| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAZ94598.1 | aroQ | ZOBELLIA_527 | ZOBELLIA_526 | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 32 and 33; Localized in the periplasmic space; Conserved hypothetical protein. | 3-dehydroquinate dehydratase; Catalyzes a trans-dehydration via an enolate intermediate. Belongs to the type-II 3-dehydroquinase family. | 0.545 |
| aroB1 | aroB2 | ZOBELLIA_493 | ZOBELLIA_4536 | 3-Dehydroquinate synthase is involved in the biosynthesis of aromatic amino acids. It catalyzes the second step of the shikimate pathway, the formation of dehydroquinate and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. It forms a monomer and binds NAD and divalent metal cation as cofactors. Localized in the cytoplasm; High confidence in function and specificity. | 3-Dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | 0.927 |
| aroB1 | aroC | ZOBELLIA_493 | ZOBELLIA_4404 | 3-Dehydroquinate synthase is involved in the biosynthesis of aromatic amino acids. It catalyzes the second step of the shikimate pathway, the formation of dehydroquinate and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. It forms a monomer and binds NAD and divalent metal cation as cofactors. Localized in the cytoplasm; High confidence in function and specificity. | 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. | 0.910 |
| aroB1 | aroE | ZOBELLIA_493 | ZOBELLIA_3668 | 3-Dehydroquinate synthase is involved in the biosynthesis of aromatic amino acids. It catalyzes the second step of the shikimate pathway, the formation of dehydroquinate and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. It forms a monomer and binds NAD and divalent metal cation as cofactors. Localized in the cytoplasm; High confidence in function and specificity. | Shikimate dehydrogenase catalyzes the fourth step of The shikimate pathway. In a NADP+-dependent reaction, AroE converts the shikimate to 3-dehydroshikimate. The N-terminal domain is the shikimate-binding domain and consists of a mainly parallel six-stranded beta-sheet and six alpha-helices. The C-terminal NADP-binding domain adopts a nearly canonical Rossmann fold; Localized in the cytoplasm; High confidence in function and specificity. | 0.750 |
| aroB1 | aroGH | ZOBELLIA_493 | ZOBELLIA_826 | 3-Dehydroquinate synthase is involved in the biosynthesis of aromatic amino acids. It catalyzes the second step of the shikimate pathway, the formation of dehydroquinate and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. It forms a monomer and binds NAD and divalent metal cation as cofactors. Localized in the cytoplasm; High confidence in function and specificity. | Bifunctional enzyme including 3-deoxy-7-phosphoheptulonate synthase (DAHP synthase) in N-terminus and chorismate mutase in C-terminus. DAHP synthase catalyzes the first step in the common pathway leading to the biosynthesis of aromatic compounds, the stereospecific condensation of phosphoenolpyruvate and D-erythrose-4-phosphate giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP). Chorismate mutase catalyzes the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. Localized in the cytoplasm; High confidence in function and speci [...] | 0.928 |
| aroB1 | aroK | ZOBELLIA_493 | ZOBELLIA_3013 | 3-Dehydroquinate synthase is involved in the biosynthesis of aromatic amino acids. It catalyzes the second step of the shikimate pathway, the formation of dehydroquinate and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. It forms a monomer and binds NAD and divalent metal cation as cofactors. Localized in the cytoplasm; High confidence in function and specificity. | 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. | 0.907 |
| aroB1 | aroQ | ZOBELLIA_493 | ZOBELLIA_526 | 3-Dehydroquinate synthase is involved in the biosynthesis of aromatic amino acids. It catalyzes the second step of the shikimate pathway, the formation of dehydroquinate and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. It forms a monomer and binds NAD and divalent metal cation as cofactors. Localized in the cytoplasm; High confidence in function and specificity. | 3-dehydroquinate dehydratase; Catalyzes a trans-dehydration via an enolate intermediate. Belongs to the type-II 3-dehydroquinase family. | 0.942 |
| aroB2 | aroB1 | ZOBELLIA_4536 | ZOBELLIA_493 | 3-Dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | 3-Dehydroquinate synthase is involved in the biosynthesis of aromatic amino acids. It catalyzes the second step of the shikimate pathway, the formation of dehydroquinate and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. It forms a monomer and binds NAD and divalent metal cation as cofactors. Localized in the cytoplasm; High confidence in function and specificity. | 0.927 |
| aroB2 | aroC | ZOBELLIA_4536 | ZOBELLIA_4404 | 3-Dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | 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. | 0.964 |
| aroB2 | aroE | ZOBELLIA_4536 | ZOBELLIA_3668 | 3-Dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | Shikimate dehydrogenase catalyzes the fourth step of The shikimate pathway. In a NADP+-dependent reaction, AroE converts the shikimate to 3-dehydroshikimate. The N-terminal domain is the shikimate-binding domain and consists of a mainly parallel six-stranded beta-sheet and six alpha-helices. The C-terminal NADP-binding domain adopts a nearly canonical Rossmann fold; Localized in the cytoplasm; High confidence in function and specificity. | 0.920 |
| aroB2 | aroGH | ZOBELLIA_4536 | ZOBELLIA_826 | 3-Dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | Bifunctional enzyme including 3-deoxy-7-phosphoheptulonate synthase (DAHP synthase) in N-terminus and chorismate mutase in C-terminus. DAHP synthase catalyzes the first step in the common pathway leading to the biosynthesis of aromatic compounds, the stereospecific condensation of phosphoenolpyruvate and D-erythrose-4-phosphate giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP). Chorismate mutase catalyzes the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. Localized in the cytoplasm; High confidence in function and speci [...] | 0.964 |
| aroB2 | aroK | ZOBELLIA_4536 | ZOBELLIA_3013 | 3-Dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | 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. | 0.931 |
| aroB2 | aroQ | ZOBELLIA_4536 | ZOBELLIA_526 | 3-Dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | 3-dehydroquinate dehydratase; Catalyzes a trans-dehydration via an enolate intermediate. Belongs to the type-II 3-dehydroquinase family. | 0.974 |
| aroC | aroB1 | ZOBELLIA_4404 | ZOBELLIA_493 | 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. | 3-Dehydroquinate synthase is involved in the biosynthesis of aromatic amino acids. It catalyzes the second step of the shikimate pathway, the formation of dehydroquinate and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. It forms a monomer and binds NAD and divalent metal cation as cofactors. Localized in the cytoplasm; High confidence in function and specificity. | 0.910 |
| aroC | aroB2 | ZOBELLIA_4404 | ZOBELLIA_4536 | 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. | 3-Dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | 0.964 |
| aroC | aroE | ZOBELLIA_4404 | ZOBELLIA_3668 | 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. | Shikimate dehydrogenase catalyzes the fourth step of The shikimate pathway. In a NADP+-dependent reaction, AroE converts the shikimate to 3-dehydroshikimate. The N-terminal domain is the shikimate-binding domain and consists of a mainly parallel six-stranded beta-sheet and six alpha-helices. The C-terminal NADP-binding domain adopts a nearly canonical Rossmann fold; Localized in the cytoplasm; High confidence in function and specificity. | 0.951 |
| aroC | aroGH | ZOBELLIA_4404 | ZOBELLIA_826 | 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. | Bifunctional enzyme including 3-deoxy-7-phosphoheptulonate synthase (DAHP synthase) in N-terminus and chorismate mutase in C-terminus. DAHP synthase catalyzes the first step in the common pathway leading to the biosynthesis of aromatic compounds, the stereospecific condensation of phosphoenolpyruvate and D-erythrose-4-phosphate giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP). Chorismate mutase catalyzes the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. Localized in the cytoplasm; High confidence in function and speci [...] | 0.996 |
| aroC | aroK | ZOBELLIA_4404 | ZOBELLIA_3013 | 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. | 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. | 0.716 |
| aroC | aroQ | ZOBELLIA_4404 | ZOBELLIA_526 | 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. | 3-dehydroquinate dehydratase; Catalyzes a trans-dehydration via an enolate intermediate. Belongs to the type-II 3-dehydroquinase family. | 0.495 |
| aroE | aroB1 | ZOBELLIA_3668 | ZOBELLIA_493 | Shikimate dehydrogenase catalyzes the fourth step of The shikimate pathway. In a NADP+-dependent reaction, AroE converts the shikimate to 3-dehydroshikimate. The N-terminal domain is the shikimate-binding domain and consists of a mainly parallel six-stranded beta-sheet and six alpha-helices. The C-terminal NADP-binding domain adopts a nearly canonical Rossmann fold; Localized in the cytoplasm; High confidence in function and specificity. | 3-Dehydroquinate synthase is involved in the biosynthesis of aromatic amino acids. It catalyzes the second step of the shikimate pathway, the formation of dehydroquinate and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. It forms a monomer and binds NAD and divalent metal cation as cofactors. Localized in the cytoplasm; High confidence in function and specificity. | 0.750 |