| Entry |
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| Symbol |
CoPKS, CrPKS
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| Name |
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| Brite |
KEGG Orthology (KO) [BR:ko00001]
09180 Brite Hierarchies
09181 Protein families: metabolism
01008 Polyketide biosynthesis proteins
K28740 CoPKS, CrPKS; 6-hydroxymusizin-2-carbonyl-ACP/atrochrysone-2-carbonyl-ACP synthase/thioesterase
Enzymes [BR:ko01000]
2. Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.335 6-hydroxymusizin-2-carbonyl-[acyl-carrier protein] synthase
K28740 CoPKS, CrPKS; 6-hydroxymusizin-2-carbonyl-ACP/atrochrysone-2-carbonyl-ACP synthase/thioesterase
2.3.1.336 atrochrysone-2-carbonyl-[acyl-carrier protein] synthase
K28740 CoPKS, CrPKS; 6-hydroxymusizin-2-carbonyl-ACP/atrochrysone-2-carbonyl-ACP synthase/thioesterase
3. Hydrolases
3.1 Acting on ester bonds
3.1.2 Thioester hydrolases
3.1.2.34 atrochrysone-2-carbonyl-[acyl-carrier protein] thioesterase
K28740 CoPKS, CrPKS; 6-hydroxymusizin-2-carbonyl-ACP/atrochrysone-2-carbonyl-ACP synthase/thioesterase
3.1.2.35 6-hydroxymusizin-2-carbonyl-[acyl-carrier protein] thioesterase
K28740 CoPKS, CrPKS; 6-hydroxymusizin-2-carbonyl-ACP/atrochrysone-2-carbonyl-ACP synthase/thioesterase
Polyketide biosynthesis proteins [BR:ko01008]
Polyketide synthase (PKS)
Iterative type I PKS
Fungal nonreducing PKS (NR-PKS)
K28740 CoPKS, CrPKS; 6-hydroxymusizin-2-carbonyl-ACP/atrochrysone-2-carbonyl-ACP synthase/thioesterase
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| Other DBs |
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| Genes |
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| Reference |
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| Authors |
Lohr NA, Eisen F, Thiele W, Platz L, Motter J, Huttel W, Gressler M, Muller M, Hoffmeister D. |
| Title |
Unprecedented Mushroom Polyketide Synthases Produce the Universal Anthraquinone Precursor. |
| Journal |
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| Sequence |
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| Reference |
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| Authors |
Lohr NA, Urban MC, Eisen F, Platz L, Huttel W, Gressler M, Muller M, Hoffmeister D. |
| Title |
The Ketosynthase Domain Controls Chain Length in Mushroom Oligocyclic Polyketide Synthases. |
| Journal |
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| Sequence |
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| Reference |
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| Authors |
Lohr NA, Rakhmanov M, Wurlitzer JM, Lackner G, Gressler M, Hoffmeister D. |
| Title |
Basidiomycete non-reducing polyketide synthases function independently of SAT domains. |
| Journal |
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| Sequence |
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| LinkDB |
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