MLAC1_METMF
ID MLAC1_METMF Reviewed; 614 AA.
AC A0A0B4HQH6;
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=MAJ_09464;
OS Metarhizium majus (strain ARSEF 297).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC Metarhizium majus.
OX NCBI_TaxID=1276143;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 297;
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; AZNE01000110; KID94572.1; -; Genomic_DNA.
DR RefSeq; XP_014573566.1; XM_014718080.1.
DR AlphaFoldDB; A0A0B4HQH6; -.
DR SMR; A0A0B4HQH6; -.
DR EnsemblFungi; KID94572; KID94572; MAJ_09464.
DR HOGENOM; CLU_006504_5_0_1; -.
DR OrthoDB; 454773at2759; -.
DR Proteomes; UP000031176; 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; Repeat; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..614
FT /note="Laccase 1"
FT /id="PRO_5002105906"
FT DOMAIN 30..143
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 172..360
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 469..599
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT BINDING 79
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 81
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 123
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 125
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 507
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 510
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 510
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 512
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="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 582
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 583
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 587
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 614 AA; 69084 MW; 0D27A0F7B81DEE32 CRC64;
MSRFARLLLM VVALFFTNAW AKTVKETLRI TWKEGAPNGQ ARELIYTNGQ FPSPTLVWDE
DDDVEITVYN EMAKNVTVHW HGLDQKDTPW SDGTPGLSQR PIQPGNKFVY KFKASPPGNH
WYHSHEKMSL VDGLYGAIHI RPKGDRTGLW SQISQDKDDI KAMENAAHDP EYLVVSDWSQ
YTSEEYWKIS TDSGLLVFCL DSILVNGKGE VYCPGQKFLQ AELAPGLVED AFPPGTEVSD
KGCFPADLDQ VQGGPWNITK RPDLIPPRVQ EGCVASSHEN ATIVVDPSRN NGWVSMHIVA
AATIAQITFS VDSHEFWLYE IDGNYVNPRK FVSAVMSAGE TFSVMIKLDQ KPGRYTMRIP
NSGASQVLGG FAEMVYKGCE SEEKTGKAYL SYGGNPTSPD VEKNSFFPWQ LDTDHMSPWP
PNKPRPGNAD EEHLLVLGRV GAPYNYTMNT KYLYPVDFQN DDPLLFYPNA TRDTENDGLV
LRTKNGSWVD LILQVSTLPG DTSSFEHFMH KHGSKTWRIG FGTGVWNYTS VEEAIKERPK
DFNLETPGLR DTWITAFSIG GEAYWSVFRY FVDNPGPWLF HCHIELHLMG GMGIAILDGV
DAWPEHIPEE YQLC
