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 |
| azo1743 | azo1744 | azo1743 | azo1744 | Conserved hypothetical protein. Homology to ebA6983 of Azoarcus sp. EbN1 of 50% (gnl|keqq|eba:ebA6983(KEGG)). Pfam: N-formylglutamate amidohydrolase. Formylglutamate amidohydrolase (FGase) catalyses the terminal reaction in the five-step pathway for histidine utilisation in Pseudomonas putida. By this action, N-formyl-L-glutamate (FG) is hydrolysed to produce L-glutamate plus formate. no signal peptide. no TMHs. | Glutamate-cysteine ligase; Hypothetical protein,32% identity (49% similarity) to SwissProt;O27977 Has PF04107;Glutamate-cysteine ligase family 2(GCS2);(IPR006336)Also known as gamma-glutamylcysteine synthetase and gamma-ECS. This enzyme catalyses the first and rate limiting step in de novo glutathione biosynthesis. Members of this family are found in archaea, bacteria and plants. May and Leaver [1] discuss the possible evolutionary origins of glutamate-cysteine ligase enzymes in different organisms and suggest that it evolved independently in different eukaryotes,from an ancestral bact [...] | 0.950 |
| azo1743 | azo1746 | azo1743 | azo1746 | Conserved hypothetical protein. Homology to ebA6983 of Azoarcus sp. EbN1 of 50% (gnl|keqq|eba:ebA6983(KEGG)). Pfam: N-formylglutamate amidohydrolase. Formylglutamate amidohydrolase (FGase) catalyses the terminal reaction in the five-step pathway for histidine utilisation in Pseudomonas putida. By this action, N-formyl-L-glutamate (FG) is hydrolysed to produce L-glutamate plus formate. no signal peptide. no TMHs. | Conserved hypothetical protein. Homology to TdenA01000334 of Thiobacillus denitrificans of 67% (gi|52008038|ref|ZP_00335415.1|(NBCI ENTREZ)). No domains present. No signal peptide. No TMHs. | 0.924 |
| azo1743 | azo1747 | azo1743 | azo1747 | Conserved hypothetical protein. Homology to ebA6983 of Azoarcus sp. EbN1 of 50% (gnl|keqq|eba:ebA6983(KEGG)). Pfam: N-formylglutamate amidohydrolase. Formylglutamate amidohydrolase (FGase) catalyses the terminal reaction in the five-step pathway for histidine utilisation in Pseudomonas putida. By this action, N-formyl-L-glutamate (FG) is hydrolysed to produce L-glutamate plus formate. no signal peptide. no TMHs. | Hypothetical secreted protein. No homology to the data bank. No TMHs Signal Peptide present. Has PS50914; BON;The BON (bacterial OsmY and nodulation) domain is found in the bacterial osmotic-shock-resistance protein OsmY, a family of haemolysins, a group of nodulation specificity proteins and secretory channels, and several hypothetical proteins. It is typically about 60 residues long and has an alpha/beta predicted fold. There is a conserved glycine residue and several hydrophobic regions. | 0.678 |
| azo1743 | azo1748 | azo1743 | azo1748 | Conserved hypothetical protein. Homology to ebA6983 of Azoarcus sp. EbN1 of 50% (gnl|keqq|eba:ebA6983(KEGG)). Pfam: N-formylglutamate amidohydrolase. Formylglutamate amidohydrolase (FGase) catalyses the terminal reaction in the five-step pathway for histidine utilisation in Pseudomonas putida. By this action, N-formyl-L-glutamate (FG) is hydrolysed to produce L-glutamate plus formate. no signal peptide. no TMHs. | Hypothetical protein yhcV. TREMBL:Q92V69:54%identity, 76% similarity. TREMBL:Q81UY6 Pfam:CBS domain, Anticodon binding domain. TIGRFAM: KpsF/GutQ family proteins. No signal peptide or transmembrane helix reported. CBS domains are small intracellular modules of unknown function. They are mostly found in 2 or four copies within a protein. Pairs of CBS domains dimerise to form a stable globular domain. Two CBS domains are found in inosine-monophosphate dehydrogenase from all species, however the CBS domains are not needed for activity. CBS domains are found attached to a wide range of oth [...] | 0.449 |
| azo1743 | rimK | azo1743 | azo1745 | Conserved hypothetical protein. Homology to ebA6983 of Azoarcus sp. EbN1 of 50% (gnl|keqq|eba:ebA6983(KEGG)). Pfam: N-formylglutamate amidohydrolase. Formylglutamate amidohydrolase (FGase) catalyses the terminal reaction in the five-step pathway for histidine utilisation in Pseudomonas putida. By this action, N-formyl-L-glutamate (FG) is hydrolysed to produce L-glutamate plus formate. no signal peptide. no TMHs. | Glutathione synthase/Ribosomal protein S6 modification enzyme (glutaminyl transferase) rimK_fam: S6 modification enzyme RimK; Specificity unclear. | 0.951 |
| azo1744 | azo1743 | azo1744 | azo1743 | Glutamate-cysteine ligase; Hypothetical protein,32% identity (49% similarity) to SwissProt;O27977 Has PF04107;Glutamate-cysteine ligase family 2(GCS2);(IPR006336)Also known as gamma-glutamylcysteine synthetase and gamma-ECS. This enzyme catalyses the first and rate limiting step in de novo glutathione biosynthesis. Members of this family are found in archaea, bacteria and plants. May and Leaver [1] discuss the possible evolutionary origins of glutamate-cysteine ligase enzymes in different organisms and suggest that it evolved independently in different eukaryotes,from an ancestral bact [...] | Conserved hypothetical protein. Homology to ebA6983 of Azoarcus sp. EbN1 of 50% (gnl|keqq|eba:ebA6983(KEGG)). Pfam: N-formylglutamate amidohydrolase. Formylglutamate amidohydrolase (FGase) catalyses the terminal reaction in the five-step pathway for histidine utilisation in Pseudomonas putida. By this action, N-formyl-L-glutamate (FG) is hydrolysed to produce L-glutamate plus formate. no signal peptide. no TMHs. | 0.950 |
| azo1744 | azo1746 | azo1744 | azo1746 | Glutamate-cysteine ligase; Hypothetical protein,32% identity (49% similarity) to SwissProt;O27977 Has PF04107;Glutamate-cysteine ligase family 2(GCS2);(IPR006336)Also known as gamma-glutamylcysteine synthetase and gamma-ECS. This enzyme catalyses the first and rate limiting step in de novo glutathione biosynthesis. Members of this family are found in archaea, bacteria and plants. May and Leaver [1] discuss the possible evolutionary origins of glutamate-cysteine ligase enzymes in different organisms and suggest that it evolved independently in different eukaryotes,from an ancestral bact [...] | Conserved hypothetical protein. Homology to TdenA01000334 of Thiobacillus denitrificans of 67% (gi|52008038|ref|ZP_00335415.1|(NBCI ENTREZ)). No domains present. No signal peptide. No TMHs. | 0.920 |
| azo1744 | azo1747 | azo1744 | azo1747 | Glutamate-cysteine ligase; Hypothetical protein,32% identity (49% similarity) to SwissProt;O27977 Has PF04107;Glutamate-cysteine ligase family 2(GCS2);(IPR006336)Also known as gamma-glutamylcysteine synthetase and gamma-ECS. This enzyme catalyses the first and rate limiting step in de novo glutathione biosynthesis. Members of this family are found in archaea, bacteria and plants. May and Leaver [1] discuss the possible evolutionary origins of glutamate-cysteine ligase enzymes in different organisms and suggest that it evolved independently in different eukaryotes,from an ancestral bact [...] | Hypothetical secreted protein. No homology to the data bank. No TMHs Signal Peptide present. Has PS50914; BON;The BON (bacterial OsmY and nodulation) domain is found in the bacterial osmotic-shock-resistance protein OsmY, a family of haemolysins, a group of nodulation specificity proteins and secretory channels, and several hypothetical proteins. It is typically about 60 residues long and has an alpha/beta predicted fold. There is a conserved glycine residue and several hydrophobic regions. | 0.707 |
| azo1744 | azo1748 | azo1744 | azo1748 | Glutamate-cysteine ligase; Hypothetical protein,32% identity (49% similarity) to SwissProt;O27977 Has PF04107;Glutamate-cysteine ligase family 2(GCS2);(IPR006336)Also known as gamma-glutamylcysteine synthetase and gamma-ECS. This enzyme catalyses the first and rate limiting step in de novo glutathione biosynthesis. Members of this family are found in archaea, bacteria and plants. May and Leaver [1] discuss the possible evolutionary origins of glutamate-cysteine ligase enzymes in different organisms and suggest that it evolved independently in different eukaryotes,from an ancestral bact [...] | Hypothetical protein yhcV. TREMBL:Q92V69:54%identity, 76% similarity. TREMBL:Q81UY6 Pfam:CBS domain, Anticodon binding domain. TIGRFAM: KpsF/GutQ family proteins. No signal peptide or transmembrane helix reported. CBS domains are small intracellular modules of unknown function. They are mostly found in 2 or four copies within a protein. Pairs of CBS domains dimerise to form a stable globular domain. Two CBS domains are found in inosine-monophosphate dehydrogenase from all species, however the CBS domains are not needed for activity. CBS domains are found attached to a wide range of oth [...] | 0.449 |
| azo1744 | rimK | azo1744 | azo1745 | Glutamate-cysteine ligase; Hypothetical protein,32% identity (49% similarity) to SwissProt;O27977 Has PF04107;Glutamate-cysteine ligase family 2(GCS2);(IPR006336)Also known as gamma-glutamylcysteine synthetase and gamma-ECS. This enzyme catalyses the first and rate limiting step in de novo glutathione biosynthesis. Members of this family are found in archaea, bacteria and plants. May and Leaver [1] discuss the possible evolutionary origins of glutamate-cysteine ligase enzymes in different organisms and suggest that it evolved independently in different eukaryotes,from an ancestral bact [...] | Glutathione synthase/Ribosomal protein S6 modification enzyme (glutaminyl transferase) rimK_fam: S6 modification enzyme RimK; Specificity unclear. | 0.962 |
| azo1746 | azo1743 | azo1746 | azo1743 | Conserved hypothetical protein. Homology to TdenA01000334 of Thiobacillus denitrificans of 67% (gi|52008038|ref|ZP_00335415.1|(NBCI ENTREZ)). No domains present. No signal peptide. No TMHs. | Conserved hypothetical protein. Homology to ebA6983 of Azoarcus sp. EbN1 of 50% (gnl|keqq|eba:ebA6983(KEGG)). Pfam: N-formylglutamate amidohydrolase. Formylglutamate amidohydrolase (FGase) catalyses the terminal reaction in the five-step pathway for histidine utilisation in Pseudomonas putida. By this action, N-formyl-L-glutamate (FG) is hydrolysed to produce L-glutamate plus formate. no signal peptide. no TMHs. | 0.924 |
| azo1746 | azo1744 | azo1746 | azo1744 | Conserved hypothetical protein. Homology to TdenA01000334 of Thiobacillus denitrificans of 67% (gi|52008038|ref|ZP_00335415.1|(NBCI ENTREZ)). No domains present. No signal peptide. No TMHs. | Glutamate-cysteine ligase; Hypothetical protein,32% identity (49% similarity) to SwissProt;O27977 Has PF04107;Glutamate-cysteine ligase family 2(GCS2);(IPR006336)Also known as gamma-glutamylcysteine synthetase and gamma-ECS. This enzyme catalyses the first and rate limiting step in de novo glutathione biosynthesis. Members of this family are found in archaea, bacteria and plants. May and Leaver [1] discuss the possible evolutionary origins of glutamate-cysteine ligase enzymes in different organisms and suggest that it evolved independently in different eukaryotes,from an ancestral bact [...] | 0.920 |
| azo1746 | azo1747 | azo1746 | azo1747 | Conserved hypothetical protein. Homology to TdenA01000334 of Thiobacillus denitrificans of 67% (gi|52008038|ref|ZP_00335415.1|(NBCI ENTREZ)). No domains present. No signal peptide. No TMHs. | Hypothetical secreted protein. No homology to the data bank. No TMHs Signal Peptide present. Has PS50914; BON;The BON (bacterial OsmY and nodulation) domain is found in the bacterial osmotic-shock-resistance protein OsmY, a family of haemolysins, a group of nodulation specificity proteins and secretory channels, and several hypothetical proteins. It is typically about 60 residues long and has an alpha/beta predicted fold. There is a conserved glycine residue and several hydrophobic regions. | 0.813 |
| azo1746 | azo1748 | azo1746 | azo1748 | Conserved hypothetical protein. Homology to TdenA01000334 of Thiobacillus denitrificans of 67% (gi|52008038|ref|ZP_00335415.1|(NBCI ENTREZ)). No domains present. No signal peptide. No TMHs. | Hypothetical protein yhcV. TREMBL:Q92V69:54%identity, 76% similarity. TREMBL:Q81UY6 Pfam:CBS domain, Anticodon binding domain. TIGRFAM: KpsF/GutQ family proteins. No signal peptide or transmembrane helix reported. CBS domains are small intracellular modules of unknown function. They are mostly found in 2 or four copies within a protein. Pairs of CBS domains dimerise to form a stable globular domain. Two CBS domains are found in inosine-monophosphate dehydrogenase from all species, however the CBS domains are not needed for activity. CBS domains are found attached to a wide range of oth [...] | 0.535 |
| azo1746 | flgC | azo1746 | azo2739 | Conserved hypothetical protein. Homology to TdenA01000334 of Thiobacillus denitrificans of 67% (gi|52008038|ref|ZP_00335415.1|(NBCI ENTREZ)). No domains present. No signal peptide. No TMHs. | Flagellar basal-body rod protein flgC. The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity. | 0.612 |
| azo1746 | rimK | azo1746 | azo1745 | Conserved hypothetical protein. Homology to TdenA01000334 of Thiobacillus denitrificans of 67% (gi|52008038|ref|ZP_00335415.1|(NBCI ENTREZ)). No domains present. No signal peptide. No TMHs. | Glutathione synthase/Ribosomal protein S6 modification enzyme (glutaminyl transferase) rimK_fam: S6 modification enzyme RimK; Specificity unclear. | 0.921 |
| azo1747 | azo1743 | azo1747 | azo1743 | Hypothetical secreted protein. No homology to the data bank. No TMHs Signal Peptide present. Has PS50914; BON;The BON (bacterial OsmY and nodulation) domain is found in the bacterial osmotic-shock-resistance protein OsmY, a family of haemolysins, a group of nodulation specificity proteins and secretory channels, and several hypothetical proteins. It is typically about 60 residues long and has an alpha/beta predicted fold. There is a conserved glycine residue and several hydrophobic regions. | Conserved hypothetical protein. Homology to ebA6983 of Azoarcus sp. EbN1 of 50% (gnl|keqq|eba:ebA6983(KEGG)). Pfam: N-formylglutamate amidohydrolase. Formylglutamate amidohydrolase (FGase) catalyses the terminal reaction in the five-step pathway for histidine utilisation in Pseudomonas putida. By this action, N-formyl-L-glutamate (FG) is hydrolysed to produce L-glutamate plus formate. no signal peptide. no TMHs. | 0.678 |
| azo1747 | azo1744 | azo1747 | azo1744 | Hypothetical secreted protein. No homology to the data bank. No TMHs Signal Peptide present. Has PS50914; BON;The BON (bacterial OsmY and nodulation) domain is found in the bacterial osmotic-shock-resistance protein OsmY, a family of haemolysins, a group of nodulation specificity proteins and secretory channels, and several hypothetical proteins. It is typically about 60 residues long and has an alpha/beta predicted fold. There is a conserved glycine residue and several hydrophobic regions. | Glutamate-cysteine ligase; Hypothetical protein,32% identity (49% similarity) to SwissProt;O27977 Has PF04107;Glutamate-cysteine ligase family 2(GCS2);(IPR006336)Also known as gamma-glutamylcysteine synthetase and gamma-ECS. This enzyme catalyses the first and rate limiting step in de novo glutathione biosynthesis. Members of this family are found in archaea, bacteria and plants. May and Leaver [1] discuss the possible evolutionary origins of glutamate-cysteine ligase enzymes in different organisms and suggest that it evolved independently in different eukaryotes,from an ancestral bact [...] | 0.707 |
| azo1747 | azo1746 | azo1747 | azo1746 | Hypothetical secreted protein. No homology to the data bank. No TMHs Signal Peptide present. Has PS50914; BON;The BON (bacterial OsmY and nodulation) domain is found in the bacterial osmotic-shock-resistance protein OsmY, a family of haemolysins, a group of nodulation specificity proteins and secretory channels, and several hypothetical proteins. It is typically about 60 residues long and has an alpha/beta predicted fold. There is a conserved glycine residue and several hydrophobic regions. | Conserved hypothetical protein. Homology to TdenA01000334 of Thiobacillus denitrificans of 67% (gi|52008038|ref|ZP_00335415.1|(NBCI ENTREZ)). No domains present. No signal peptide. No TMHs. | 0.813 |
| azo1747 | azo1748 | azo1747 | azo1748 | Hypothetical secreted protein. No homology to the data bank. No TMHs Signal Peptide present. Has PS50914; BON;The BON (bacterial OsmY and nodulation) domain is found in the bacterial osmotic-shock-resistance protein OsmY, a family of haemolysins, a group of nodulation specificity proteins and secretory channels, and several hypothetical proteins. It is typically about 60 residues long and has an alpha/beta predicted fold. There is a conserved glycine residue and several hydrophobic regions. | Hypothetical protein yhcV. TREMBL:Q92V69:54%identity, 76% similarity. TREMBL:Q81UY6 Pfam:CBS domain, Anticodon binding domain. TIGRFAM: KpsF/GutQ family proteins. No signal peptide or transmembrane helix reported. CBS domains are small intracellular modules of unknown function. They are mostly found in 2 or four copies within a protein. Pairs of CBS domains dimerise to form a stable globular domain. Two CBS domains are found in inosine-monophosphate dehydrogenase from all species, however the CBS domains are not needed for activity. CBS domains are found attached to a wide range of oth [...] | 0.649 |
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