node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
GV64_01955 | GV64_09925 | GV64_01955 | GV64_09925 | Cytochrome B559 subunit alpha; 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). | Zn-dependent hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.776 |
GV64_01955 | GV64_09965 | GV64_01955 | GV64_09965 | Cytochrome B559 subunit alpha; 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). | 3-ketosteroid-9-alpha-hydroxylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.850 |
GV64_01955 | GV64_14480 | GV64_01955 | GV64_14480 | Cytochrome B559 subunit alpha; 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). | Sulfite reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.859 |
GV64_01955 | GV64_16790 | GV64_01955 | GV64_16790 | Cytochrome B559 subunit alpha; 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. | 0.850 |
GV64_01955 | GV64_19005 | GV64_01955 | GV64_19005 | Cytochrome B559 subunit alpha; 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 Cbb3; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.985 |
GV64_01955 | GV64_22315 | GV64_01955 | GV64_22315 | Cytochrome B559 subunit alpha; 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. | 0.890 |
GV64_01955 | msrP | GV64_01955 | GV64_02665 | Cytochrome B559 subunit alpha; 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). | Sulfoxide reductase catalytic subunit YedY; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to re [...] | 0.776 |
GV64_02655 | msrP | GV64_02655 | GV64_02665 | CDP-diacylglycerol--serine O-phosphatidyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | Sulfoxide reductase catalytic subunit YedY; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to re [...] | 0.802 |
GV64_05715 | msrP | GV64_05715 | GV64_02665 | AraC family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | Sulfoxide reductase catalytic subunit YedY; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to re [...] | 0.641 |
GV64_05715 | msrQ | GV64_05715 | GV64_02670 | AraC family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | Ferric reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the qui [...] | 0.501 |
GV64_09925 | GV64_01955 | GV64_09925 | GV64_01955 | Zn-dependent hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B559 subunit alpha; 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). | 0.776 |
GV64_09925 | GV64_09965 | GV64_09925 | GV64_09965 | Zn-dependent hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 3-ketosteroid-9-alpha-hydroxylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.785 |
GV64_09925 | GV64_14480 | GV64_09925 | GV64_14480 | Zn-dependent hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Sulfite reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.867 |
GV64_09925 | GV64_16790 | GV64_09925 | GV64_16790 | Zn-dependent hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.791 |
GV64_09925 | msrP | GV64_09925 | GV64_02665 | Zn-dependent hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Sulfoxide reductase catalytic subunit YedY; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to re [...] | 0.859 |
GV64_09965 | GV64_01955 | GV64_09965 | GV64_01955 | 3-ketosteroid-9-alpha-hydroxylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B559 subunit alpha; 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). | 0.850 |
GV64_09965 | GV64_09925 | GV64_09965 | GV64_09925 | 3-ketosteroid-9-alpha-hydroxylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Zn-dependent hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.785 |
GV64_09965 | GV64_14480 | GV64_09965 | GV64_14480 | 3-ketosteroid-9-alpha-hydroxylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Sulfite reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.916 |
GV64_09965 | GV64_16790 | GV64_09965 | GV64_16790 | 3-ketosteroid-9-alpha-hydroxylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.894 |
GV64_09965 | GV64_19005 | GV64_09965 | GV64_19005 | 3-ketosteroid-9-alpha-hydroxylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome Cbb3; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.807 |