MLAC1_METBS
ID MLAC1_METBS Reviewed; 613 AA.
AC A0A0B4F5S2;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Laccase 1 {ECO:0000250|UniProtKB:E9F648};
DE EC=1.10.3.- {ECO:0000305|PubMed:29958281};
DE AltName: Full=Conidial pigment biosynthesis oxidase Mlac1 {ECO:0000250|UniProtKB:E9F648};
DE Flags: Precursor;
GN Name=Mlac1 {ECO:0000250|UniProtKB:E9F648};
GN Synonyms=Abr2 {ECO:0000303|PubMed:29958281}; ORFNames=MBR_10248;
OS Metarhizium brunneum (strain ARSEF 3297).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1276141;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 3297;
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 IDENTIFICATION, FUNCTION, AND PATHWAY.
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 (Probable).
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:0000305|PubMed:29958281}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:E9RBR0}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; AZNG01000033; KID61216.1; -; Genomic_DNA.
DR RefSeq; XP_014539687.1; XM_014684201.1.
DR AlphaFoldDB; A0A0B4F5S2; -.
DR SMR; A0A0B4F5S2; -.
DR EnsemblFungi; KID61216; KID61216; MBR_10248.
DR GeneID; 26247518; -.
DR HOGENOM; CLU_006504_5_0_1; -.
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 3: Inferred from homology;
KW Copper; Glycoprotein; Metal-binding; Oxidoreductase; Repeat; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..613
FT /note="Laccase 1"
FT /id="PRO_5002086819"
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 613 AA; 69094 MW; 5EF56B8ECA1422C1 CRC64;
MSRFARLLLI VALFFTNAWA KTVKETLRIT WKEGAPNGQA 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 AEMVYKGCER EEKAGKAYLS YGGNPTSPDV EKNSFFPWQL DTDHMSPWPP
NKPRPGNADE EHLLVLGRVG APYNYTMNTK YLYPVDFQND DPLLFYPNAT RDTENDGLVL
RTKNGSWVDL ILQVSTLPGD TSSFEHFMHK HGSKTWRIGF GTGVWNYTSV EEAIQERPQD
FNLETPGLRD TWITAFSIGG EAYWSVFRYF VDNPGPWLFH CHIELHLMGG MGIAILDGVD
AWPEHIPEEY QVC
