| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADN56282.1 | ADN56349.1 | BC1003_0278 | BC1003_0345 | 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). | KEGG: bpy:Bphyt_0625 gluconate 2-dehydrogenase (acceptor); PFAM: cytochrome c class I. | 0.990 |
| ADN56282.1 | ADN59154.1 | BC1003_0278 | BC1003_3207 | 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). | KEGG: bxe:Bxe_A0348 cytochrome c assembly protein; TIGRFAM: cytochrome c-type biogenesis protein CcsB; PFAM: cytochrome c assembly protein. | 0.451 |
| ADN56282.1 | ADN59970.1 | BC1003_0278 | BC1003_4034 | 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). | KEGG: bph:Bphy_4792 cytochrome c oxidase, subunit II; TIGRFAM: cytochrome c oxidase, subunit II; PFAM: cytochrome c oxidase subunit II; cytochrome c class I. | 0.999 |
| ADN56282.1 | msrP | BC1003_0278 | BC1003_3206 | 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). | Oxidoreductase molybdopterin binding protein; 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 [...] | 0.467 |
| ADN56349.1 | ADN56282.1 | BC1003_0345 | BC1003_0278 | KEGG: bpy:Bphyt_0625 gluconate 2-dehydrogenase (acceptor); PFAM: cytochrome c class I. | 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). | 0.990 |
| ADN56349.1 | ADN57338.1 | BC1003_0345 | BC1003_1363 | KEGG: bpy:Bphyt_0625 gluconate 2-dehydrogenase (acceptor); PFAM: cytochrome c class I. | KEGG: bpy:Bphyt_6318 putative cytochrome c552. | 0.482 |
| ADN56349.1 | ADN59970.1 | BC1003_0345 | BC1003_4034 | KEGG: bpy:Bphyt_0625 gluconate 2-dehydrogenase (acceptor); PFAM: cytochrome c class I. | KEGG: bph:Bphy_4792 cytochrome c oxidase, subunit II; TIGRFAM: cytochrome c oxidase, subunit II; PFAM: cytochrome c oxidase subunit II; cytochrome c class I. | 0.988 |
| ADN56349.1 | msrP | BC1003_0345 | BC1003_3206 | KEGG: bpy:Bphyt_0625 gluconate 2-dehydrogenase (acceptor); PFAM: cytochrome c class I. | Oxidoreductase molybdopterin binding protein; 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 [...] | 0.813 |
| ADN57338.1 | ADN56349.1 | BC1003_1363 | BC1003_0345 | KEGG: bpy:Bphyt_6318 putative cytochrome c552. | KEGG: bpy:Bphyt_0625 gluconate 2-dehydrogenase (acceptor); PFAM: cytochrome c class I. | 0.482 |
| ADN57338.1 | msrP | BC1003_1363 | BC1003_3206 | KEGG: bpy:Bphyt_6318 putative cytochrome c552. | Oxidoreductase molybdopterin binding protein; 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 [...] | 0.458 |
| ADN57495.1 | msrP | BC1003_1524 | BC1003_3206 | PFAM: molybdopterin biosynthesis MoaE protein; KEGG: bxe:Bxe_A2377 molybdopterin synthase subunit MoaE. | Oxidoreductase molybdopterin binding protein; 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 [...] | 0.471 |
| ADN57495.1 | msrQ | BC1003_1524 | BC1003_3205 | PFAM: molybdopterin biosynthesis MoaE protein; KEGG: bxe:Bxe_A2377 molybdopterin synthase subunit MoaE. | Ferric reductase domain protein protein transmembrane component domain protein; 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 re [...] | 0.432 |
| ADN57886.1 | msrP | BC1003_1923 | BC1003_3206 | TIGRFAM: hydroxyisourate hydrolase; KEGG: bpy:Bphyt_2324 hydroxyisourate hydrolase; PFAM: Transthyretin; Belongs to the transthyretin family. 5-hydroxyisourate hydrolase subfamily. | Oxidoreductase molybdopterin binding protein; 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 [...] | 0.445 |
| ADN57886.1 | msrQ | BC1003_1923 | BC1003_3205 | TIGRFAM: hydroxyisourate hydrolase; KEGG: bpy:Bphyt_2324 hydroxyisourate hydrolase; PFAM: Transthyretin; Belongs to the transthyretin family. 5-hydroxyisourate hydrolase subfamily. | Ferric reductase domain protein protein transmembrane component domain protein; 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 re [...] | 0.672 |
| ADN59154.1 | ADN56282.1 | BC1003_3207 | BC1003_0278 | KEGG: bxe:Bxe_A0348 cytochrome c assembly protein; TIGRFAM: cytochrome c-type biogenesis protein CcsB; PFAM: cytochrome c assembly protein. | 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). | 0.451 |
| ADN59154.1 | ADN59155.1 | BC1003_3207 | BC1003_3208 | KEGG: bxe:Bxe_A0348 cytochrome c assembly protein; TIGRFAM: cytochrome c-type biogenesis protein CcsB; PFAM: cytochrome c assembly protein. | KEGG: bxe:Bxe_A0347 cytochrome c biogenesis protein. | 0.994 |
| ADN59154.1 | ADN59970.1 | BC1003_3207 | BC1003_4034 | KEGG: bxe:Bxe_A0348 cytochrome c assembly protein; TIGRFAM: cytochrome c-type biogenesis protein CcsB; PFAM: cytochrome c assembly protein. | KEGG: bph:Bphy_4792 cytochrome c oxidase, subunit II; TIGRFAM: cytochrome c oxidase, subunit II; PFAM: cytochrome c oxidase subunit II; cytochrome c class I. | 0.537 |
| ADN59154.1 | msrP | BC1003_3207 | BC1003_3206 | KEGG: bxe:Bxe_A0348 cytochrome c assembly protein; TIGRFAM: cytochrome c-type biogenesis protein CcsB; PFAM: cytochrome c assembly protein. | Oxidoreductase molybdopterin binding protein; 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 [...] | 0.494 |
| ADN59154.1 | msrQ | BC1003_3207 | BC1003_3205 | KEGG: bxe:Bxe_A0348 cytochrome c assembly protein; TIGRFAM: cytochrome c-type biogenesis protein CcsB; PFAM: cytochrome c assembly protein. | Ferric reductase domain protein protein transmembrane component domain protein; 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 re [...] | 0.533 |
| ADN59155.1 | ADN59154.1 | BC1003_3208 | BC1003_3207 | KEGG: bxe:Bxe_A0347 cytochrome c biogenesis protein. | KEGG: bxe:Bxe_A0348 cytochrome c assembly protein; TIGRFAM: cytochrome c-type biogenesis protein CcsB; PFAM: cytochrome c assembly protein. | 0.994 |