node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
PA1024 | lipA | PA1024 | PA2862 | 2-Nitropropane Dioxygenase; Catalyzes the NADH-dependent reduction of a broad spectrum of quinone substrates, generating the corresponding hydroquinones. Highly prefers NADH to NADPH as a reducing substrate. Also displays a small NADH oxidase activity. Does not exhibit nitronate monooxygenase activity; is inactive against propionate 3-nitronate, 3- nitropropionate, nitroethane, 1-nitropropane, 2-nitropropane, and the anionic forms ethylnitronate, propyl-1-nitronate, and propyl-2- nitronate. Has no azoreductase activity since it is not able to reduce the azo dye methyl red with NADH. Ma [...] | Lactonizing lipase precursor; Catalyzes the hydrolysis of triacylglycerol. It also exhibits some esterase activity with p-nitrophenyl acetate and Tween 80 as substrates, however the lipase activity is approximately eight times the esterase activity. It shows a marked specificity for the 1,3-oleyl residues of triolein. | 0.605 |
PA1024 | lipC | PA1024 | PA4813 | 2-Nitropropane Dioxygenase; Catalyzes the NADH-dependent reduction of a broad spectrum of quinone substrates, generating the corresponding hydroquinones. Highly prefers NADH to NADPH as a reducing substrate. Also displays a small NADH oxidase activity. Does not exhibit nitronate monooxygenase activity; is inactive against propionate 3-nitronate, 3- nitropropionate, nitroethane, 1-nitropropane, 2-nitropropane, and the anionic forms ethylnitronate, propyl-1-nitronate, and propyl-2- nitronate. Has no azoreductase activity since it is not able to reduce the azo dye methyl red with NADH. Ma [...] | Lipase LipC; Product name confidence: Class 1 (Function experimentally demonstrated in P. aeruginosa). | 0.568 |
PA3342 | lipA | PA3342 | PA2862 | Hypothetical protein; Product name confidence: Class 4 (Homologs of previously reported genes of unknown function, or no similarity to any previously reported sequences). | Lactonizing lipase precursor; Catalyzes the hydrolysis of triacylglycerol. It also exhibits some esterase activity with p-nitrophenyl acetate and Tween 80 as substrates, however the lipase activity is approximately eight times the esterase activity. It shows a marked specificity for the 1,3-oleyl residues of triolein. | 0.565 |
PA3342 | lipC | PA3342 | PA4813 | Hypothetical protein; Product name confidence: Class 4 (Homologs of previously reported genes of unknown function, or no similarity to any previously reported sequences). | Lipase LipC; Product name confidence: Class 1 (Function experimentally demonstrated in P. aeruginosa). | 0.551 |
PA3342 | lipH | PA3342 | PA2863 | Hypothetical protein; Product name confidence: Class 4 (Homologs of previously reported genes of unknown function, or no similarity to any previously reported sequences). | Lipase modulator protein; May be involved in the folding of the extracellular lipase during its passage through the periplasm; Belongs to the lipase chaperone family. | 0.693 |
dgkA | lipA | PA3603 | PA2862 | Diacylglycerol kinase; Recycling of diacylglycerol produced during the turnover of membrane phospholipid. | Lactonizing lipase precursor; Catalyzes the hydrolysis of triacylglycerol. It also exhibits some esterase activity with p-nitrophenyl acetate and Tween 80 as substrates, however the lipase activity is approximately eight times the esterase activity. It shows a marked specificity for the 1,3-oleyl residues of triolein. | 0.900 |
dgkA | lipC | PA3603 | PA4813 | Diacylglycerol kinase; Recycling of diacylglycerol produced during the turnover of membrane phospholipid. | Lipase LipC; Product name confidence: Class 1 (Function experimentally demonstrated in P. aeruginosa). | 0.900 |
estA | lasB | PA5112 | PA3724 | Esterase EstA; Esterase whose enzymatic activity is required for rhamnolipid production, all kinds of cell motility (swimming, swarming, and twitching), and biofilm formation; the exact role of EstA in these processes is unclear. In vitro, has pronounced esterase activities towards p-nitrophenyl esters of short acyl chain length (C4-C6) and Tween detergents. Also shows relatively high activity towards beta- naphthyl butyrate, whereas its activities towards triacylglycerols and acyls-CoA are negligible. | Elastase LasB; Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase. Autocatalyses processing of its pro-peptide. Processes the pro-peptide of pro-chitin-binding protein (cbpD). Involved in the pathogenesis of P.aeruginosa infections. | 0.412 |
estA | lipA | PA5112 | PA2862 | Esterase EstA; Esterase whose enzymatic activity is required for rhamnolipid production, all kinds of cell motility (swimming, swarming, and twitching), and biofilm formation; the exact role of EstA in these processes is unclear. In vitro, has pronounced esterase activities towards p-nitrophenyl esters of short acyl chain length (C4-C6) and Tween detergents. Also shows relatively high activity towards beta- naphthyl butyrate, whereas its activities towards triacylglycerols and acyls-CoA are negligible. | Lactonizing lipase precursor; Catalyzes the hydrolysis of triacylglycerol. It also exhibits some esterase activity with p-nitrophenyl acetate and Tween 80 as substrates, however the lipase activity is approximately eight times the esterase activity. It shows a marked specificity for the 1,3-oleyl residues of triolein. | 0.785 |
estA | lipC | PA5112 | PA4813 | Esterase EstA; Esterase whose enzymatic activity is required for rhamnolipid production, all kinds of cell motility (swimming, swarming, and twitching), and biofilm formation; the exact role of EstA in these processes is unclear. In vitro, has pronounced esterase activities towards p-nitrophenyl esters of short acyl chain length (C4-C6) and Tween detergents. Also shows relatively high activity towards beta- naphthyl butyrate, whereas its activities towards triacylglycerols and acyls-CoA are negligible. | Lipase LipC; Product name confidence: Class 1 (Function experimentally demonstrated in P. aeruginosa). | 0.716 |
fadD1 | fadD2 | PA3299 | PA3300 | long-chain-fatty-acid--CoA ligase; Product name confidence: Class 2 (High similarity to functionally studied protein). | long-chain-fatty-acid--CoA ligase; Product name confidence: Class 2 (High similarity to functionally studied protein). | 0.947 |
fadD1 | lipA | PA3299 | PA2862 | long-chain-fatty-acid--CoA ligase; Product name confidence: Class 2 (High similarity to functionally studied protein). | Lactonizing lipase precursor; Catalyzes the hydrolysis of triacylglycerol. It also exhibits some esterase activity with p-nitrophenyl acetate and Tween 80 as substrates, however the lipase activity is approximately eight times the esterase activity. It shows a marked specificity for the 1,3-oleyl residues of triolein. | 0.801 |
fadD1 | lipC | PA3299 | PA4813 | long-chain-fatty-acid--CoA ligase; Product name confidence: Class 2 (High similarity to functionally studied protein). | Lipase LipC; Product name confidence: Class 1 (Function experimentally demonstrated in P. aeruginosa). | 0.800 |
fadD2 | fadD1 | PA3300 | PA3299 | long-chain-fatty-acid--CoA ligase; Product name confidence: Class 2 (High similarity to functionally studied protein). | long-chain-fatty-acid--CoA ligase; Product name confidence: Class 2 (High similarity to functionally studied protein). | 0.947 |
fadD2 | lipA | PA3300 | PA2862 | long-chain-fatty-acid--CoA ligase; Product name confidence: Class 2 (High similarity to functionally studied protein). | Lactonizing lipase precursor; Catalyzes the hydrolysis of triacylglycerol. It also exhibits some esterase activity with p-nitrophenyl acetate and Tween 80 as substrates, however the lipase activity is approximately eight times the esterase activity. It shows a marked specificity for the 1,3-oleyl residues of triolein. | 0.833 |
fadD2 | lipC | PA3300 | PA4813 | long-chain-fatty-acid--CoA ligase; Product name confidence: Class 2 (High similarity to functionally studied protein). | Lipase LipC; Product name confidence: Class 1 (Function experimentally demonstrated in P. aeruginosa). | 0.801 |
lasB | estA | PA3724 | PA5112 | Elastase LasB; Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase. Autocatalyses processing of its pro-peptide. Processes the pro-peptide of pro-chitin-binding protein (cbpD). Involved in the pathogenesis of P.aeruginosa infections. | Esterase EstA; Esterase whose enzymatic activity is required for rhamnolipid production, all kinds of cell motility (swimming, swarming, and twitching), and biofilm formation; the exact role of EstA in these processes is unclear. In vitro, has pronounced esterase activities towards p-nitrophenyl esters of short acyl chain length (C4-C6) and Tween detergents. Also shows relatively high activity towards beta- naphthyl butyrate, whereas its activities towards triacylglycerols and acyls-CoA are negligible. | 0.412 |
lasB | lipA | PA3724 | PA2862 | Elastase LasB; Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase. Autocatalyses processing of its pro-peptide. Processes the pro-peptide of pro-chitin-binding protein (cbpD). Involved in the pathogenesis of P.aeruginosa infections. | Lactonizing lipase precursor; Catalyzes the hydrolysis of triacylglycerol. It also exhibits some esterase activity with p-nitrophenyl acetate and Tween 80 as substrates, however the lipase activity is approximately eight times the esterase activity. It shows a marked specificity for the 1,3-oleyl residues of triolein. | 0.452 |
lasB | lipC | PA3724 | PA4813 | Elastase LasB; Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase. Autocatalyses processing of its pro-peptide. Processes the pro-peptide of pro-chitin-binding protein (cbpD). Involved in the pathogenesis of P.aeruginosa infections. | Lipase LipC; Product name confidence: Class 1 (Function experimentally demonstrated in P. aeruginosa). | 0.612 |
lipA | PA1024 | PA2862 | PA1024 | Lactonizing lipase precursor; Catalyzes the hydrolysis of triacylglycerol. It also exhibits some esterase activity with p-nitrophenyl acetate and Tween 80 as substrates, however the lipase activity is approximately eight times the esterase activity. It shows a marked specificity for the 1,3-oleyl residues of triolein. | 2-Nitropropane Dioxygenase; Catalyzes the NADH-dependent reduction of a broad spectrum of quinone substrates, generating the corresponding hydroquinones. Highly prefers NADH to NADPH as a reducing substrate. Also displays a small NADH oxidase activity. Does not exhibit nitronate monooxygenase activity; is inactive against propionate 3-nitronate, 3- nitropropionate, nitroethane, 1-nitropropane, 2-nitropropane, and the anionic forms ethylnitronate, propyl-1-nitronate, and propyl-2- nitronate. Has no azoreductase activity since it is not able to reduce the azo dye methyl red with NADH. Ma [...] | 0.605 |