| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Ssed_0120 | Ssed_4377 | Ssed_0120 | Ssed_4377 | Molybdopterin-guanine dinucleotide biosynthesis protein B; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | Molybdenum cofactor synthesis domain protein; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | 0.962 |
| Ssed_0120 | Ssed_4397 | Ssed_0120 | Ssed_4397 | Molybdopterin-guanine dinucleotide biosynthesis protein B; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | KEGG: slo:Shew_0092 molybdenum ABC transporter, periplasmic molybdate-binding protein. | 0.848 |
| Ssed_0120 | msrA-2 | Ssed_0120 | Ssed_2636 | Molybdopterin-guanine dinucleotide biosynthesis protein B; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | Peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.577 |
| Ssed_0120 | msrP | Ssed_0120 | Ssed_1981 | Molybdopterin-guanine dinucleotide biosynthesis protein B; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | Twin-arginine translocation pathway signal; 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 [...] | 0.566 |
| Ssed_0198 | Ssed_1106 | Ssed_0198 | Ssed_1106 | 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). | KEGG: sil:SPOA0154 hypothetical protein. | 0.859 |
| Ssed_0198 | Ssed_2214 | Ssed_0198 | Ssed_2214 | 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). | Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.988 |
| Ssed_0198 | Ssed_4438 | Ssed_0198 | Ssed_4438 | 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). | KEGG: pat:Patl_3910 hypothetical protein. | 0.524 |
| Ssed_0198 | msrP | Ssed_0198 | Ssed_1981 | 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). | Twin-arginine translocation pathway signal; 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 [...] | 0.782 |
| Ssed_1106 | Ssed_0198 | Ssed_1106 | Ssed_0198 | KEGG: sil:SPOA0154 hypothetical protein. | 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). | 0.859 |
| Ssed_1106 | msrP | Ssed_1106 | Ssed_1981 | KEGG: sil:SPOA0154 hypothetical protein. | Twin-arginine translocation pathway signal; 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 [...] | 0.702 |
| Ssed_1168 | msrP | Ssed_1168 | Ssed_1981 | KEGG: slo:Shew_1072 chorismate mutase. | Twin-arginine translocation pathway signal; 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 [...] | 0.478 |
| Ssed_2214 | Ssed_0198 | Ssed_2214 | Ssed_0198 | Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 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). | 0.988 |
| Ssed_2214 | msrP | Ssed_2214 | Ssed_1981 | Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | Twin-arginine translocation pathway signal; 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 [...] | 0.702 |
| Ssed_4377 | Ssed_0120 | Ssed_4377 | Ssed_0120 | Molybdenum cofactor synthesis domain protein; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | Molybdopterin-guanine dinucleotide biosynthesis protein B; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | 0.962 |
| Ssed_4377 | Ssed_4397 | Ssed_4377 | Ssed_4397 | Molybdenum cofactor synthesis domain protein; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | KEGG: slo:Shew_0092 molybdenum ABC transporter, periplasmic molybdate-binding protein. | 0.831 |
| Ssed_4377 | msrP | Ssed_4377 | Ssed_1981 | Molybdenum cofactor synthesis domain protein; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | Twin-arginine translocation pathway signal; 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 [...] | 0.497 |
| Ssed_4397 | Ssed_0120 | Ssed_4397 | Ssed_0120 | KEGG: slo:Shew_0092 molybdenum ABC transporter, periplasmic molybdate-binding protein. | Molybdopterin-guanine dinucleotide biosynthesis protein B; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | 0.848 |
| Ssed_4397 | Ssed_4377 | Ssed_4397 | Ssed_4377 | KEGG: slo:Shew_0092 molybdenum ABC transporter, periplasmic molybdate-binding protein. | Molybdenum cofactor synthesis domain protein; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | 0.831 |
| Ssed_4397 | msrP | Ssed_4397 | Ssed_1981 | KEGG: slo:Shew_0092 molybdenum ABC transporter, periplasmic molybdate-binding protein. | Twin-arginine translocation pathway signal; 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 [...] | 0.508 |
| Ssed_4438 | Ssed_0198 | Ssed_4438 | Ssed_0198 | KEGG: pat:Patl_3910 hypothetical protein. | 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). | 0.524 |