| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| avtA | bcd | PSHAa1703 | PSHAa1167 | Valine-pyruvate aminotransferase; Function of strongly homologous gene; enzyme. | Leucine dehydrogenase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | 0.900 |
| avtA | ilvD | PSHAa1703 | PSHAa2769 | Valine-pyruvate aminotransferase; Function of strongly homologous gene; enzyme. | Dihydroxyacid dehydratase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family. | 0.900 |
| avtA | ilvD2 | PSHAa1703 | PSHAb0129 | Valine-pyruvate aminotransferase; Function of strongly homologous gene; enzyme. | Putative dihydroxyacid dehydratase (ilvD-like); Function of strongly homologous gene; enzyme; Belongs to the IlvD/Edd family. | 0.900 |
| avtA | ilvE | PSHAa1703 | PSHAa1270 | Valine-pyruvate aminotransferase; Function of strongly homologous gene; enzyme. | Putative branched-chain amino acid aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 0.927 |
| avtA | leuA | PSHAa1703 | PSHAa2894 | Valine-pyruvate aminotransferase; Function of strongly homologous gene; enzyme. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. | 0.903 |
| avtA | yfbQ | PSHAa1703 | PSHAa1323 | Valine-pyruvate aminotransferase; Function of strongly homologous gene; enzyme. | Putative PLP-dependent aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 0.911 |
| bcd | avtA | PSHAa1167 | PSHAa1703 | Leucine dehydrogenase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | Valine-pyruvate aminotransferase; Function of strongly homologous gene; enzyme. | 0.900 |
| bcd | ilvD | PSHAa1167 | PSHAa2769 | Leucine dehydrogenase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | Dihydroxyacid dehydratase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family. | 0.907 |
| bcd | ilvD2 | PSHAa1167 | PSHAb0129 | Leucine dehydrogenase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | Putative dihydroxyacid dehydratase (ilvD-like); Function of strongly homologous gene; enzyme; Belongs to the IlvD/Edd family. | 0.907 |
| bcd | ilvE | PSHAa1167 | PSHAa1270 | Leucine dehydrogenase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | Putative branched-chain amino acid aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 0.928 |
| bcd | leuA | PSHAa1167 | PSHAa2894 | Leucine dehydrogenase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. | 0.906 |
| bcd | yfbQ | PSHAa1167 | PSHAa1323 | Leucine dehydrogenase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | Putative PLP-dependent aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 0.912 |
| ilvA | ilvD | PSHAa2768 | PSHAa2769 | Threonine deaminase; 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. | Dihydroxyacid dehydratase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family. | 0.971 |
| ilvA | ilvD2 | PSHAa2768 | PSHAb0129 | Threonine deaminase; 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. | Putative dihydroxyacid dehydratase (ilvD-like); Function of strongly homologous gene; enzyme; Belongs to the IlvD/Edd family. | 0.803 |
| ilvA | ilvE | PSHAa2768 | PSHAa1270 | Threonine deaminase; 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. | Putative branched-chain amino acid aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 0.964 |
| ilvA | metL | PSHAa2768 | PSHAa2722 | Threonine deaminase; 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. | Bifunctional: aspartokinase II (N-terminal); Function of homologous gene experimentally demonstrated in an other organism; enzyme; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.644 |
| ilvA | thrA | PSHAa2768 | PSHAa2379 | Threonine deaminase; 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. | Bifunctional aspartokinase/homoserine dehydrogenase I; Function of homologous gene experimentally demonstrated in an other organism; enzyme; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.644 |
| ilvD | avtA | PSHAa2769 | PSHAa1703 | Dihydroxyacid dehydratase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family. | Valine-pyruvate aminotransferase; Function of strongly homologous gene; enzyme. | 0.900 |
| ilvD | bcd | PSHAa2769 | PSHAa1167 | Dihydroxyacid dehydratase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family. | Leucine dehydrogenase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | 0.907 |
| ilvD | ilvA | PSHAa2769 | PSHAa2768 | Dihydroxyacid dehydratase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family. | Threonine deaminase; 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. | 0.971 |