| IED ID | IndEnz0015000035 |
| Enzyme Type ID | laccase000035 |
| Protein Name |
Multicopper oxidase aurL2 EC 1.-.-.- Aurofusarin biosynthesis cluster protein L2 Gibberella pigment protein 10 Laccase-2 |
| Gene Name | aurL2 GIP10 lac2 FG02330 FGRAMPH1_01T05605 |
| Organism | Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Nectriaceae Fusarium Fusarium sambucinum species complex Gibberella zeae (Wheat head blight fungus) (Fusarium graminearum) Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum) |
| Enzyme Sequence | MLFRFLALLPFVAGAFAEYKVHDDTFKPDYVLEATLDDIKINCVSRSSIVFNGTSPGPTIYLQEEQTTWIRVYNKIPDNNVTVHWHGLSQRAAPFSDGTPLVSQWPIPAGQFFDYEIRPEIGDAGSYFYHSHVGFQIVTAFGALIVRDARKPEYKYDGDIPLLVGDNYAAEDEVIEQGLLADPFKWSGEPQAITIQGNSGNKSFYEAPDSSCMPHVVHVDPGKTYRLRFISATALSMIKLGIEDHENLTVIEADGSYTKPAKIDHVQVSPGQRYSYLMKTKTSKEVCGGDKSQYWIRYESRDRPKVISGYALLKYRCDKNQKLPKSLPETSPIELSNSTADYLEYALEGLSEKNNQAFPKLSEVTRTVVIQINQILTTGAYVNGTLNGTVAWAQNGLPWKENVQAERRQVPYLIQIYENGTTPNYTLALEHHGFDPETKAFPAKVGEVLDIVWENNNGPTGGWDYHPMHVHGYHVYDLGSGNGTYNATENEAHFENFTPVLRDTTNLYRYAVKGVPHHTAGWRAWRIRITEENIGAWMMHCHIAQHQVMGMATVWVFGDAEQIRGKFPAPPYTQGYLTYGGSAYGTEDDQPWVNEYYSDKNN |
| Enzyme Length | 602 |
| Uniprot Accession Number | I1RF64 |
| 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 aurofusarin, a red mycelium pigment which is acting as a mycotoxin (PubMed:15811992, PubMed:15809006, PubMed:16879655). The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide and yellow pigment YWA1 (PubMed:21296881, PubMed:23557488). The C2 hydroxyl group in the pyrone ring of YWA1 is probably formed during ring closure by an aldol-type cyclization reaction (PubMed:21296881). The dehydratase aurZ then acts as the first tailoring enzyme in the aurofusarin biosynthetic pathway by converting YWA1 to nor-rubrofusarin (PubMed:21296881, PubMed:23557488). Nor-rubrofusarin is then methylated to rubrofusarin by the O-methyltransferase aurJ (PubMed:21296881, PubMed:23557488). Rubrofusarin is then transported across the plasma membrane by the rubrofusarin-specific pump aurT for further enzymatic processing by the extracellular complex composed of GIP1, aurF, aurO and aurS to yield aurofusarin (PubMed:21296881). {ECO:0000269|PubMed:15809006, ECO:0000269|PubMed:15811992, ECO:0000269|PubMed:16879655, ECO:0000269|PubMed:21296881, ECO:0000269|PubMed:23557488}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:15809006, ECO:0000269|PubMed:16879655}. |
| nucleotide Binding | |
| Features | Chain (1); Domain (3); Glycosylation (11); Metal binding (5); Signal peptide (1) |
| Keywords | Copper;Glycoprotein;Metal-binding;Oxidoreductase;Reference proteome;Repeat;Signal |
| Interact With | |
| Induction | INDUCTION: Expression is regulated by the aurofusarin biosynthesis cluster-specific transcription factor aurR1/GIP2 (PubMed:16461721). {ECO:0000269|PubMed:16461721}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 67,889 |
| Kinetics | |
| Metal Binding | METAL 84; /note=Copper 1; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 86; /note=Copper 2; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 130; /note=Copper 2; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 132; /note=Copper 3; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 469; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3 |
| Rhea ID | |
| Cross Reference Brenda |