| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| aroC | pabA | PSHAa0983 | PSHAa0192 | Chorismate synthase (5-enolpyruvylshikimate-3-phosphate phospholyase); 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 glutamine amidotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | 0.914 |
| aroC | pabB | PSHAa0983 | PSHAa1165 | Chorismate synthase (5-enolpyruvylshikimate-3-phosphate phospholyase); 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 I, component of p-aminobenzoate synthase multienzyme complex; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.934 |
| aroC | pheA | PSHAa0983 | PSHAa0950 | Chorismate synthase (5-enolpyruvylshikimate-3-phosphate phospholyase); 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. | Bifunctional protein [Includes: chorismate mutase P (N-terminal); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.989 |
| aroC | trpA | PSHAa0983 | PSHAa1288 | Chorismate synthase (5-enolpyruvylshikimate-3-phosphate phospholyase); 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 protein; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.697 |
| aroC | trpB | PSHAa0983 | PSHAa1289 | Chorismate synthase (5-enolpyruvylshikimate-3-phosphate phospholyase); 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 protein; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.575 |
| aroC | trpCF | PSHAa0983 | PSHAa1290 | Chorismate synthase (5-enolpyruvylshikimate-3-phosphate phospholyase); 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. | Bifunctional: indole-3-glycerolphosphate synthetase (N-terminal); Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the TrpC family. | 0.835 |
| aroC | trpD | PSHAa0983 | PSHAa1291 | Chorismate synthase (5-enolpyruvylshikimate-3-phosphate phospholyase); 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). | 0.958 |
| aroC | trpE | PSHAa0983 | PSHAa1293 | Chorismate synthase (5-enolpyruvylshikimate-3-phosphate phospholyase); 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; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.965 |
| aroC | trpG | PSHAa0983 | PSHAa1292 | Chorismate synthase (5-enolpyruvylshikimate-3-phosphate phospholyase); 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 (Glutamine amido-transferase); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.957 |
| aroC | tyrA | PSHAa0983 | PSHAa0949 | Chorismate synthase (5-enolpyruvylshikimate-3-phosphate phospholyase); 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. | Bifunctional protein [Includes: chorismate mutase T (N-terminal); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.998 |
| pabA | aroC | PSHAa0192 | PSHAa0983 | Putative glutamine amidotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Chorismate synthase (5-enolpyruvylshikimate-3-phosphate phospholyase); 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. | 0.914 |
| pabA | pabB | PSHAa0192 | PSHAa1165 | Putative glutamine amidotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Aminodeoxychorismate synthase subunit I, component of p-aminobenzoate synthase multienzyme complex; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.999 |
| pabA | pheA | PSHAa0192 | PSHAa0950 | Putative glutamine amidotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Bifunctional protein [Includes: chorismate mutase P (N-terminal); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.898 |
| pabA | trpA | PSHAa0192 | PSHAa1288 | Putative glutamine amidotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Tryptophan synthase, alpha protein; 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 |
| pabA | trpB | PSHAa0192 | PSHAa1289 | Putative glutamine amidotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Tryptophan synthase, beta protein; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.931 |
| pabA | trpCF | PSHAa0192 | PSHAa1290 | Putative glutamine amidotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Bifunctional: indole-3-glycerolphosphate synthetase (N-terminal); Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the TrpC family. | 0.999 |
| pabA | trpD | PSHAa0192 | PSHAa1291 | Putative glutamine amidotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Anthranilate phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). | 0.999 |
| pabA | trpE | PSHAa0192 | PSHAa1293 | Putative glutamine amidotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Anthranilate synthase component I; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.999 |
| pabA | trpG | PSHAa0192 | PSHAa1292 | Putative glutamine amidotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Anthranilate synthase component II (Glutamine amido-transferase); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.826 |
| pabA | tyrA | PSHAa0192 | PSHAa0949 | Putative glutamine amidotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Bifunctional protein [Includes: chorismate mutase T (N-terminal); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.878 |
