| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEB82543.1 | AEB83199.1 | Alide2_0105 | Alide2_0783 | 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. | KEGG: vei:Veis_1349 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | 0.929 |
| AEB82543.1 | AEB85394.1 | Alide2_0105 | Alide2_3047 | 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. | Acetolactate synthase; KEGG: ajs:Ajs_2520 thiamine pyrophosphate protein; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Belongs to the TPP enzyme family. | 0.936 |
| AEB82543.1 | AEB85472.1 | Alide2_0105 | Alide2_3130 | 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. | KEGG: ctt:CtCNB1_1659 acetolactate synthase, small subunit; TIGRFAM: Acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT. | 0.957 |
| AEB82543.1 | AEB85473.1 | Alide2_0105 | Alide2_3131 | 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. | TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: ajs:Ajs_1769 acetolactate synthase 3 catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, central domain. | 0.936 |
| AEB82543.1 | AEB86557.1 | Alide2_0105 | Alide2_4242 | 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. | Threonine ammonia-lyase; KEGG: dia:Dtpsy_3120 hypothetical protein; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. | 0.924 |
| AEB82543.1 | ilvA | Alide2_0105 | Alide2_0760 | 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. | Threonine dehydratase, biosynthetic; 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. | 0.917 |
| AEB82543.1 | ilvC | Alide2_0105 | Alide2_3129 | 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. | 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. | 0.469 |
| AEB82543.1 | leuB | Alide2_0105 | Alide2_1305 | 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. | 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. | 0.932 |
| AEB83199.1 | AEB82543.1 | Alide2_0783 | Alide2_0105 | KEGG: vei:Veis_1349 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | 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. | 0.929 |
| AEB83199.1 | AEB85394.1 | Alide2_0783 | Alide2_3047 | KEGG: vei:Veis_1349 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | Acetolactate synthase; KEGG: ajs:Ajs_2520 thiamine pyrophosphate protein; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Belongs to the TPP enzyme family. | 0.944 |
| AEB83199.1 | AEB85472.1 | Alide2_0783 | Alide2_3130 | KEGG: vei:Veis_1349 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | KEGG: ctt:CtCNB1_1659 acetolactate synthase, small subunit; TIGRFAM: Acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT. | 0.975 |
| AEB83199.1 | AEB85473.1 | Alide2_0783 | Alide2_3131 | KEGG: vei:Veis_1349 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: ajs:Ajs_1769 acetolactate synthase 3 catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, central domain. | 0.958 |
| AEB83199.1 | AEB86557.1 | Alide2_0783 | Alide2_4242 | KEGG: vei:Veis_1349 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | Threonine ammonia-lyase; KEGG: dia:Dtpsy_3120 hypothetical protein; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. | 0.928 |
| AEB83199.1 | ilvA | Alide2_0783 | Alide2_0760 | KEGG: vei:Veis_1349 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | Threonine dehydratase, biosynthetic; 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. | 0.918 |
| AEB83199.1 | ilvC | Alide2_0783 | Alide2_3129 | KEGG: vei:Veis_1349 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | 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. | 0.805 |
| AEB83199.1 | leuB | Alide2_0783 | Alide2_1305 | KEGG: vei:Veis_1349 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | 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. | 0.919 |
| AEB83747.1 | AEB84100.1 | Alide2_1344 | Alide2_1710 | TIGRFAM: Tartrate dehydrogenase; KEGG: ajs:Ajs_1120 tartrate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | TIGRFAM: Tartrate dehydrogenase; KEGG: aav:Aave_2087 tartrate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | 0.905 |
| AEB83747.1 | AEB85394.1 | Alide2_1344 | Alide2_3047 | TIGRFAM: Tartrate dehydrogenase; KEGG: ajs:Ajs_1120 tartrate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | Acetolactate synthase; KEGG: ajs:Ajs_2520 thiamine pyrophosphate protein; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Belongs to the TPP enzyme family. | 0.944 |
| AEB83747.1 | AEB85472.1 | Alide2_1344 | Alide2_3130 | TIGRFAM: Tartrate dehydrogenase; KEGG: ajs:Ajs_1120 tartrate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | KEGG: ctt:CtCNB1_1659 acetolactate synthase, small subunit; TIGRFAM: Acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT. | 0.975 |
| AEB83747.1 | AEB85473.1 | Alide2_1344 | Alide2_3131 | TIGRFAM: Tartrate dehydrogenase; KEGG: ajs:Ajs_1120 tartrate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: ajs:Ajs_1769 acetolactate synthase 3 catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, central domain. | 0.952 |
STRING v12.5 is now available!
