MLAC1_METAF
ID MLAC1_METAF Reviewed; 612 AA.
AC A0A0B4F1I0;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 03-AUG-2022, entry version 23.
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}; ORFNames=MAN_10477;
OS Metarhizium anisopliae (strain ARSEF 549).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1276135;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 549;
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
RN [2]
RP INDUCTION, DISRUPTION PHENOTYPE, FUNCTION, AND PATHWAY.
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 [3]
RP IDENTIFICATION, AND FUNCTION.
RC STRAIN=ARSEF 1941;
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:20382249, PubMed:29958281). The polyketide
CC synthase Pks1 produces 1-acetyl-2,4,6,8-tetrahydroxy-9,10-anthraquinone
CC though condensation of acetyl-CoA with malonyl-CoA (Probable). The
CC dehydratase EthD and the laccase Mlac1 further convert the
CC anthraquinone derivative into the final conidial pigment
CC (PubMed:20382249) (Probable). {ECO:0000269|PubMed:20382249,
CC ECO:0000269|PubMed:29958281, 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; AZNF01000025; KID59671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B4F1I0; -.
DR SMR; A0A0B4F1I0; -.
DR EnsemblFungi; KID59671; KID59671; MAN_10477.
DR HOGENOM; CLU_006504_5_0_1; -.
DR Proteomes; UP000031186; Unassembled WGS sequence.
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; 1.
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..612
FT /note="Laccase 1"
FT /id="PRO_5002102158"
FT DOMAIN 29..142
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 171..359
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 468..598
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT BINDING 78
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 80
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 122
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 124
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 506
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 509
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 509
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 511
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 580
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 581
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 582
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 586
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 612 AA; 68949 MW; 993E39D1567EB1B2 CRC64;
MSRFARLLLI VALFFTSAWA KTVKETLRIT WEEGAPNGQA RELIYTNGQF PSPTLVWDED
DDIEVTVYNE MAKNVTVHWH GLDQKDTPWS DGTPGLSQRP IQPGNKFVYR FKASPPGNHW
YHSHEKMSLV DGLYGAIHIR PKGDRTGLWS QISQDKDDIK AMENAAYDPE YLVVSDWSQY
TSEEYWKIST DSGLLVFCLD SILVNGKGEV YCPGQKFLQA ELAPGLVEDA FPPGTEVSDK
GCFPADLDQV QGGPWNITKR PDLIPPRVQE GCVASRHENA TIVVDPSKNN GWVSMHFVAA
ATIAQITFSV DSHEFWLYEI DGNYVNPRKF VSAVMSAGET FSVMIKLDQE PGKYTMRIPN
SGASQVLGGF AEMVYKGCEH EEKAGKAYLS YGGNPTSPDV EKNSFFPWQL DTDHMSPWPP
NKPRPGNADE EHLLVLGRVG APYNYTMNTK YLYPVDFQND DPLLFYPNAT RDTENDGLVL
RTKNGSWVDL ILQVSTLPGD TSSFEHFMHK HGSKTWRIGF GTGVWNYTSV EEAIQERPQD
FNLETPGLRD TWITAFSIGG EAYWSVFRYF VDNPGPWLFH CHIELHLMGG MGIAILDGVD
AWPEHIPEEY QC
