node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AMS39617.1 | AMS41793.1 | AA2016_0678 | AA2016_2868 | Putative 2-ketoarginine decarboxylase AruI; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Belongs to the TPP enzyme family. | Pfam:pfam10369 Small subunit of acetolactate synthase. | 0.940 |
AMS39617.1 | ilvA | AA2016_0678 | AA2016_3278 | Putative 2-ketoarginine decarboxylase AruI; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Belongs to the TPP enzyme 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. | 0.942 |
AMS39617.1 | ilvC | AA2016_0678 | AA2016_2890 | Putative 2-ketoarginine decarboxylase AruI; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Belongs to the TPP enzyme 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. | 0.987 |
AMS39617.1 | leuB | AA2016_0678 | AA2016_0852 | Putative 2-ketoarginine decarboxylase AruI; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Belongs to the TPP enzyme family. | 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. | 0.975 |
AMS39617.1 | leuC | AA2016_0678 | AA2016_0998 | Putative 2-ketoarginine decarboxylase AruI; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Belongs to the TPP enzyme family. | Isopropylmalate isomerase; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.659 |
AMS39617.1 | leuD | AA2016_0678 | AA2016_0856 | Putative 2-ketoarginine decarboxylase AruI; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Belongs to the TPP enzyme family. | Isopropylmalate isomerase; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.648 |
AMS40070.1 | AMS41793.1 | AA2016_1133 | AA2016_2868 | Hypothetical protein; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Belongs to the TPP enzyme family. | Pfam:pfam10369 Small subunit of acetolactate synthase. | 0.941 |
AMS40070.1 | ilvA | AA2016_1133 | AA2016_3278 | Hypothetical protein; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Belongs to the TPP enzyme 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. | 0.941 |
AMS40070.1 | ilvC | AA2016_1133 | AA2016_2890 | Hypothetical protein; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Belongs to the TPP enzyme 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. | 0.988 |
AMS40070.1 | leuB | AA2016_1133 | AA2016_0852 | Hypothetical protein; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Belongs to the TPP enzyme family. | 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. | 0.980 |
AMS40070.1 | leuC | AA2016_1133 | AA2016_0998 | Hypothetical protein; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Belongs to the TPP enzyme family. | Isopropylmalate isomerase; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.664 |
AMS40070.1 | leuD | AA2016_1133 | AA2016_0856 | Hypothetical protein; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Belongs to the TPP enzyme family. | Isopropylmalate isomerase; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.670 |
AMS40117.1 | AMS41793.1 | AA2016_1181 | AA2016_2868 | Decarboxylase; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain. | Pfam:pfam10369 Small subunit of acetolactate synthase. | 0.917 |
AMS40117.1 | ilvA | AA2016_1181 | AA2016_3278 | Decarboxylase; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain. | 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. | 0.925 |
AMS40117.1 | ilvC | AA2016_1181 | AA2016_2890 | Decarboxylase; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain. | 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. | 0.964 |
AMS40117.1 | leuB | AA2016_1181 | AA2016_0852 | Decarboxylase; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain. | 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. | 0.953 |
AMS40117.1 | leuC | AA2016_1181 | AA2016_0998 | Decarboxylase; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain. | Isopropylmalate isomerase; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.458 |
AMS40117.1 | leuD | AA2016_1181 | AA2016_0856 | Decarboxylase; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain. | Isopropylmalate isomerase; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.491 |
AMS41690.1 | AMS41793.1 | AA2016_2765 | AA2016_2868 | Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Belongs to the TPP enzyme family. | Pfam:pfam10369 Small subunit of acetolactate synthase. | 0.920 |
AMS41690.1 | ilvA | AA2016_2765 | AA2016_3278 | Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Belongs to the TPP enzyme 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. | 0.925 |