node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
PA0400 | bkdA2 | PA0400 | PA2248 | Probable cystathionine gamma-lyase; Product name confidence: Class 3 (Function proposed based on presence of conserved amino acid motif, structural feature or limited sequence similarity to an experimentally studied gene). | 2-oxoisovalerate dehydrogenase (beta subunit); The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). | 0.809 |
PA0400 | ilvA1 | PA0400 | PA0331 | Probable cystathionine gamma-lyase; Product name confidence: Class 3 (Function proposed based on presence of conserved amino acid motif, structural feature or limited sequence similarity to an experimentally studied gene). | 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. | 0.831 |
PA0400 | ilvA2 | PA0400 | PA1326 | Probable cystathionine gamma-lyase; Product name confidence: Class 3 (Function proposed based on presence of conserved amino acid motif, structural feature or limited sequence similarity to an experimentally studied gene). | 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. | 0.831 |
PA0400 | ilvE | PA0400 | PA5013 | Probable cystathionine gamma-lyase; Product name confidence: Class 3 (Function proposed based on presence of conserved amino acid motif, structural feature or limited sequence similarity to an experimentally studied gene). | Branched-chain amino acid transferase; Acts on leucine, isoleucine and valine; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.922 |
PA1217 | ilvC | PA1217 | PA4694 | Probable 2-isopropylmalate synthase; Product name confidence: Class 3 (Function proposed based on presence of conserved amino acid motif, structural feature or limited sequence similarity to an experimentally studied gene); Belongs to the alpha-IPM synthase/homocitrate synthase 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. | 0.906 |
PA1217 | ilvD | PA1217 | PA0353 | Probable 2-isopropylmalate synthase; Product name confidence: Class 3 (Function proposed based on presence of conserved amino acid motif, structural feature or limited sequence similarity to an experimentally studied gene); Belongs to the alpha-IPM synthase/homocitrate synthase family. | Dihydroxy-acid dehydratase; Product name confidence: Class 2 (High similarity to functionally studied protein); Belongs to the IlvD/Edd family. | 0.987 |
PA1217 | ilvE | PA1217 | PA5013 | Probable 2-isopropylmalate synthase; Product name confidence: Class 3 (Function proposed based on presence of conserved amino acid motif, structural feature or limited sequence similarity to an experimentally studied gene); Belongs to the alpha-IPM synthase/homocitrate synthase family. | Branched-chain amino acid transferase; Acts on leucine, isoleucine and valine; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.974 |
PA1217 | ldh | PA1217 | PA3418 | Probable 2-isopropylmalate synthase; Product name confidence: Class 3 (Function proposed based on presence of conserved amino acid motif, structural feature or limited sequence similarity to an experimentally studied gene); Belongs to the alpha-IPM synthase/homocitrate synthase family. | Leucine dehydrogenase; Product name confidence: Class 2 (High similarity to functionally studied protein); Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | 0.913 |
PA1217 | leuA | PA1217 | PA3792 | Probable 2-isopropylmalate synthase; Product name confidence: Class 3 (Function proposed based on presence of conserved amino acid motif, structural feature or limited sequence similarity to an experimentally studied gene); Belongs to the alpha-IPM synthase/homocitrate synthase 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 2 subfamily. | 0.900 |
bkdA2 | PA0400 | PA2248 | PA0400 | 2-oxoisovalerate dehydrogenase (beta subunit); The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). | Probable cystathionine gamma-lyase; Product name confidence: Class 3 (Function proposed based on presence of conserved amino acid motif, structural feature or limited sequence similarity to an experimentally studied gene). | 0.809 |
bkdA2 | ilvA1 | PA2248 | PA0331 | 2-oxoisovalerate dehydrogenase (beta subunit); The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). | 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. | 0.811 |
bkdA2 | ilvA2 | PA2248 | PA1326 | 2-oxoisovalerate dehydrogenase (beta subunit); The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). | 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. | 0.811 |
bkdA2 | ilvE | PA2248 | PA5013 | 2-oxoisovalerate dehydrogenase (beta subunit); The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). | Branched-chain amino acid transferase; Acts on leucine, isoleucine and valine; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.921 |
bkdA2 | ldh | PA2248 | PA3418 | 2-oxoisovalerate dehydrogenase (beta subunit); The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). | Leucine dehydrogenase; Product name confidence: Class 2 (High similarity to functionally studied protein); Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | 0.949 |
ilvA1 | PA0400 | PA0331 | PA0400 | 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. | Probable cystathionine gamma-lyase; Product name confidence: Class 3 (Function proposed based on presence of conserved amino acid motif, structural feature or limited sequence similarity to an experimentally studied gene). | 0.831 |
ilvA1 | bkdA2 | PA0331 | PA2248 | 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. | 2-oxoisovalerate dehydrogenase (beta subunit); The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). | 0.811 |
ilvA1 | ilvA2 | PA0331 | PA1326 | 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. | 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. | 0.901 |
ilvA1 | ilvC | PA0331 | PA4694 | 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. | 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. | 0.863 |
ilvA1 | ilvD | PA0331 | PA0353 | 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. | Dihydroxy-acid dehydratase; Product name confidence: Class 2 (High similarity to functionally studied protein); Belongs to the IlvD/Edd family. | 0.958 |
ilvA1 | ilvE | PA0331 | PA5013 | 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. | Branched-chain amino acid transferase; Acts on leucine, isoleucine and valine; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.954 |