| IED ID | IndEnz0015000030 |
| Enzyme Type ID | laccase000030 |
| Protein Name |
Multicopper oxidase CTB12 EC 1.-.-.- Cercosporin toxin biosynthesis cluster protein 12 Laccase CTB12 |
| Gene Name | CTB12 CB0940_00845 |
| Organism | Cercospora beticola (Sugarbeet leaf spot fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Dothideomycetidae Mycosphaerellales Mycosphaerellaceae Cercospora Cercospora beticola (Sugarbeet leaf spot fungus) |
| Enzyme Sequence | MWSVRLYPLALTLLFQCVSPAAARPSGCVDDVEVVQEIGSKEIQAPVVRFEISLTTQSIDAAGIGFREAIFINDAFIGPTLYAKQGDRIEFVVHNYMQQDTSIHFHGIDQRSTPWSDGVPGLTQSQIRPGASFLYNWTAHDAGTYFYHSHAKSQMMDGLYGAVVIAPDDEAPRPFHLISSGEADQAAMLAAEKLMRPIFVSDWSQYTSAEYHGIQHAANIDFSCMDSILVQGVGSQYCLSEEELDDMTNPIVLQLLKELAGGHMTPKGCIPPLQMFNGDFELHLENVPELAYNKCKGGQSSKGNYTIDVDTSIGWAALTFVNPGGLYPLQLSIDSHELYVYAVDGQYVYPIVADRVLVNTGSRISVMIKLDQEKARHVVRVANDYLNQILGGFAELAYDGATNAPKHPHPKTNYGGKLISSEMVSFVPEDSSPYPALRPAQSADSTFKLRLKKLGQPYRAYEWTQTGSLGYNISHEHDDPPLLLQNVEDVPATELTLKTQIGDWVDLVLVTAGPFAQAHPMHKHGNKVFLIGSGSGSFPWESVEEAIPHLPEGTFNFQDPPYLDTFNTVEMEGQANDTWTAVRYKAEYAGAWLFHCHVQTHLSGGMGMVVLDGVDAWPEVPLAYQEWNGFEPPALS |
| Enzyme Length | 636 |
| Uniprot Accession Number | A0A2G5I8N8 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 1.-.-.- |
| Enzyme Function | FUNCTION: Multicopper oxidase; part of the gene cluster that mediates the biosynthesis of cercosporin, a light-activated, non-host-selective toxin (PubMed:29844193). The perylenequinone chromophore of cercosporin absorbs light energy to attain an electronically-activated triplet state and produces active oxygen species such as the hydroxyl radical, superoxide, hydrogen peroxide or singlet oxygen upon reaction with oxygen molecules (PubMed:11701851). These reactive oxygen species cause damage to various cellular components including lipids, proteins and nucleic acids (PubMed:11701851). The first step of cercosporin biosynthesis is performed by the polyketide synthase CTB1 which catalyzes the formation of nor-toralactone (Probable). The starter unit acyltransferase (SAT) domain of CTB1 initiates polyketide extension by the selective utilization of acetyl-CoA, which is elongated to the heptaketide in the beta-ketoacyl synthase (KS) domain by successive condensations with six malonyl units introduced by the malonyl acyltransferase (MAT) domain. The product template (PT) domain catalyzes C4-C9 and C2-C11 aldol cyclizations and dehydrations to a trihydroxynaphthalene, which is thought to be delivered to the thioesterase (TE) domain for product release (Probable). The bifunctional enzyme CTB3 then methylates nor-toralactone to toralactone before conducting an unusual oxidative aromatic ring opening (Probable). The O-methyltransferase CTB2 further methylates the nascent OH-6 of the CBT3 product, blocking further oxidation at this site before the reductase CTB6 reduces the 2-oxopropyl ketone at position C7, giving naphthalene (Probable). The FAD-dependent monooxygenase CTB5 in concert with the multicopper oxidase CTB12 are responsible for homodimerization of naphthalene with CTB7 installing the dioxepine moiety, finally producing cercosporin (Probable). The fasciclin domain-containing protein CTB11 might act with CTB5 and CTB12 whereas the roles of CTB9 and CTB10 have still to be elucidated (By similarity). {ECO:0000250|UniProtKB:Q0UHZ9, ECO:0000269|PubMed:29844193, ECO:0000303|PubMed:11701851, ECO:0000305|PubMed:29844193}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:29844193}. |
| nucleotide Binding | |
| Features | Chain (1); Domain (3); Glycosylation (4); Metal binding (11); Signal peptide (1) |
| Keywords | Copper;Glycoprotein;Metal-binding;Oxidoreductase;Repeat;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 70,180 |
| Kinetics | |
| Metal Binding | METAL 104; /note=Copper 1; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 106; /note=Copper 2; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 148; /note=Copper 2; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 150; /note=Copper 3; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 519; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 522; /note=Copper 1; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 524; /note=Copper 3; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 595; /note=Copper 3; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 596; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 597; /note=Copper 2; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 601; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3 |
| Rhea ID | |
| Cross Reference Brenda |