node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
entH | fadM | b0597 | b0443 | Proofreading thioesterase in enterobactin biosynthesis; Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules. Displays esterase activity toward a wide range of substrates, including acyl-CoAs and aryl-CoAs | Long-chain acyl-coa thioesterase iii; Long-chain acyl-CoA thioesterase with a preference for 3,5- tetradecadienoyl-CoA. Could be involved in beta-oxidation of fatty acids | 0.609 |
entH | paaI | b0597 | b1396 | Proofreading thioesterase in enterobactin biosynthesis; Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules. Displays esterase activity toward a wide range of substrates, including acyl-CoAs and aryl-CoAs | Thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters. Hydrolyzes 3,4-dihydroxyphenylacetyl-CoA, 3- hydroxyphenylacetyl-CoA and 4-hydroxyphenylacetyl-CoA. Inactive towards 4-hydroxybenzoyl-CoA and 4-hydroxyphenacyl-CoA | 0.734 |
entH | tesB | b0597 | b0452 | Proofreading thioesterase in enterobactin biosynthesis; Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules. Displays esterase activity toward a wide range of substrates, including acyl-CoAs and aryl-CoAs | Acyl-coa thioesterase ii; Can hydrolyze a broad range of acyl-CoA thioesters. Its physiological function is not known | 0.607 |
entH | ybgC | b0597 | b0736 | Proofreading thioesterase in enterobactin biosynthesis; Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules. Displays esterase activity toward a wide range of substrates, including acyl-CoAs and aryl-CoAs | Acyl-coa thioester hydrolase; Thioesterase that appears to be involved in phospholipid metabolism. Some specific acyl-ACPs could be physiological substrates. Displays acyl-CoA thioesterase activity on malonyl-CoA in vitro, catalyzing the hydrolysis of the thioester bond | 0.759 |
entH | yciA | b0597 | b1253 | Proofreading thioesterase in enterobactin biosynthesis; Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules. Displays esterase activity toward a wide range of substrates, including acyl-CoAs and aryl-CoAs | Acyl-coa thioesterase ycia; Catalyzes the hydrolysis of the thioester bond in palmitoyl- CoA and malonyl-CoA | 0.781 |
fadM | entH | b0443 | b0597 | Long-chain acyl-coa thioesterase iii; Long-chain acyl-CoA thioesterase with a preference for 3,5- tetradecadienoyl-CoA. Could be involved in beta-oxidation of fatty acids | Proofreading thioesterase in enterobactin biosynthesis; Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules. Displays esterase activity toward a wide range of substrates, including acyl-CoAs and aryl-CoAs | 0.609 |
fadM | menI | b0443 | b1686 | Long-chain acyl-coa thioesterase iii; Long-chain acyl-CoA thioesterase with a preference for 3,5- tetradecadienoyl-CoA. Could be involved in beta-oxidation of fatty acids | 1,4-dihydroxy-2-naphthoyl-CoA hydrolase; Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA). Also shows significant activity toward a wide range of acyl-CoA thioesters, and minimal activity toward benzoyl-holoEntB | 0.841 |
fadM | paaI | b0443 | b1396 | Long-chain acyl-coa thioesterase iii; Long-chain acyl-CoA thioesterase with a preference for 3,5- tetradecadienoyl-CoA. Could be involved in beta-oxidation of fatty acids | Thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters. Hydrolyzes 3,4-dihydroxyphenylacetyl-CoA, 3- hydroxyphenylacetyl-CoA and 4-hydroxyphenylacetyl-CoA. Inactive towards 4-hydroxybenzoyl-CoA and 4-hydroxyphenacyl-CoA | 0.890 |
fadM | tesA | b0443 | b0494 | Long-chain acyl-coa thioesterase iii; Long-chain acyl-CoA thioesterase with a preference for 3,5- tetradecadienoyl-CoA. Could be involved in beta-oxidation of fatty acids | TesA is a multifunctional esterase that can act as a thioesterase, lysophospholipase and protease TesA functions as a thioesterase specific for fatty acyl thioesters of greater than ten carbons, with highest activity on palmitoyl-CoA, cis-vaccenyl-CoA and palmitoleoyl-CoA TesA also possesses an arylesterase activity towards short acyl-chain aromatic esters such as alpha-naphthyl acetate, alpha-naphthyl butyrate, benzyl acetate and phenyl acetate . Also able to hydrolyze short acyl-chain triacylglycerols such as triacetin and tributyrin, and p-nitrophenyl esters such as p-nitrophenyl he [...] | 0.828 |
fadM | tesB | b0443 | b0452 | Long-chain acyl-coa thioesterase iii; Long-chain acyl-CoA thioesterase with a preference for 3,5- tetradecadienoyl-CoA. Could be involved in beta-oxidation of fatty acids | Acyl-coa thioesterase ii; Can hydrolyze a broad range of acyl-CoA thioesters. Its physiological function is not known | 0.883 |
fadM | yciA | b0443 | b1253 | Long-chain acyl-coa thioesterase iii; Long-chain acyl-CoA thioesterase with a preference for 3,5- tetradecadienoyl-CoA. Could be involved in beta-oxidation of fatty acids | Acyl-coa thioesterase ycia; Catalyzes the hydrolysis of the thioester bond in palmitoyl- CoA and malonyl-CoA | 0.881 |
menI | fadM | b1686 | b0443 | 1,4-dihydroxy-2-naphthoyl-CoA hydrolase; Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA). Also shows significant activity toward a wide range of acyl-CoA thioesters, and minimal activity toward benzoyl-holoEntB | Long-chain acyl-coa thioesterase iii; Long-chain acyl-CoA thioesterase with a preference for 3,5- tetradecadienoyl-CoA. Could be involved in beta-oxidation of fatty acids | 0.841 |
menI | paaI | b1686 | b1396 | 1,4-dihydroxy-2-naphthoyl-CoA hydrolase; Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA). Also shows significant activity toward a wide range of acyl-CoA thioesters, and minimal activity toward benzoyl-holoEntB | Thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters. Hydrolyzes 3,4-dihydroxyphenylacetyl-CoA, 3- hydroxyphenylacetyl-CoA and 4-hydroxyphenylacetyl-CoA. Inactive towards 4-hydroxybenzoyl-CoA and 4-hydroxyphenacyl-CoA | 0.877 |
menI | tesA | b1686 | b0494 | 1,4-dihydroxy-2-naphthoyl-CoA hydrolase; Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA). Also shows significant activity toward a wide range of acyl-CoA thioesters, and minimal activity toward benzoyl-holoEntB | TesA is a multifunctional esterase that can act as a thioesterase, lysophospholipase and protease TesA functions as a thioesterase specific for fatty acyl thioesters of greater than ten carbons, with highest activity on palmitoyl-CoA, cis-vaccenyl-CoA and palmitoleoyl-CoA TesA also possesses an arylesterase activity towards short acyl-chain aromatic esters such as alpha-naphthyl acetate, alpha-naphthyl butyrate, benzyl acetate and phenyl acetate . Also able to hydrolyze short acyl-chain triacylglycerols such as triacetin and tributyrin, and p-nitrophenyl esters such as p-nitrophenyl he [...] | 0.731 |
menI | tesB | b1686 | b0452 | 1,4-dihydroxy-2-naphthoyl-CoA hydrolase; Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA). Also shows significant activity toward a wide range of acyl-CoA thioesters, and minimal activity toward benzoyl-holoEntB | Acyl-coa thioesterase ii; Can hydrolyze a broad range of acyl-CoA thioesters. Its physiological function is not known | 0.874 |
menI | ybgC | b1686 | b0736 | 1,4-dihydroxy-2-naphthoyl-CoA hydrolase; Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA). Also shows significant activity toward a wide range of acyl-CoA thioesters, and minimal activity toward benzoyl-holoEntB | Acyl-coa thioester hydrolase; Thioesterase that appears to be involved in phospholipid metabolism. Some specific acyl-ACPs could be physiological substrates. Displays acyl-CoA thioesterase activity on malonyl-CoA in vitro, catalyzing the hydrolysis of the thioester bond | 0.890 |
menI | yciA | b1686 | b1253 | 1,4-dihydroxy-2-naphthoyl-CoA hydrolase; Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA). Also shows significant activity toward a wide range of acyl-CoA thioesters, and minimal activity toward benzoyl-holoEntB | Acyl-coa thioesterase ycia; Catalyzes the hydrolysis of the thioester bond in palmitoyl- CoA and malonyl-CoA | 0.904 |
paaI | entH | b1396 | b0597 | Thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters. Hydrolyzes 3,4-dihydroxyphenylacetyl-CoA, 3- hydroxyphenylacetyl-CoA and 4-hydroxyphenylacetyl-CoA. Inactive towards 4-hydroxybenzoyl-CoA and 4-hydroxyphenacyl-CoA | Proofreading thioesterase in enterobactin biosynthesis; Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules. Displays esterase activity toward a wide range of substrates, including acyl-CoAs and aryl-CoAs | 0.734 |
paaI | fadM | b1396 | b0443 | Thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters. Hydrolyzes 3,4-dihydroxyphenylacetyl-CoA, 3- hydroxyphenylacetyl-CoA and 4-hydroxyphenylacetyl-CoA. Inactive towards 4-hydroxybenzoyl-CoA and 4-hydroxyphenacyl-CoA | Long-chain acyl-coa thioesterase iii; Long-chain acyl-CoA thioesterase with a preference for 3,5- tetradecadienoyl-CoA. Could be involved in beta-oxidation of fatty acids | 0.890 |
paaI | menI | b1396 | b1686 | Thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters. Hydrolyzes 3,4-dihydroxyphenylacetyl-CoA, 3- hydroxyphenylacetyl-CoA and 4-hydroxyphenylacetyl-CoA. Inactive towards 4-hydroxybenzoyl-CoA and 4-hydroxyphenacyl-CoA | 1,4-dihydroxy-2-naphthoyl-CoA hydrolase; Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA). Also shows significant activity toward a wide range of acyl-CoA thioesters, and minimal activity toward benzoyl-holoEntB | 0.877 |