node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AND68467.1 | AND69952.1 | ATSB10_10130 | ATSB10_24980 | Acetolactate synthase; Pfam: Thiamine pyrophosphate enzyme, central domain; Pfam: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Pfam: Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Belongs to the TPP enzyme family. | Pfam: Malic enzyme, NAD binding domain; Pfam: Malic enzyme, N-terminal domain; Pfam: Phosphate acetyl/butaryl transferase; SMART: Malic enzyme, NAD binding domain. | 0.913 |
AND68467.1 | AND70551.1 | ATSB10_10130 | ATSB10_30970 | Acetolactate synthase; Pfam: Thiamine pyrophosphate enzyme, central domain; Pfam: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Pfam: Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Belongs to the TPP enzyme family. | Serine/threonine dehydratase; Pfam: Pyridoxal-phosphate dependent enzyme. | 0.943 |
AND68467.1 | AND70570.1 | ATSB10_10130 | ATSB10_31160 | Acetolactate synthase; Pfam: Thiamine pyrophosphate enzyme, central domain; Pfam: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Pfam: Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Belongs to the TPP enzyme family. | Acetolactate synthase; Pfam: ACT domain; TIGRFAM: acolac_sm: acetolactate synthase, small subunit. | 0.997 |
AND68467.1 | AND70571.1 | ATSB10_10130 | ATSB10_31170 | Acetolactate synthase; Pfam: Thiamine pyrophosphate enzyme, central domain; Pfam: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Pfam: Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Belongs to the TPP enzyme family. | Acetolactate synthase; Pfam: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Pfam: Thiamine pyrophosphate enzyme, central domain; TIGRFAM: acolac_lg: acetolactate synthase, large subunit, biosynthetic type; Pfam: Thiamine pyrophosphate enzyme, C-terminal TPP binding domain. | 0.924 |
AND68467.1 | ilvA | ATSB10_10130 | ATSB10_31150 | Acetolactate synthase; Pfam: Thiamine pyrophosphate enzyme, central domain; Pfam: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Pfam: Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Belongs to the TPP enzyme family. | Threonine ammonia-lyase; 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. | 0.931 |
AND68467.1 | ilvC | ATSB10_10130 | ATSB10_31180 | Acetolactate synthase; Pfam: Thiamine pyrophosphate enzyme, central domain; Pfam: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Pfam: Thiamine pyrophosphate enzyme, C-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. | 0.983 |
AND68467.1 | ilvD | ATSB10_10130 | ATSB10_31190 | Acetolactate synthase; Pfam: Thiamine pyrophosphate enzyme, central domain; Pfam: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Pfam: Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Belongs to the TPP enzyme family. | Pfam: Dehydratase family; Belongs to the IlvD/Edd family. | 0.824 |
AND68467.1 | leuA | ATSB10_10130 | ATSB10_31240 | Acetolactate synthase; Pfam: Thiamine pyrophosphate enzyme, central domain; Pfam: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Pfam: Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Belongs to the TPP enzyme family. | 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. | 0.916 |
AND68467.1 | leuB | ATSB10_10130 | ATSB10_31200 | Acetolactate synthase; Pfam: Thiamine pyrophosphate enzyme, central domain; Pfam: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Pfam: Thiamine pyrophosphate enzyme, C-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. | 0.959 |
AND68467.1 | leuD | ATSB10_10130 | ATSB10_31210 | Acetolactate synthase; Pfam: Thiamine pyrophosphate enzyme, central domain; Pfam: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Pfam: Thiamine pyrophosphate enzyme, C-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. | 0.608 |
AND69952.1 | AND68467.1 | ATSB10_24980 | ATSB10_10130 | Pfam: Malic enzyme, NAD binding domain; Pfam: Malic enzyme, N-terminal domain; Pfam: Phosphate acetyl/butaryl transferase; SMART: Malic enzyme, NAD binding domain. | Acetolactate synthase; Pfam: Thiamine pyrophosphate enzyme, central domain; Pfam: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Pfam: Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; Belongs to the TPP enzyme family. | 0.913 |
AND69952.1 | AND70551.1 | ATSB10_24980 | ATSB10_30970 | Pfam: Malic enzyme, NAD binding domain; Pfam: Malic enzyme, N-terminal domain; Pfam: Phosphate acetyl/butaryl transferase; SMART: Malic enzyme, NAD binding domain. | Serine/threonine dehydratase; Pfam: Pyridoxal-phosphate dependent enzyme. | 0.427 |
AND69952.1 | AND70570.1 | ATSB10_24980 | ATSB10_31160 | Pfam: Malic enzyme, NAD binding domain; Pfam: Malic enzyme, N-terminal domain; Pfam: Phosphate acetyl/butaryl transferase; SMART: Malic enzyme, NAD binding domain. | Acetolactate synthase; Pfam: ACT domain; TIGRFAM: acolac_sm: acetolactate synthase, small subunit. | 0.870 |
AND69952.1 | AND70571.1 | ATSB10_24980 | ATSB10_31170 | Pfam: Malic enzyme, NAD binding domain; Pfam: Malic enzyme, N-terminal domain; Pfam: Phosphate acetyl/butaryl transferase; SMART: Malic enzyme, NAD binding domain. | Acetolactate synthase; Pfam: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Pfam: Thiamine pyrophosphate enzyme, central domain; TIGRFAM: acolac_lg: acetolactate synthase, large subunit, biosynthetic type; Pfam: Thiamine pyrophosphate enzyme, C-terminal TPP binding domain. | 0.913 |
AND69952.1 | ilvA | ATSB10_24980 | ATSB10_31150 | Pfam: Malic enzyme, NAD binding domain; Pfam: Malic enzyme, N-terminal domain; Pfam: Phosphate acetyl/butaryl transferase; SMART: Malic enzyme, NAD binding domain. | Threonine ammonia-lyase; 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. | 0.427 |
AND69952.1 | ilvC | ATSB10_24980 | ATSB10_31180 | Pfam: Malic enzyme, NAD binding domain; Pfam: Malic enzyme, N-terminal domain; Pfam: Phosphate acetyl/butaryl transferase; SMART: Malic enzyme, NAD 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. | 0.475 |
AND69952.1 | ilvD | ATSB10_24980 | ATSB10_31190 | Pfam: Malic enzyme, NAD binding domain; Pfam: Malic enzyme, N-terminal domain; Pfam: Phosphate acetyl/butaryl transferase; SMART: Malic enzyme, NAD binding domain. | Pfam: Dehydratase family; Belongs to the IlvD/Edd family. | 0.555 |
AND69952.1 | leuA | ATSB10_24980 | ATSB10_31240 | Pfam: Malic enzyme, NAD binding domain; Pfam: Malic enzyme, N-terminal domain; Pfam: Phosphate acetyl/butaryl transferase; SMART: Malic enzyme, NAD binding domain. | 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. | 0.873 |
AND69952.1 | leuB | ATSB10_24980 | ATSB10_31200 | Pfam: Malic enzyme, NAD binding domain; Pfam: Malic enzyme, N-terminal domain; Pfam: Phosphate acetyl/butaryl transferase; SMART: Malic enzyme, NAD 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. | 0.412 |
AND69952.1 | leuD | ATSB10_24980 | ATSB10_31210 | Pfam: Malic enzyme, NAD binding domain; Pfam: Malic enzyme, N-terminal domain; Pfam: Phosphate acetyl/butaryl transferase; SMART: Malic enzyme, NAD 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. | 0.839 |