| IED ID | IndEnz0015000041 |
| Enzyme Type ID | laccase000041 |
| Protein Name |
Multicopper oxidase abr1 EC 1.-.-.- Conidial pigment biosynthesis oxidase abr1 |
| Gene Name | abr1 AFUA_2G17540 |
| Organism | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Enzyme Sequence | MFHSRALLLSWLVGFTAAKDIHLDWNITWVWAAPDGFGRPMIGINNEWPCPIVNADLGDRLIVDVHNGLGNQSTGIHWHGFHQYMTGTMDGSNQVTQCALPPGSSMRYEFDVNQTGTYWYHSHEMGQYPDGLRGPFIVRDPSPPFAYDDEFTLTLTDHYHEQMSVLLQQYEADSVGAQAGVNEPLPAAALINEGFDTTTLRVEPNKTYLIHLVCVGNWPGHVIVFDDHEISVVEVDGTWVDAYPARDKKIRLATGQRMSILLKTKDNTDRNYAIWDSMDVNMMFFYQNRAIPEGFNPNTTAWLVYDEAKELPPAPDVHELDPNNDFVDDLVFVPASHEPLLEKVDRQIIFDTGVTQRDGRSVYTINGQTYVDPEEPTLYTALAASPENASNASLYGQVNPFVVQYGEVVEIIINNHHGNLHPWHMHGHQFQVLQRTIPEGGYFDGYFANISSTPVKRDTIMVQNHGHAVLRFRANNPGVWLIHCHIEWHVTKGLTGTLIEAPAQMHKISVPLDHQRICPSYGTPPGGTPSSPPHDAPRPDGASGSPQYPPKPWGEPDASAPEQDDSQPGGTPDSPEDFPQPWGEPEESPQEPPQPWSPSNNAQPPANTYAPEYPSGYVPVAPGPVIIDSELHYGGKSSHVECSGVNAGHTQDTTTGGDGCANAS |
| Enzyme Length | 664 |
| Uniprot Accession Number | Q4WZB4 |
| 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 and a structural component of the conidial wall (PubMed:10515939, PubMed:14970241, PubMed:19156203). The first step of the pathway is the production of the heptaketide naphtopyrone YWA1 by the polyketide synthase alb1 though condensation of acetyl-CoA with malonyl-CoA (PubMed:10515939). The naphtopyrone YWA1 is then converted to the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the heptaketide hydrolyase ayg1 though chain-length shortening (PubMed:10515939,). 1,3,6,8-THN is substrate of the hydroxynaphthalene reductase arp2 to yield scytalone (PubMed:10515939). The scytalone dehydratase arp1 then reduces scytalone to 1,3,8-THN (PubMed:10515939). 1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to yield vermelone (PubMed:10515939). Vermelone is further converted by the multicopper oxidase abr1 to 1,8-DHN (PubMed:10515939). Finally the laccase abr2 transforms 1,8-DHN to DHN-melanin (PubMed:10515939). DHN-melanin biosynthesis appears to be initiated in endosomes where early enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading to melanin deposition on the cell surface where late enzymes (abr1 and abr2) localize (PubMed:26972005). DHN-melanin is an important structural component of the outer cell wall and is required for the presence of conidial surface hydrophobins (PubMed:19703288). DHN-melanin plays also a crucial role in fungal virulence, including a protective role against the host's immune defenses (PubMed:19156203, PubMed:20145078, PubMed:21747802, PubMed:21573171, PubMed:24818666). DHN-melanin protects also conidia against amoeba predation (PubMed:25684622). {ECO:0000269|PubMed:10515939, ECO:0000269|PubMed:14970241, ECO:0000269|PubMed:19156203, ECO:0000269|PubMed:19703288, ECO:0000269|PubMed:20145078, ECO:0000269|PubMed:21573171, ECO:0000269|PubMed:21747802, ECO:0000269|PubMed:24818666, ECO:0000269|PubMed:25684622, ECO:0000269|PubMed:26972005}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Pigment biosynthesis; melanin biosynthesis. {ECO:0000269|PubMed:10515939, ECO:0000269|PubMed:19156203}. |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (2); Domain (3); Glycosylation (8); Metal binding (11); Region (2); Signal peptide (1) |
| Keywords | Copper;Glycoprotein;Metal-binding;Oxidoreductase;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Expression is up-regulated upon hyphal competency and drastically increased during conidiation (PubMed:24123270). Expression is controlled by brlA, the master regulator of conidiophore development, and is responsive to the copper level in the medium (PubMed:24123270). {ECO:0000269|PubMed:24123270}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26972005}. Cell surface {ECO:0000269|PubMed:24123270, ECO:0000269|PubMed:26972005}. Note=Localized at the surface of stalks and conidiophores, but not in young hyphae (PubMed:24123270). {ECO:0000269|PubMed:24123270}. |
| 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 | 73,445 |
| Kinetics | |
| Metal Binding | METAL 77; /note=Copper 1; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 79; /note=Copper 2; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 121; /note=Copper 2; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 123; /note=Copper 3; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 421; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 424; /note=Copper 1; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 426; /note=Copper 3; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 483; /note=Copper 3; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 484; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 485; /note=Copper 2; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 489; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3 |
| Rhea ID | |
| Cross Reference Brenda |