MLAC1_METAQ
ID MLAC1_METAQ Reviewed; 613 AA.
AC E9E686;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 2.
DT 03-AUG-2022, entry version 45.
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=MAC_05384;
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102;
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFY88619.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GL698509; EFY88619.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_007811724.1; XM_007813533.1.
DR AlphaFoldDB; E9E686; -.
DR SMR; E9E686; -.
DR STRING; 92637.XP_007811724.1; -.
DR EnsemblFungi; EFY88619; EFY88619; MAC_05384.
DR GeneID; 19249695; -.
DR KEGG; maw:MAC_05384; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_5_0_1; -.
DR InParanoid; E9E686; -.
DR OrthoDB; 454773at2759; -.
DR Proteomes; UP000002499; 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 3: Inferred from homology;
KW Copper; Glycoprotein; Metal-binding; Oxidoreductase; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..613
FT /note="Laccase 1"
FT /id="PRO_0000445735"
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 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; 69080 MW; E937E3FDAEB14B1A CRC64;
MSSSVRLLLI VALLYTNSWA KTVKETLRIT WEEGAPNGQA RELIYTNGQF PGPPLIWDEG
DDVEVTVWNE MAKNVTVHWH GLDQKDSPWS DGTPGLSQRP IQPGQSFVYK FKASPPGNHW
YHSHEKMSLV DGLYGAIHIR PKEDRTGLWS QISQDKEDIK AMEKAARDPE YLVVSDWSQY
TSEEYWKMST DSGLLVFCLD SILVNGKGEV YCPGQEFLQK ELAPGLVQDA FPPGTEVSDK
GCFPADLDQV QGGPWNITKR PDLIPPRVQE GCVASKHENE TIVVDPHRNN GWVSMHIVAA
ATIAQIAFSV DSHEFWLYEI DGNYVNPKKF VSAVMSAGET FSIMMKLDQE PGRYTMRVPN
SGASQVLGAF AEMVYEGHER AEKSGRAYLS YGGNPTSPDV EKNSFFPWQL DTDHMSPWPA
NKPRPGKADE EHLLVLGRVG APYKYTMNTK YLYPVDFQNN DPLLFYPDAT CGTENDGLVL
RTKNGSWVDL ILQVSTLPGD TSSFEHFMHK HGSKTWRIGF GTGVWNYTSV EEAIQERPQD
FNLETPGLRD TWITAFSIGG EAYWSVFRYY VDNPGPWLFH CHIELHLMGG MGIAILDGVD
AWPEHIPEEY RLD
