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 |
| Ava_3697 | fbp | Ava_3697 | Ava_1680 | Sedoheptulose 1,7-bisphosphatase / D-fructose 1,6-bisphosphatase; Catalyzes the hydrolysis of fructose 1,6-bisphosphate (Fru 1,6-P2) and sedoheptulose 1,7-bisphosphate (Sed 1,7-P2) to fructose 6- phosphate and sedoheptulose 7-phosphate, respectively; Belongs to the FBPase class 2 family. | D-fructose 1,6-bisphosphatase. | 0.923 |
| Ava_3903 | Ava_3905 | Ava_3903 | Ava_3905 | Ribulose 1,5-bisphosphate carboxylase small subunit. | Ribulose 1,5-bisphosphate carboxylase small subunit. | 0.977 |
| Ava_3903 | cbbL | Ava_3903 | Ava_3907 | Ribulose 1,5-bisphosphate carboxylase small subunit. | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | 0.984 |
| Ava_3905 | Ava_3903 | Ava_3905 | Ava_3903 | Ribulose 1,5-bisphosphate carboxylase small subunit. | Ribulose 1,5-bisphosphate carboxylase small subunit. | 0.977 |
| Ava_3905 | cbbL | Ava_3905 | Ava_3907 | Ribulose 1,5-bisphosphate carboxylase small subunit. | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | 0.999 |
| cbbL | Ava_3903 | Ava_3907 | Ava_3903 | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | Ribulose 1,5-bisphosphate carboxylase small subunit. | 0.984 |
| cbbL | Ava_3905 | Ava_3907 | Ava_3905 | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | Ribulose 1,5-bisphosphate carboxylase small subunit. | 0.999 |
| cbbL | fbp | Ava_3907 | Ava_1680 | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | D-fructose 1,6-bisphosphatase. | 0.468 |
| chlB | chlL | Ava_3466 | Ava_2332 | Light-independent protochlorophyllide reductase, B subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | Light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. | 0.999 |
| chlB | chlN | Ava_3466 | Ava_2330 | Light-independent protochlorophyllide reductase, B subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | Light-independent protochlorophyllide reductase, N subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | 0.999 |
| chlL | chlB | Ava_2332 | Ava_3466 | Light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. | Light-independent protochlorophyllide reductase, B subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | 0.999 |
| chlL | chlN | Ava_2332 | Ava_2330 | Light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. | Light-independent protochlorophyllide reductase, N subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | 0.998 |
| chlN | chlB | Ava_2330 | Ava_3466 | Light-independent protochlorophyllide reductase, N subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | Light-independent protochlorophyllide reductase, B subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | 0.999 |
| chlN | chlL | Ava_2330 | Ava_2332 | Light-independent protochlorophyllide reductase, N subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | Light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. | 0.998 |
| fbp | Ava_3697 | Ava_1680 | Ava_3697 | D-fructose 1,6-bisphosphatase. | Sedoheptulose 1,7-bisphosphatase / D-fructose 1,6-bisphosphatase; Catalyzes the hydrolysis of fructose 1,6-bisphosphate (Fru 1,6-P2) and sedoheptulose 1,7-bisphosphate (Sed 1,7-P2) to fructose 6- phosphate and sedoheptulose 7-phosphate, respectively; Belongs to the FBPase class 2 family. | 0.923 |
| fbp | cbbL | Ava_1680 | Ava_3907 | D-fructose 1,6-bisphosphatase. | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | 0.468 |
| fbp | gap2 | Ava_1680 | Ava_2318 | D-fructose 1,6-bisphosphatase. | Glyceraldehyde 3-phosphate dehydrogenase (NADP+); Gap2 has a major role in carbon fixation as a component of the Calvin cycle. Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorgan [...] | 0.492 |
| gap2 | fbp | Ava_2318 | Ava_1680 | Glyceraldehyde 3-phosphate dehydrogenase (NADP+); Gap2 has a major role in carbon fixation as a component of the Calvin cycle. Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorgan [...] | D-fructose 1,6-bisphosphatase. | 0.492 |