node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
PMM1692 | aroC | PMM1692 | PMM0224 | Possible p-aminobenzoate synthetase; Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62; Alternative locus ID: PMED4_19031. | 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. | 0.873 |
PMM1692 | pabA | PMM1692 | PMM0184 | Possible p-aminobenzoate synthetase; Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62; Alternative locus ID: PMED4_19031. | Para-aminobenzoate synthase component II; CONTAINS 1 TYPE-1 GLUTAMINE AMIDOTRANSFERASE DOMAIN; Citation: Kapland and Nichols (1983) J. Mol. Biol. 168:451-468; Tran et al. (1990) J. Bacteriol. 172:397-410; Alternative locus ID: PMED4_01901. | 0.999 |
PMM1692 | trpA | PMM1692 | PMM0572 | Possible p-aminobenzoate synthetase; Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62; Alternative locus ID: PMED4_19031. | Tryptophan synthase alpha chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.838 |
PMM1692 | trpB | PMM1692 | PMM0164 | Possible p-aminobenzoate synthetase; Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62; Alternative locus ID: PMED4_19031. | Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.808 |
PMM1692 | trpC | PMM1692 | PMM1297 | Possible p-aminobenzoate synthetase; Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62; Alternative locus ID: PMED4_19031. | Indole-3-glycerol phosphate synthase; Putative assignment; Alternative locus ID: PMED4_14631; Belongs to the TrpC family. | 0.980 |
PMM1692 | trpD/G | PMM1692 | PMM0952 | Possible p-aminobenzoate synthetase; Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62; Alternative locus ID: PMED4_19031. | Putative Anthranilate synthase component II; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). | 0.993 |
PMM1692 | trpE | PMM1692 | PMM1577 | Possible p-aminobenzoate synthetase; Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62; Alternative locus ID: PMED4_19031. | Anthranilate synthase component I and chorismate binding enzyme; Definite assignment; Alternative locus ID: PMED4_17871. | 0.846 |
PMM1692 | trpF | PMM1692 | PMM0537 | Possible p-aminobenzoate synthetase; Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62; Alternative locus ID: PMED4_19031. | Phosphoribosylanthranilate isomerase; Alternative locus ID: PMED4_05861; Belongs to the TrpF family. | 0.784 |
PMM1692 | tyrA | PMM1692 | PMM1181 | Possible p-aminobenzoate synthetase; Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62; Alternative locus ID: PMED4_19031. | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis. | 0.807 |
aroC | PMM1692 | PMM0224 | PMM1692 | 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. | Possible p-aminobenzoate synthetase; Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62; Alternative locus ID: PMED4_19031. | 0.873 |
aroC | menF | PMM0224 | PMM0177 | 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. | Isochorismate synthase; Alternative locus ID: PMED4_01831. | 0.923 |
aroC | pabA | PMM0224 | PMM0184 | 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. | Para-aminobenzoate synthase component II; CONTAINS 1 TYPE-1 GLUTAMINE AMIDOTRANSFERASE DOMAIN; Citation: Kapland and Nichols (1983) J. Mol. Biol. 168:451-468; Tran et al. (1990) J. Bacteriol. 172:397-410; Alternative locus ID: PMED4_01901. | 0.859 |
aroC | trpA | PMM0224 | PMM0572 | 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; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.701 |
aroC | trpB | PMM0224 | PMM0164 | 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 chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.588 |
aroC | trpC | PMM0224 | PMM1297 | 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. | Indole-3-glycerol phosphate synthase; Putative assignment; Alternative locus ID: PMED4_14631; Belongs to the TrpC family. | 0.422 |
aroC | trpD/G | PMM0224 | PMM0952 | 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 Anthranilate synthase component II; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). | 0.546 |
aroC | trpE | PMM0224 | PMM1577 | 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 synthase component I and chorismate binding enzyme; Definite assignment; Alternative locus ID: PMED4_17871. | 0.925 |
aroC | tyrA | PMM0224 | PMM1181 | 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. | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis. | 0.944 |
menF | aroC | PMM0177 | PMM0224 | Isochorismate synthase; Alternative locus ID: PMED4_01831. | 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. | 0.923 |
menF | pabA | PMM0177 | PMM0184 | Isochorismate synthase; Alternative locus ID: PMED4_01831. | Para-aminobenzoate synthase component II; CONTAINS 1 TYPE-1 GLUTAMINE AMIDOTRANSFERASE DOMAIN; Citation: Kapland and Nichols (1983) J. Mol. Biol. 168:451-468; Tran et al. (1990) J. Bacteriol. 172:397-410; Alternative locus ID: PMED4_01901. | 0.754 |