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 |
| AIL62586.1 | AIL62595.1 | PSAKL28_34340 | PSAKL28_34430 | Isocitrate dehydrogenase, NADP-dependent, prokaryotic type. | Isocitrate lyase. | 0.472 |
| AIL62586.1 | aceK | PSAKL28_34340 | PSAKL28_39180 | Isocitrate dehydrogenase, NADP-dependent, prokaryotic type. | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | 0.921 |
| AIL62586.1 | glcB | PSAKL28_34340 | PSAKL28_03900 | Isocitrate dehydrogenase, NADP-dependent, prokaryotic type. | Malate synthase G; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily. | 0.643 |
| AIL62586.1 | putA | PSAKL28_34340 | PSAKL28_48400 | Isocitrate dehydrogenase, NADP-dependent, prokaryotic type. | Proline dehydrogenase/delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | 0.472 |
| AIL62595.1 | AIL62586.1 | PSAKL28_34430 | PSAKL28_34340 | Isocitrate lyase. | Isocitrate dehydrogenase, NADP-dependent, prokaryotic type. | 0.472 |
| AIL62595.1 | aceK | PSAKL28_34430 | PSAKL28_39180 | Isocitrate lyase. | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | 0.867 |
| AIL62595.1 | glcB | PSAKL28_34430 | PSAKL28_03900 | Isocitrate lyase. | Malate synthase G; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily. | 0.996 |
| AIL62749.1 | aceK | PSAKL28_35970 | PSAKL28_39180 | Amidohydrolase. | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | 0.425 |
| AIL63069.1 | aceK | PSAKL28_39190 | PSAKL28_39180 | Drug/metabolite transporter permease. | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | 0.645 |
| aceK | AIL62586.1 | PSAKL28_39180 | PSAKL28_34340 | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | Isocitrate dehydrogenase, NADP-dependent, prokaryotic type. | 0.921 |
| aceK | AIL62595.1 | PSAKL28_39180 | PSAKL28_34430 | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | Isocitrate lyase. | 0.867 |
| aceK | AIL62749.1 | PSAKL28_39180 | PSAKL28_35970 | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | Amidohydrolase. | 0.425 |
| aceK | AIL63069.1 | PSAKL28_39180 | PSAKL28_39190 | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | Drug/metabolite transporter permease. | 0.645 |
| aceK | glcB | PSAKL28_39180 | PSAKL28_03900 | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | Malate synthase G; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily. | 0.508 |
| aceK | putA | PSAKL28_39180 | PSAKL28_48400 | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | Proline dehydrogenase/delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | 0.432 |
| glcB | AIL62586.1 | PSAKL28_03900 | PSAKL28_34340 | Malate synthase G; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily. | Isocitrate dehydrogenase, NADP-dependent, prokaryotic type. | 0.643 |
| glcB | AIL62595.1 | PSAKL28_03900 | PSAKL28_34430 | Malate synthase G; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily. | Isocitrate lyase. | 0.996 |
| glcB | aceK | PSAKL28_03900 | PSAKL28_39180 | Malate synthase G; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily. | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | 0.508 |
| putA | AIL62586.1 | PSAKL28_48400 | PSAKL28_34340 | Proline dehydrogenase/delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | Isocitrate dehydrogenase, NADP-dependent, prokaryotic type. | 0.472 |
| putA | aceK | PSAKL28_48400 | PSAKL28_39180 | Proline dehydrogenase/delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | Bifunctional isocitrate dehydrogenase kinase/phosphatase protein; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | 0.432 |