| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SSA_1964 | SSA_1965 | SSA_1964 | SSA_1965 | Conserved uncharacterized protein; Staph./S.pneum; GC: 35.19%; Codon Adaptation Index (CAI): 0.839. Curator(s): J. Alves. | Stomatin/prohibitin-like membrane protease subunits, putative; GC: 42.55%; Transmembrane domains: 1. Codon Adaptation Index (CAI): 0.768. | 0.720 |
| SSA_1964 | ilvA | SSA_1964 | SSA_1967 | Conserved uncharacterized protein; Staph./S.pneum; GC: 35.19%; Codon Adaptation Index (CAI): 0.839. Curator(s): J. Alves. | Threonine desaminase, putative; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | 0.662 |
| SSA_1964 | ilvC | SSA_1964 | SSA_1968 | Conserved uncharacterized protein; Staph./S.pneum; GC: 35.19%; Codon Adaptation Index (CAI): 0.839. Curator(s): J. Alves. | Ketol-acid reductoisomerase, putative; 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. | 0.549 |
| SSA_1964 | ilvN | SSA_1964 | SSA_1969 | Conserved uncharacterized protein; Staph./S.pneum; GC: 35.19%; Codon Adaptation Index (CAI): 0.839. Curator(s): J. Alves. | Acetolactate synthase small subunit, putative; GC: 47.8%; Codon Adaptation Index (CAI): 0.77; Protein involved in amino acid binding. | 0.452 |
| SSA_1965 | SSA_1964 | SSA_1965 | SSA_1964 | Stomatin/prohibitin-like membrane protease subunits, putative; GC: 42.55%; Transmembrane domains: 1. Codon Adaptation Index (CAI): 0.768. | Conserved uncharacterized protein; Staph./S.pneum; GC: 35.19%; Codon Adaptation Index (CAI): 0.839. Curator(s): J. Alves. | 0.720 |
| SSA_1965 | ilvA | SSA_1965 | SSA_1967 | Stomatin/prohibitin-like membrane protease subunits, putative; GC: 42.55%; Transmembrane domains: 1. Codon Adaptation Index (CAI): 0.768. | Threonine desaminase, putative; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | 0.781 |
| SSA_1965 | ilvC | SSA_1965 | SSA_1968 | Stomatin/prohibitin-like membrane protease subunits, putative; GC: 42.55%; Transmembrane domains: 1. Codon Adaptation Index (CAI): 0.768. | Ketol-acid reductoisomerase, putative; 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. | 0.683 |
| SSA_1965 | ilvN | SSA_1965 | SSA_1969 | Stomatin/prohibitin-like membrane protease subunits, putative; GC: 42.55%; Transmembrane domains: 1. Codon Adaptation Index (CAI): 0.768. | Acetolactate synthase small subunit, putative; GC: 47.8%; Codon Adaptation Index (CAI): 0.77; Protein involved in amino acid binding. | 0.627 |
| ilvA | SSA_1964 | SSA_1967 | SSA_1964 | Threonine desaminase, putative; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | Conserved uncharacterized protein; Staph./S.pneum; GC: 35.19%; Codon Adaptation Index (CAI): 0.839. Curator(s): J. Alves. | 0.662 |
| ilvA | SSA_1965 | SSA_1967 | SSA_1965 | Threonine desaminase, putative; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | Stomatin/prohibitin-like membrane protease subunits, putative; GC: 42.55%; Transmembrane domains: 1. Codon Adaptation Index (CAI): 0.768. | 0.781 |
| ilvA | ilvC | SSA_1967 | SSA_1968 | Threonine desaminase, putative; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | Ketol-acid reductoisomerase, putative; 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. | 0.966 |
| ilvA | ilvN | SSA_1967 | SSA_1969 | Threonine desaminase, putative; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | Acetolactate synthase small subunit, putative; GC: 47.8%; Codon Adaptation Index (CAI): 0.77; Protein involved in amino acid binding. | 0.986 |
| ilvC | SSA_1964 | SSA_1968 | SSA_1964 | Ketol-acid reductoisomerase, putative; 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. | Conserved uncharacterized protein; Staph./S.pneum; GC: 35.19%; Codon Adaptation Index (CAI): 0.839. Curator(s): J. Alves. | 0.549 |
| ilvC | SSA_1965 | SSA_1968 | SSA_1965 | Ketol-acid reductoisomerase, putative; 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. | Stomatin/prohibitin-like membrane protease subunits, putative; GC: 42.55%; Transmembrane domains: 1. Codon Adaptation Index (CAI): 0.768. | 0.683 |
| ilvC | ilvA | SSA_1968 | SSA_1967 | Ketol-acid reductoisomerase, putative; 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. | Threonine desaminase, putative; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | 0.966 |
| ilvC | ilvN | SSA_1968 | SSA_1969 | Ketol-acid reductoisomerase, putative; 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. | Acetolactate synthase small subunit, putative; GC: 47.8%; Codon Adaptation Index (CAI): 0.77; Protein involved in amino acid binding. | 0.999 |
| ilvN | SSA_1964 | SSA_1969 | SSA_1964 | Acetolactate synthase small subunit, putative; GC: 47.8%; Codon Adaptation Index (CAI): 0.77; Protein involved in amino acid binding. | Conserved uncharacterized protein; Staph./S.pneum; GC: 35.19%; Codon Adaptation Index (CAI): 0.839. Curator(s): J. Alves. | 0.452 |
| ilvN | SSA_1965 | SSA_1969 | SSA_1965 | Acetolactate synthase small subunit, putative; GC: 47.8%; Codon Adaptation Index (CAI): 0.77; Protein involved in amino acid binding. | Stomatin/prohibitin-like membrane protease subunits, putative; GC: 42.55%; Transmembrane domains: 1. Codon Adaptation Index (CAI): 0.768. | 0.627 |
| ilvN | ilvA | SSA_1969 | SSA_1967 | Acetolactate synthase small subunit, putative; GC: 47.8%; Codon Adaptation Index (CAI): 0.77; Protein involved in amino acid binding. | Threonine desaminase, putative; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | 0.986 |
| ilvN | ilvC | SSA_1969 | SSA_1968 | Acetolactate synthase small subunit, putative; GC: 47.8%; Codon Adaptation Index (CAI): 0.77; Protein involved in amino acid binding. | Ketol-acid reductoisomerase, putative; 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 |
