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 | 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 | azo3312 | azo1744 | azo3312 | 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 secreted protein. Homology to PP2729 of P.putida of 36% (tremble:Q88JC0). No domains predicted. Signal peptide present. NO TMH reported present; Conserved hypothetical protein. | 0.419 |
| azo1744 | ggt | azo1744 | azo1475 | 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 [...] | Ggt protein; Gamma-glutamyltranspeptidase catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification. Similar to trembl|Q88H30 (43%)and to trembl|Q8UJH0 (36%). TIGRfam (TIGR00066): Gamma-glutamyltranspeptidase Pfam (PF01019): Gamma-glutamyltranspeptidase SignalP reporting Signal peptide; Specificity unclear. | 0.484 |
| 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 | 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 | rimK | azo1747 | azo1745 | 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. | Glutathione synthase/Ribosomal protein S6 modification enzyme (glutaminyl transferase) rimK_fam: S6 modification enzyme RimK; Specificity unclear. | 0.641 |
| azo3312 | azo1744 | azo3312 | azo1744 | Conserved hypothetical secreted protein. Homology to PP2729 of P.putida of 36% (tremble:Q88JC0). No domains predicted. Signal peptide present. NO TMH reported present; Conserved hypothetical protein. | 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 [...] | 0.419 |
| azo3312 | rimK | azo3312 | azo1745 | Conserved hypothetical secreted protein. Homology to PP2729 of P.putida of 36% (tremble:Q88JC0). No domains predicted. Signal peptide present. NO TMH reported present; Conserved hypothetical protein. | Glutathione synthase/Ribosomal protein S6 modification enzyme (glutaminyl transferase) rimK_fam: S6 modification enzyme RimK; Specificity unclear. | 0.528 |
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