| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| STM3531 | avtA | STM3531 | STM3665 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | Valine-pyruvate aminotransferase; Similar to E. coli alanine-alpha-ketoisovalerate (or valine-pyruvate) transaminase, transaminase C (AAC76596.1); Blastp hit to AAC76596.1 (417 aa), 92% identity in aa 1 - 415. | 0.907 |
| STM3531 | ilvA | STM3531 | STM3905 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | Threonine deaminase; 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 (By similarity). Belongs to the serine/threon [...] | 0.723 |
| STM3531 | ilvC | STM3531 | STM3909 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | 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. | 0.995 |
| STM3531 | ilvD | STM3531 | STM3904 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | Dihydroxy-acid dehydratase. (SW:ILVD_SALTY); Belongs to the IlvD/Edd family. | 0.919 |
| STM3531 | ilvE | STM3531 | STM3903 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | Branched-chain amino-acid aminotransferase; Acts on leucine, isoleucine and valine. | 0.981 |
| STM3531 | ilvG | STM3531 | STM3901 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | Fragment 1; cryptic; similar to E. coli acetolactate synthase II, large subunit, cryptic, interrupted (AAC77488.1); Blastp hit to AAC77488.1 (327 aa), 93% identity in aa 1 - 325. | 0.909 |
| STM3531 | leuA | STM3531 | STM0113 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd 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 1 subfamily. | 0.996 |
| STM3531 | panB | STM3531 | STM0182 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | 3-methyl-2-oxobutanoate hydroxymethyltransferase; Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha- ketoisovalerate to form ketopantoate; Belongs to the PanB family. | 0.914 |
| STM3531 | tdcB | STM3531 | STM3244 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | Threonine dehydratase; 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. TdcB also dehydrates serine to yield pyruv [...] | 0.757 |
| STM3531 | thrA | STM3531 | STM0002 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | Bifunctional; N-terminaus is aspartokinase I and C terminus is homoserine dehydrogenase I; similar to E. coli aspartokinase I, homoserine dehydrogenase I (AAC73113.1); Blastp hit to AAC73113.1 (820 aa), 94% identity in aa 1 - 820; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.660 |
| avtA | STM3531 | STM3665 | STM3531 | Valine-pyruvate aminotransferase; Similar to E. coli alanine-alpha-ketoisovalerate (or valine-pyruvate) transaminase, transaminase C (AAC76596.1); Blastp hit to AAC76596.1 (417 aa), 92% identity in aa 1 - 415. | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | 0.907 |
| avtA | ilvA | STM3665 | STM3905 | Valine-pyruvate aminotransferase; Similar to E. coli alanine-alpha-ketoisovalerate (or valine-pyruvate) transaminase, transaminase C (AAC76596.1); Blastp hit to AAC76596.1 (417 aa), 92% identity in aa 1 - 415. | Threonine deaminase; 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 (By similarity). Belongs to the serine/threon [...] | 0.489 |
| avtA | ilvD | STM3665 | STM3904 | Valine-pyruvate aminotransferase; Similar to E. coli alanine-alpha-ketoisovalerate (or valine-pyruvate) transaminase, transaminase C (AAC76596.1); Blastp hit to AAC76596.1 (417 aa), 92% identity in aa 1 - 415. | Dihydroxy-acid dehydratase. (SW:ILVD_SALTY); Belongs to the IlvD/Edd family. | 0.923 |
| avtA | ilvE | STM3665 | STM3903 | Valine-pyruvate aminotransferase; Similar to E. coli alanine-alpha-ketoisovalerate (or valine-pyruvate) transaminase, transaminase C (AAC76596.1); Blastp hit to AAC76596.1 (417 aa), 92% identity in aa 1 - 415. | Branched-chain amino-acid aminotransferase; Acts on leucine, isoleucine and valine. | 0.979 |
| avtA | leuA | STM3665 | STM0113 | Valine-pyruvate aminotransferase; Similar to E. coli alanine-alpha-ketoisovalerate (or valine-pyruvate) transaminase, transaminase C (AAC76596.1); Blastp hit to AAC76596.1 (417 aa), 92% identity in aa 1 - 415. | 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 1 subfamily. | 0.950 |
| ilvA | STM3531 | STM3905 | STM3531 | Threonine deaminase; 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 (By similarity). Belongs to the serine/threon [...] | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | 0.723 |
| ilvA | avtA | STM3905 | STM3665 | Threonine deaminase; 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 (By similarity). Belongs to the serine/threon [...] | Valine-pyruvate aminotransferase; Similar to E. coli alanine-alpha-ketoisovalerate (or valine-pyruvate) transaminase, transaminase C (AAC76596.1); Blastp hit to AAC76596.1 (417 aa), 92% identity in aa 1 - 415. | 0.489 |
| ilvA | ilvC | STM3905 | STM3909 | Threonine deaminase; 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 (By similarity). Belongs to the serine/threon [...] | 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. | 0.917 |
| ilvA | ilvD | STM3905 | STM3904 | Threonine deaminase; 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 (By similarity). Belongs to the serine/threon [...] | Dihydroxy-acid dehydratase. (SW:ILVD_SALTY); Belongs to the IlvD/Edd family. | 0.998 |
| ilvA | ilvE | STM3905 | STM3903 | Threonine deaminase; 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 (By similarity). Belongs to the serine/threon [...] | Branched-chain amino-acid aminotransferase; Acts on leucine, isoleucine and valine. | 0.998 |