node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
KQV32951.1 | KQV35330.1 | ASC93_27545 | ASC93_23655 | Formate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | 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). | 0.732 |
KQV32951.1 | KQV43244.1 | ASC93_27545 | ASC93_15765 | Formate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | Molybdopterin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | 0.967 |
KQV32951.1 | KQV43252.1 | ASC93_27545 | ASC93_15730 | Formate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | Cytochrome B; 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). | 0.732 |
KQV32951.1 | KQV49872.1 | ASC93_27545 | ASC93_10045 | Formate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | MFS transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.766 |
KQV32951.1 | KQV49873.1 | ASC93_27545 | ASC93_10050 | Formate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | Nitrite reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. | 0.738 |
KQV32951.1 | KQV49874.1 | ASC93_27545 | ASC93_10055 | Formate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | Nitrite reductase small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.759 |
KQV32951.1 | KQV49875.1 | ASC93_27545 | ASC93_10060 | Formate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.938 |
KQV32951.1 | KQV49876.1 | ASC93_27545 | ASC93_10065 | Formate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | Nitrate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. | 0.983 |
KQV32951.1 | KQV50161.1 | ASC93_27545 | ASC93_11635 | Formate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | CDP-6-deoxy-delta-3,4-glucoseen reductase; Catalyzes the formation of 3,6-dideoxy-D-glycero-D-glycero-4-hexulose; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.804 |
KQV32951.1 | KQV52076.1 | ASC93_27545 | ASC93_05415 | Formate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | Pyridoxamine 5'-phosphate oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.487 |
KQV35330.1 | KQV32951.1 | ASC93_23655 | ASC93_27545 | 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; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | 0.732 |
KQV35330.1 | KQV43244.1 | ASC93_23655 | ASC93_15765 | 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). | Molybdopterin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | 0.988 |
KQV35330.1 | KQV43252.1 | ASC93_23655 | ASC93_15730 | 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). | Cytochrome B; 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). | 0.998 |
KQV35330.1 | KQV49872.1 | ASC93_23655 | ASC93_10045 | 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). | MFS transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.721 |
KQV35330.1 | KQV49873.1 | ASC93_23655 | ASC93_10050 | 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). | Nitrite reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. | 0.723 |
KQV35330.1 | KQV49874.1 | ASC93_23655 | ASC93_10055 | 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). | Nitrite reductase small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.707 |
KQV35330.1 | KQV49875.1 | ASC93_23655 | ASC93_10060 | 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). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.723 |
KQV35330.1 | KQV49876.1 | ASC93_23655 | ASC93_10065 | 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). | Nitrate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. | 0.929 |
KQV35330.1 | KQV50161.1 | ASC93_23655 | ASC93_11635 | 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). | CDP-6-deoxy-delta-3,4-glucoseen reductase; Catalyzes the formation of 3,6-dideoxy-D-glycero-D-glycero-4-hexulose; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.636 |
KQV35330.1 | KQV52076.1 | ASC93_23655 | ASC93_05415 | 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). | Pyridoxamine 5'-phosphate oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.753 |