node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AFL72547.1 | AFL74771.1 | Thivi_0486 | Thivi_2860 | Modular FeS cluster scaffolding protein NifU; May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins. | PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II. | 0.881 |
AFL72547.1 | ilvD | Thivi_0486 | Thivi_1905 | Modular FeS cluster scaffolding protein NifU; May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins. | PFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.949 |
AFL72547.1 | leuA | Thivi_0486 | Thivi_3771 | Modular FeS cluster scaffolding protein NifU; May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins. | 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. | 0.581 |
AFL72547.1 | leuA-2 | Thivi_0486 | Thivi_4590 | Modular FeS cluster scaffolding protein NifU; May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins. | 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. | 0.581 |
AFL73035.1 | AFL74096.1 | Thivi_1004 | Thivi_2146 | Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | 0.910 |
AFL73035.1 | AFL74771.1 | Thivi_1004 | Thivi_2860 | Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II. | 0.677 |
AFL73035.1 | ilvA | Thivi_1004 | Thivi_3675 | Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | Threonine ammonia-lyase, biosynthetic, long form; 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. | 0.956 |
AFL73035.1 | ilvC | Thivi_1004 | Thivi_0995 | Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | 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. | 0.996 |
AFL73035.1 | ilvD | Thivi_1004 | Thivi_1905 | Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | PFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.967 |
AFL73035.1 | ilvE | Thivi_1004 | Thivi_0737 | Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | Branched-chain amino acid aminotransferase, group I; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.763 |
AFL73035.1 | leuA | Thivi_1004 | Thivi_3771 | Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | 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. | 0.941 |
AFL73035.1 | leuA-2 | Thivi_1004 | Thivi_4590 | Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | 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. | 0.908 |
AFL73035.1 | leuC | Thivi_1004 | Thivi_0924 | Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | 3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.780 |
AFL74096.1 | AFL73035.1 | Thivi_2146 | Thivi_1004 | Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | 0.910 |
AFL74096.1 | AFL74771.1 | Thivi_2146 | Thivi_2860 | Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II. | 0.677 |
AFL74096.1 | ilvA | Thivi_2146 | Thivi_3675 | Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | Threonine ammonia-lyase, biosynthetic, long form; 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. | 0.957 |
AFL74096.1 | ilvC | Thivi_2146 | Thivi_0995 | Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | 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. | 0.995 |
AFL74096.1 | ilvD | Thivi_2146 | Thivi_1905 | Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | PFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.951 |
AFL74096.1 | ilvE | Thivi_2146 | Thivi_0737 | Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | Branched-chain amino acid aminotransferase, group I; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.716 |
AFL74096.1 | leuA | Thivi_2146 | Thivi_3771 | Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type. | 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. | 0.936 |