| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AKU12873.1 | AKU13603.1 | AzCIB_2980 | AzCIB_3710 | Hydrogen dehydrogenase, alpha subunit. | Cytochrome c oxidase subunit II; 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). | 0.940 |
| AKU12873.1 | AKU14480.1 | AzCIB_2980 | AzCIB_4594 | Hydrogen dehydrogenase, alpha subunit. | Formate dehydrogenase, NAD(P) reducing, beta subunit. | 0.997 |
| AKU12873.1 | nuoA | AzCIB_2980 | AzCIB_2996 | Hydrogen dehydrogenase, alpha subunit. | NADH dehydrogenase I subunit A; 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 subunit 3 family. | 0.997 |
| AKU12873.1 | nuoC | AzCIB_2980 | AzCIB_2994 | Hydrogen dehydrogenase, alpha subunit. | NADH dehydrogenase subunit 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. | 0.997 |
| AKU12873.1 | nuoD | AzCIB_2980 | AzCIB_2993 | Hydrogen dehydrogenase, alpha subunit. | NADH dehydrogenase subunit 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; Belongs to the complex I 49 kDa subunit family. | 0.997 |
| AKU12873.1 | pcm | AzCIB_2980 | AzCIB_3586 | Hydrogen dehydrogenase, alpha subunit. | protein-L-isoaspartate(D-aspartate) 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. | 0.795 |
| AKU13478.1 | pcm | AzCIB_3585 | AzCIB_3586 | Putative peptidase. | protein-L-isoaspartate(D-aspartate) 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. | 0.851 |
| AKU13478.1 | rpoS | AzCIB_3585 | AzCIB_3584 | Putative peptidase. | RNA polymerase factor sigma-38 subunit; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the master transcriptional regulator of the stationary phase and the general stress response. | 0.889 |
| AKU13478.1 | surE | AzCIB_3585 | AzCIB_3587 | Putative peptidase. | Stationary phase survival protein; Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates; Belongs to the SurE nucleotidase family. | 0.870 |
| AKU13603.1 | AKU12873.1 | AzCIB_3710 | AzCIB_2980 | Cytochrome c oxidase subunit II; 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). | Hydrogen dehydrogenase, alpha subunit. | 0.940 |
| AKU13603.1 | AKU14480.1 | AzCIB_3710 | AzCIB_4594 | Cytochrome c oxidase subunit II; 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). | Formate dehydrogenase, NAD(P) reducing, beta subunit. | 0.940 |
| AKU13603.1 | nuoA | AzCIB_3710 | AzCIB_2996 | Cytochrome c oxidase subunit II; 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 dehydrogenase I subunit A; 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 subunit 3 family. | 0.977 |
| AKU13603.1 | nuoC | AzCIB_3710 | AzCIB_2994 | Cytochrome c oxidase subunit II; 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 dehydrogenase subunit 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. | 0.933 |
| AKU13603.1 | nuoD | AzCIB_3710 | AzCIB_2993 | Cytochrome c oxidase subunit II; 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 dehydrogenase subunit 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; Belongs to the complex I 49 kDa subunit family. | 0.895 |
| AKU13603.1 | pcm | AzCIB_3710 | AzCIB_3586 | Cytochrome c oxidase subunit II; 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(D-aspartate) 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. | 0.749 |
| AKU14480.1 | AKU12873.1 | AzCIB_4594 | AzCIB_2980 | Formate dehydrogenase, NAD(P) reducing, beta subunit. | Hydrogen dehydrogenase, alpha subunit. | 0.997 |
| AKU14480.1 | AKU13603.1 | AzCIB_4594 | AzCIB_3710 | Formate dehydrogenase, NAD(P) reducing, beta subunit. | Cytochrome c oxidase subunit II; 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). | 0.940 |
| AKU14480.1 | nuoA | AzCIB_4594 | AzCIB_2996 | Formate dehydrogenase, NAD(P) reducing, beta subunit. | NADH dehydrogenase I subunit A; 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 subunit 3 family. | 0.997 |
| AKU14480.1 | nuoC | AzCIB_4594 | AzCIB_2994 | Formate dehydrogenase, NAD(P) reducing, beta subunit. | NADH dehydrogenase subunit 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. | 0.997 |
| AKU14480.1 | nuoD | AzCIB_4594 | AzCIB_2993 | Formate dehydrogenase, NAD(P) reducing, beta subunit. | NADH dehydrogenase subunit 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; Belongs to the complex I 49 kDa subunit family. | 0.997 |
