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 |
| CAZ95620.1 | CAZ95621.1 | ZOBELLIA_1565 | ZOBELLIA_1566 | Protein containing a N-terminal Type I phosphodiesterase domain and a C-terminal PA14 domain. These enzymes catalyze the cleavage of phosphodiester and phosphosulphate bonds in various compounds such as NAD, deoxynucleotides and nucleotide sugars. The PA14 domain sequence suggests a binding function, rather than a catalytic role and its distribution is compatible with carbohydrate binding; Signal peptide cleaved between the residues 23 and 24; Localized in the periplasm; Family membership. | Metallohydrolase; Protein belonging to the Metallo-beta-lactamase superfamily. This superfamily includes various zinc-dependent hydrolases. The residues involved in metal ion binding are strictly conserved in this protein; Localized in the cytoplasm; Family membership. | 0.918 |
| CAZ95620.1 | CAZ95622.1 | ZOBELLIA_1565 | ZOBELLIA_1567 | Protein containing a N-terminal Type I phosphodiesterase domain and a C-terminal PA14 domain. These enzymes catalyze the cleavage of phosphodiester and phosphosulphate bonds in various compounds such as NAD, deoxynucleotides and nucleotide sugars. The PA14 domain sequence suggests a binding function, rather than a catalytic role and its distribution is compatible with carbohydrate binding; Signal peptide cleaved between the residues 23 and 24; Localized in the periplasm; Family membership. | Aminotransferases share certain mechanistic features with other pyridoxalphosphate-dependent enzymes, such as the covalent binding of the pyridoxalphosphate group to a lysine residue; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; Family membership. | 0.893 |
| CAZ95620.1 | CAZ95623.1 | ZOBELLIA_1565 | ZOBELLIA_1568 | Protein containing a N-terminal Type I phosphodiesterase domain and a C-terminal PA14 domain. These enzymes catalyze the cleavage of phosphodiester and phosphosulphate bonds in various compounds such as NAD, deoxynucleotides and nucleotide sugars. The PA14 domain sequence suggests a binding function, rather than a catalytic role and its distribution is compatible with carbohydrate binding; Signal peptide cleaved between the residues 23 and 24; Localized in the periplasm; Family membership. | Metallophosphoesterase; Protein containing a N-terminal Fibronectin type III domain, a central metallophosphoesterase domain and a second Fibronectin type III domain at the C-terminus. The most conserved regions in the metallophosphoesterase family centre around the metal chelating residues; Signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; Family membership. | 0.933 |
| CAZ95621.1 | CAZ95620.1 | ZOBELLIA_1566 | ZOBELLIA_1565 | Metallohydrolase; Protein belonging to the Metallo-beta-lactamase superfamily. This superfamily includes various zinc-dependent hydrolases. The residues involved in metal ion binding are strictly conserved in this protein; Localized in the cytoplasm; Family membership. | Protein containing a N-terminal Type I phosphodiesterase domain and a C-terminal PA14 domain. These enzymes catalyze the cleavage of phosphodiester and phosphosulphate bonds in various compounds such as NAD, deoxynucleotides and nucleotide sugars. The PA14 domain sequence suggests a binding function, rather than a catalytic role and its distribution is compatible with carbohydrate binding; Signal peptide cleaved between the residues 23 and 24; Localized in the periplasm; Family membership. | 0.918 |
| CAZ95621.1 | CAZ95622.1 | ZOBELLIA_1566 | ZOBELLIA_1567 | Metallohydrolase; Protein belonging to the Metallo-beta-lactamase superfamily. This superfamily includes various zinc-dependent hydrolases. The residues involved in metal ion binding are strictly conserved in this protein; Localized in the cytoplasm; Family membership. | Aminotransferases share certain mechanistic features with other pyridoxalphosphate-dependent enzymes, such as the covalent binding of the pyridoxalphosphate group to a lysine residue; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; Family membership. | 0.866 |
| CAZ95621.1 | CAZ95623.1 | ZOBELLIA_1566 | ZOBELLIA_1568 | Metallohydrolase; Protein belonging to the Metallo-beta-lactamase superfamily. This superfamily includes various zinc-dependent hydrolases. The residues involved in metal ion binding are strictly conserved in this protein; Localized in the cytoplasm; Family membership. | Metallophosphoesterase; Protein containing a N-terminal Fibronectin type III domain, a central metallophosphoesterase domain and a second Fibronectin type III domain at the C-terminus. The most conserved regions in the metallophosphoesterase family centre around the metal chelating residues; Signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; Family membership. | 0.841 |
| CAZ95622.1 | CAZ95620.1 | ZOBELLIA_1567 | ZOBELLIA_1565 | Aminotransferases share certain mechanistic features with other pyridoxalphosphate-dependent enzymes, such as the covalent binding of the pyridoxalphosphate group to a lysine residue; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; Family membership. | Protein containing a N-terminal Type I phosphodiesterase domain and a C-terminal PA14 domain. These enzymes catalyze the cleavage of phosphodiester and phosphosulphate bonds in various compounds such as NAD, deoxynucleotides and nucleotide sugars. The PA14 domain sequence suggests a binding function, rather than a catalytic role and its distribution is compatible with carbohydrate binding; Signal peptide cleaved between the residues 23 and 24; Localized in the periplasm; Family membership. | 0.893 |
| CAZ95622.1 | CAZ95621.1 | ZOBELLIA_1567 | ZOBELLIA_1566 | Aminotransferases share certain mechanistic features with other pyridoxalphosphate-dependent enzymes, such as the covalent binding of the pyridoxalphosphate group to a lysine residue; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; Family membership. | Metallohydrolase; Protein belonging to the Metallo-beta-lactamase superfamily. This superfamily includes various zinc-dependent hydrolases. The residues involved in metal ion binding are strictly conserved in this protein; Localized in the cytoplasm; Family membership. | 0.866 |
| CAZ95622.1 | CAZ95623.1 | ZOBELLIA_1567 | ZOBELLIA_1568 | Aminotransferases share certain mechanistic features with other pyridoxalphosphate-dependent enzymes, such as the covalent binding of the pyridoxalphosphate group to a lysine residue; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; Family membership. | Metallophosphoesterase; Protein containing a N-terminal Fibronectin type III domain, a central metallophosphoesterase domain and a second Fibronectin type III domain at the C-terminus. The most conserved regions in the metallophosphoesterase family centre around the metal chelating residues; Signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; Family membership. | 0.845 |
| CAZ95622.1 | CAZ98616.1 | ZOBELLIA_1567 | ZOBELLIA_4481 | Aminotransferases share certain mechanistic features with other pyridoxalphosphate-dependent enzymes, such as the covalent binding of the pyridoxalphosphate group to a lysine residue; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; Family membership. | Aldehyde dehydrogenases are enzymes which oxidize a wide variety of aliphatic and aromatic aldehydes using NADP as a cofactor.A glutamic acid and a cysteine residue have been implicated in the catalytic activity of mammalian aldehyde dehydrogenase. These residues are conserved in all the enzymes of this family.Located in the cytoplasm; Family membership. | 0.936 |
| CAZ95622.1 | aldA | ZOBELLIA_1567 | ZOBELLIA_3155 | Aminotransferases share certain mechanistic features with other pyridoxalphosphate-dependent enzymes, such as the covalent binding of the pyridoxalphosphate group to a lysine residue; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; Family membership. | Lactaldehyde dehydrogenase catalyze the NAD-dependent oxidation of lactaldehyde into lactate. This protein is a tetramer. AldA is involved in the catabolism of L-fucose and L-rhamnose and is induced by these sugars. In aerobic condition, the lactaldehyde is produced by the cleavage of L-fucose or L-rhamnose; Belongs to the aldehyde dehydrogenase fold family; Localized in the cytoplasm; High confidence in function and specificity. | 0.936 |
| CAZ95622.1 | ddc | ZOBELLIA_1567 | ZOBELLIA_4235 | Aminotransferases share certain mechanistic features with other pyridoxalphosphate-dependent enzymes, such as the covalent binding of the pyridoxalphosphate group to a lysine residue; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; Family membership. | L-2,4-diaminobutyrate decarboxylase catalyzes the reaction : L-2,4-diaminobutanoate = propane-1,3-diamine + CO2. It is involved in 1,3-diaminopropane biosynthesis. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity. | 0.845 |
| CAZ95622.1 | gabD | ZOBELLIA_1567 | ZOBELLIA_4145 | Aminotransferases share certain mechanistic features with other pyridoxalphosphate-dependent enzymes, such as the covalent binding of the pyridoxalphosphate group to a lysine residue; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; Family membership. | Aldehyde dehydrogenases are enzymes which oxidize a wide variety of aliphatic and aromatic aldehydes using NADP as a cofactor.A glutamic acid and a cysteine residue have been implicated in the catalytic activity of mammalian aldehyde dehydrogenase. These residues are conserved in all the enzymes of this family.Located in the cytoplasm; Family membership. | 0.936 |
| CAZ95622.1 | panC | ZOBELLIA_1567 | ZOBELLIA_1411 | Aminotransferases share certain mechanistic features with other pyridoxalphosphate-dependent enzymes, such as the covalent binding of the pyridoxalphosphate group to a lysine residue; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; Family membership. | Pantoate-beta-alanine ligase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Belongs to the pantothenate synthetase family. | 0.907 |
| CAZ95622.1 | panD | ZOBELLIA_1567 | ZOBELLIA_1412 | Aminotransferases share certain mechanistic features with other pyridoxalphosphate-dependent enzymes, such as the covalent binding of the pyridoxalphosphate group to a lysine residue; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; Family membership. | Aspartate 1-decarboxylase; Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. | 0.915 |
| CAZ95622.1 | pcdA | ZOBELLIA_1567 | ZOBELLIA_1480 | Aminotransferases share certain mechanistic features with other pyridoxalphosphate-dependent enzymes, such as the covalent binding of the pyridoxalphosphate group to a lysine residue; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; Family membership. | Piperideine-6-carboxylate dehydrogenase, aldehyde dehydrogenase family; Piperideine-6-carboxylate dehydrogenase catalyses the conversion of Delta-1-Piperideine-6-carboxylate into alpha-aminoadipic acid. This latter compound is a precursor of cephamycin C antibiotic; Localized in the cytoplasm; High confidence in function and specificity. | 0.936 |
| CAZ95623.1 | CAZ95620.1 | ZOBELLIA_1568 | ZOBELLIA_1565 | Metallophosphoesterase; Protein containing a N-terminal Fibronectin type III domain, a central metallophosphoesterase domain and a second Fibronectin type III domain at the C-terminus. The most conserved regions in the metallophosphoesterase family centre around the metal chelating residues; Signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; Family membership. | Protein containing a N-terminal Type I phosphodiesterase domain and a C-terminal PA14 domain. These enzymes catalyze the cleavage of phosphodiester and phosphosulphate bonds in various compounds such as NAD, deoxynucleotides and nucleotide sugars. The PA14 domain sequence suggests a binding function, rather than a catalytic role and its distribution is compatible with carbohydrate binding; Signal peptide cleaved between the residues 23 and 24; Localized in the periplasm; Family membership. | 0.933 |
| CAZ95623.1 | CAZ95621.1 | ZOBELLIA_1568 | ZOBELLIA_1566 | Metallophosphoesterase; Protein containing a N-terminal Fibronectin type III domain, a central metallophosphoesterase domain and a second Fibronectin type III domain at the C-terminus. The most conserved regions in the metallophosphoesterase family centre around the metal chelating residues; Signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; Family membership. | Metallohydrolase; Protein belonging to the Metallo-beta-lactamase superfamily. This superfamily includes various zinc-dependent hydrolases. The residues involved in metal ion binding are strictly conserved in this protein; Localized in the cytoplasm; Family membership. | 0.841 |
| CAZ95623.1 | CAZ95622.1 | ZOBELLIA_1568 | ZOBELLIA_1567 | Metallophosphoesterase; Protein containing a N-terminal Fibronectin type III domain, a central metallophosphoesterase domain and a second Fibronectin type III domain at the C-terminus. The most conserved regions in the metallophosphoesterase family centre around the metal chelating residues; Signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; Family membership. | Aminotransferases share certain mechanistic features with other pyridoxalphosphate-dependent enzymes, such as the covalent binding of the pyridoxalphosphate group to a lysine residue; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; Family membership. | 0.845 |
| CAZ98616.1 | CAZ95622.1 | ZOBELLIA_4481 | ZOBELLIA_1567 | Aldehyde dehydrogenases are enzymes which oxidize a wide variety of aliphatic and aromatic aldehydes using NADP as a cofactor.A glutamic acid and a cysteine residue have been implicated in the catalytic activity of mammalian aldehyde dehydrogenase. These residues are conserved in all the enzymes of this family.Located in the cytoplasm; Family membership. | Aminotransferases share certain mechanistic features with other pyridoxalphosphate-dependent enzymes, such as the covalent binding of the pyridoxalphosphate group to a lysine residue; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; Family membership. | 0.936 |
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