| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ANIA_01899 | aptB | C8VKK0 | Q5B0C9 | 4-hydroxyphenylpyruvate dioxygenase. | Lactamase-like protein aptB; Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of aptB into endocrocin-9- anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis [...] | 0.463 |
| ANIA_01899 | trpC | C8VKK0 | P06531 | 4-hydroxyphenylpyruvate dioxygenase. | Multifunctional tryptophan biosynthesis protein; Trifunctional enzyme bearing the Gln amidotransferase (GATase) domain of anthranilate synthase, indole-glycerolphosphate synthase, and phosphoribosylanthranilate isomerase activities. | 0.586 |
| ANIA_07071 | aptB | Q5AXA9 | Q5B0C9 | Polyketide synthase, putative (JCVI). | Lactamase-like protein aptB; Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of aptB into endocrocin-9- anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis [...] | 0.582 |
| ANIA_07819 | aptB | C8VDU3 | Q5B0C9 | Uncharacterized protein. | Lactamase-like protein aptB; Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of aptB into endocrocin-9- anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis [...] | 0.463 |
| ANIA_07819 | mdpK | C8VDU3 | C8VQ62 | Uncharacterized protein. | Monooxygenase mdpK; Monooxygenase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG. The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG. The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone. The next step is performed by the anthrone oxygenase mdpH that catalyzes the oxidation of emo [...] | 0.541 |
| ANIA_07819 | stcQ | C8VDU3 | Q00713 | Uncharacterized protein. | Averufin oxidase A homolog; Involved in the conversion of averufin (AVF) to versiconal hemiacetal acetate (VHA); Belongs to the avfA family. | 0.450 |
| aptA | aptB | Q5B0D0 | Q5B0C9 | Non-reducing polyketide synthase aptA; Non-reducing polyketide synthase (NRPKS); part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Through its product template (PT) domain, catalyzes the cyclization of the polyketide backbone via C6-C11 aldolcondensation. Polyketide is subsequently hydrolyzed from the NRPKS by the action of the hydrolase aptB into endocrocin-9-anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by [...] | Lactamase-like protein aptB; Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of aptB into endocrocin-9- anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis [...] | 0.641 |
| aptA | aptC | Q5B0D0 | Q5B0C8 | Non-reducing polyketide synthase aptA; Non-reducing polyketide synthase (NRPKS); part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Through its product template (PT) domain, catalyzes the cyclization of the polyketide backbone via C6-C11 aldolcondensation. Polyketide is subsequently hydrolyzed from the NRPKS by the action of the hydrolase aptB into endocrocin-9-anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by [...] | FAD-dependent monooxygenase aptC; FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of the hydrolase aptB into endocrocin-9-anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by the monooxygenase aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no deca [...] | 0.410 |
| aptB | ANIA_01899 | Q5B0C9 | C8VKK0 | Lactamase-like protein aptB; Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of aptB into endocrocin-9- anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis [...] | 4-hydroxyphenylpyruvate dioxygenase. | 0.463 |
| aptB | ANIA_07071 | Q5B0C9 | Q5AXA9 | Lactamase-like protein aptB; Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of aptB into endocrocin-9- anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis [...] | Polyketide synthase, putative (JCVI). | 0.582 |
| aptB | ANIA_07819 | Q5B0C9 | C8VDU3 | Lactamase-like protein aptB; Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of aptB into endocrocin-9- anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis [...] | Uncharacterized protein. | 0.463 |
| aptB | aptA | Q5B0C9 | Q5B0D0 | Lactamase-like protein aptB; Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of aptB into endocrocin-9- anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis [...] | Non-reducing polyketide synthase aptA; Non-reducing polyketide synthase (NRPKS); part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Through its product template (PT) domain, catalyzes the cyclization of the polyketide backbone via C6-C11 aldolcondensation. Polyketide is subsequently hydrolyzed from the NRPKS by the action of the hydrolase aptB into endocrocin-9-anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by [...] | 0.641 |
| aptB | aptC | Q5B0C9 | Q5B0C8 | Lactamase-like protein aptB; Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of aptB into endocrocin-9- anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis [...] | FAD-dependent monooxygenase aptC; FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of the hydrolase aptB into endocrocin-9-anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by the monooxygenase aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no deca [...] | 0.662 |
| aptB | mdpA | Q5B0C9 | C8VQ72 | Lactamase-like protein aptB; Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of aptB into endocrocin-9- anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis [...] | Monodictyphenone cluster transcriptional coactivator mdpA; Transcriptional coactivator; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative. With mdpE, coregulates the production of monodictyphenone. | 0.463 |
| aptB | mdpG | Q5B0C9 | Q5BH30 | Lactamase-like protein aptB; Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of aptB into endocrocin-9- anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis [...] | Atrochrysone carboxylic acid synthase; Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG. The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG. The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone. The next step is performed by the anthrone oxygenase md [...] | 0.661 |
| aptB | mdpK | Q5B0C9 | C8VQ62 | Lactamase-like protein aptB; Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of aptB into endocrocin-9- anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis [...] | Monooxygenase mdpK; Monooxygenase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG. The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG. The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone. The next step is performed by the anthrone oxygenase mdpH that catalyzes the oxidation of emo [...] | 0.486 |
| aptB | stcQ | Q5B0C9 | Q00713 | Lactamase-like protein aptB; Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of aptB into endocrocin-9- anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis [...] | Averufin oxidase A homolog; Involved in the conversion of averufin (AVF) to versiconal hemiacetal acetate (VHA); Belongs to the avfA family. | 0.486 |
| aptB | trpC | Q5B0C9 | P06531 | Lactamase-like protein aptB; Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of aptB into endocrocin-9- anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis [...] | Multifunctional tryptophan biosynthesis protein; Trifunctional enzyme bearing the Gln amidotransferase (GATase) domain of anthranilate synthase, indole-glycerolphosphate synthase, and phosphoribosylanthranilate isomerase activities. | 0.536 |
| aptC | aptA | Q5B0C8 | Q5B0D0 | FAD-dependent monooxygenase aptC; FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of the hydrolase aptB into endocrocin-9-anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by the monooxygenase aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no deca [...] | Non-reducing polyketide synthase aptA; Non-reducing polyketide synthase (NRPKS); part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Through its product template (PT) domain, catalyzes the cyclization of the polyketide backbone via C6-C11 aldolcondensation. Polyketide is subsequently hydrolyzed from the NRPKS by the action of the hydrolase aptB into endocrocin-9-anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by [...] | 0.410 |
| aptC | aptB | Q5B0C8 | Q5B0C9 | FAD-dependent monooxygenase aptC; FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of the hydrolase aptB into endocrocin-9-anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by the monooxygenase aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no deca [...] | Lactamase-like protein aptB; Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of aptB into endocrocin-9- anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis [...] | 0.662 |