| 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. | 0.923 |
| 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. | 0.950 |
| 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. | 0.702 |
| 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 | 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. | 0.497 |
| azo1744 | gltB | azo1744 | azo3642 | 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 [...] | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | 0.888 |
| azo1744 | gshB | azo1744 | azo3755 | 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 synthetase (GSH synthetase) (GSH-S) (GSHase). InterPro: Prokaryotic glutathione synthetase ATP-binding domain; High confidence in function and specificity; Belongs to the prokaryotic GSH synthase family. | 0.691 |
| azo1744 | metZ | azo1744 | azo1054 | 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 [...] | Cys/Met metabolism pyridoxal-phosphate-dependent enzyme; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide. | 0.426 |
| azo1744 | putA | azo1744 | azo3753 | 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 [...] | Probable bifunctional PutA protein; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | 0.754 |
| 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. | 0.966 |
| 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. | 0.923 |
| 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. | 0.812 |
| 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 | 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 |
