.1 | nuoG | SRM1_05059 | SRM1_03450 | Hypothetical protein. | NADH-quinone oxidoreductase subunit G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 75 kDa subunit family. | 0.955 |
| CEL31690.1 | nuoI | SRM1_05059 | SRM1_03452 | Hypothetical protein. | NADH-quinone oxidoreductase subunit I; 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. | 0.930 |
| CEL31690.1 | pcm | SRM1_05059 | SRM1_01158 | Hypothetical protein. | Protein-L-isoaspartate O-methyltransferase; Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. | 0.830 |
| CEL31690.1 | yhbU | SRM1_05059 | SRM1_03649 | Hypothetical protein. | Putative protease YhbU precursor. | 0.742 |
| ctaC | CEL31690.1 | SRM1_00136 | SRM1_05059 | Cytochrome c oxidase subunit 2 precursor; 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). | Hypothetical protein. | 0.877 |
| ctaC | fdx_2 | SRM1_00136 | SRM1_05444 | Cytochrome c oxidase subunit 2 precursor; 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). | Ferredoxin. | 0.907 |
| ctaC | nuoC | SRM1_00136 | SRM1_03447 | Cytochrome c oxidase subunit 2 precursor; 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). | NADH-quinone oxidoreductase subunit C/D; 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; In the N-terminal section; belongs to the complex I 30 kDa subunit family. | 0.999 |
| ctaC | nuoE | SRM1_00136 | SRM1_03448 | Cytochrome c oxidase subunit 2 precursor; 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). | NADH-quinone oxidoreductase subunit E. | 0.931 |
| ctaC | nuoF | SRM1_00136 | SRM1_03449 | Cytochrome c oxidase subunit 2 precursor; 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). | NADH-quinone oxidoreductase subunit 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. | 0.920 |
| ctaC | nuoG | SRM1_00136 | SRM1_03450 | Cytochrome c oxidase subunit 2 precursor; 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). | NADH-quinone oxidoreductase subunit G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 75 kDa subunit family. | 0.928 |
| ctaC | nuoI | SRM1_00136 | SRM1_03452 | Cytochrome c oxidase subunit 2 precursor; 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). | NADH-quinone oxidoreductase subunit I; 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. | 0.907 |
| ctaC | pcm | SRM1_00136 | SRM1_01158 | Cytochrome c oxidase subunit 2 precursor; 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). | Protein-L-isoaspartate O-methyltransferase; Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. | 0.834 |
| ctaC | yhbU | SRM1_00136 | SRM1_03649 | Cytochrome c oxidase subunit 2 precursor; 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). | Putative protease YhbU precursor. | 0.804 |
| fdx_2 | CEL31690.1 | SRM1_05444 | SRM1_05059 | Ferredoxin. | Hypothetical protein. | 0.930 |
| fdx_2 | ctaC | SRM1_05444 | SRM1_00136 | Ferredoxin. | Cytochrome c oxidase subunit 2 precursor; 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). | 0.907 |
