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 |
| CAZ98530.1 | udpA | ZOBELLIA_4395 | ZOBELLIA_4396 | Conserved hypothetical protein; Localized in the cytoplasm. | Uridine phosphorylase catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis; Forms a homohexamer; Localized in the cytoplasm; High confidence in function and specificity. | 0.822 |
| cdd | nutA | ZOBELLIA_889 | ZOBELLIA_4772 | Cytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis; Belongs to the cytidine and deoxycytidylate deaminase family. | 5'-Nucleotidase, phosphatase subunit; The 5'-Nucleotidase is involved in the degradation of extracellular 5'-nucleotides into membrane permeable nucleosides. Usually It is composed of a N-terminal phosphatase domain that provides the ligands to the dimetal cluster and a conserved histidine, which together form the catalytic site and of a C-terminal domain involved in the substrate binding; This lipoprotein corresponds only to the phosphatase domain that hydrolyses the phosphate esterified at carbon 5' of the ribose and deoxyribose portions of nucleotide molecules; Binds a chloride ion [...] | 0.908 |
| cdd | punA | ZOBELLIA_889 | ZOBELLIA_1204 | Cytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis; Belongs to the cytidine and deoxycytidylate deaminase family. | Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | 0.951 |
| cdd | surE | ZOBELLIA_889 | ZOBELLIA_1184 | Cytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis; Belongs to the cytidine and deoxycytidylate deaminase family. | Stationary-phase survival protein surE; Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates; Belongs to the SurE nucleotidase family. | 0.921 |
| cdd | tdkA | ZOBELLIA_889 | ZOBELLIA_1526 | Cytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis; Belongs to the cytidine and deoxycytidylate deaminase family. | Thymidine kinase is an ubiquitous enzyme that catalyzes the ATP-dependent phosphorylation of thymidine; Localized in the cytoplasm; High confidence in function and specificity. | 0.937 |
| cdd | udk | ZOBELLIA_889 | ZOBELLIA_3714 | Cytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis; Belongs to the cytidine and deoxycytidylate deaminase family. | Uridine kinase (pyrimidine ribonucleoside kinase) is the rate-limiting enzyme in the pyrimidine salvage pathway. It catalyzes the reactions: ATP + uridine = ADP + UMP and ATP + cytidine = ADP + CMP. It forms a homotetramer and binds a ATP per subunit as cofactor. Localized in the cytoplasm; High confidence in function and specificity. | 0.932 |
| cdd | udpA | ZOBELLIA_889 | ZOBELLIA_4396 | Cytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis; Belongs to the cytidine and deoxycytidylate deaminase family. | Uridine phosphorylase catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis; Forms a homohexamer; Localized in the cytoplasm; High confidence in function and specificity. | 0.982 |
| cdd | uppA | ZOBELLIA_889 | ZOBELLIA_3487 | Cytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis; Belongs to the cytidine and deoxycytidylate deaminase family. | Uracil phosphoribosyltransferase is involved in pyrimidine metabolism. In presence of diphosphate, it converts UMP to uracyl and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP); Uses magnesium ion as a cofactor; Localized in the cytoplasm; High confidence in function and specificity. | 0.523 |
| nutA | cdd | ZOBELLIA_4772 | ZOBELLIA_889 | 5'-Nucleotidase, phosphatase subunit; The 5'-Nucleotidase is involved in the degradation of extracellular 5'-nucleotides into membrane permeable nucleosides. Usually It is composed of a N-terminal phosphatase domain that provides the ligands to the dimetal cluster and a conserved histidine, which together form the catalytic site and of a C-terminal domain involved in the substrate binding; This lipoprotein corresponds only to the phosphatase domain that hydrolyses the phosphate esterified at carbon 5' of the ribose and deoxyribose portions of nucleotide molecules; Binds a chloride ion [...] | Cytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis; Belongs to the cytidine and deoxycytidylate deaminase family. | 0.908 |
| nutA | punA | ZOBELLIA_4772 | ZOBELLIA_1204 | 5'-Nucleotidase, phosphatase subunit; The 5'-Nucleotidase is involved in the degradation of extracellular 5'-nucleotides into membrane permeable nucleosides. Usually It is composed of a N-terminal phosphatase domain that provides the ligands to the dimetal cluster and a conserved histidine, which together form the catalytic site and of a C-terminal domain involved in the substrate binding; This lipoprotein corresponds only to the phosphatase domain that hydrolyses the phosphate esterified at carbon 5' of the ribose and deoxyribose portions of nucleotide molecules; Binds a chloride ion [...] | Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | 0.915 |
| nutA | pyrR1 | ZOBELLIA_4772 | ZOBELLIA_505 | 5'-Nucleotidase, phosphatase subunit; The 5'-Nucleotidase is involved in the degradation of extracellular 5'-nucleotides into membrane permeable nucleosides. Usually It is composed of a N-terminal phosphatase domain that provides the ligands to the dimetal cluster and a conserved histidine, which together form the catalytic site and of a C-terminal domain involved in the substrate binding; This lipoprotein corresponds only to the phosphatase domain that hydrolyses the phosphate esterified at carbon 5' of the ribose and deoxyribose portions of nucleotide molecules; Binds a chloride ion [...] | Bifunctional protein pyrR; PyrR regulates transcriptional attenuation of the pyrimidine nucleotide (pyr) operon by binding in a uridine-dependent manner to specific sites on pyr mRNA. This disrupts an antiterminator hairpin in the RNA and favors formation of a downstream transcription terminator, leading to a reduced expression of downstream genes. Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant. It forms in equilibrium a homodimer and a homohexamer. Localized in the cytoplasm; High confidence in function and specificity. | 0.900 |
| nutA | pyrR2 | ZOBELLIA_4772 | ZOBELLIA_3014 | 5'-Nucleotidase, phosphatase subunit; The 5'-Nucleotidase is involved in the degradation of extracellular 5'-nucleotides into membrane permeable nucleosides. Usually It is composed of a N-terminal phosphatase domain that provides the ligands to the dimetal cluster and a conserved histidine, which together form the catalytic site and of a C-terminal domain involved in the substrate binding; This lipoprotein corresponds only to the phosphatase domain that hydrolyses the phosphate esterified at carbon 5' of the ribose and deoxyribose portions of nucleotide molecules; Binds a chloride ion [...] | Bifunctional protein PyrR; PyrR regulates transcriptional attenuation of the pyrimidine nucleotide operon by binding in a uridine-dependent manner to specific sites on pyr mRNA. This disrupts an antiterminator hairpin in the RNA and favors formation of a downstream transcription terminator, leading to a reduced expression of downstream genes. Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant. Forms momodimer and homohexamer in equilibrium. Localized in the cytoplasm; High confidence in function and specificity. | 0.900 |
| nutA | surE | ZOBELLIA_4772 | ZOBELLIA_1184 | 5'-Nucleotidase, phosphatase subunit; The 5'-Nucleotidase is involved in the degradation of extracellular 5'-nucleotides into membrane permeable nucleosides. Usually It is composed of a N-terminal phosphatase domain that provides the ligands to the dimetal cluster and a conserved histidine, which together form the catalytic site and of a C-terminal domain involved in the substrate binding; This lipoprotein corresponds only to the phosphatase domain that hydrolyses the phosphate esterified at carbon 5' of the ribose and deoxyribose portions of nucleotide molecules; Binds a chloride ion [...] | Stationary-phase survival protein surE; Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates; Belongs to the SurE nucleotidase family. | 0.911 |
| nutA | tdkA | ZOBELLIA_4772 | ZOBELLIA_1526 | 5'-Nucleotidase, phosphatase subunit; The 5'-Nucleotidase is involved in the degradation of extracellular 5'-nucleotides into membrane permeable nucleosides. Usually It is composed of a N-terminal phosphatase domain that provides the ligands to the dimetal cluster and a conserved histidine, which together form the catalytic site and of a C-terminal domain involved in the substrate binding; This lipoprotein corresponds only to the phosphatase domain that hydrolyses the phosphate esterified at carbon 5' of the ribose and deoxyribose portions of nucleotide molecules; Binds a chloride ion [...] | Thymidine kinase is an ubiquitous enzyme that catalyzes the ATP-dependent phosphorylation of thymidine; Localized in the cytoplasm; High confidence in function and specificity. | 0.917 |
| nutA | udk | ZOBELLIA_4772 | ZOBELLIA_3714 | 5'-Nucleotidase, phosphatase subunit; The 5'-Nucleotidase is involved in the degradation of extracellular 5'-nucleotides into membrane permeable nucleosides. Usually It is composed of a N-terminal phosphatase domain that provides the ligands to the dimetal cluster and a conserved histidine, which together form the catalytic site and of a C-terminal domain involved in the substrate binding; This lipoprotein corresponds only to the phosphatase domain that hydrolyses the phosphate esterified at carbon 5' of the ribose and deoxyribose portions of nucleotide molecules; Binds a chloride ion [...] | Uridine kinase (pyrimidine ribonucleoside kinase) is the rate-limiting enzyme in the pyrimidine salvage pathway. It catalyzes the reactions: ATP + uridine = ADP + UMP and ATP + cytidine = ADP + CMP. It forms a homotetramer and binds a ATP per subunit as cofactor. Localized in the cytoplasm; High confidence in function and specificity. | 0.920 |
| nutA | udpA | ZOBELLIA_4772 | ZOBELLIA_4396 | 5'-Nucleotidase, phosphatase subunit; The 5'-Nucleotidase is involved in the degradation of extracellular 5'-nucleotides into membrane permeable nucleosides. Usually It is composed of a N-terminal phosphatase domain that provides the ligands to the dimetal cluster and a conserved histidine, which together form the catalytic site and of a C-terminal domain involved in the substrate binding; This lipoprotein corresponds only to the phosphatase domain that hydrolyses the phosphate esterified at carbon 5' of the ribose and deoxyribose portions of nucleotide molecules; Binds a chloride ion [...] | Uridine phosphorylase catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis; Forms a homohexamer; Localized in the cytoplasm; High confidence in function and specificity. | 0.902 |
| nutA | uppA | ZOBELLIA_4772 | ZOBELLIA_3487 | 5'-Nucleotidase, phosphatase subunit; The 5'-Nucleotidase is involved in the degradation of extracellular 5'-nucleotides into membrane permeable nucleosides. Usually It is composed of a N-terminal phosphatase domain that provides the ligands to the dimetal cluster and a conserved histidine, which together form the catalytic site and of a C-terminal domain involved in the substrate binding; This lipoprotein corresponds only to the phosphatase domain that hydrolyses the phosphate esterified at carbon 5' of the ribose and deoxyribose portions of nucleotide molecules; Binds a chloride ion [...] | Uracil phosphoribosyltransferase is involved in pyrimidine metabolism. In presence of diphosphate, it converts UMP to uracyl and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP); Uses magnesium ion as a cofactor; Localized in the cytoplasm; High confidence in function and specificity. | 0.914 |
| punA | cdd | ZOBELLIA_1204 | ZOBELLIA_889 | Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | Cytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis; Belongs to the cytidine and deoxycytidylate deaminase family. | 0.951 |
| punA | nutA | ZOBELLIA_1204 | ZOBELLIA_4772 | Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | 5'-Nucleotidase, phosphatase subunit; The 5'-Nucleotidase is involved in the degradation of extracellular 5'-nucleotides into membrane permeable nucleosides. Usually It is composed of a N-terminal phosphatase domain that provides the ligands to the dimetal cluster and a conserved histidine, which together form the catalytic site and of a C-terminal domain involved in the substrate binding; This lipoprotein corresponds only to the phosphatase domain that hydrolyses the phosphate esterified at carbon 5' of the ribose and deoxyribose portions of nucleotide molecules; Binds a chloride ion [...] | 0.915 |
| punA | pyrR1 | ZOBELLIA_1204 | ZOBELLIA_505 | Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | Bifunctional protein pyrR; PyrR regulates transcriptional attenuation of the pyrimidine nucleotide (pyr) operon by binding in a uridine-dependent manner to specific sites on pyr mRNA. This disrupts an antiterminator hairpin in the RNA and favors formation of a downstream transcription terminator, leading to a reduced expression of downstream genes. Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant. It forms in equilibrium a homodimer and a homohexamer. Localized in the cytoplasm; High confidence in function and specificity. | 0.900 |
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