node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CCM62396.1 | CCM62571.1 | BN381_110062 | BN381_130129 | Putative Formate dehydrogenase related protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | 0.571 |
CCM62396.1 | CCM64743.1 | BN381_110062 | BN381_450054 | Putative Formate dehydrogenase related protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative Cytochrome-c oxidase; 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). | 0.577 |
CCM62396.1 | CCM65001.1 | BN381_110062 | BN381_50143 | Putative Formate dehydrogenase related protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Exported hypothetical protein; No homology to any previously reported sequences. | 0.598 |
CCM62396.1 | CCM65302.1 | BN381_110062 | BN381_70001 | Putative Formate dehydrogenase related protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Hypothetical protein; No homology to any previously reported sequences. | 0.491 |
CCM62396.1 | CCM65846.1 | BN381_110062 | BN381_80376 | Putative Formate dehydrogenase related protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative Nitrite reductase (NO-forming); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.874 |
CCM62396.1 | CCM65861.1 | BN381_110062 | BN381_80391 | Putative Formate dehydrogenase related protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | CoA-disulfide reductase. | 0.557 |
CCM62396.1 | CCM65926.1 | BN381_110062 | BN381_840004 | Putative Formate dehydrogenase related protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Conserved hypothetical protein; Homologs of previously reported genes of unknown function. | 0.491 |
CCM62396.1 | nodQ | BN381_110062 | BN381_350087 | Putative Formate dehydrogenase related protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Bifunctional enzyme nodQ (Includes: Sulfate adenylyltransferase subunit 1; Catalyzes the synthesis of activated sulfate. Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. CysN/NodQ subfamily. | 0.800 |
CCM62571.1 | CCM62396.1 | BN381_130129 | BN381_110062 | FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | Putative Formate dehydrogenase related protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.571 |
CCM62571.1 | CCM65001.1 | BN381_130129 | BN381_50143 | FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | Exported hypothetical protein; No homology to any previously reported sequences. | 0.656 |
CCM62571.1 | CCM65846.1 | BN381_130129 | BN381_80376 | FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | Putative Nitrite reductase (NO-forming); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.440 |
CCM62571.1 | CCM65861.1 | BN381_130129 | BN381_80391 | FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | CoA-disulfide reductase. | 0.637 |
CCM62613.1 | CCM64743.1 | BN381_130171 | BN381_450054 | Membrane hypothetical protein; No homology to any previously reported sequences. | Putative Cytochrome-c oxidase; 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). | 0.577 |
CCM62613.1 | CCM65001.1 | BN381_130171 | BN381_50143 | Membrane hypothetical protein; No homology to any previously reported sequences. | Exported hypothetical protein; No homology to any previously reported sequences. | 0.983 |
CCM62613.1 | CCM65302.1 | BN381_130171 | BN381_70001 | Membrane hypothetical protein; No homology to any previously reported sequences. | Hypothetical protein; No homology to any previously reported sequences. | 0.421 |
CCM62613.1 | CCM65846.1 | BN381_130171 | BN381_80376 | Membrane hypothetical protein; No homology to any previously reported sequences. | Putative Nitrite reductase (NO-forming); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.711 |
CCM62613.1 | CCM65926.1 | BN381_130171 | BN381_840004 | Membrane hypothetical protein; No homology to any previously reported sequences. | Conserved hypothetical protein; Homologs of previously reported genes of unknown function. | 0.421 |
CCM64290.1 | CCM65001.1 | BN381_350150 | BN381_50143 | Hypothetical protein; No homology to any previously reported sequences. | Exported hypothetical protein; No homology to any previously reported sequences. | 0.581 |
CCM64743.1 | CCM62396.1 | BN381_450054 | BN381_110062 | Putative Cytochrome-c oxidase; 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). | Putative Formate dehydrogenase related protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.577 |
CCM64743.1 | CCM62613.1 | BN381_450054 | BN381_130171 | Putative Cytochrome-c oxidase; 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). | Membrane hypothetical protein; No homology to any previously reported sequences. | 0.577 |