| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| MJ_0672 | trpA | MJ_0672 | MJ_1038 | Membrane bound transport protein, putative; Similar to GB:L42023 PID:1005433 PID:1220685 PID:1204859 SP:Q57486 percent identity: 40.00; identified by sequence similarity; putative. | Tryptophan synthase alpha subunit (trpA); The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.900 |
| MJ_0672 | trpB | MJ_0672 | MJ_1037 | Membrane bound transport protein, putative; Similar to GB:L42023 PID:1005433 PID:1220685 PID:1204859 SP:Q57486 percent identity: 40.00; identified by sequence similarity; putative. | Tryptophan synthase beta subunit (trpB); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.900 |
| MJ_1594 | glyA | MJ_1594 | MJ_1597 | Phosphoserine phosphatase (serB); Similar to SP:P06862 GB:X03046 PID:42948 PID:537228 GB:U00096 percent identity: 39.80; identified by sequence similarity; putative. | Serine hydroxymethyltransferase (glyA); Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo- beta-phenylserine; Belongs to the SHMT family. | 0.969 |
| MJ_1594 | trpA | MJ_1594 | MJ_1038 | Phosphoserine phosphatase (serB); Similar to SP:P06862 GB:X03046 PID:42948 PID:537228 GB:U00096 percent identity: 39.80; identified by sequence similarity; putative. | Tryptophan synthase alpha subunit (trpA); The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.912 |
| MJ_1594 | trpB | MJ_1594 | MJ_1037 | Phosphoserine phosphatase (serB); Similar to SP:P06862 GB:X03046 PID:42948 PID:537228 GB:U00096 percent identity: 39.80; identified by sequence similarity; putative. | Tryptophan synthase beta subunit (trpB); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.933 |
| aroC | glyA | MJ_1175 | MJ_1597 | Chorismate synthase (aroC); Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Serine hydroxymethyltransferase (glyA); Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo- beta-phenylserine; Belongs to the SHMT family. | 0.519 |
| aroC | trpA | MJ_1175 | MJ_1038 | Chorismate synthase (aroC); Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Tryptophan synthase alpha subunit (trpA); The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.890 |
| aroC | trpB | MJ_1175 | MJ_1037 | Chorismate synthase (aroC); Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Tryptophan synthase beta subunit (trpB); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.748 |
| aroC | trpC | MJ_1175 | MJ_0918 | Chorismate synthase (aroC); Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Indole-3-glycerol phosphate synthase/phosphoribosylanthranilate isomerase (trpC); Similar to SP:P18304 PID:149042 percent identity: 42.65; identified by sequence similarity; putative; Belongs to the TrpC family. | 0.643 |
| aroC | trpD | MJ_1175 | MJ_0234 | Chorismate synthase (aroC); Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Anthranilate synthase component II (trpD); Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). | 0.738 |
| aroC | trpE | MJ_1175 | MJ_1075 | Chorismate synthase (aroC); Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Anthranilate synthase component I (trpE); Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high c [...] | 0.969 |
| aroC | trpF | MJ_1175 | MJ_0451 | Chorismate synthase (aroC); Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Phosphoribosylanthranilate isomerase (trpF); Similar to GB:M83788 PID:149038 SP:P52563 percent identity: 41.23; identified by sequence similarity; putative; Belongs to the TrpF family. | 0.453 |
| aroC | trpG | MJ_1175 | MJ_0238 | Chorismate synthase (aroC); Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Anthranilate synthase component II (trpG); Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high [...] | 0.958 |
| glyA | MJ_1594 | MJ_1597 | MJ_1594 | Serine hydroxymethyltransferase (glyA); Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo- beta-phenylserine; Belongs to the SHMT family. | Phosphoserine phosphatase (serB); Similar to SP:P06862 GB:X03046 PID:42948 PID:537228 GB:U00096 percent identity: 39.80; identified by sequence similarity; putative. | 0.969 |
| glyA | aroC | MJ_1597 | MJ_1175 | Serine hydroxymethyltransferase (glyA); Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo- beta-phenylserine; Belongs to the SHMT family. | Chorismate synthase (aroC); Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | 0.519 |
| glyA | trpA | MJ_1597 | MJ_1038 | Serine hydroxymethyltransferase (glyA); Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo- beta-phenylserine; Belongs to the SHMT family. | Tryptophan synthase alpha subunit (trpA); The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.946 |
| glyA | trpB | MJ_1597 | MJ_1037 | Serine hydroxymethyltransferase (glyA); Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo- beta-phenylserine; Belongs to the SHMT family. | Tryptophan synthase beta subunit (trpB); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.941 |
| glyA | trpD | MJ_1597 | MJ_0234 | Serine hydroxymethyltransferase (glyA); Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo- beta-phenylserine; Belongs to the SHMT family. | Anthranilate synthase component II (trpD); Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). | 0.436 |
| glyA | trpE | MJ_1597 | MJ_1075 | Serine hydroxymethyltransferase (glyA); Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo- beta-phenylserine; Belongs to the SHMT family. | Anthranilate synthase component I (trpE); Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high c [...] | 0.572 |
| glyA | trpG | MJ_1597 | MJ_0238 | Serine hydroxymethyltransferase (glyA); Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo- beta-phenylserine; Belongs to the SHMT family. | Anthranilate synthase component II (trpG); Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high [...] | 0.415 |
