node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Daud_0066 | Daud_0352 | Daud_0066 | Daud_0352 | 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: mma:MM0670 acetolactate synthase large subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein. | 0.948 |
Daud_0066 | Daud_0353 | Daud_0066 | Daud_0353 | 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, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: chy:CHY_0518 acetolactate synthase III small subunit. | 0.973 |
Daud_0066 | Daud_1279 | Daud_0066 | Daud_1279 | 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. | PFAM: isocitrate/isopropylmalate dehydrogenase; KEGG: sat:SYN_00088 3-isopropylmalate dehydrogenase. | 0.924 |
Daud_0066 | ilvC | Daud_0066 | Daud_0354 | 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. | 0.809 |
Daud_0066 | ilvD | Daud_0066 | Daud_0540 | 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: cch:Cag_1906 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | 0.956 |
Daud_0352 | Daud_0066 | Daud_0352 | Daud_0066 | KEGG: mma:MM0670 acetolactate synthase large subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein. | 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. | 0.948 |
Daud_0352 | Daud_0353 | Daud_0352 | Daud_0353 | KEGG: mma:MM0670 acetolactate synthase large subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein. | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: chy:CHY_0518 acetolactate synthase III small subunit. | 0.999 |
Daud_0352 | Daud_1279 | Daud_0352 | Daud_1279 | KEGG: mma:MM0670 acetolactate synthase large subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein. | PFAM: isocitrate/isopropylmalate dehydrogenase; KEGG: sat:SYN_00088 3-isopropylmalate dehydrogenase. | 0.973 |
Daud_0352 | ilvC | Daud_0352 | Daud_0354 | KEGG: mma:MM0670 acetolactate synthase large subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein. | 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. | 0.998 |
Daud_0352 | ilvD | Daud_0352 | Daud_0540 | KEGG: mma:MM0670 acetolactate synthase large subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein. | KEGG: cch:Cag_1906 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | 0.992 |
Daud_0352 | leuC | Daud_0352 | Daud_0356 | KEGG: mma:MM0670 acetolactate synthase large subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein. | 3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.586 |
Daud_0352 | leuC-2 | Daud_0352 | Daud_1036 | KEGG: mma:MM0670 acetolactate synthase large subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein. | Homoaconitate hydratase family protein; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.490 |
Daud_0352 | leuD | Daud_0352 | Daud_0357 | KEGG: mma:MM0670 acetolactate synthase large subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein. | 3-isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 2 subfamily. | 0.723 |
Daud_0352 | leuD-2 | Daud_0352 | Daud_1037 | KEGG: mma:MM0670 acetolactate synthase large subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein. | 3-isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 2 subfamily. | 0.659 |
Daud_0353 | Daud_0066 | Daud_0353 | Daud_0066 | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: chy:CHY_0518 acetolactate synthase III small subunit. | 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. | 0.973 |
Daud_0353 | Daud_0352 | Daud_0353 | Daud_0352 | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: chy:CHY_0518 acetolactate synthase III small subunit. | KEGG: mma:MM0670 acetolactate synthase large subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein. | 0.999 |
Daud_0353 | Daud_1279 | Daud_0353 | Daud_1279 | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: chy:CHY_0518 acetolactate synthase III small subunit. | PFAM: isocitrate/isopropylmalate dehydrogenase; KEGG: sat:SYN_00088 3-isopropylmalate dehydrogenase. | 0.979 |
Daud_0353 | ilvC | Daud_0353 | Daud_0354 | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: chy:CHY_0518 acetolactate synthase III small subunit. | 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. | 0.999 |
Daud_0353 | ilvD | Daud_0353 | Daud_0540 | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: chy:CHY_0518 acetolactate synthase III small subunit. | KEGG: cch:Cag_1906 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | 0.926 |
Daud_0353 | leuC | Daud_0353 | Daud_0356 | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: chy:CHY_0518 acetolactate synthase III small subunit. | 3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.816 |