| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Meso_0309 | ilvA | Meso_0309 | Meso_1421 | L-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: ret:RHE_CH03537 probable threonine dehydratase protein. | 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. | 0.924 |
| Meso_0309 | ilvD | Meso_0309 | Meso_1688 | L-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: ret:RHE_CH03537 probable threonine dehydratase protein. | TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; KEGG: mlo:mll1102 dihydroxyacid dehydratase; Belongs to the IlvD/Edd family. | 0.554 |
| Meso_0309 | ilvD-2 | Meso_0309 | Meso_2666 | L-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: ret:RHE_CH03537 probable threonine dehydratase protein. | TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; KEGG: mlo:mlr5361 dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.484 |
| Meso_0309 | ilvE | Meso_0309 | Meso_2140 | L-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: ret:RHE_CH03537 probable threonine dehydratase protein. | Branched chain amino acid: 2-keto-4-methylthiobutyrate aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.883 |
| Meso_0373 | ilvE | Meso_0373 | Meso_2140 | Glutamate--cysteine ligase; Catalyzes the synthesis of gamma-glutamylcysteine (gamma-GC). Belongs to the glutamate--cysteine ligase type 2 family. EgtA subfamily. | Branched chain amino acid: 2-keto-4-methylthiobutyrate aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.900 |
| Meso_0969 | Meso_3241 | Meso_0969 | Meso_3241 | TIGRFAM: 2-isopropylmalate synthase/homocitrate synthase family protein; PFAM: pyruvate carboxyltransferase LeuA allosteric (dimerisation) domain; KEGG: mlo:mlr7805 homocitrate synthase nifV candidate; Belongs to the alpha-IPM synthase/homocitrate synthase family. | PFAM: Glu/Leu/Phe/Val dehydrogenase, C terminal Glu/Leu/Phe/Val dehydrogenase, dimerisation region; KEGG: sth:STH1827 leucine dehydrogenase; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | 0.916 |
| Meso_0969 | ilvD | Meso_0969 | Meso_1688 | TIGRFAM: 2-isopropylmalate synthase/homocitrate synthase family protein; PFAM: pyruvate carboxyltransferase LeuA allosteric (dimerisation) domain; KEGG: mlo:mlr7805 homocitrate synthase nifV candidate; Belongs to the alpha-IPM synthase/homocitrate synthase family. | TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; KEGG: mlo:mll1102 dihydroxyacid dehydratase; Belongs to the IlvD/Edd family. | 0.942 |
| Meso_0969 | ilvD-2 | Meso_0969 | Meso_2666 | TIGRFAM: 2-isopropylmalate synthase/homocitrate synthase family protein; PFAM: pyruvate carboxyltransferase LeuA allosteric (dimerisation) domain; KEGG: mlo:mlr7805 homocitrate synthase nifV candidate; Belongs to the alpha-IPM synthase/homocitrate synthase family. | TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; KEGG: mlo:mlr5361 dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.943 |
| Meso_0969 | ilvE | Meso_0969 | Meso_2140 | TIGRFAM: 2-isopropylmalate synthase/homocitrate synthase family protein; PFAM: pyruvate carboxyltransferase LeuA allosteric (dimerisation) domain; KEGG: mlo:mlr7805 homocitrate synthase nifV candidate; Belongs to the alpha-IPM synthase/homocitrate synthase family. | Branched chain amino acid: 2-keto-4-methylthiobutyrate aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.969 |
| Meso_0969 | leuA | Meso_0969 | Meso_2190 | TIGRFAM: 2-isopropylmalate synthase/homocitrate synthase family protein; PFAM: pyruvate carboxyltransferase LeuA allosteric (dimerisation) domain; KEGG: mlo:mlr7805 homocitrate synthase nifV candidate; Belongs to the alpha-IPM synthase/homocitrate synthase 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 2 subfamily. | 0.900 |
| Meso_1922 | ilvE | Meso_1922 | Meso_2140 | PFAM: homoserine dehydrogenase amino acid-binding ACT homoserine dehydrogenase, NAD-binding; KEGG: mlo:mll0934 homoserine dehydrogenase. | Branched chain amino acid: 2-keto-4-methylthiobutyrate aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.866 |
| Meso_3241 | Meso_0969 | Meso_3241 | Meso_0969 | PFAM: Glu/Leu/Phe/Val dehydrogenase, C terminal Glu/Leu/Phe/Val dehydrogenase, dimerisation region; KEGG: sth:STH1827 leucine dehydrogenase; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | TIGRFAM: 2-isopropylmalate synthase/homocitrate synthase family protein; PFAM: pyruvate carboxyltransferase LeuA allosteric (dimerisation) domain; KEGG: mlo:mlr7805 homocitrate synthase nifV candidate; Belongs to the alpha-IPM synthase/homocitrate synthase family. | 0.916 |
| Meso_3241 | ilvD | Meso_3241 | Meso_1688 | PFAM: Glu/Leu/Phe/Val dehydrogenase, C terminal Glu/Leu/Phe/Val dehydrogenase, dimerisation region; KEGG: sth:STH1827 leucine dehydrogenase; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; KEGG: mlo:mll1102 dihydroxyacid dehydratase; Belongs to the IlvD/Edd family. | 0.918 |
| Meso_3241 | ilvD-2 | Meso_3241 | Meso_2666 | PFAM: Glu/Leu/Phe/Val dehydrogenase, C terminal Glu/Leu/Phe/Val dehydrogenase, dimerisation region; KEGG: sth:STH1827 leucine dehydrogenase; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; KEGG: mlo:mlr5361 dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.918 |
| Meso_3241 | ilvE | Meso_3241 | Meso_2140 | PFAM: Glu/Leu/Phe/Val dehydrogenase, C terminal Glu/Leu/Phe/Val dehydrogenase, dimerisation region; KEGG: sth:STH1827 leucine dehydrogenase; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | Branched chain amino acid: 2-keto-4-methylthiobutyrate aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.919 |
| Meso_3241 | leuA | Meso_3241 | Meso_2190 | PFAM: Glu/Leu/Phe/Val dehydrogenase, C terminal Glu/Leu/Phe/Val dehydrogenase, dimerisation region; KEGG: sth:STH1827 leucine dehydrogenase; 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 2 subfamily. | 0.916 |
| ilvA | Meso_0309 | Meso_1421 | Meso_0309 | 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-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: ret:RHE_CH03537 probable threonine dehydratase protein. | 0.924 |
| ilvA | ilvD | Meso_1421 | Meso_1688 | 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: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; KEGG: mlo:mll1102 dihydroxyacid dehydratase; Belongs to the IlvD/Edd family. | 0.633 |
| ilvA | ilvD-2 | Meso_1421 | Meso_2666 | 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: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; KEGG: mlo:mlr5361 dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.569 |
| ilvA | ilvE | Meso_1421 | Meso_2140 | 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. | Branched chain amino acid: 2-keto-4-methylthiobutyrate aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.883 |