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 proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| MMP0188 | MMP0307 | MMP0188 | MMP0307 | Conserved hypothetical protein; Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L- methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2). Belongs to the DPH1/DPH2 family. | Conserved hypothetical archaeal protein. | 0.408 |
| MMP0188 | tyrA | MMP0188 | MMP1514 | Conserved hypothetical protein; Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L- methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2). Belongs to the DPH1/DPH2 family. | Prephenate dehydrogenase; Citation: MacBeath G, Kast P, Hilvert D. (1998) Biochemistry 37:10062-73. | 0.646 |
| MMP0307 | MMP0188 | MMP0307 | MMP0188 | Conserved hypothetical archaeal protein. | Conserved hypothetical protein; Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L- methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2). Belongs to the DPH1/DPH2 family. | 0.408 |
| MMP0307 | tyrA | MMP0307 | MMP1514 | Conserved hypothetical archaeal protein. | Prephenate dehydrogenase; Citation: MacBeath G, Kast P, Hilvert D. (1998) Biochemistry 37:10062-73. | 0.625 |
| MMP0307 | xseA | MMP0307 | MMP0732 | Conserved hypothetical archaeal protein. | Exonuclease VII, large subunit:OB-fold nucleic acid binding domain. | 0.681 |
| MMP1072 | aroC | MMP1072 | MMP1333 | Aminotransferase (subgroup I) similar to Aromatic Aminotransferase; Ward DE, de Vos WM, van der Oost J (2002) Archaea 1:133-141; Citation: Matsui I, Matsui E, Sakai Y, Kikuchi H, Kawarabayasi Y, Ura H, Kawaguchi S, Kuramitsu S, Harata K. (2000)J Biol Chem 275:4871-9. | 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. | 0.450 |
| MMP1072 | hisC | MMP1072 | MMP1216 | Aminotransferase (subgroup I) similar to Aromatic Aminotransferase; Ward DE, de Vos WM, van der Oost J (2002) Archaea 1:133-141; Citation: Matsui I, Matsui E, Sakai Y, Kikuchi H, Kawarabayasi Y, Ura H, Kawaguchi S, Kuramitsu S, Harata K. (2000)J Biol Chem 275:4871-9. | Histidinol-phosphate aminotransferase; Citation: Conover RK, Doolittle WF. (1990) J Bacteriol 172:3244-9. | 0.938 |
| MMP1072 | pheA | MMP1072 | MMP1528 | Aminotransferase (subgroup I) similar to Aromatic Aminotransferase; Ward DE, de Vos WM, van der Oost J (2002) Archaea 1:133-141; Citation: Matsui I, Matsui E, Sakai Y, Kikuchi H, Kawarabayasi Y, Ura H, Kawaguchi S, Kuramitsu S, Harata K. (2000)J Biol Chem 275:4871-9. | Prephenate dehydratase; Citation: MacBeath G, Kast P, Hilvert D. (1998). Biochemistry 37:10062-73. | 0.992 |
| MMP1072 | tyrA | MMP1072 | MMP1514 | Aminotransferase (subgroup I) similar to Aromatic Aminotransferase; Ward DE, de Vos WM, van der Oost J (2002) Archaea 1:133-141; Citation: Matsui I, Matsui E, Sakai Y, Kikuchi H, Kawarabayasi Y, Ura H, Kawaguchi S, Kuramitsu S, Harata K. (2000)J Biol Chem 275:4871-9. | Prephenate dehydrogenase; Citation: MacBeath G, Kast P, Hilvert D. (1998) Biochemistry 37:10062-73. | 0.951 |
| aroA | aroC | MMP1205 | MMP1333 | 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. | 0.999 |
| aroA | aroQ | MMP1205 | MMP0578 | 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 mutase; Citation: MacBeath G, Kast P, Hilvert D. (1998). Biochemistry 37:10062-73. | 0.932 |
| aroA | hisC | MMP1205 | MMP1216 | 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. | Histidinol-phosphate aminotransferase; Citation: Conover RK, Doolittle WF. (1990) J Bacteriol 172:3244-9. | 0.828 |
| aroA | pheA | MMP1205 | MMP1528 | 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. | Prephenate dehydratase; Citation: MacBeath G, Kast P, Hilvert D. (1998). Biochemistry 37:10062-73. | 0.832 |
| aroA | tyrA | MMP1205 | MMP1514 | 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. | Prephenate dehydrogenase; Citation: MacBeath G, Kast P, Hilvert D. (1998) Biochemistry 37:10062-73. | 0.713 |
| aroC | MMP1072 | MMP1333 | MMP1072 | 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. | Aminotransferase (subgroup I) similar to Aromatic Aminotransferase; Ward DE, de Vos WM, van der Oost J (2002) Archaea 1:133-141; Citation: Matsui I, Matsui E, Sakai Y, Kikuchi H, Kawarabayasi Y, Ura H, Kawaguchi S, Kuramitsu S, Harata K. (2000)J Biol Chem 275:4871-9. | 0.450 |
| aroC | aroA | MMP1333 | MMP1205 | 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-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. | 0.999 |
| aroC | aroQ | MMP1333 | MMP0578 | 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; Citation: MacBeath G, Kast P, Hilvert D. (1998). Biochemistry 37:10062-73. | 0.990 |
| aroC | hisC | MMP1333 | MMP1216 | 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. | Histidinol-phosphate aminotransferase; Citation: Conover RK, Doolittle WF. (1990) J Bacteriol 172:3244-9. | 0.887 |
| aroC | pheA | MMP1333 | MMP1528 | 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. | Prephenate dehydratase; Citation: MacBeath G, Kast P, Hilvert D. (1998). Biochemistry 37:10062-73. | 0.800 |
| aroC | tyrA | MMP1333 | MMP1514 | 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. | Prephenate dehydrogenase; Citation: MacBeath G, Kast P, Hilvert D. (1998) Biochemistry 37:10062-73. | 0.754 |
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