5 items (Aspergillus nidulans) - STRING interaction network

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	aptC	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 [...] (417 aa)
	xptB	Xanthone prenyltransferase B; Dehydrogenase involved in the conversion of monodictyphenone to the prenyl xanthones such as emericellin, shamixanthone and epishamixanthone. Monodictyphenone is first converted to variecoxanthone A via a paeciloxanthone intermediate by the consecutive actions of the FAD-dependent monooxygenase mdpD and the xanthone prenyltransferase xptB. XptB catalyzes regular O-prenylation at the hydroxy group of C-7 of the xanthone ring. Variecoxanthone A is further prenylated to emericellin by xptA before being reduced to shamixanthone and epishamixanthone by the dehy [...] (463 aa)
	xptA	Xanthone prenyltransferase A; Dehydrogenase involved in the conversion of monodictyphenone to the prenyl xanthones such as emericellin, shamixanthone and epishamixanthone. Monodictyphenone is first converted to variecoxanthone A via a paeciloxanthone intermediate by the consecutive actions of the FAD-dependent monooxygenase mdpD and the xanthone prenyltransferase xptB. XptB catalyzes regular O-prenylation at the hydroxy group of C-7 of the xanthone ring. Variecoxanthone A is further prenylated to emericellin by xptA before being reduced to shamixanthone and epishamixanthone by the dehy [...] (446 aa)
	aptB	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 [...] (309 aa)
	aptA	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 [...] (1792 aa)

Your Current Organism:

Aspergillus nidulans

NCBI taxonomy Id: 227321
Other names: A. nidulans FGSC A4, Aspergillus nidulans FGSC A4, Emericella nidulans FGSC A4

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
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	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
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