| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| XM1_1377 | aroC | XM1_1377 | XM1_3854 | Putative Chorismate mutase(Chorismate mutase,12-90); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Chorismate synthase; 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. | 0.981 |
| XM1_1377 | pabA | XM1_1377 | XM1_2800 | Putative Chorismate mutase(Chorismate mutase,12-90); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Aminodeoxychorismate synthase, subunit II; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.942 |
| XM1_1377 | trpA | XM1_1377 | XM1_1307 | Putative Chorismate mutase(Chorismate mutase,12-90); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Tryptophan synthase alpha chain(Aldolase-type TIM barrel,2-265); The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.448 |
| XM1_1377 | trpB | XM1_1377 | XM1_1308 | Putative Chorismate mutase(Chorismate mutase,12-90); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Tryptophan synthase, beta subunit(Tryptophan synthase, beta chain,11-398); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.448 |
| XM1_1377 | trpC | XM1_1377 | XM1_2798 | Putative Chorismate mutase(Chorismate mutase,12-90); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative Indole-3-glycerol phosphate synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the TrpC family. | 0.471 |
| XM1_1377 | trpE | XM1_1377 | XM1_3609 | Putative Chorismate mutase(Chorismate mutase,12-90); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Anthranilate synthase component 1; 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 concentr [...] | 0.943 |
| XM1_1841 | aroC | XM1_1841 | XM1_3854 | Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Chorismate synthase; 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. | 0.531 |
| XM1_1841 | pabA | XM1_1841 | XM1_2800 | Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Aminodeoxychorismate synthase, subunit II; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.915 |
| XM1_1841 | trpA | XM1_1841 | XM1_1307 | Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Tryptophan synthase alpha chain(Aldolase-type TIM barrel,2-265); The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.937 |
| XM1_1841 | trpB | XM1_1841 | XM1_1308 | Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Tryptophan synthase, beta subunit(Tryptophan synthase, beta chain,11-398); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.920 |
| XM1_1841 | trpC | XM1_1841 | XM1_2798 | Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative Indole-3-glycerol phosphate synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the TrpC family. | 0.924 |
| XM1_1841 | trpE | XM1_1841 | XM1_3609 | Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Anthranilate synthase component 1; 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 concentr [...] | 0.969 |
| XM1_1841 | trpF | XM1_1841 | XM1_1317 | Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | N-(5'-phosphoribosyl)anthranilate isomerase(Aldolase-type TIM barrel,4-211) Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the TrpF family. | 0.928 |
| aroC | XM1_1377 | XM1_3854 | XM1_1377 | Chorismate synthase; 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. | Putative Chorismate mutase(Chorismate mutase,12-90); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.981 |
| aroC | XM1_1841 | XM1_3854 | XM1_1841 | Chorismate synthase; 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. | Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.531 |
| aroC | pabA | XM1_3854 | XM1_2800 | Chorismate synthase; 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. | Aminodeoxychorismate synthase, subunit II; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.971 |
| aroC | trpA | XM1_3854 | XM1_1307 | Chorismate synthase; 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 chain(Aldolase-type TIM barrel,2-265); The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.829 |
| aroC | trpB | XM1_3854 | XM1_1308 | Chorismate synthase; 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(Tryptophan synthase, beta chain,11-398); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.715 |
| aroC | trpC | XM1_3854 | XM1_2798 | Chorismate synthase; 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. | Putative Indole-3-glycerol phosphate synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the TrpC family. | 0.607 |
| aroC | trpD | XM1_3854 | XM1_2799 | Chorismate synthase; 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 phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). | 0.652 |