| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| cysE | hom | CSING_11065 | CSING_05735 | Serine O-acetyltransferase; PFAM: Bacterial transferase hexapeptide (six repeats); TIGRFAM: serine O-acetyltransferase. | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | 0.812 |
| cysE | ilvA | CSING_11065 | CSING_08880 | Serine O-acetyltransferase; PFAM: Bacterial transferase hexapeptide (six repeats); TIGRFAM: serine O-acetyltransferase. | 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. | 0.809 |
| cysE | metB | CSING_11065 | CSING_10590 | Serine O-acetyltransferase; PFAM: Bacterial transferase hexapeptide (six repeats); TIGRFAM: serine O-acetyltransferase. | Cystathionine beta-lyase/cystathionine gamma-synthase; PFAM: Cys/Met metabolism PLP-dependent enzyme. | 0.456 |
| cysE | tdcG | CSING_11065 | CSING_07665 | Serine O-acetyltransferase; PFAM: Bacterial transferase hexapeptide (six repeats); TIGRFAM: serine O-acetyltransferase. | PFAM: Serine dehydratase alpha chain; Serine dehydratase beta chain; TIGRFAM: L-serine dehydratase, iron-sulfur-dependent, single chain form. | 0.908 |
| cysE | thrB | CSING_11065 | CSING_05740 | Serine O-acetyltransferase; PFAM: Bacterial transferase hexapeptide (six repeats); TIGRFAM: serine O-acetyltransferase. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.819 |
| hom | cysE | CSING_05735 | CSING_11065 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | Serine O-acetyltransferase; PFAM: Bacterial transferase hexapeptide (six repeats); TIGRFAM: serine O-acetyltransferase. | 0.812 |
| 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. | 0.847 |
| 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. | 0.866 |
| 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. | 0.903 |
| hom | metE | CSING_05735 | CSING_00105 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | Methionine synthase (B12-independent); Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation; Belongs to the vitamin-B12 independent methionine synthase family. | 0.840 |
| hom | tdcG | CSING_05735 | CSING_07665 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | PFAM: Serine dehydratase alpha chain; Serine dehydratase beta chain; TIGRFAM: L-serine dehydratase, iron-sulfur-dependent, single chain form. | 0.820 |
| 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 |
| hom | thrC | CSING_05735 | CSING_09490 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | PFAM: Threonine synthase N terminus; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. | 0.973 |
| hom | yhcE | CSING_05735 | CSING_08895 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | Methionine synthase II (cobalamin-independent); PFAM: Cobalamin-independent synthase, Catalytic domain. | 0.840 |
| ilvA | cysE | CSING_08880 | CSING_11065 | 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. | Serine O-acetyltransferase; PFAM: Bacterial transferase hexapeptide (six repeats); TIGRFAM: serine O-acetyltransferase. | 0.809 |
| 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. | 0.847 |
| 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. | 0.968 |
| 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. | 0.876 |
| ilvA | metE | CSING_08880 | CSING_00105 | 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. | Methionine synthase (B12-independent); Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation; Belongs to the vitamin-B12 independent methionine synthase family. | 0.813 |
| ilvA | tdcG | CSING_08880 | CSING_07665 | 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: Serine dehydratase alpha chain; Serine dehydratase beta chain; TIGRFAM: L-serine dehydratase, iron-sulfur-dependent, single chain form. | 0.950 |