| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 |
| ilvA | ilvG | STM3905 | STM3901 | 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 [...] | 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. | 0.994 |
| ilvA | ilvH | STM3905 | STM0117 | 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 [...] | Acetolactate synthase isozyme III small subunit. (SW:ILVH_SALTY). | 0.985 |
| ilvA | ilvL | STM3905 | STM3900 | 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 [...] | ilvGmedA operon leader peptide (attenuator peptide). (SW:LPID_ECOLI). | 0.465 |
| ilvA | ilvM | STM3905 | STM3902 | 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 acetolactate synthase II, valine insensitive, small subunit (AAC77489.1); Blastp hit to AAC77489.1 (87 aa), 93% identity in aa 2 - 87. | 0.947 |
| ilvA | leuA | STM3905 | STM0113 | 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 [...] | 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. | 0.889 |
| ilvD | ilvA | STM3904 | STM3905 | Dihydroxy-acid dehydratase. (SW:ILVD_SALTY); 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 [...] | 0.998 |
| ilvD | ilvE | STM3904 | STM3903 | Dihydroxy-acid dehydratase. (SW:ILVD_SALTY); Belongs to the IlvD/Edd family. | Branched-chain amino-acid aminotransferase; Acts on leucine, isoleucine and valine. | 0.999 |
| ilvD | ilvG | STM3904 | STM3901 | Dihydroxy-acid dehydratase. (SW:ILVD_SALTY); 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. | 0.988 |
| ilvD | ilvH | STM3904 | STM0117 | Dihydroxy-acid dehydratase. (SW:ILVD_SALTY); Belongs to the IlvD/Edd family. | Acetolactate synthase isozyme III small subunit. (SW:ILVH_SALTY). | 0.953 |
| ilvD | ilvL | STM3904 | STM3900 | Dihydroxy-acid dehydratase. (SW:ILVD_SALTY); Belongs to the IlvD/Edd family. | ilvGmedA operon leader peptide (attenuator peptide). (SW:LPID_ECOLI). | 0.564 |
| ilvD | ilvM | STM3904 | STM3902 | Dihydroxy-acid dehydratase. (SW:ILVD_SALTY); Belongs to the IlvD/Edd family. | Similar to E. coli acetolactate synthase II, valine insensitive, small subunit (AAC77489.1); Blastp hit to AAC77489.1 (87 aa), 93% identity in aa 2 - 87. | 0.889 |
| ilvD | leuA | STM3904 | STM0113 | Dihydroxy-acid dehydratase. (SW:ILVD_SALTY); 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. | 0.995 |
| ilvE | ilvA | STM3903 | STM3905 | Branched-chain amino-acid aminotransferase; Acts on leucine, isoleucine and valine. | 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 [...] | 0.998 |
| ilvE | ilvD | STM3903 | STM3904 | Branched-chain amino-acid aminotransferase; Acts on leucine, isoleucine and valine. | Dihydroxy-acid dehydratase. (SW:ILVD_SALTY); Belongs to the IlvD/Edd family. | 0.999 |
| ilvE | ilvG | STM3903 | STM3901 | Branched-chain amino-acid aminotransferase; Acts on leucine, isoleucine and valine. | 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. | 0.972 |
| ilvE | ilvH | STM3903 | STM0117 | Branched-chain amino-acid aminotransferase; Acts on leucine, isoleucine and valine. | Acetolactate synthase isozyme III small subunit. (SW:ILVH_SALTY). | 0.871 |
| ilvE | ilvL | STM3903 | STM3900 | Branched-chain amino-acid aminotransferase; Acts on leucine, isoleucine and valine. | ilvGmedA operon leader peptide (attenuator peptide). (SW:LPID_ECOLI). | 0.578 |
| ilvE | ilvM | STM3903 | STM3902 | Branched-chain amino-acid aminotransferase; Acts on leucine, isoleucine and valine. | Similar to E. coli acetolactate synthase II, valine insensitive, small subunit (AAC77489.1); Blastp hit to AAC77489.1 (87 aa), 93% identity in aa 2 - 87. | 0.910 |
