| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| APA94940.1 | APA98492.1 | NS506_00864 | NS506_04444 | 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. | Belongs to the dehydroquinate synthase family; KEGG: ppu:PP_5078 3-dehydroquinate synthase. | 0.788 |
| APA94940.1 | APA99981.1 | NS506_00864 | NS506_05945 | 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. | C7-cyclitol synthase using sedo-heptulose 7-phosphate, but not ido-heptulose 7-phosphate and 3-deoxy-arabino- heptulosonate 7-phosphate, as a substrate. Involved in the biosynthesis of the acarviose moiety of the alpha-glucosidase inhibitor acarbose. Belongs to the dehydroquinate synthase family; KEGG: mmi:MMAR_0578 3-dehydroquinate synthase. | 0.758 |
| APA94940.1 | APB01828.1 | NS506_00864 | NS506_07810 | 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. | 3-deoxy-7-phosphoheptulonate synthase; Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino- heptulosonate-7-phosphate (DAHP). | 0.805 |
| APA94940.1 | aroA | NS506_00864 | NS506_02112 | 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. | 3-phosphoshikimate 1-carboxyvinyltransferase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. | 0.855 |
| APA94940.1 | aroB | NS506_00864 | NS506_04077 | 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. | 3-dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | 0.796 |
| 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 | aroK | NS506_00864 | NS506_04078 | 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. | Shikimate kinase; Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate; Belongs to the shikimate kinase family. | 0.769 |
| APA98492.1 | APA94940.1 | NS506_04444 | NS506_00864 | Belongs to the dehydroquinate synthase family; KEGG: ppu:PP_5078 3-dehydroquinate synthase. | 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. | 0.788 |
| APA98492.1 | APB01828.1 | NS506_04444 | NS506_07810 | Belongs to the dehydroquinate synthase family; KEGG: ppu:PP_5078 3-dehydroquinate synthase. | 3-deoxy-7-phosphoheptulonate synthase; Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino- heptulosonate-7-phosphate (DAHP). | 0.954 |
| APA98492.1 | aroA | NS506_04444 | NS506_02112 | Belongs to the dehydroquinate synthase family; KEGG: ppu:PP_5078 3-dehydroquinate synthase. | 3-phosphoshikimate 1-carboxyvinyltransferase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. | 0.981 |
| APA98492.1 | aroB | NS506_04444 | NS506_04077 | Belongs to the dehydroquinate synthase family; KEGG: ppu:PP_5078 3-dehydroquinate synthase. | 3-dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | 0.925 |
| APA98492.1 | aroC | NS506_04444 | NS506_04079 | Belongs to the dehydroquinate synthase family; KEGG: ppu:PP_5078 3-dehydroquinate synthase. | 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. | 0.954 |
| APA98492.1 | aroE | NS506_04444 | NS506_04073 | Belongs to the dehydroquinate synthase family; KEGG: ppu:PP_5078 3-dehydroquinate synthase. | Shikimate dehydrogenase; The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis; In the N-terminal sectio; belongs to the dehydroquinate synthase family; In the 2nd sectio; belongs to the EPSP synthase family; In the 3rd sectio; belongs to the shikimate kinase family; In the 4th sectio; belongs to the type-I 3- dehydroquinase family; In the C-terminal sectio; belongs to the shikimate dehydrogenase family; KEGG: mtu:Rv2552c shikimate dehydrogenase. | 0.912 |
| APA98492.1 | aroF | NS506_04444 | NS506_03330 | Belongs to the dehydroquinate synthase family; KEGG: ppu:PP_5078 3-dehydroquinate synthase. | 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. | 0.939 |
| APA98492.1 | aroK | NS506_04444 | NS506_04078 | Belongs to the dehydroquinate synthase family; KEGG: ppu:PP_5078 3-dehydroquinate synthase. | Shikimate kinase; Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate; Belongs to the shikimate kinase family. | 0.996 |
| APA98492.1 | aroQ | NS506_04444 | NS506_01013 | Belongs to the dehydroquinate synthase family; KEGG: ppu:PP_5078 3-dehydroquinate synthase. | 3-dehydroquinate dehydratase; Catalyzes a trans-dehydration via an enolate intermediate. Belongs to the type-II 3-dehydroquinase family. | 0.966 |
| APA99981.1 | APA94940.1 | NS506_05945 | NS506_00864 | C7-cyclitol synthase using sedo-heptulose 7-phosphate, but not ido-heptulose 7-phosphate and 3-deoxy-arabino- heptulosonate 7-phosphate, as a substrate. Involved in the biosynthesis of the acarviose moiety of the alpha-glucosidase inhibitor acarbose. Belongs to the dehydroquinate synthase family; KEGG: mmi:MMAR_0578 3-dehydroquinate synthase. | 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. | 0.758 |
| APA99981.1 | APB01828.1 | NS506_05945 | NS506_07810 | C7-cyclitol synthase using sedo-heptulose 7-phosphate, but not ido-heptulose 7-phosphate and 3-deoxy-arabino- heptulosonate 7-phosphate, as a substrate. Involved in the biosynthesis of the acarviose moiety of the alpha-glucosidase inhibitor acarbose. Belongs to the dehydroquinate synthase family; KEGG: mmi:MMAR_0578 3-dehydroquinate synthase. | 3-deoxy-7-phosphoheptulonate synthase; Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino- heptulosonate-7-phosphate (DAHP). | 0.512 |
| APA99981.1 | aroA | NS506_05945 | NS506_02112 | C7-cyclitol synthase using sedo-heptulose 7-phosphate, but not ido-heptulose 7-phosphate and 3-deoxy-arabino- heptulosonate 7-phosphate, as a substrate. Involved in the biosynthesis of the acarviose moiety of the alpha-glucosidase inhibitor acarbose. Belongs to the dehydroquinate synthase family; KEGG: mmi:MMAR_0578 3-dehydroquinate synthase. | 3-phosphoshikimate 1-carboxyvinyltransferase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. | 0.968 |
| APA99981.1 | aroC | NS506_05945 | NS506_04079 | C7-cyclitol synthase using sedo-heptulose 7-phosphate, but not ido-heptulose 7-phosphate and 3-deoxy-arabino- heptulosonate 7-phosphate, as a substrate. Involved in the biosynthesis of the acarviose moiety of the alpha-glucosidase inhibitor acarbose. Belongs to the dehydroquinate synthase family; KEGG: mmi:MMAR_0578 3-dehydroquinate synthase. | 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. | 0.931 |