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 |
| CAZ94094.1 | kmoA | ZOBELLIA_21 | ZOBELLIA_717 | Members of the Nudix hydrolase family catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. They require Mg2+ or Mn2+, for their activity. Substrates include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. In general, the role of the nudix hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & \house- cleaning\ enzymes; Belong to the Nudix hydrolase superfamily; Localized in the cytoplasm; Family membership. | Kynurenine 3-monooxygenase; Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid; Belongs to the aromatic-ring hydroxylase family. KMO subfamily. | 0.579 |
| CAZ94094.1 | mvaA | ZOBELLIA_21 | ZOBELLIA_1191 | Members of the Nudix hydrolase family catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. They require Mg2+ or Mn2+, for their activity. Substrates include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. In general, the role of the nudix hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & \house- cleaning\ enzymes; Belong to the Nudix hydrolase superfamily; Localized in the cytoplasm; Family membership. | 3-Hydroxy-3-methylglutaryl-coenzyme A reductase catalyzes the reversible conversion of mevalonate into 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA), using coenzyme A and NAD(P) as cofactors. In Archeae, NADP-depedent HMG-CoA reductase is involved in the biosynthesis of the isoprenoids side chains of lipids. Some bacteria, such as Pseudomonas mevalonii, use an NAD-dependent HMG-CoA reductase to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. These bacteria can use mevalonate as sole carbon source. Localized in the cytoplasm; High confidence in function and specificity. | 0.448 |
| CAZ94094.1 | mvdA | ZOBELLIA_21 | ZOBELLIA_1243 | Members of the Nudix hydrolase family catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. They require Mg2+ or Mn2+, for their activity. Substrates include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. In general, the role of the nudix hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & \house- cleaning\ enzymes; Belong to the Nudix hydrolase superfamily; Localized in the cytoplasm; Family membership. | Mevalonate diphosphate decarboxylase or diphosphomevalonate decarboxylase catalyzes the decarboxylation of mevalonate pyrophosphate to isopentyl pyrophosphate (IPP), the last step in the synthesis of IPP in the mevalonate pathway. Mevalonate is a key intermediate in the biosynthesis of sterols and non-sterol isoprenes; Belongs to the GHMP kinase domain superfamily; Localized in the cytoplasm; High confidence in function and specificity. | 0.948 |
| CAZ95249.1 | dppA1 | ZOBELLIA_1192 | ZOBELLIA_1190 | Protein that is probably a kinase; belongs to the GHMP (galacto, homoserine, mevalonate, phosphomevalonate) kinase family; Localized in the cytoplasm; Family membership. | Dipeptidyl-peptidase IV, family S9; Dipeptidyl-peptidase IV releases an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Belongs to the family S9 of the serine peptidases. The active site residues are in the order Ser, Asp, His in the sequence. The motif around the active site serine is G W S (Y/F) G G. DppA displays a two domain architecture, with a N-terminal eight-bladed beta-propeller and a C-terminal S9 peptidase domain. Features a signal peptide cleaved between the residues 20 and 21. Localiz [...] | 0.544 |
| CAZ95249.1 | mvaA | ZOBELLIA_1192 | ZOBELLIA_1191 | Protein that is probably a kinase; belongs to the GHMP (galacto, homoserine, mevalonate, phosphomevalonate) kinase family; Localized in the cytoplasm; Family membership. | 3-Hydroxy-3-methylglutaryl-coenzyme A reductase catalyzes the reversible conversion of mevalonate into 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA), using coenzyme A and NAD(P) as cofactors. In Archeae, NADP-depedent HMG-CoA reductase is involved in the biosynthesis of the isoprenoids side chains of lipids. Some bacteria, such as Pseudomonas mevalonii, use an NAD-dependent HMG-CoA reductase to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. These bacteria can use mevalonate as sole carbon source. Localized in the cytoplasm; High confidence in function and specificity. | 0.964 |
| CAZ95249.1 | mvdA | ZOBELLIA_1192 | ZOBELLIA_1243 | Protein that is probably a kinase; belongs to the GHMP (galacto, homoserine, mevalonate, phosphomevalonate) kinase family; Localized in the cytoplasm; Family membership. | Mevalonate diphosphate decarboxylase or diphosphomevalonate decarboxylase catalyzes the decarboxylation of mevalonate pyrophosphate to isopentyl pyrophosphate (IPP), the last step in the synthesis of IPP in the mevalonate pathway. Mevalonate is a key intermediate in the biosynthesis of sterols and non-sterol isoprenes; Belongs to the GHMP kinase domain superfamily; Localized in the cytoplasm; High confidence in function and specificity. | 0.942 |
| CAZ95249.1 | mvkA | ZOBELLIA_1192 | ZOBELLIA_1242 | Protein that is probably a kinase; belongs to the GHMP (galacto, homoserine, mevalonate, phosphomevalonate) kinase family; Localized in the cytoplasm; Family membership. | Mevalonate kinase catalyses the phosphorylation of mevalonate to phosphomevalonate from AT as donor; Uses the magnesium ions as cofactor; CTP, GTP and UTP can also act as donors; Belongs to the GHMP kinase family; Localized in the cytoplasm; High confidence in function and specificity. | 0.792 |
| dppA1 | CAZ95249.1 | ZOBELLIA_1190 | ZOBELLIA_1192 | Dipeptidyl-peptidase IV, family S9; Dipeptidyl-peptidase IV releases an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Belongs to the family S9 of the serine peptidases. The active site residues are in the order Ser, Asp, His in the sequence. The motif around the active site serine is G W S (Y/F) G G. DppA displays a two domain architecture, with a N-terminal eight-bladed beta-propeller and a C-terminal S9 peptidase domain. Features a signal peptide cleaved between the residues 20 and 21. Localiz [...] | Protein that is probably a kinase; belongs to the GHMP (galacto, homoserine, mevalonate, phosphomevalonate) kinase family; Localized in the cytoplasm; Family membership. | 0.544 |
| dppA1 | mvaA | ZOBELLIA_1190 | ZOBELLIA_1191 | Dipeptidyl-peptidase IV, family S9; Dipeptidyl-peptidase IV releases an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Belongs to the family S9 of the serine peptidases. The active site residues are in the order Ser, Asp, His in the sequence. The motif around the active site serine is G W S (Y/F) G G. DppA displays a two domain architecture, with a N-terminal eight-bladed beta-propeller and a C-terminal S9 peptidase domain. Features a signal peptide cleaved between the residues 20 and 21. Localiz [...] | 3-Hydroxy-3-methylglutaryl-coenzyme A reductase catalyzes the reversible conversion of mevalonate into 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA), using coenzyme A and NAD(P) as cofactors. In Archeae, NADP-depedent HMG-CoA reductase is involved in the biosynthesis of the isoprenoids side chains of lipids. Some bacteria, such as Pseudomonas mevalonii, use an NAD-dependent HMG-CoA reductase to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. These bacteria can use mevalonate as sole carbon source. Localized in the cytoplasm; High confidence in function and specificity. | 0.551 |
| fadA | mvaA | ZOBELLIA_98 | ZOBELLIA_1191 | 3-Ketoacyl-CoA thiolase, also known as acetyl-CoA C-acyltransferase, has a broad chain-length specificity for its substrates and is involved in degradative pathways such as fatty acid beta-oxidation. It catalyzes the reaction: Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the thiolase-like superfamily. Thiolase family. | 3-Hydroxy-3-methylglutaryl-coenzyme A reductase catalyzes the reversible conversion of mevalonate into 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA), using coenzyme A and NAD(P) as cofactors. In Archeae, NADP-depedent HMG-CoA reductase is involved in the biosynthesis of the isoprenoids side chains of lipids. Some bacteria, such as Pseudomonas mevalonii, use an NAD-dependent HMG-CoA reductase to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. These bacteria can use mevalonate as sole carbon source. Localized in the cytoplasm; High confidence in function and specificity. | 0.912 |
| fadA | mvaB | ZOBELLIA_98 | ZOBELLIA_2854 | 3-Ketoacyl-CoA thiolase, also known as acetyl-CoA C-acyltransferase, has a broad chain-length specificity for its substrates and is involved in degradative pathways such as fatty acid beta-oxidation. It catalyzes the reaction: Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the thiolase-like superfamily. Thiolase family. | Hydroxymethylglutaryl-CoA lyase is involved in mevalonate catabolism. It cleaves the (S)-3-hydroxy-3-methylglutaryl-CoA to acetyl-CoA and acetoacetate; Localized in the cytoplasm; High confidence in function and specificity. | 0.924 |
| fadA | thlA | ZOBELLIA_98 | ZOBELLIA_465 | 3-Ketoacyl-CoA thiolase, also known as acetyl-CoA C-acyltransferase, has a broad chain-length specificity for its substrates and is involved in degradative pathways such as fatty acid beta-oxidation. It catalyzes the reaction: Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the thiolase-like superfamily. Thiolase family. | Acetyl-CoA acetyltransferase is specific for the thiolysis of acetoacetyl-CoA and involved in biosynthetic pathways such as poly beta-hydroxybutyrate synthesis or mevalonate biogenesis. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the thiolase-like superfamily. Thiolase family. | 0.916 |
| kmoA | CAZ94094.1 | ZOBELLIA_717 | ZOBELLIA_21 | Kynurenine 3-monooxygenase; Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid; Belongs to the aromatic-ring hydroxylase family. KMO subfamily. | Members of the Nudix hydrolase family catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. They require Mg2+ or Mn2+, for their activity. Substrates include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. In general, the role of the nudix hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & \house- cleaning\ enzymes; Belong to the Nudix hydrolase superfamily; Localized in the cytoplasm; Family membership. | 0.579 |
| kmoA | mvaA | ZOBELLIA_717 | ZOBELLIA_1191 | Kynurenine 3-monooxygenase; Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid; Belongs to the aromatic-ring hydroxylase family. KMO subfamily. | 3-Hydroxy-3-methylglutaryl-coenzyme A reductase catalyzes the reversible conversion of mevalonate into 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA), using coenzyme A and NAD(P) as cofactors. In Archeae, NADP-depedent HMG-CoA reductase is involved in the biosynthesis of the isoprenoids side chains of lipids. Some bacteria, such as Pseudomonas mevalonii, use an NAD-dependent HMG-CoA reductase to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. These bacteria can use mevalonate as sole carbon source. Localized in the cytoplasm; High confidence in function and specificity. | 0.737 |
| menA | mvaA | ZOBELLIA_4025 | ZOBELLIA_1191 | 1,4-dihydroxy-2-naphthoate octaprenyltransferase; Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK); Belongs to the MenA family. Type 1 subfamily. | 3-Hydroxy-3-methylglutaryl-coenzyme A reductase catalyzes the reversible conversion of mevalonate into 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA), using coenzyme A and NAD(P) as cofactors. In Archeae, NADP-depedent HMG-CoA reductase is involved in the biosynthesis of the isoprenoids side chains of lipids. Some bacteria, such as Pseudomonas mevalonii, use an NAD-dependent HMG-CoA reductase to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. These bacteria can use mevalonate as sole carbon source. Localized in the cytoplasm; High confidence in function and specificity. | 0.869 |
| mvaA | CAZ94094.1 | ZOBELLIA_1191 | ZOBELLIA_21 | 3-Hydroxy-3-methylglutaryl-coenzyme A reductase catalyzes the reversible conversion of mevalonate into 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA), using coenzyme A and NAD(P) as cofactors. In Archeae, NADP-depedent HMG-CoA reductase is involved in the biosynthesis of the isoprenoids side chains of lipids. Some bacteria, such as Pseudomonas mevalonii, use an NAD-dependent HMG-CoA reductase to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. These bacteria can use mevalonate as sole carbon source. Localized in the cytoplasm; High confidence in function and specificity. | Members of the Nudix hydrolase family catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. They require Mg2+ or Mn2+, for their activity. Substrates include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. In general, the role of the nudix hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & \house- cleaning\ enzymes; Belong to the Nudix hydrolase superfamily; Localized in the cytoplasm; Family membership. | 0.448 |
| mvaA | CAZ95249.1 | ZOBELLIA_1191 | ZOBELLIA_1192 | 3-Hydroxy-3-methylglutaryl-coenzyme A reductase catalyzes the reversible conversion of mevalonate into 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA), using coenzyme A and NAD(P) as cofactors. In Archeae, NADP-depedent HMG-CoA reductase is involved in the biosynthesis of the isoprenoids side chains of lipids. Some bacteria, such as Pseudomonas mevalonii, use an NAD-dependent HMG-CoA reductase to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. These bacteria can use mevalonate as sole carbon source. Localized in the cytoplasm; High confidence in function and specificity. | Protein that is probably a kinase; belongs to the GHMP (galacto, homoserine, mevalonate, phosphomevalonate) kinase family; Localized in the cytoplasm; Family membership. | 0.964 |
| mvaA | dppA1 | ZOBELLIA_1191 | ZOBELLIA_1190 | 3-Hydroxy-3-methylglutaryl-coenzyme A reductase catalyzes the reversible conversion of mevalonate into 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA), using coenzyme A and NAD(P) as cofactors. In Archeae, NADP-depedent HMG-CoA reductase is involved in the biosynthesis of the isoprenoids side chains of lipids. Some bacteria, such as Pseudomonas mevalonii, use an NAD-dependent HMG-CoA reductase to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. These bacteria can use mevalonate as sole carbon source. Localized in the cytoplasm; High confidence in function and specificity. | Dipeptidyl-peptidase IV, family S9; Dipeptidyl-peptidase IV releases an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Belongs to the family S9 of the serine peptidases. The active site residues are in the order Ser, Asp, His in the sequence. The motif around the active site serine is G W S (Y/F) G G. DppA displays a two domain architecture, with a N-terminal eight-bladed beta-propeller and a C-terminal S9 peptidase domain. Features a signal peptide cleaved between the residues 20 and 21. Localiz [...] | 0.551 |
| mvaA | fadA | ZOBELLIA_1191 | ZOBELLIA_98 | 3-Hydroxy-3-methylglutaryl-coenzyme A reductase catalyzes the reversible conversion of mevalonate into 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA), using coenzyme A and NAD(P) as cofactors. In Archeae, NADP-depedent HMG-CoA reductase is involved in the biosynthesis of the isoprenoids side chains of lipids. Some bacteria, such as Pseudomonas mevalonii, use an NAD-dependent HMG-CoA reductase to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. These bacteria can use mevalonate as sole carbon source. Localized in the cytoplasm; High confidence in function and specificity. | 3-Ketoacyl-CoA thiolase, also known as acetyl-CoA C-acyltransferase, has a broad chain-length specificity for its substrates and is involved in degradative pathways such as fatty acid beta-oxidation. It catalyzes the reaction: Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the thiolase-like superfamily. Thiolase family. | 0.912 |
| mvaA | kmoA | ZOBELLIA_1191 | ZOBELLIA_717 | 3-Hydroxy-3-methylglutaryl-coenzyme A reductase catalyzes the reversible conversion of mevalonate into 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA), using coenzyme A and NAD(P) as cofactors. In Archeae, NADP-depedent HMG-CoA reductase is involved in the biosynthesis of the isoprenoids side chains of lipids. Some bacteria, such as Pseudomonas mevalonii, use an NAD-dependent HMG-CoA reductase to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. These bacteria can use mevalonate as sole carbon source. Localized in the cytoplasm; High confidence in function and specificity. | Kynurenine 3-monooxygenase; Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid; Belongs to the aromatic-ring hydroxylase family. KMO subfamily. | 0.737 |
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