node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
PFICI_00329 | ptaA | W3XMI9 | A0A067XNI2 | AMP-binding domain-containing protein. | Non-reducing polyketide synthase ptaA; Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain. The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and t [...] | 0.515 |
PFICI_02081 | ptaA | W3XQE5 | A0A067XNI2 | Carrier domain-containing protein. | Non-reducing polyketide synthase ptaA; Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain. The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and t [...] | 0.441 |
PFICI_03827 | PFICI_09514 | W3XK15 | W3X3E1 | KR domain-containing protein. | Uncharacterized protein. | 0.437 |
PFICI_03827 | ptaA | W3XK15 | A0A067XNI2 | KR domain-containing protein. | Non-reducing polyketide synthase ptaA; Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain. The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and t [...] | 0.427 |
PFICI_03942 | ptaA | W3XKC7 | A0A067XNI2 | PKS_ER domain-containing protein. | Non-reducing polyketide synthase ptaA; Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain. The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and t [...] | 0.932 |
PFICI_05764 | ptaA | W3XCR1 | A0A067XNI2 | Uncharacterized protein. | Non-reducing polyketide synthase ptaA; Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain. The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and t [...] | 0.427 |
PFICI_07948 | ptaA | W3X336 | A0A067XNI2 | Uncharacterized protein. | Non-reducing polyketide synthase ptaA; Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain. The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and t [...] | 0.897 |
PFICI_08881 | ptaA | W3WYS6 | A0A067XNI2 | PKS_ER domain-containing protein. | Non-reducing polyketide synthase ptaA; Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain. The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and t [...] | 0.920 |
PFICI_09514 | PFICI_03827 | W3X3E1 | W3XK15 | Uncharacterized protein. | KR domain-containing protein. | 0.437 |
PFICI_09514 | PFICI_12664 | W3X3E1 | W3WPB8 | Uncharacterized protein. | Carrier domain-containing protein. | 0.428 |
PFICI_09514 | ptaA | W3X3E1 | A0A067XNI2 | Uncharacterized protein. | Non-reducing polyketide synthase ptaA; Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain. The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and t [...] | 0.468 |
PFICI_11756 | ptaA | W3WRA3 | A0A067XNI2 | L-aminoadipate-semialdehyde dehydrogenase large subunit. | Non-reducing polyketide synthase ptaA; Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain. The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and t [...] | 0.422 |
PFICI_12664 | PFICI_09514 | W3WPB8 | W3X3E1 | Carrier domain-containing protein. | Uncharacterized protein. | 0.428 |
PFICI_12664 | ptaA | W3WPB8 | A0A067XNI2 | Carrier domain-containing protein. | Non-reducing polyketide synthase ptaA; Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain. The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and t [...] | 0.913 |
ptaA | PFICI_00329 | A0A067XNI2 | W3XMI9 | Non-reducing polyketide synthase ptaA; Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain. The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and t [...] | AMP-binding domain-containing protein. | 0.515 |
ptaA | PFICI_02081 | A0A067XNI2 | W3XQE5 | Non-reducing polyketide synthase ptaA; Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain. The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and t [...] | Carrier domain-containing protein. | 0.441 |
ptaA | PFICI_03827 | A0A067XNI2 | W3XK15 | Non-reducing polyketide synthase ptaA; Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain. The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and t [...] | KR domain-containing protein. | 0.427 |
ptaA | PFICI_03942 | A0A067XNI2 | W3XKC7 | Non-reducing polyketide synthase ptaA; Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain. The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and t [...] | PKS_ER domain-containing protein. | 0.932 |
ptaA | PFICI_05764 | A0A067XNI2 | W3XCR1 | Non-reducing polyketide synthase ptaA; Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain. The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and t [...] | Uncharacterized protein. | 0.427 |
ptaA | PFICI_07948 | A0A067XNI2 | W3X336 | Non-reducing polyketide synthase ptaA; Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain. The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and t [...] | Uncharacterized protein. | 0.897 |