| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ANW22741.1 | msrP | BA953_00180 | BA953_00185 | DUF2986 domain-containing protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Mononuclear molybdenum enzyme 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 reduce bot [...] | 0.508 |
| ANW22741.1 | msrQ | BA953_00180 | BA953_00190 | DUF2986 domain-containing protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Sulfoxide reductase heme-binding subunit YedZ; 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 catalyti [...] | 0.508 |
| ANW22802.1 | ANW25179.1 | BA953_00510 | BA953_13805 | Molybdopterin molybdenumtransferase; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | Molybdopterin synthase catalytic subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.986 |
| ANW22802.1 | ANW25883.1 | BA953_00510 | BA953_16965 | Molybdopterin molybdenumtransferase; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | Molybdopterin molybdenumtransferase MoeA; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | 0.973 |
| ANW22802.1 | msrP | BA953_00510 | BA953_00185 | Molybdopterin molybdenumtransferase; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | Mononuclear molybdenum enzyme 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 reduce bot [...] | 0.488 |
| ANW25179.1 | ANW22802.1 | BA953_13805 | BA953_00510 | Molybdopterin synthase catalytic subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molybdopterin molybdenumtransferase; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | 0.986 |
| ANW25179.1 | ANW25883.1 | BA953_13805 | BA953_16965 | Molybdopterin synthase catalytic subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molybdopterin molybdenumtransferase MoeA; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | 0.946 |
| ANW25179.1 | msrP | BA953_13805 | BA953_00185 | Molybdopterin synthase catalytic subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | Mononuclear molybdenum enzyme 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 reduce bot [...] | 0.445 |
| ANW25454.1 | ccoP | BA953_15285 | BA953_00905 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Cytochrome c oxidase, cbb3-type subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.821 |
| ANW25454.1 | coxB | BA953_15285 | BA953_19405 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 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). | 0.969 |
| ANW25454.1 | msrP | BA953_15285 | BA953_00185 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Mononuclear molybdenum enzyme 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 reduce bot [...] | 0.735 |
| ANW25883.1 | ANW22802.1 | BA953_16965 | BA953_00510 | Molybdopterin molybdenumtransferase MoeA; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | Molybdopterin molybdenumtransferase; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | 0.973 |
| ANW25883.1 | ANW25179.1 | BA953_16965 | BA953_13805 | Molybdopterin molybdenumtransferase MoeA; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | Molybdopterin synthase catalytic subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.946 |
| ANW25883.1 | msrP | BA953_16965 | BA953_00185 | Molybdopterin molybdenumtransferase MoeA; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | Mononuclear molybdenum enzyme 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 reduce bot [...] | 0.436 |
| BA953_05935 | msrP | BA953_05935 | BA953_00185 | LysR family transcriptional regulator; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. | Mononuclear molybdenum enzyme 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 reduce bot [...] | 0.477 |
| ccoP | ANW25454.1 | BA953_00905 | BA953_15285 | Cytochrome c oxidase, cbb3-type subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.821 |
| ccoP | coxB | BA953_00905 | BA953_19405 | Cytochrome c oxidase, cbb3-type subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 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). | 0.980 |
| ccoP | msrP | BA953_00905 | BA953_00185 | Cytochrome c oxidase, cbb3-type subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | Mononuclear molybdenum enzyme 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 reduce bot [...] | 0.669 |
| coxB | ANW25454.1 | BA953_19405 | BA953_15285 | 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: GeneMarkS+. | 0.969 |
| coxB | ccoP | BA953_19405 | BA953_00905 | 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 c oxidase, cbb3-type subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.980 |