node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ctaC | ctaD | BSU14890 | BSU14900 | Cytochrome caa3 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 caa3 oxidase (subunit I); Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme a of subunit 1 to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. | 0.999 |
ctaC | qcrA | BSU14890 | BSU22560 | Cytochrome caa3 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). | Menaquinol:cytochrome c oxidoreductase (iron-sulfur subunit); Component of the menaquinol-cytochrome c reductase complex. The Rieske protein is a high potential 2Fe-2S protein. | 0.999 |
ctaC | ydjH | BSU14890 | BSU06200 | Cytochrome caa3 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). | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.737 |
ctaC | yhfW | BSU14890 | BSU10390 | Cytochrome caa3 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). | Putative Rieske [2Fe-2S] oxygenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.999 |
ctaD | ctaC | BSU14900 | BSU14890 | Cytochrome caa3 oxidase (subunit I); Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme a of subunit 1 to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. | Cytochrome caa3 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 |
ctaD | qcrA | BSU14900 | BSU22560 | Cytochrome caa3 oxidase (subunit I); Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme a of subunit 1 to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. | Menaquinol:cytochrome c oxidoreductase (iron-sulfur subunit); Component of the menaquinol-cytochrome c reductase complex. The Rieske protein is a high potential 2Fe-2S protein. | 0.990 |
ctaD | ydjH | BSU14900 | BSU06200 | Cytochrome caa3 oxidase (subunit I); Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme a of subunit 1 to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.729 |
ctaD | yhfW | BSU14900 | BSU10390 | Cytochrome caa3 oxidase (subunit I); Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme a of subunit 1 to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. | Putative Rieske [2Fe-2S] oxygenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.875 |
dynA | liaG | BSU22030 | BSU33110 | Dynamin-like GTPase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | Conserved hypothetical protein (response to antibiotic stress); Evidence 1a: Function experimentally demonstrated in the studied strain; PubMedId: 15273097, 16816187. | 0.408 |
dynA | ydjG | BSU22030 | BSU06190 | Dynamin-like GTPase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | Putative phage replication protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type h: extrachromosomal origin. | 0.680 |
dynA | ydjH | BSU22030 | BSU06200 | Dynamin-like GTPase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.737 |
dynA | ydjI | BSU22030 | BSU06210 | Dynamin-like GTPase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | Putative phage protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type h: extrachromosomal origin. | 0.687 |
liaG | dynA | BSU33110 | BSU22030 | Conserved hypothetical protein (response to antibiotic stress); Evidence 1a: Function experimentally demonstrated in the studied strain; PubMedId: 15273097, 16816187. | Dynamin-like GTPase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | 0.408 |
liaG | liaI | BSU33110 | BSU33130 | Conserved hypothetical protein (response to antibiotic stress); Evidence 1a: Function experimentally demonstrated in the studied strain; PubMedId: 15273097, 16816187. | Permease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type t: transporter. | 0.990 |
liaG | pspA | BSU33110 | BSU06180 | Conserved hypothetical protein (response to antibiotic stress); Evidence 1a: Function experimentally demonstrated in the studied strain; PubMedId: 15273097, 16816187. | Phage shock protein A homolog; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type h: extrachromosomal origin. | 0.741 |
liaG | ydjG | BSU33110 | BSU06190 | Conserved hypothetical protein (response to antibiotic stress); Evidence 1a: Function experimentally demonstrated in the studied strain; PubMedId: 15273097, 16816187. | Putative phage replication protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type h: extrachromosomal origin. | 0.836 |
liaG | ydjH | BSU33110 | BSU06200 | Conserved hypothetical protein (response to antibiotic stress); Evidence 1a: Function experimentally demonstrated in the studied strain; PubMedId: 15273097, 16816187. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.849 |
liaG | ydjI | BSU33110 | BSU06210 | Conserved hypothetical protein (response to antibiotic stress); Evidence 1a: Function experimentally demonstrated in the studied strain; PubMedId: 15273097, 16816187. | Putative phage protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type h: extrachromosomal origin. | 0.848 |
liaI | liaG | BSU33130 | BSU33110 | Permease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type t: transporter. | Conserved hypothetical protein (response to antibiotic stress); Evidence 1a: Function experimentally demonstrated in the studied strain; PubMedId: 15273097, 16816187. | 0.990 |
liaI | pspA | BSU33130 | BSU06180 | Permease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type t: transporter. | Phage shock protein A homolog; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type h: extrachromosomal origin. | 0.915 |