node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
PC1_2699 | PC1_4032 | PC1_2699 | PC1_4032 | PFAM: aminotransferase class IV; KEGG: eca:ECA2971 putative branched-chain amino acid aminotransferase. | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; KEGG: eca:ECA4229 acetolactate synthase 2 catalytic subunit. | 0.445 |
PC1_2699 | ilvA | PC1_2699 | PC1_4028 | PFAM: aminotransferase class IV; KEGG: eca:ECA2971 putative branched-chain amino acid aminotransferase. | 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. | 0.874 |
PC1_2699 | ilvC | PC1_2699 | PC1_4021 | PFAM: aminotransferase class IV; KEGG: eca:ECA2971 putative branched-chain amino acid aminotransferase. | 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. | 0.459 |
PC1_2699 | ilvD | PC1_2699 | PC1_4029 | PFAM: aminotransferase class IV; KEGG: eca:ECA2971 putative branched-chain amino acid aminotransferase. | KEGG: eca:ECA4226 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | 0.971 |
PC1_2699 | ilvE | PC1_2699 | PC1_4030 | PFAM: aminotransferase class IV; KEGG: eca:ECA2971 putative branched-chain amino acid aminotransferase. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.918 |
PC1_2699 | leuA | PC1_2699 | PC1_2338 | PFAM: aminotransferase class IV; KEGG: eca:ECA2971 putative branched-chain amino acid aminotransferase. | 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 2 subfamily. | 0.963 |
PC1_2699 | leuA-2 | PC1_2699 | PC1_3607 | PFAM: aminotransferase class IV; KEGG: eca:ECA2971 putative branched-chain amino acid aminotransferase. | 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. | 0.963 |
PC1_2699 | leuC | PC1_2699 | PC1_3609 | PFAM: aminotransferase class IV; KEGG: eca:ECA2971 putative branched-chain amino acid aminotransferase. | 3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.470 |
PC1_2699 | panB | PC1_2699 | PC1_3118 | PFAM: aminotransferase class IV; KEGG: eca:ECA2971 putative branched-chain amino acid aminotransferase. | 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. | 0.913 |
PC1_4032 | PC1_2699 | PC1_4032 | PC1_2699 | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; KEGG: eca:ECA4229 acetolactate synthase 2 catalytic subunit. | PFAM: aminotransferase class IV; KEGG: eca:ECA2971 putative branched-chain amino acid aminotransferase. | 0.445 |
PC1_4032 | ilvA | PC1_4032 | PC1_4028 | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; KEGG: eca:ECA4229 acetolactate synthase 2 catalytic subunit. | 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. | 0.963 |
PC1_4032 | ilvC | PC1_4032 | PC1_4021 | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; KEGG: eca:ECA4229 acetolactate synthase 2 catalytic 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. | 0.981 |
PC1_4032 | ilvD | PC1_4032 | PC1_4029 | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; KEGG: eca:ECA4229 acetolactate synthase 2 catalytic subunit. | KEGG: eca:ECA4226 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | 0.940 |
PC1_4032 | ilvE | PC1_4032 | PC1_4030 | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; KEGG: eca:ECA4229 acetolactate synthase 2 catalytic subunit. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.769 |
PC1_4032 | leuA | PC1_4032 | PC1_2338 | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; KEGG: eca:ECA4229 acetolactate synthase 2 catalytic subunit. | 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 2 subfamily. | 0.894 |
PC1_4032 | leuA-2 | PC1_4032 | PC1_3607 | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; KEGG: eca:ECA4229 acetolactate synthase 2 catalytic subunit. | 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. | 0.958 |
PC1_4032 | leuB | PC1_4032 | PC1_3608 | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; KEGG: eca:ECA4229 acetolactate synthase 2 catalytic subunit. | 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. | 0.983 |
PC1_4032 | leuC | PC1_4032 | PC1_3609 | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; KEGG: eca:ECA4229 acetolactate synthase 2 catalytic subunit. | 3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.774 |
ilvA | PC1_2699 | PC1_4028 | PC1_2699 | 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. | PFAM: aminotransferase class IV; KEGG: eca:ECA2971 putative branched-chain amino acid aminotransferase. | 0.874 |
ilvA | PC1_4032 | PC1_4028 | PC1_4032 | 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. | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; KEGG: eca:ECA4229 acetolactate synthase 2 catalytic subunit. | 0.963 |