| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PP_0990 | PP_2397 | PP_0990 | PP_2397 | DoxX family protein. | EF hand domain protein. | 0.468 |
| PP_0990 | msrQ | PP_0990 | PP_4675 | DoxX family protein. | Methionine sulfoxide reductase heme-binding subunit; 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 ca [...] | 0.412 |
| PP_2397 | PP_0990 | PP_2397 | PP_0990 | EF hand domain protein. | DoxX family protein. | 0.468 |
| PP_2397 | PP_2400 | PP_2397 | PP_2400 | EF hand domain protein. | Homologs of previously reported genes of unknown function. | 0.987 |
| PP_2397 | msrQ | PP_2397 | PP_4675 | EF hand domain protein. | Methionine sulfoxide reductase heme-binding subunit; 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 ca [...] | 0.403 |
| PP_2400 | PP_2397 | PP_2400 | PP_2397 | Homologs of previously reported genes of unknown function. | EF hand domain protein. | 0.987 |
| PP_2400 | msrQ | PP_2400 | PP_4675 | Homologs of previously reported genes of unknown function. | Methionine sulfoxide reductase heme-binding subunit; 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 ca [...] | 0.463 |
| PP_4677 | ilvC | PP_4677 | PP_4678 | CDP-diacylglycerol--serine O-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.720 |
| PP_4677 | ilvH | PP_4677 | PP_4679 | CDP-diacylglycerol--serine O-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | Acetohydroxybutanoate synthase / acetolactate synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Aminoacidbiosynthesis : Pyruvate family. | 0.671 |
| PP_4677 | msrP | PP_4677 | PP_4676 | CDP-diacylglycerol--serine O-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | Methionine sulfoxide reductase catalytic subunit; 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 [...] | 0.932 |
| PP_4677 | msrQ | PP_4677 | PP_4675 | CDP-diacylglycerol--serine O-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | Methionine sulfoxide reductase heme-binding subunit; 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 ca [...] | 0.773 |
| ilvC | PP_4677 | PP_4678 | PP_4677 | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | CDP-diacylglycerol--serine O-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | 0.720 |
| ilvC | ilvH | PP_4678 | PP_4679 | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | Acetohydroxybutanoate synthase / acetolactate synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Aminoacidbiosynthesis : Pyruvate family. | 0.999 |
| ilvC | msrP | PP_4678 | PP_4676 | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | Methionine sulfoxide reductase catalytic subunit; 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 [...] | 0.665 |
| ilvC | msrQ | PP_4678 | PP_4675 | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | Methionine sulfoxide reductase heme-binding subunit; 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 ca [...] | 0.665 |
| ilvH | PP_4677 | PP_4679 | PP_4677 | Acetohydroxybutanoate synthase / acetolactate synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Aminoacidbiosynthesis : Pyruvate family. | CDP-diacylglycerol--serine O-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | 0.671 |
| ilvH | ilvC | PP_4679 | PP_4678 | Acetohydroxybutanoate synthase / acetolactate synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Aminoacidbiosynthesis : Pyruvate family. | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.999 |
| ilvH | msrP | PP_4679 | PP_4676 | Acetohydroxybutanoate synthase / acetolactate synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Aminoacidbiosynthesis : Pyruvate family. | Methionine sulfoxide reductase catalytic subunit; 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 [...] | 0.478 |
| ilvH | msrQ | PP_4679 | PP_4675 | Acetohydroxybutanoate synthase / acetolactate synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Aminoacidbiosynthesis : Pyruvate family. | Methionine sulfoxide reductase heme-binding subunit; 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 ca [...] | 0.473 |
| moaE | msrP | PP_1294 | PP_4676 | Molybdopterin synthase large subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Biosynthesisofcofactors,prostheticgroups,andcarriers : Molybdopterin. | Methionine sulfoxide reductase catalytic subunit; 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 [...] | 0.433 |