| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| aspC | ilvD | CSING_12170 | CSING_06165 | PFAM: Aminotransferase class I and II. | PFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.913 |
| aspC | ilvE | CSING_12170 | CSING_09255 | PFAM: Aminotransferase class I and II. | PFAM: Aminotransferase class IV; Branched-chain amino acid aminotransferase; TIGRFAM: branched-chain amino acid aminotransferase, group II. | 0.906 |
| aspC | ldh | CSING_12170 | CSING_12550 | PFAM: Aminotransferase class I and II. | L-lactate dehydrogenase; Catalyzes the conversion of lactate to pyruvate. Belongs to the LDH/MDH superfamily. LDH family. | 0.885 |
| aspC | leuA | CSING_12170 | CSING_00990 | PFAM: Aminotransferase class I and II. | 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 2 subfamily. | 0.907 |
| aspC | pflB | CSING_12170 | CSING_10800 | PFAM: Aminotransferase class I and II. | Formate acetyltransferase 1; PFAM: Glycine radical; Pyruvate formate lyase; TIGRFAM: formate acetyltransferase 1. | 0.803 |
| hom | ilvA | CSING_05735 | CSING_08880 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | L-threonine ammonia-lyase; 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. | 0.569 |
| hom | ilvE | CSING_05735 | CSING_09255 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | PFAM: Aminotransferase class IV; Branched-chain amino acid aminotransferase; TIGRFAM: branched-chain amino acid aminotransferase, group II. | 0.860 |
| hom | leuA | CSING_05735 | CSING_00990 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | 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 2 subfamily. | 0.445 |
| hom | metB | CSING_05735 | CSING_10590 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | Cystathionine beta-lyase/cystathionine gamma-synthase; PFAM: Cys/Met metabolism PLP-dependent enzyme. | 0.891 |
| hom | thrB | CSING_05735 | CSING_05740 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.999 |
| ilvA | hom | CSING_08880 | CSING_05735 | L-threonine ammonia-lyase; 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. | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | 0.569 |
| ilvA | ilvD | CSING_08880 | CSING_06165 | L-threonine ammonia-lyase; 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. | PFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.807 |
| ilvA | ilvE | CSING_08880 | CSING_09255 | L-threonine ammonia-lyase; 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. | PFAM: Aminotransferase class IV; Branched-chain amino acid aminotransferase; TIGRFAM: branched-chain amino acid aminotransferase, group II. | 0.957 |
| ilvA | ldh | CSING_08880 | CSING_12550 | L-threonine ammonia-lyase; 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. | L-lactate dehydrogenase; Catalyzes the conversion of lactate to pyruvate. Belongs to the LDH/MDH superfamily. LDH family. | 0.827 |
| ilvA | leuA | CSING_08880 | CSING_00990 | L-threonine ammonia-lyase; 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. | 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 2 subfamily. | 0.488 |
| ilvA | metB | CSING_08880 | CSING_10590 | L-threonine ammonia-lyase; 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. | Cystathionine beta-lyase/cystathionine gamma-synthase; PFAM: Cys/Met metabolism PLP-dependent enzyme. | 0.864 |
| ilvA | pflB | CSING_08880 | CSING_10800 | L-threonine ammonia-lyase; 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. | Formate acetyltransferase 1; PFAM: Glycine radical; Pyruvate formate lyase; TIGRFAM: formate acetyltransferase 1. | 0.810 |
| ilvA | thrB | CSING_08880 | CSING_05740 | L-threonine ammonia-lyase; 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. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.511 |
| ilvD | aspC | CSING_06165 | CSING_12170 | PFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | PFAM: Aminotransferase class I and II. | 0.913 |
| ilvD | ilvA | CSING_06165 | CSING_08880 | PFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | L-threonine ammonia-lyase; 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. | 0.807 |
