node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
APD09251.1 | APD09706.1 | A0O31_01108 | A0O31_01597 | Cytochrome Caa3 oxidase subunit IIC; 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 13. | 0.999 |
APD09251.1 | APD09707.1 | A0O31_01108 | A0O31_01598 | Cytochrome Caa3 oxidase subunit IIC; 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 12. | 0.652 |
APD09251.1 | APD09714.1 | A0O31_01108 | A0O31_01605 | Cytochrome Caa3 oxidase subunit IIC; 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 2. | 0.999 |
APD09251.1 | nuoC | A0O31_01108 | A0O31_01607 | Cytochrome Caa3 oxidase subunit IIC; 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 5; 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 30 kDa subunit family. | 0.999 |
APD09251.1 | nuoD | A0O31_01108 | A0O31_01606 | Cytochrome Caa3 oxidase subunit IIC; 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 4; 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 |
APD09251.1 | nuoH | A0O31_01108 | A0O31_01602 | Cytochrome Caa3 oxidase subunit IIC; 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 8; 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. This subunit may bind ubiquinone. | 0.999 |
APD09251.1 | nuoI | A0O31_01108 | A0O31_01601 | Cytochrome Caa3 oxidase subunit IIC; 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 9; 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 |
APD09251.1 | nuoN | A0O31_01108 | A0O31_01596 | Cytochrome Caa3 oxidase subunit IIC; 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 14; 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. | 0.999 |
APD09706.1 | APD09251.1 | A0O31_01597 | A0O31_01108 | NADH-quinone oxidoreductase subunit 13. | Cytochrome Caa3 oxidase subunit IIC; 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 |
APD09706.1 | APD09707.1 | A0O31_01597 | A0O31_01598 | NADH-quinone oxidoreductase subunit 13. | NADH-quinone oxidoreductase subunit 12. | 0.999 |
APD09706.1 | APD09709.1 | A0O31_01597 | A0O31_01600 | NADH-quinone oxidoreductase subunit 13. | NADH-quinone oxidoreductase subunit 10; 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. | 0.999 |
APD09706.1 | APD09714.1 | A0O31_01597 | A0O31_01605 | NADH-quinone oxidoreductase subunit 13. | NADH-quinone oxidoreductase subunit 2. | 0.999 |
APD09706.1 | nuoC | A0O31_01597 | A0O31_01607 | NADH-quinone oxidoreductase subunit 13. | NADH-quinone oxidoreductase subunit 5; 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 30 kDa subunit family. | 0.999 |
APD09706.1 | nuoD | A0O31_01597 | A0O31_01606 | NADH-quinone oxidoreductase subunit 13. | NADH-quinone oxidoreductase subunit 4; 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 |
APD09706.1 | nuoH | A0O31_01597 | A0O31_01602 | NADH-quinone oxidoreductase subunit 13. | NADH-quinone oxidoreductase subunit 8; 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. This subunit may bind ubiquinone. | 0.999 |
APD09706.1 | nuoI | A0O31_01597 | A0O31_01601 | NADH-quinone oxidoreductase subunit 13. | NADH-quinone oxidoreductase subunit 9; 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 |
APD09706.1 | nuoK | A0O31_01597 | A0O31_01599 | NADH-quinone oxidoreductase subunit 13. | NADH-quinone oxidoreductase subunit 11; 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 4L family. | 0.999 |
APD09706.1 | nuoN | A0O31_01597 | A0O31_01596 | NADH-quinone oxidoreductase subunit 13. | NADH-quinone oxidoreductase subunit 14; 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. | 0.999 |
APD09707.1 | APD09251.1 | A0O31_01598 | A0O31_01108 | NADH-quinone oxidoreductase subunit 12. | Cytochrome Caa3 oxidase subunit IIC; 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). | 0.652 |
APD09707.1 | APD09706.1 | A0O31_01598 | A0O31_01597 | NADH-quinone oxidoreductase subunit 12. | NADH-quinone oxidoreductase subunit 13. | 0.999 |