IED ID | IndEnz0015000046 |
Enzyme Type ID | laccase000046 |
Protein Name |
Laccase 1 EC 1.10.3.- Conidial pigment biosynthesis oxidase Mlac1 |
Gene Name | Mlac1 Abr2 MAJ_09464 |
Organism | Metarhizium majus (strain ARSEF 297) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Clavicipitaceae Metarhizium Metarhizium majus Metarhizium majus (strain ARSEF 297) |
Enzyme Sequence | MSRFARLLLMVVALFFTNAWAKTVKETLRITWKEGAPNGQARELIYTNGQFPSPTLVWDEDDDVEITVYNEMAKNVTVHWHGLDQKDTPWSDGTPGLSQRPIQPGNKFVYKFKASPPGNHWYHSHEKMSLVDGLYGAIHIRPKGDRTGLWSQISQDKDDIKAMENAAHDPEYLVVSDWSQYTSEEYWKISTDSGLLVFCLDSILVNGKGEVYCPGQKFLQAELAPGLVEDAFPPGTEVSDKGCFPADLDQVQGGPWNITKRPDLIPPRVQEGCVASSHENATIVVDPSRNNGWVSMHIVAAATIAQITFSVDSHEFWLYEIDGNYVNPRKFVSAVMSAGETFSVMIKLDQKPGRYTMRIPNSGASQVLGGFAEMVYKGCESEEKTGKAYLSYGGNPTSPDVEKNSFFPWQLDTDHMSPWPPNKPRPGNADEEHLLVLGRVGAPYNYTMNTKYLYPVDFQNDDPLLFYPNATRDTENDGLVLRTKNGSWVDLILQVSTLPGDTSSFEHFMHKHGSKTWRIGFGTGVWNYTSVEEAIKERPKDFNLETPGLRDTWITAFSIGGEAYWSVFRYFVDNPGPWLFHCHIELHLMGGMGIAILDGVDAWPEHIPEEYQLC |
Enzyme Length | 614 |
Uniprot Accession Number | A0A0B4HQH6 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 1.10.3.- |
Enzyme Function | FUNCTION: Laccase; part of the Pks1 gene cluster that mediates the biosynthesis of an anthraquinone derivative pigment that contributes to conidial pigmentation that provides protection from UV radiation, heat and cold stress (PubMed:29958281). The polyketide synthase Pks1 produces 1-acetyl-2,4,6,8-tetrahydroxy-9,10-anthraquinone though condensation of acetyl-CoA with malonyl-CoA (Probable). The dehydratase EthD and the laccase Mlac1 further convert the anthraquinone derivative into the final conidial pigment (Probable). {ECO:0000269|PubMed:29958281, ECO:0000305|PubMed:29958281}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Pigment biosynthesis. {ECO:0000305|PubMed:29958281}. |
nucleotide Binding | |
Features | Chain (1); Domain (3); Glycosylation (7); Metal binding (12); Signal peptide (1) |
Keywords | Copper;Glycoprotein;Metal-binding;Oxidoreductase;Repeat;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:E9RBR0}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 69,084 |
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 507; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 510; /note=Copper 1; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 510; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 512; /note=Copper 3; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 581; /note=Copper 3; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 582; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 583; /note=Copper 2; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 587; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3 |
Rhea ID | |
Cross Reference Brenda |