| IED ID | IndEnz0015000029 |
| Enzyme Type ID | laccase000029 |
| Protein Name |
Multicopper oxidase elcG EC 1.-.-.- Elsinochrome C biosynthesis cluster protein G Laccase elcG |
| Gene Name | elcG SNOG_08616 |
| Organism | Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Parastagonospora nodorum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Pleosporomycetidae Pleosporales Pleosporineae Phaeosphaeriaceae Parastagonospora Phaeosphaeria nodorum (Glume blotch fungus) (Parastagonospora nodorum) Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Parastagonospora nodorum) |
| Enzyme Sequence | MACNILNFLTGLLSLSSTLPSTYFPSCIKPSNSHVSQNPVRFEVHLTPGRANPTGAGFRDVILVNGTFTGPTLRLSRGDNVEFLVRNHLREDTAVHFHGITQSLSPWADGTPGIAQRPIRPGAAYLYRWRADESGVFFYHAHSRGQLMDGMYGAIVIERGEDEPSPFHMISHEASDWELMREAEREVQTLMISDWSQFSFGEVMGVEREANIDFTCMDAIVVNGAGSEYCLERELLNEYTNPLVKFILSHTDEKEITDKGCVPPLRLFQGNYSLHLDTLPPEAFRKCIPGVGGGANHTVTVHSSNRWAALTFINPGGLYPLKVTIDNHPMHVFAVDGHYIYPQIVDQILVNNGERYSVFVKLDQEVGRYTIRIANDLLGQVLGGFAALSYNGVMDDPPHPKPLMNYAGGSLVKNIRVFDEFNTRPYPPKPPASVADRTHKFMVRKLAQPHGAYEWTMSGIEGLNMTTEDVASPFLFQDPSQIETSELMLTTKKNEWVDLIIEVEGPFAQSHPMHKHGNKAFIVGRGVGFFPWATVEEAEKHLPRGTFNFIDPPYKDTFKTLEGVNNNAWLALRYHANSPGAWLFHCHIQTHLAGGMGVVILDGVDEWPELPEAYAEWNGFEAPV |
| Enzyme Length | 624 |
| Uniprot Accession Number | Q0UHZ8 |
| 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 elsinochrome C, a perelyenequinone phytotoxin structurally similar to cercosporin (PubMed:28251756, PubMed:30809363). The first step of elsinochrome C biosynthesis is performed by the polyketide synthase elcA which catalyzes the formation of nor-toralactone (PubMed:28251756, PubMed:30809363). The starter unit acyltransferase (SAT) domain of elcA 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 (By similarity). 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 (By similarity). The bifunctional enzyme elcB then methylates nor-toralactone to toralactone before conducting an unusual oxidative aromatic ring opening (PubMed:28251756, PubMed:30809363). The next step in perylenequinone biosynthesis is an O-methylation at the nascent OH-6 of the elcB product performed by the O-methyltransferase elcD (PubMed:30809363). The oxidative coupling of the two monomeric naphthol units in perylenequinone biosynthesis is catalyzed by the FAD-dependent monooxygenase elcE and the multicopper oxidase elcG (PubMed:30809363). ElcG might catalyze the first intermolecular coupling in a regio- and stereo-selective manner via a phenol radical coupling mechanism and the elcE could forge the second C-C bond intramolecularly via a hydride transfer mechanism (PubMed:30809363). The fasciclin domain-containing protein elcF might also play a role duting this step (Probable). The last piece of the puzzle in the biosynthesis of elsinochrome C is the additional annulation by enolate coupling to afford the dihydrobenzo(ghi)perylenequinone system, catalyzed by the FAD-dependent monooxygenase elcH (PubMed:30809363). {ECO:0000250|UniProtKB:Q6DQW3, ECO:0000269|PubMed:28251756, ECO:0000269|PubMed:30809363, ECO:0000305|PubMed:30809363}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:28251756, ECO:0000269|PubMed:30809363}. |
| nucleotide Binding | |
| Features | Chain (1); Domain (3); Glycosylation (4); Metal binding (11); Signal peptide (1) |
| Keywords | Copper;Glycoprotein;Metal-binding;Oxidoreductase;Reference proteome;Repeat;Signal |
| Interact With | |
| Induction | INDUCTION: Expression is up-regulated during the late stage of P.nodorum wheat leaf infection and is controlled by the cluster specific transporter elcR. {ECO:0000269|PubMed:28251756}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 69,719 |
| Kinetics | |
| Metal Binding | METAL 96; /note=Copper 1; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 98; /note=Copper 2; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 140; /note=Copper 2; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 142; /note=Copper 3; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 511; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 514; /note=Copper 1; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 516; /note=Copper 3; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 585; /note=Copper 3; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 586; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 587; /note=Copper 2; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 591; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3 |
| Rhea ID | |
| Cross Reference Brenda |