MLAC1_METAN
ID MLAC1_METAN Reviewed; 603 AA.
AC C3SAH7;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Laccase 1 {ECO:0000303|PubMed:20382249};
DE EC=1.10.3.- {ECO:0000305|PubMed:20382249};
DE AltName: Full=Conidial pigment biosynthesis oxidase Mlac1 {ECO:0000303|PubMed:20382249};
DE Flags: Precursor;
GN Name=Mlac1 {ECO:0000303|PubMed:20382249};
GN Synonyms=Abr2 {ECO:0000303|PubMed:29958281};
OS Metarhizium anisopliae (Entomophthora anisopliae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=5530;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, DISRUPTION PHENOTYPE,
RP FUNCTION, AND PATHWAY.
RC STRAIN=ARSEF 2575;
RX PubMed=20382249; DOI=10.1016/j.fgb.2010.03.011;
RA Fang W., Fernandes E.K., Roberts D.W., Bidochka M.J., St Leger R.J.;
RT "A laccase exclusively expressed by Metarhizium anisopliae during isotropic
RT growth is involved in pigmentation, tolerance to abiotic stresses and
RT virulence.";
RL Fungal Genet. Biol. 47:602-607(2010).
RN [2]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=29958281; DOI=10.1371/journal.pgen.1007472;
RA Zeng G., Zhang P., Zhang Q., Zhao H., Li Z., Zhang X., Wang C., Yin W.B.,
RA Fang W.;
RT "Duplication of a Pks gene cluster and subsequent functional
RT diversification facilitate environmental adaptation in Metarhizium
RT species.";
RL PLoS Genet. 14:E1007472-E1007472(2018).
CC -!- FUNCTION: Laccase; part of the Pks1 gene cluster that mediates the
CC biosynthesis of an anthraquinone derivative pigment that contributes to
CC conidial pigmentation that provides protection from UV radiation, heat
CC and cold stress (PubMed:29958281). The polyketide synthase Pks1
CC produces 1-acetyl-2,4,6,8-tetrahydroxy-9,10-anthraquinone though
CC condensation of acetyl-CoA with malonyl-CoA (Probable). The dehydratase
CC EthD and the laccase Mlac1 further convert the anthraquinone derivative
CC into the final conidial pigment (PubMed:20382249) (Probable).
CC {ECO:0000269|PubMed:20382249, ECO:0000269|PubMed:29958281,
CC ECO:0000305|PubMed:29958281}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:Q70KY3};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:Q70KY3};
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:20382249}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:E9RBR0}.
CC -!- INDUCTION: Expressed during isotropic growth (swelling) but not during
CC polarized growth (germ tubes and hyphae) (PubMed:20382249). Expressed
CC exclusively in the later stages of conidiation and in blastospores when
CC M.anisopliae is living as a saprophyte (PubMed:20382249). During
CC infection processes, is also expressed by appressoria on the cuticle
CC surface and hyphal bodies inside the insect haemocoel
CC (PubMed:20382249). {ECO:0000269|PubMed:20382249}.
CC -!- DISRUPTION PHENOTYPE: Reduces virulence to caterpillars because of
CC impaired appressoria and delayed post-infection events
CC (PubMed:20382249). Produces a yellow-conidia phenotype with increased
CC conidial susceptibility to heat shock and UV-B stress
CC (PubMed:20382249). {ECO:0000269|PubMed:20382249}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; EU769126; ACQ65735.1; -; Genomic_DNA.
DR AlphaFoldDB; C3SAH7; -.
DR SMR; C3SAH7; -.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; PTHR11709; 2.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 2: Evidence at transcript level;
KW Copper; Glycoprotein; Metal-binding; Oxidoreductase; Repeat; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..603
FT /note="Laccase 1"
FT /id="PRO_5002932445"
FT DOMAIN 66..108
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 159..349
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 460..588
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT BINDING 90
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 92
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 496
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 499
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 499
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 501
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 570
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 571
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 572
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 576
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 603 AA; 67960 MW; 0FBADED929B6EC39 CRC64;
MSRFARLLLI VALFFTNAWA KTVKETLRIT WKEGAPNGQA RELIYTNGQF PSPTLVWDED
DDIEGQRPIQ PGNKFVYRFK ASPPGNHWYH SHEKMSLVDG LYGAIHIRLT GTPRRFHMND
AKSQARRPKG DRTGLWSQIS QDKDDIKAME NAAYDPEYLV VSDWSQYTSE EYWKISTDSG
LLVLYAYVAP SILVNGKGEV YCPGQKFLQA ELAPGLVEDA FPPGTEVSDK GCFPADLDQV
QGGPWNITKR PDLIPPRVRE GCVASRHENA TIVVDPSKNN GWVSMHFVAA ATTAQITFSV
DSHEFWLYEI DGNYVNPRKF ASAVMSAGET FSVMIKLDQE PGKYTMRIPN SGASQVLGGF
AEMVYKGCER EEKAGKAYLS YGGNPTSPDV EKNSFFPWQL DTDHMSPWPP NKPRPGNADE
EHLLVLGRVG APYNYTMNTK YLYPVDFQND DPLLFYPSAT RDTENDGLVL RTKNGSWVDL
ILQVSTLPGD TASSEHFMHK HGSKTWRIGF GTGVWNYTSV EEAIQERPQD FNLETPGLRD
TWITAFSIGG EAYWSVFRYF VDNPGPWLFH CHIELHLMGG MGIAILDGVD AWPEHIPEEY
QLR
