node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ADH63169.1 | ADH63280.1 | Mesil_1274 | Mesil_1387 | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. | beta-Ig-H3/fasciclin; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: vsp:VS_II0883 conserved hypothetical protein-putative fasciclin domain; PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; SPTR: C1XW13 Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | 0.650 |
ADH63169.1 | nuoA | Mesil_1274 | Mesil_1283 | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. | 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. | 0.999 |
ADH63169.1 | nuoB | Mesil_1274 | Mesil_1282 | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. | 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 |
ADH63169.1 | nuoC | Mesil_1274 | Mesil_1281 | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. | NADH (or F420H2) 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 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 |
ADH63169.1 | nuoD | Mesil_1274 | Mesil_1280 | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. | 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 |
ADH63169.1 | nuoH | Mesil_1274 | Mesil_1276 | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. | NADH dehydrogenase (quinone); 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 |
ADH63169.1 | nuoI | Mesil_1274 | Mesil_1275 | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. | 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 |
ADH63169.1 | nuoK | Mesil_1274 | Mesil_1273 | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. | NADH-ubiquinone oxidoreductase chain 4L; 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 |
ADH63169.1 | nuoN | Mesil_1274 | Mesil_1270 | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. | 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. | 0.999 |
ADH63279.1 | ADH63280.1 | Mesil_1386 | Mesil_1387 | COGs: COG0415 Deoxyribodipyrimidine photolyase; InterPro IPR006050:IPR005101:IPR002081:IPR014729; KEGG: tth:TT_P0058 deoxyribodipyrimidine photolyase; PFAM: DNA photolyase FAD-binding; DNA photolyase domain protein; PRIAM: Deoxyribodipyrimidine photo-lyase; SPTR: C1XW14 Deoxyribodipyrimidine photo-lyase type I; PFAM: FAD binding domain of DNA photolyase; DNA photolyase. | beta-Ig-H3/fasciclin; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: vsp:VS_II0883 conserved hypothetical protein-putative fasciclin domain; PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; SPTR: C1XW13 Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | 0.775 |
ADH63280.1 | ADH63169.1 | Mesil_1387 | Mesil_1274 | beta-Ig-H3/fasciclin; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: vsp:VS_II0883 conserved hypothetical protein-putative fasciclin domain; PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; SPTR: C1XW13 Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. | 0.650 |
ADH63280.1 | ADH63279.1 | Mesil_1387 | Mesil_1386 | beta-Ig-H3/fasciclin; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: vsp:VS_II0883 conserved hypothetical protein-putative fasciclin domain; PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; SPTR: C1XW13 Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | COGs: COG0415 Deoxyribodipyrimidine photolyase; InterPro IPR006050:IPR005101:IPR002081:IPR014729; KEGG: tth:TT_P0058 deoxyribodipyrimidine photolyase; PFAM: DNA photolyase FAD-binding; DNA photolyase domain protein; PRIAM: Deoxyribodipyrimidine photo-lyase; SPTR: C1XW14 Deoxyribodipyrimidine photo-lyase type I; PFAM: FAD binding domain of DNA photolyase; DNA photolyase. | 0.775 |
ADH63280.1 | nuoA | Mesil_1387 | Mesil_1283 | beta-Ig-H3/fasciclin; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: vsp:VS_II0883 conserved hypothetical protein-putative fasciclin domain; PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; SPTR: C1XW13 Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | 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. | 0.650 |
ADH63280.1 | nuoB | Mesil_1387 | Mesil_1282 | beta-Ig-H3/fasciclin; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: vsp:VS_II0883 conserved hypothetical protein-putative fasciclin domain; PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; SPTR: C1XW13 Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | 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. | 0.650 |
ADH63280.1 | nuoC | Mesil_1387 | Mesil_1281 | beta-Ig-H3/fasciclin; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: vsp:VS_II0883 conserved hypothetical protein-putative fasciclin domain; PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; SPTR: C1XW13 Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | NADH (or F420H2) 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 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. | 0.650 |
ADH63280.1 | nuoD | Mesil_1387 | Mesil_1280 | beta-Ig-H3/fasciclin; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: vsp:VS_II0883 conserved hypothetical protein-putative fasciclin domain; PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; SPTR: C1XW13 Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | 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. | 0.904 |
ADH63280.1 | nuoH | Mesil_1387 | Mesil_1276 | beta-Ig-H3/fasciclin; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: vsp:VS_II0883 conserved hypothetical protein-putative fasciclin domain; PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; SPTR: C1XW13 Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | NADH dehydrogenase (quinone); 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. | 0.650 |
ADH63280.1 | nuoI | Mesil_1387 | Mesil_1275 | beta-Ig-H3/fasciclin; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: vsp:VS_II0883 conserved hypothetical protein-putative fasciclin domain; PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; SPTR: C1XW13 Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | 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. | 0.676 |
ADH63280.1 | nuoK | Mesil_1387 | Mesil_1273 | beta-Ig-H3/fasciclin; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: vsp:VS_II0883 conserved hypothetical protein-putative fasciclin domain; PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; SPTR: C1XW13 Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | NADH-ubiquinone oxidoreductase chain 4L; 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. | 0.650 |
ADH63280.1 | nuoN | Mesil_1387 | Mesil_1270 | beta-Ig-H3/fasciclin; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: vsp:VS_II0883 conserved hypothetical protein-putative fasciclin domain; PFAM: beta-Ig-H3/fasciclin; SMART: beta-Ig-H3/fasciclin; SPTR: C1XW13 Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | 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. | 0.659 |