| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EDS73752.1 | EDS75030.1 | CLOSPI_02177 | CLOSPI_01345 | KEGG: cno:NT01CX_0140 1.6e-202 aconitate hydratase K01680; COG: COG1048 Aconitase A; Psort location: Cytoplasmic, score: 8.87. | KEGG: cno:NT01CX_0234 4.8e-116 citrate synthase I K01647; COG: COG0372 Citrate synthase; Psort location: Cytoplasmic, score: 9.98. | 0.995 |
| EDS73752.1 | ilvD | CLOSPI_02177 | CLOSPI_02512 | KEGG: cno:NT01CX_0140 1.6e-202 aconitate hydratase K01680; COG: COG1048 Aconitase A; Psort location: Cytoplasmic, score: 8.87. | KEGG: sat:SYN_01708 4.0e-199 dihydroxy-acid dehydratase K01687; COG: COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; Psort location: Cytoplasmic, score: 8.87; Belongs to the IlvD/Edd family. | 0.647 |
| EDS73752.1 | leuA | CLOSPI_02177 | CLOSPI_02506 | KEGG: cno:NT01CX_0140 1.6e-202 aconitate hydratase K01680; COG: COG1048 Aconitase A; Psort location: Cytoplasmic, score: 8.87. | 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. | 0.495 |
| EDS73752.1 | leuB | CLOSPI_02177 | CLOSPI_02511 | KEGG: cno:NT01CX_0140 1.6e-202 aconitate hydratase K01680; COG: COG1048 Aconitase A; Psort location: Cytoplasmic, score: 8.87. | 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 |
| EDS75030.1 | EDS73752.1 | CLOSPI_01345 | CLOSPI_02177 | KEGG: cno:NT01CX_0234 4.8e-116 citrate synthase I K01647; COG: COG0372 Citrate synthase; Psort location: Cytoplasmic, score: 9.98. | KEGG: cno:NT01CX_0140 1.6e-202 aconitate hydratase K01680; COG: COG1048 Aconitase A; Psort location: Cytoplasmic, score: 8.87. | 0.995 |
| EDS75030.1 | leuB | CLOSPI_01345 | CLOSPI_02511 | KEGG: cno:NT01CX_0234 4.8e-116 citrate synthase I K01647; COG: COG0372 Citrate synthase; Psort location: Cytoplasmic, score: 9.98. | 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. | 0.833 |
| ilvA | ilvB | CLOSPI_00160 | CLOSPI_02513 | 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. | KEGG: chy:CHY_0517 2.1e-163 ilvB1; acetolactate synthase, large subunit, biosynthetic type K01652; COG: COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]; Psort location: Cytoplasmic, score: 8.87. | 0.978 |
| ilvA | ilvC | CLOSPI_00160 | CLOSPI_02508 | 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. | 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. | 0.801 |
| ilvA | ilvD | CLOSPI_00160 | CLOSPI_02512 | 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. | KEGG: sat:SYN_01708 4.0e-199 dihydroxy-acid dehydratase K01687; COG: COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; Psort location: Cytoplasmic, score: 8.87; Belongs to the IlvD/Edd family. | 0.965 |
| ilvA | ilvN | CLOSPI_00160 | CLOSPI_02507 | 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. | KEGG: mta:Moth_2257 1.1e-40 acetolactate synthase, small subunit K01653; COG: COG0440 Acetolactate synthase, small (regulatory) subunit; Psort location: Cytoplasmic, score: 8.87. | 0.975 |
| ilvA | leuA | CLOSPI_00160 | CLOSPI_02506 | 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. | 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. | 0.587 |
| ilvA | leuB | CLOSPI_00160 | CLOSPI_02511 | 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. | 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. | 0.971 |
| ilvA | leuC | CLOSPI_00160 | CLOSPI_02509 | 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. | 3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.617 |
| ilvA | leuD | CLOSPI_00160 | CLOSPI_02510 | 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. | 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. | 0.610 |
| ilvB | ilvA | CLOSPI_02513 | CLOSPI_00160 | KEGG: chy:CHY_0517 2.1e-163 ilvB1; acetolactate synthase, large subunit, biosynthetic type K01652; COG: COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]; Psort location: Cytoplasmic, score: 8.87. | 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. | 0.978 |
| ilvB | ilvC | CLOSPI_02513 | CLOSPI_02508 | KEGG: chy:CHY_0517 2.1e-163 ilvB1; acetolactate synthase, large subunit, biosynthetic type K01652; COG: COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]; Psort location: Cytoplasmic, score: 8.87. | 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 |
| ilvB | ilvD | CLOSPI_02513 | CLOSPI_02512 | KEGG: chy:CHY_0517 2.1e-163 ilvB1; acetolactate synthase, large subunit, biosynthetic type K01652; COG: COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]; Psort location: Cytoplasmic, score: 8.87. | KEGG: sat:SYN_01708 4.0e-199 dihydroxy-acid dehydratase K01687; COG: COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; Psort location: Cytoplasmic, score: 8.87; Belongs to the IlvD/Edd family. | 0.996 |
| ilvB | ilvN | CLOSPI_02513 | CLOSPI_02507 | KEGG: chy:CHY_0517 2.1e-163 ilvB1; acetolactate synthase, large subunit, biosynthetic type K01652; COG: COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]; Psort location: Cytoplasmic, score: 8.87. | KEGG: mta:Moth_2257 1.1e-40 acetolactate synthase, small subunit K01653; COG: COG0440 Acetolactate synthase, small (regulatory) subunit; Psort location: Cytoplasmic, score: 8.87. | 0.999 |
| ilvB | leuA | CLOSPI_02513 | CLOSPI_02506 | KEGG: chy:CHY_0517 2.1e-163 ilvB1; acetolactate synthase, large subunit, biosynthetic type K01652; COG: COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]; Psort location: Cytoplasmic, score: 8.87. | 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 |
| ilvB | leuB | CLOSPI_02513 | CLOSPI_02511 | KEGG: chy:CHY_0517 2.1e-163 ilvB1; acetolactate synthase, large subunit, biosynthetic type K01652; COG: COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]; Psort location: Cytoplasmic, score: 8.87. | 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. | 0.993 |
