node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Meso_1489 | Meso_1922 | Meso_1489 | Meso_1922 | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT; KEGG: mlo:mll1432 acetolactate synthase small subunit. | PFAM: homoserine dehydrogenase amino acid-binding ACT homoserine dehydrogenase, NAD-binding; KEGG: mlo:mll0934 homoserine dehydrogenase. | 0.860 |
Meso_1489 | Meso_4087 | Meso_1489 | Meso_4087 | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT; KEGG: mlo:mll1432 acetolactate synthase small subunit. | PFAM: prephenate dehydratase amino acid-binding ACT; KEGG: bmb:BruAb1_0037 PheA, prephenate dehydratase. | 0.579 |
Meso_1489 | ilvA | Meso_1489 | Meso_1421 | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT; KEGG: mlo:mll1432 acetolactate synthase small subunit. | 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. | 0.961 |
Meso_1922 | Meso_1489 | Meso_1922 | Meso_1489 | PFAM: homoserine dehydrogenase amino acid-binding ACT homoserine dehydrogenase, NAD-binding; KEGG: mlo:mll0934 homoserine dehydrogenase. | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT; KEGG: mlo:mll1432 acetolactate synthase small subunit. | 0.860 |
Meso_1922 | Meso_3001 | Meso_1922 | Meso_3001 | PFAM: homoserine dehydrogenase amino acid-binding ACT homoserine dehydrogenase, NAD-binding; KEGG: mlo:mll0934 homoserine dehydrogenase. | TIGRFAM: aspartate kinase aspartate kinase, monofunctional class; PFAM: aspartate/glutamate/uridylate kinase amino acid-binding ACT; KEGG: bmb:BruAb1_1850 aspartate kinase, monofunctional class; Belongs to the aspartokinase family. | 0.914 |
Meso_1922 | Meso_3161 | Meso_1922 | Meso_3161 | PFAM: homoserine dehydrogenase amino acid-binding ACT homoserine dehydrogenase, NAD-binding; KEGG: mlo:mll0934 homoserine dehydrogenase. | TIGRFAM: D-3-phosphoglycerate dehydrogenase; PFAM: amino acid-binding ACT D-isomer specific 2-hydroxyacid dehydrogenase, catalytic region D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; KEGG: mlo:mll3875 phosphoglycerate dehydrogenase. | 0.539 |
Meso_1922 | Meso_4087 | Meso_1922 | Meso_4087 | PFAM: homoserine dehydrogenase amino acid-binding ACT homoserine dehydrogenase, NAD-binding; KEGG: mlo:mll0934 homoserine dehydrogenase. | PFAM: prephenate dehydratase amino acid-binding ACT; KEGG: bmb:BruAb1_0037 PheA, prephenate dehydratase. | 0.402 |
Meso_1922 | ilvA | Meso_1922 | Meso_1421 | PFAM: homoserine dehydrogenase amino acid-binding ACT homoserine dehydrogenase, NAD-binding; KEGG: mlo:mll0934 homoserine dehydrogenase. | 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. | 0.402 |
Meso_3001 | Meso_1922 | Meso_3001 | Meso_1922 | TIGRFAM: aspartate kinase aspartate kinase, monofunctional class; PFAM: aspartate/glutamate/uridylate kinase amino acid-binding ACT; KEGG: bmb:BruAb1_1850 aspartate kinase, monofunctional class; Belongs to the aspartokinase family. | PFAM: homoserine dehydrogenase amino acid-binding ACT homoserine dehydrogenase, NAD-binding; KEGG: mlo:mll0934 homoserine dehydrogenase. | 0.914 |
Meso_3161 | Meso_1922 | Meso_3161 | Meso_1922 | TIGRFAM: D-3-phosphoglycerate dehydrogenase; PFAM: amino acid-binding ACT D-isomer specific 2-hydroxyacid dehydrogenase, catalytic region D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; KEGG: mlo:mll3875 phosphoglycerate dehydrogenase. | PFAM: homoserine dehydrogenase amino acid-binding ACT homoserine dehydrogenase, NAD-binding; KEGG: mlo:mll0934 homoserine dehydrogenase. | 0.539 |
Meso_4087 | Meso_1489 | Meso_4087 | Meso_1489 | PFAM: prephenate dehydratase amino acid-binding ACT; KEGG: bmb:BruAb1_0037 PheA, prephenate dehydratase. | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT; KEGG: mlo:mll1432 acetolactate synthase small subunit. | 0.579 |
Meso_4087 | Meso_1922 | Meso_4087 | Meso_1922 | PFAM: prephenate dehydratase amino acid-binding ACT; KEGG: bmb:BruAb1_0037 PheA, prephenate dehydratase. | PFAM: homoserine dehydrogenase amino acid-binding ACT homoserine dehydrogenase, NAD-binding; KEGG: mlo:mll0934 homoserine dehydrogenase. | 0.402 |
ilvA | Meso_1489 | Meso_1421 | Meso_1489 | 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. | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT; KEGG: mlo:mll1432 acetolactate synthase small subunit. | 0.961 |
ilvA | Meso_1922 | Meso_1421 | Meso_1922 | 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 amino acid-binding ACT homoserine dehydrogenase, NAD-binding; KEGG: mlo:mll0934 homoserine dehydrogenase. | 0.402 |