| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Bsel_1624 | Bsel_2115 | Bsel_1624 | Bsel_2115 | 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). | PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: gur:Gura_2379 Rieske (2Fe-2S) domain-containing protein. | 0.999 |
| Bsel_1624 | Bsel_2674 | Bsel_1624 | Bsel_2674 | 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). | PFAM: NmrA family protein; KEGG: hypothetical protein. | 0.986 |
| Bsel_1624 | Bsel_3141 | Bsel_1624 | Bsel_3141 | 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). | KEGG: gme:Gmet_3343 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). | 0.999 |
| Bsel_1624 | Bsel_3148 | Bsel_1624 | Bsel_3148 | 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). | PFAM: NADH dehydrogenase (ubiquinone) 30 kDa subunit; KEGG: scl:sce9060 NADH dehydrogenase (ubiquinone). | 0.999 |
| Bsel_1624 | acpP | Bsel_1624 | Bsel_1711 | 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). | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 0.998 |
| Bsel_1624 | nuoA | Bsel_1624 | Bsel_3150 | 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-ubiquinone/plastoquinone oxidoreductase chain 3; 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 a menaquinone. 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. | 0.998 |
| Bsel_1624 | nuoB | Bsel_1624 | Bsel_3149 | 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-quinone oxidoreductase, B subunit; 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 a menaquinone. 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. | 0.999 |
| Bsel_1624 | nuoD | Bsel_1624 | Bsel_3147 | 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, D subunit; 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 a menaquinone. 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. | 0.999 |
| Bsel_1624 | nuoI | Bsel_1624 | Bsel_3145 | 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-quinone oxidoreductase, chain 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. | 0.999 |
| Bsel_1624 | nuoN | Bsel_1624 | Bsel_3140 | 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). | Proton-translocating NADH-quinone oxidoreductase, chain N; 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 a menaquinone. 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 2 family. | 0.997 |
| Bsel_2115 | Bsel_1624 | Bsel_2115 | Bsel_1624 | PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: gur:Gura_2379 Rieske (2Fe-2S) domain-containing protein. | 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). | 0.999 |
| Bsel_2115 | Bsel_2674 | Bsel_2115 | Bsel_2674 | PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: gur:Gura_2379 Rieske (2Fe-2S) domain-containing protein. | PFAM: NmrA family protein; KEGG: hypothetical protein. | 0.844 |
| Bsel_2115 | Bsel_3141 | Bsel_2115 | Bsel_3141 | PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: gur:Gura_2379 Rieske (2Fe-2S) domain-containing protein. | KEGG: gme:Gmet_3343 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). | 0.940 |
| Bsel_2115 | Bsel_3148 | Bsel_2115 | Bsel_3148 | PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: gur:Gura_2379 Rieske (2Fe-2S) domain-containing protein. | PFAM: NADH dehydrogenase (ubiquinone) 30 kDa subunit; KEGG: scl:sce9060 NADH dehydrogenase (ubiquinone). | 0.970 |
| Bsel_2115 | acpP | Bsel_2115 | Bsel_1711 | PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: gur:Gura_2379 Rieske (2Fe-2S) domain-containing protein. | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 0.946 |
| Bsel_2115 | nuoA | Bsel_2115 | Bsel_3150 | PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: gur:Gura_2379 Rieske (2Fe-2S) domain-containing protein. | NADH-ubiquinone/plastoquinone oxidoreductase chain 3; 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 a menaquinone. 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. | 0.950 |
| Bsel_2115 | nuoB | Bsel_2115 | Bsel_3149 | PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: gur:Gura_2379 Rieske (2Fe-2S) domain-containing protein. | NADH-quinone oxidoreductase, B subunit; 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 a menaquinone. 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. | 0.970 |
| Bsel_2115 | nuoD | Bsel_2115 | Bsel_3147 | PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: gur:Gura_2379 Rieske (2Fe-2S) domain-containing protein. | NADH dehydrogenase I, D subunit; 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 a menaquinone. 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. | 0.986 |
| Bsel_2115 | nuoI | Bsel_2115 | Bsel_3145 | PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: gur:Gura_2379 Rieske (2Fe-2S) domain-containing protein. | NADH-quinone oxidoreductase, chain 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. | 0.989 |
| Bsel_2115 | nuoN | Bsel_2115 | Bsel_3140 | PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: gur:Gura_2379 Rieske (2Fe-2S) domain-containing protein. | Proton-translocating NADH-quinone oxidoreductase, chain N; 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 a menaquinone. 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 2 family. | 0.929 |