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 |
| KLO38273.1 | KLO40035.1 | ABW17_21030 | ABW17_17765 | Acyl-phosphate glycerol 3-phosphate acyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family. | 0.989 |
| KLO38273.1 | KLO40037.1 | ABW17_21030 | ABW17_17775 | Acyl-phosphate glycerol 3-phosphate acyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.992 |
| KLO38273.1 | KLO41224.1 | ABW17_21030 | ABW17_14885 | Acyl-phosphate glycerol 3-phosphate acyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Fatty acyl-AMP ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.994 |
| KLO38273.1 | KLO42174.1 | ABW17_21030 | ABW17_12825 | Acyl-phosphate glycerol 3-phosphate acyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Beta-ketoacyl synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KLO38273.1 | KLO45106.1 | ABW17_21030 | ABW17_06975 | Acyl-phosphate glycerol 3-phosphate acyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Nucleoside-diphosphate sugar epimerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.921 |
| KLO38273.1 | KLO46990.1 | ABW17_21030 | ABW17_00430 | Acyl-phosphate glycerol 3-phosphate acyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | TspO and MBR s; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.928 |
| KLO38273.1 | nuoB | ABW17_21030 | ABW17_17790 | Acyl-phosphate glycerol 3-phosphate acyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. | 0.910 |
| KLO38273.1 | nuoC | ABW17_21030 | ABW17_17785 | Acyl-phosphate glycerol 3-phosphate acyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 30 kDa subunit family. | 0.926 |
| KLO38273.1 | nuoD | ABW17_21030 | ABW17_17780 | Acyl-phosphate glycerol 3-phosphate acyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family. | 0.883 |
| KLO38273.1 | nuoI | ABW17_21030 | ABW17_17755 | Acyl-phosphate glycerol 3-phosphate acyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. | 0.993 |
| KLO40035.1 | KLO38273.1 | ABW17_17765 | ABW17_21030 | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family. | Acyl-phosphate glycerol 3-phosphate acyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.989 |
| KLO40035.1 | KLO40037.1 | ABW17_17765 | ABW17_17775 | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family. | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KLO40035.1 | KLO41224.1 | ABW17_17765 | ABW17_14885 | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family. | Fatty acyl-AMP ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.989 |
| KLO40035.1 | KLO42174.1 | ABW17_17765 | ABW17_12825 | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family. | Beta-ketoacyl synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.990 |
| KLO40035.1 | KLO45106.1 | ABW17_17765 | ABW17_06975 | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family. | Nucleoside-diphosphate sugar epimerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.952 |
| KLO40035.1 | KLO46990.1 | ABW17_17765 | ABW17_00430 | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family. | TspO and MBR s; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.952 |
| KLO40035.1 | nuoB | ABW17_17765 | ABW17_17790 | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family. | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. | 0.999 |
| KLO40035.1 | nuoC | ABW17_17765 | ABW17_17785 | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family. | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 30 kDa subunit family. | 0.999 |
| KLO40035.1 | nuoD | ABW17_17765 | ABW17_17780 | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family. | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family. | 0.999 |
| KLO40035.1 | nuoI | ABW17_17765 | ABW17_17755 | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family. | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. | 0.999 |
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