| IED ID | IndEnz0015000109 |
| Enzyme Type ID | laccase000109 |
| Protein Name |
Multicopper oxidase PfmaD EC 1.-.-.- Conidial pigment biosynthesis cluster protein D |
| Gene Name | PfmaD PFICI_07100 |
| Organism | Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Xylariomycetidae Xylariales Sporocadaceae Pestalotiopsis Pestalotiopsis fici Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) |
| Enzyme Sequence | MWTARLSSIAVLTQVVGTWADTITLNWEITWVNAAPDGFHRPVIGVNGKWPCPPIHATVGDTVVINMKNSLGNQTTGLHFHGINQLDTNYMDGASMVNSCPVVPGSSMTYSFTADEPGTYWYHSHNMAQYPDGLRGPLIIHDDNDPFDGEFDNEVILTISDWYHQQTLTLVQNMLVSSNDQWRPPLPDGMIVNEGGNTDIELDIGTTTRVRILNFGALTAFMLRFGSRDMDVIMTDASYVQRETIHQLRIAPGQRYDVLVSATKKDKGKNIPYLISMDLNRDFTVSGTWTFNQTGYLITDAKAPCTAKEVVQQWRPFDEALFTPLDEMPLLGPLDRTWTLNFALCKDMNNIPRMCFNDQTYVMQKTPTLYTAATVGNANTDPSVYGAVLPFIIEYGDVLEIVINNLDPAIHPFHLHGHQFQVVERPESGSGSFDGSSTANPVPPRRDVISINGGSYARLRITADNPGVFLFHCHIEWHVEMGLTATLIEAPEMLDGYDIPQAMIDSCKAQGYPVAGNAAGDTINVWDDSGYLTDPPSTYSGSQWPVPKGGNSQKSRPRRKPSGQSSQTRQISNMSGEFQHRITW |
| Enzyme Length | 584 |
| Uniprot Accession Number | W3X7K0 |
| 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 dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment forming a dark layer in the conidial wall that protects the conidia from UV radiations (PubMed:28517364). The first step of the pathway is the production of the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN or T4HN) by the polyketide synthase PfmaE though condensation of acetyl-CoA with malonyl-CoA. T4HN is not stable and easily oxidizes into the stable form flaviolin (PubMed:28517364). T4HN is also substrate of the hydroxynaphthalene reductase PfmaG to yield scytalone (PubMed:28517364). The scytalone dehydratase PfmaJ then reduces scytalone to 1,3,8-THN (PubMed:31116900). 1,3,8-THN is then substrate of the hydroxynaphthalene reductase PfmaI to yield vermelone (Probable). Vermelone is further converted by the multicopper oxidase PfmaD to 1,8-DHN (Probable). Finally the laccase PFICI_06862 transforms 1,8-DHN to DHN-melanin (Probable). The roles of the 5-oxoprolinase PfmaA and the proline iminopeptidase PfmaB within the cluster have not been elucidated yet (Probable). {ECO:0000269|PubMed:28517364, ECO:0000269|PubMed:31116900, ECO:0000305|PubMed:28517364, ECO:0000305|PubMed:31116900}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Pigment biosynthesis; melanin biosynthesis. {ECO:0000269|PubMed:28517364}. |
| nucleotide Binding | |
| Features | Chain (1); Domain (3); Metal binding (11); Region (2); Signal peptide (1) |
| Keywords | Copper;Melanin biosynthesis;Metal-binding;Oxidoreductase;Reference proteome;Repeat;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Expression is positively regulazed by the cluster-specific transcription factor pfmaF. {ECO:0000269|PubMed:28517364, ECO:0000269|PubMed:31116900}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q4WZB4}. Cell surface {ECO:0000250|UniProtKB:Q4WZB4}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 64,884 |
| Kinetics | |
| Metal Binding | METAL 79; /note=Copper 1; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 81; /note=Copper 2; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 123; /note=Copper 2; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 125; /note=Copper 3; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 411; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 414; /note=Copper 1; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 416; /note=Copper 3; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 472; /note=Copper 3; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 473; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 474; /note=Copper 2; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 478; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3 |
| Rhea ID | |
| Cross Reference Brenda |