Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAZ98902.1 | aroK | ZOBELLIA_4767 | ZOBELLIA_3013 | Conserved hypothetical protein. Localized in the cytoplasm. | 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. | 0.559 |
| aroA | aroB1 | ZOBELLIA_819 | ZOBELLIA_493 | 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. | 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. | 0.971 |
| aroA | aroB2 | ZOBELLIA_819 | ZOBELLIA_4536 | 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. | 3-Dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | 0.986 |
| aroA | aroC | ZOBELLIA_819 | ZOBELLIA_4404 | 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. | 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. | 0.998 |
| aroA | aroE | ZOBELLIA_819 | ZOBELLIA_3668 | 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. | 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. | 0.979 |
| aroA | aroGH | ZOBELLIA_819 | ZOBELLIA_826 | 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. | 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 [...] | 0.980 |
| aroA | aroK | ZOBELLIA_819 | ZOBELLIA_3013 | 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. | 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. | 0.971 |
| aroA | aroQ | ZOBELLIA_819 | ZOBELLIA_526 | 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. | 3-dehydroquinate dehydratase; Catalyzes a trans-dehydration via an enolate intermediate. Belongs to the type-II 3-dehydroquinase family. | 0.433 |
| aroA | trpG | ZOBELLIA_819 | ZOBELLIA_668 | 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. | Anthranilate synthase component II (glutamine amidotransferase); The anthranilate synthase catalyzes the formation of anthranilate from chorismate and L-glutamine, the first step in the biosynthesis of tryptophan. The enzyme is a Tetramer of two components I and two components II. Associated with the component I, the component II of the anthranilate synthase provides the glutamine amidotransferase activity (GATase, 2.4.2.-) that catalyses the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen g [...] | 0.539 |
| aroB1 | aroA | ZOBELLIA_493 | ZOBELLIA_819 | 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-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. | 0.971 |
| 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 |
| aroB1 | trpG | ZOBELLIA_493 | ZOBELLIA_668 | 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. | Anthranilate synthase component II (glutamine amidotransferase); The anthranilate synthase catalyzes the formation of anthranilate from chorismate and L-glutamine, the first step in the biosynthesis of tryptophan. The enzyme is a Tetramer of two components I and two components II. Associated with the component I, the component II of the anthranilate synthase provides the glutamine amidotransferase activity (GATase, 2.4.2.-) that catalyses the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen g [...] | 0.535 |
| aroB2 | aroA | ZOBELLIA_4536 | ZOBELLIA_819 | 3-Dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | 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. | 0.986 |
| 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 |
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