| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| APA94940.1 | APA95565.1 | NS506_00864 | NS506_01494 | Prephenate dehydrogenase; Catalyzes the NAD(+)-dependent conversion of prephenate to p-hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key regulatory enzyme in tyrosine biosynthesis. Displays no chorismate mutase (CM) activity, in contrast to TyrA from E. coli and some other bacteria, that are bifunctional and possess a CM domain; Contains 1 prephenate/arogenate dehydrogenase domain; KEGG: pdx:Psed_0331 prephenate dehydrogenase. | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis; Contains 1 chorismate mutase domain; KEGG: rpy:Y013_21125 chorismate mutase. | 0.949 |
| APA94940.1 | APA96431.1 | NS506_00864 | NS506_02365 | Prephenate dehydrogenase; Catalyzes the NAD(+)-dependent conversion of prephenate to p-hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key regulatory enzyme in tyrosine biosynthesis. Displays no chorismate mutase (CM) activity, in contrast to TyrA from E. coli and some other bacteria, that are bifunctional and possess a CM domain; Contains 1 prephenate/arogenate dehydrogenase domain; KEGG: pdx:Psed_0331 prephenate dehydrogenase. | KEGG: nbr:O3I_000260 chorismate mutase. | 0.936 |
| APA94940.1 | APA97045.1 | NS506_00864 | NS506_02987 | Prephenate dehydrogenase; Catalyzes the NAD(+)-dependent conversion of prephenate to p-hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key regulatory enzyme in tyrosine biosynthesis. Displays no chorismate mutase (CM) activity, in contrast to TyrA from E. coli and some other bacteria, that are bifunctional and possess a CM domain; Contains 1 prephenate/arogenate dehydrogenase domain; KEGG: pdx:Psed_0331 prephenate dehydrogenase. | Aminodeoxychorismate synthase; Bifunctional enzyme that catalyzes the biosynthesis of 4-amino-4-deoxychorismate (ADC) from chorismate and glutamine. In the first step, a glutamine amidotransferase generates ammonia that is channelled between the binding sites of glutamine and chorismate and used along with chorismate in the second step, catalyzed by aminodeoxychorismate synthase, to produce ADC. Required for the synthesis of 4-aminobenzoate (PABA), an important component in tetrahydrofolate biosynthesis. Does not possess ADC lyase activity; In the C-terminal sectio; belongs to the anth [...] | 0.517 |
| APA94940.1 | APA98968.1 | NS506_00864 | NS506_04922 | Prephenate dehydrogenase; Catalyzes the NAD(+)-dependent conversion of prephenate to p-hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key regulatory enzyme in tyrosine biosynthesis. Displays no chorismate mutase (CM) activity, in contrast to TyrA from E. coli and some other bacteria, that are bifunctional and possess a CM domain; Contains 1 prephenate/arogenate dehydrogenase domain; KEGG: pdx:Psed_0331 prephenate dehydrogenase. | KEGG: nbr:O3I_000260 chorismate mutase. | 0.936 |
| APA94940.1 | aroC | NS506_00864 | NS506_04079 | Prephenate dehydrogenase; Catalyzes the NAD(+)-dependent conversion of prephenate to p-hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key regulatory enzyme in tyrosine biosynthesis. Displays no chorismate mutase (CM) activity, in contrast to TyrA from E. coli and some other bacteria, that are bifunctional and possess a CM domain; Contains 1 prephenate/arogenate dehydrogenase domain; KEGG: pdx:Psed_0331 prephenate dehydrogenase. | 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. | 0.927 |
| APA94940.1 | mbtI | NS506_00864 | NS506_07818 | Prephenate dehydrogenase; Catalyzes the NAD(+)-dependent conversion of prephenate to p-hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key regulatory enzyme in tyrosine biosynthesis. Displays no chorismate mutase (CM) activity, in contrast to TyrA from E. coli and some other bacteria, that are bifunctional and possess a CM domain; Contains 1 prephenate/arogenate dehydrogenase domain; KEGG: pdx:Psed_0331 prephenate dehydrogenase. | Isochorismate synthase; Involved in the incorporation of salicylate into the virulence-conferring salicylate-based siderophore mycobactin. Catalyzes the initial conversion of chorismate to yield the intermediate isochorismate (isochorismate synthase activity), and the subsequent elimination of the enolpyruvyl side chain in a lyase reaction to give salicylate (isochorismate pyruvate-lyase activity). In the absence of magnesium, MbtI displays a chorismate mutase activity and converts chorismate to prephenate; Belongs to the anthranilate synthase component I family. Salicylate synthase su [...] | 0.433 |
| APA94940.1 | pheA | NS506_00864 | NS506_00714 | Prephenate dehydrogenase; Catalyzes the NAD(+)-dependent conversion of prephenate to p-hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key regulatory enzyme in tyrosine biosynthesis. Displays no chorismate mutase (CM) activity, in contrast to TyrA from E. coli and some other bacteria, that are bifunctional and possess a CM domain; Contains 1 prephenate/arogenate dehydrogenase domain; KEGG: pdx:Psed_0331 prephenate dehydrogenase. | Contains 1 ACT domain; Contains 1 prephenate dehydratase domain; KEGG: asd:AS9A_0084 prephenate dehydratase. | 0.991 |
| APA94940.1 | trpE | NS506_00864 | NS506_03511 | Prephenate dehydrogenase; Catalyzes the NAD(+)-dependent conversion of prephenate to p-hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key regulatory enzyme in tyrosine biosynthesis. Displays no chorismate mutase (CM) activity, in contrast to TyrA from E. coli and some other bacteria, that are bifunctional and possess a CM domain; Contains 1 prephenate/arogenate dehydrogenase domain; KEGG: pdx:Psed_0331 prephenate dehydrogenase. | Anthranilate synthase; 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 concentrations of ammonia. | 0.526 |
| APA95565.1 | APA94940.1 | NS506_01494 | NS506_00864 | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis; Contains 1 chorismate mutase domain; KEGG: rpy:Y013_21125 chorismate mutase. | Prephenate dehydrogenase; Catalyzes the NAD(+)-dependent conversion of prephenate to p-hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key regulatory enzyme in tyrosine biosynthesis. Displays no chorismate mutase (CM) activity, in contrast to TyrA from E. coli and some other bacteria, that are bifunctional and possess a CM domain; Contains 1 prephenate/arogenate dehydrogenase domain; KEGG: pdx:Psed_0331 prephenate dehydrogenase. | 0.949 |
| APA95565.1 | APA96431.1 | NS506_01494 | NS506_02365 | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis; Contains 1 chorismate mutase domain; KEGG: rpy:Y013_21125 chorismate mutase. | KEGG: nbr:O3I_000260 chorismate mutase. | 0.932 |
| APA95565.1 | APA97045.1 | NS506_01494 | NS506_02987 | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis; Contains 1 chorismate mutase domain; KEGG: rpy:Y013_21125 chorismate mutase. | Aminodeoxychorismate synthase; Bifunctional enzyme that catalyzes the biosynthesis of 4-amino-4-deoxychorismate (ADC) from chorismate and glutamine. In the first step, a glutamine amidotransferase generates ammonia that is channelled between the binding sites of glutamine and chorismate and used along with chorismate in the second step, catalyzed by aminodeoxychorismate synthase, to produce ADC. Required for the synthesis of 4-aminobenzoate (PABA), an important component in tetrahydrofolate biosynthesis. Does not possess ADC lyase activity; In the C-terminal sectio; belongs to the anth [...] | 0.862 |
| APA95565.1 | APA98968.1 | NS506_01494 | NS506_04922 | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis; Contains 1 chorismate mutase domain; KEGG: rpy:Y013_21125 chorismate mutase. | KEGG: nbr:O3I_000260 chorismate mutase. | 0.932 |
| APA95565.1 | aroC | NS506_01494 | NS506_04079 | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis; Contains 1 chorismate mutase domain; KEGG: rpy:Y013_21125 chorismate mutase. | 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. | 0.959 |
| APA95565.1 | aroF | NS506_01494 | NS506_03330 | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis; Contains 1 chorismate mutase domain; KEGG: rpy:Y013_21125 chorismate mutase. | 3-deoxy-7-phosphoheptulonate synthase; Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate; Belongs to the class-II DAHP synthase family; KEGG: mtu:Rv2178c 3-deoxy-7-phosphoheptulonate synthase. | 0.973 |
| APA95565.1 | mbtI | NS506_01494 | NS506_07818 | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis; Contains 1 chorismate mutase domain; KEGG: rpy:Y013_21125 chorismate mutase. | Isochorismate synthase; Involved in the incorporation of salicylate into the virulence-conferring salicylate-based siderophore mycobactin. Catalyzes the initial conversion of chorismate to yield the intermediate isochorismate (isochorismate synthase activity), and the subsequent elimination of the enolpyruvyl side chain in a lyase reaction to give salicylate (isochorismate pyruvate-lyase activity). In the absence of magnesium, MbtI displays a chorismate mutase activity and converts chorismate to prephenate; Belongs to the anthranilate synthase component I family. Salicylate synthase su [...] | 0.864 |
| APA95565.1 | pabA | NS506_01494 | NS506_00653 | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis; Contains 1 chorismate mutase domain; KEGG: rpy:Y013_21125 chorismate mutase. | Aminodeoxychorismate synthase; 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 concentratio [...] | 0.914 |
| APA95565.1 | pheA | NS506_01494 | NS506_00714 | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis; Contains 1 chorismate mutase domain; KEGG: rpy:Y013_21125 chorismate mutase. | Contains 1 ACT domain; Contains 1 prephenate dehydratase domain; KEGG: asd:AS9A_0084 prephenate dehydratase. | 0.931 |
| APA95565.1 | trpE | NS506_01494 | NS506_03511 | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis; Contains 1 chorismate mutase domain; KEGG: rpy:Y013_21125 chorismate mutase. | Anthranilate synthase; 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 concentrations of ammonia. | 0.932 |
| APA96431.1 | APA94940.1 | NS506_02365 | NS506_00864 | KEGG: nbr:O3I_000260 chorismate mutase. | Prephenate dehydrogenase; Catalyzes the NAD(+)-dependent conversion of prephenate to p-hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key regulatory enzyme in tyrosine biosynthesis. Displays no chorismate mutase (CM) activity, in contrast to TyrA from E. coli and some other bacteria, that are bifunctional and possess a CM domain; Contains 1 prephenate/arogenate dehydrogenase domain; KEGG: pdx:Psed_0331 prephenate dehydrogenase. | 0.936 |
| APA96431.1 | APA95565.1 | NS506_02365 | NS506_01494 | KEGG: nbr:O3I_000260 chorismate mutase. | Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis; Contains 1 chorismate mutase domain; KEGG: rpy:Y013_21125 chorismate mutase. | 0.932 |