MLAC1_METAS
ID MLAC1_METAS Reviewed; 602 AA.
AC A0A0B2WJN5;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 03-AUG-2022, entry version 27.
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=MAM_08216;
OS Metarhizium album (strain ARSEF 1941).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1081103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 1941;
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; AZHE01000047; KHN93909.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2WJN5; -.
DR SMR; A0A0B2WJN5; -.
DR EnsemblFungi; KHN93909; KHN93909; MAM_08216.
DR HOGENOM; CLU_006504_5_0_1; -.
DR OrthoDB; 454773at2759; -.
DR Proteomes; UP000030816; 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..602
FT /note="Laccase 1"
FT /id="PRO_5002096638"
FT DOMAIN 30..128
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 157..345
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 461..584
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 108
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 110
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 492
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 495
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 495
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 497
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 566
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 567
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 568
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 572
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 602 AA; 67773 MW; 00CB03EF43B9CA2C CRC64;
MDHFARVSLV AALLYTNTWA KTVRETLRIT WEEGAPNGQQ RELIYINGRF PGPNLVWDED
DDVEVTVIND MTQSVTVHWH GLDQRPIQPG DSFVHKFKAF PPGNHWYHSH QKMSLVDGLY
GAVHVRPKGD RKGLWSQISQ DDKDIEAMEK AACDPEYLVV SDWSQYTSDE YWKISNDSGL
PVFCLDSILV NGKGEVYCPG QKFLQGELAP GVLDAFPPGT EVSDKGCFSP ALDRIKGGPW
NMTERPDLIP PHVETGCVAS RHENETIVVD PGRNNGWVSM HIVAAATIAQ IAISFDSHKF
WLYEVDGNYV NPREYFSAII SAGETFSIMM KLDQEPGRYT VRIPNTGASQ VFSAFAEMVY
KGHEENDKKL GEARLSYGGV PTSPEIKNNS YFPWKLDTDH MSPWPPSTPR PGNADEEHLL
VLGRVGSPNN HTMNAKYLYP LGFRDEEPLL FYPNATLGTE NEGLLLRTRN ASWVDLIMQV
STLAGDEVAF KHFIHKHGGK TWRIGFGTGV WNYSSVQEAI QARPNDFNLE TPGFRDTWIT
APSASGEKHW SVLRYYVDNP GPWLLHCHIE LHLMGGMGMV IMDGVDAWPD QLPEQYRLGK
RL
