| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CUS_5221 | CUS_5391 | CUS_5221 | CUS_5391 | Aminotransferase, class I/II; Identified by match to protein family HMM PF00155. | Putative branched-chain-amino-acid aminotransferase 2. | 0.874 |
| CUS_5221 | ilvA | CUS_5221 | CUS_6532 | Aminotransferase, class I/II; Identified by match to protein family HMM PF00155. | 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. | 0.823 |
| CUS_5221 | ilvB | CUS_5221 | CUS_6658 | Aminotransferase, class I/II; Identified by match to protein family HMM PF00155. | Acetolactate synthase, large subunit, biosynthetic type. | 0.468 |
| CUS_5221 | ilvB-2 | CUS_5221 | CUS_7529 | Aminotransferase, class I/II; Identified by match to protein family HMM PF00155. | Acetolactate synthase, large subunit, biosynthetic type; Identified by match to protein family HMM PF00205; match to protein family HMM PF02775; match to protein family HMM PF02776; match to protein family HMM TIGR00118. | 0.468 |
| CUS_5221 | ilvD | CUS_5221 | CUS_7638 | Aminotransferase, class I/II; Identified by match to protein family HMM PF00155. | Dihydroxy-acid dehydratase; Identified by match to protein family HMM PF00920; match to protein family HMM TIGR00110; Belongs to the IlvD/Edd family. | 0.870 |
| CUS_5221 | leuA | CUS_5221 | CUS_6186 | Aminotransferase, class I/II; Identified by match to protein family HMM PF00155. | 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. | 0.861 |
| CUS_5221 | leuB | CUS_5221 | CUS_5078 | Aminotransferase, class I/II; Identified by match to protein family HMM PF00155. | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. | 0.659 |
| CUS_5391 | CUS_5221 | CUS_5391 | CUS_5221 | Putative branched-chain-amino-acid aminotransferase 2. | Aminotransferase, class I/II; Identified by match to protein family HMM PF00155. | 0.874 |
| CUS_5391 | ilvA | CUS_5391 | CUS_6532 | Putative branched-chain-amino-acid aminotransferase 2. | 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. | 0.943 |
| CUS_5391 | ilvB | CUS_5391 | CUS_6658 | Putative branched-chain-amino-acid aminotransferase 2. | Acetolactate synthase, large subunit, biosynthetic type. | 0.529 |
| CUS_5391 | ilvB-2 | CUS_5391 | CUS_7529 | Putative branched-chain-amino-acid aminotransferase 2. | Acetolactate synthase, large subunit, biosynthetic type; Identified by match to protein family HMM PF00205; match to protein family HMM PF02775; match to protein family HMM PF02776; match to protein family HMM TIGR00118. | 0.529 |
| CUS_5391 | ilvC | CUS_5391 | CUS_7532 | Putative branched-chain-amino-acid aminotransferase 2. | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.581 |
| CUS_5391 | ilvD | CUS_5391 | CUS_7638 | Putative branched-chain-amino-acid aminotransferase 2. | Dihydroxy-acid dehydratase; Identified by match to protein family HMM PF00920; match to protein family HMM TIGR00110; Belongs to the IlvD/Edd family. | 0.993 |
| CUS_5391 | ilvN | CUS_5391 | CUS_7531 | Putative branched-chain-amino-acid aminotransferase 2. | Acetolactate synthase, small subunit; Identified by match to protein family HMM PF01842; match to protein family HMM TIGR00119. | 0.832 |
| CUS_5391 | leuA | CUS_5391 | CUS_6186 | Putative branched-chain-amino-acid aminotransferase 2. | 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. | 0.963 |
| CUS_5391 | leuB | CUS_5391 | CUS_5078 | Putative branched-chain-amino-acid aminotransferase 2. | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. | 0.563 |
| CUS_5391 | leuC | CUS_5391 | CUS_4606 | Putative branched-chain-amino-acid aminotransferase 2. | 3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.538 |
| ilvA | CUS_5221 | CUS_6532 | CUS_5221 | 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. | Aminotransferase, class I/II; Identified by match to protein family HMM PF00155. | 0.823 |
| ilvA | CUS_5391 | CUS_6532 | CUS_5391 | 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. | Putative branched-chain-amino-acid aminotransferase 2. | 0.943 |
| ilvA | ilvB | CUS_6532 | CUS_6658 | 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. | Acetolactate synthase, large subunit, biosynthetic type. | 0.970 |