| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AQM59735.1 | AQM60991.1 | NPD11_1091 | NPD11_1549 | Pterin binding enzyme family protein; [E] COG1410 Methionine synthase I, cobalamin-binding domain. | OAH_OAS_sulfhy: O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein; [E] COG2873 O-acetylhomoserine sulfhydrylase. | 0.690 |
| AQM59735.1 | NPD11_31 | NPD11_1091 | NPD11_31 | Pterin binding enzyme family protein; [E] COG1410 Methionine synthase I, cobalamin-binding domain. | ACT domain protein; [E] COG0460 Homoserine dehydrogenase. | 0.783 |
| AQM59735.1 | glyA | NPD11_1091 | NPD11_90 | Pterin binding enzyme family protein; [E] COG1410 Methionine synthase I, cobalamin-binding domain. | Beta-eliminating lyase family protein; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | 0.467 |
| AQM59735.1 | ilvA | NPD11_1091 | NPD11_1219 | Pterin binding enzyme family protein; [E] COG1410 Methionine synthase I, cobalamin-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. | 0.513 |
| AQM59735.1 | metA | NPD11_1091 | NPD11_2821 | Pterin binding enzyme family protein; [E] COG1410 Methionine synthase I, cobalamin-binding domain. | Homoserine O-succinyltransferase; Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine; Belongs to the MetA family. | 0.820 |
| AQM59735.1 | metF | NPD11_1091 | NPD11_1094 | Pterin binding enzyme family protein; [E] COG1410 Methionine synthase I, cobalamin-binding domain. | Fadh2: methylenetetrahydrofolate reductase [NAD(P)H]; [E] COG0685 5,10-methylenetetrahydrofolate reductase; Belongs to the methylenetetrahydrofolate reductase family. | 0.999 |
| AQM59735.1 | pssA | NPD11_1091 | NPD11_2639 | Pterin binding enzyme family protein; [E] COG1410 Methionine synthase I, cobalamin-binding domain. | pssA: CDP-diacylglycerol-serine O-phosphatidyltransferase; [I] COG1183 Phosphatidylserine synthase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | 0.424 |
| AQM60991.1 | AQM59735.1 | NPD11_1549 | NPD11_1091 | OAH_OAS_sulfhy: O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein; [E] COG2873 O-acetylhomoserine sulfhydrylase. | Pterin binding enzyme family protein; [E] COG1410 Methionine synthase I, cobalamin-binding domain. | 0.690 |
| AQM60991.1 | NPD11_31 | NPD11_1549 | NPD11_31 | OAH_OAS_sulfhy: O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein; [E] COG2873 O-acetylhomoserine sulfhydrylase. | ACT domain protein; [E] COG0460 Homoserine dehydrogenase. | 0.866 |
| AQM60991.1 | ilvA | NPD11_1549 | NPD11_1219 | OAH_OAS_sulfhy: O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein; [E] COG2873 O-acetylhomoserine sulfhydrylase. | 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. | 0.835 |
| AQM60991.1 | metA | NPD11_1549 | NPD11_2821 | OAH_OAS_sulfhy: O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein; [E] COG2873 O-acetylhomoserine sulfhydrylase. | Homoserine O-succinyltransferase; Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine; Belongs to the MetA family. | 0.985 |
| NPD11_31 | AQM59735.1 | NPD11_31 | NPD11_1091 | ACT domain protein; [E] COG0460 Homoserine dehydrogenase. | Pterin binding enzyme family protein; [E] COG1410 Methionine synthase I, cobalamin-binding domain. | 0.783 |
| NPD11_31 | AQM60991.1 | NPD11_31 | NPD11_1549 | ACT domain protein; [E] COG0460 Homoserine dehydrogenase. | OAH_OAS_sulfhy: O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein; [E] COG2873 O-acetylhomoserine sulfhydrylase. | 0.866 |
| NPD11_31 | ilvA | NPD11_31 | NPD11_1219 | ACT domain protein; [E] COG0460 Homoserine dehydrogenase. | 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. | 0.537 |
| NPD11_31 | metA | NPD11_31 | NPD11_2821 | ACT domain protein; [E] COG0460 Homoserine dehydrogenase. | Homoserine O-succinyltransferase; Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine; Belongs to the MetA family. | 0.948 |
| NPD11_31 | metF | NPD11_31 | NPD11_1094 | ACT domain protein; [E] COG0460 Homoserine dehydrogenase. | Fadh2: methylenetetrahydrofolate reductase [NAD(P)H]; [E] COG0685 5,10-methylenetetrahydrofolate reductase; Belongs to the methylenetetrahydrofolate reductase family. | 0.575 |
| NPD11_31 | sdaAA | NPD11_31 | NPD11_2614 | ACT domain protein; [E] COG0460 Homoserine dehydrogenase. | Sda_alpha: L-serine dehydratase, iron-sulfur-dependent, alpha subunit; [E] COG1760 L-serine deaminase. | 0.820 |
| NPD11_31 | sdaAB | NPD11_31 | NPD11_2613 | ACT domain protein; [E] COG0460 Homoserine dehydrogenase. | Sda_beta: L-serine dehydratase, iron-sulfur-dependent, beta subunit; [E] COG1760 L-serine deaminase. | 0.820 |
| glyA | AQM59735.1 | NPD11_90 | NPD11_1091 | Beta-eliminating lyase family protein; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | Pterin binding enzyme family protein; [E] COG1410 Methionine synthase I, cobalamin-binding domain. | 0.467 |
| glyA | ilvA | NPD11_90 | NPD11_1219 | Beta-eliminating lyase family protein; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | 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. | 0.919 |
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