MLAC1_METRA
ID MLAC1_METRA Reviewed; 613 AA.
AC E9F648;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 2.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Laccase 1 {ECO:0000303|PubMed:28447400};
DE EC=1.10.3.- {ECO:0000305|PubMed:28447400};
DE AltName: Full=Conidial pigment biosynthesis oxidase Mlac1 {ECO:0000303|PubMed:28447400};
DE Flags: Precursor;
GN Name=Mlac1 {ECO:0000303|PubMed:28447400};
GN Synonyms=Abr2 {ECO:0000303|PubMed:29958281}; ORFNames=MAA_07747;
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
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 GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
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 [3]
RP FUNCTION.
RX PubMed=25445307; DOI=10.1016/j.fgb.2014.10.018;
RA Chen Y., Feng P., Shang Y., Xu Y.J., Wang C.;
RT "Biosynthesis of non-melanin pigment by a divergent polyketide synthase in
RT Metarhizium robertsii.";
RL Fungal Genet. Biol. 81:142-149(2015).
RN [4]
RP IDENTIFICATION, FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28447400; DOI=10.1111/1462-2920.13777;
RA Zeng G., Chen X., Zhang X., Zhang Q., Xu C., Mi W., Guo N., Zhao H.,
RA You Y., Dryburgh F.J., Bidochka M.J., St Leger R.J., Zhang L., Fang W.;
RT "Genome-wide identification of pathogenicity, conidiation and colony
RT sectorization genes in Metarhizium robertsii.";
RL Environ. Microbiol. 19:3896-3908(2017).
RN [5]
RP IDENTIFICATION, AND FUNCTION.
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:28447400, 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 (PubMed:25445307,
CC PubMed:28447400, PubMed:29958281). The dehydratase EthD and the laccase
CC Mlac1 further convert the anthraquinone derivative into the final
CC conidial pigment (PubMed:28447400, PubMed:29958281).
CC {ECO:0000269|PubMed:25445307, ECO:0000269|PubMed:28447400,
CC ECO:0000269|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:28447400}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:E9RBR0}.
CC -!- INDUCTION: Highly expressed during conidiation (PubMed:28447400). A
CC conserved conidiation regulatory pathway containing BrlA, AbaA and WetA
CC regulates expression. During conidiation BlrA up-regulates AbaA, which
CC in turn controls WetA. Moreover, the Hog1 MAPK regulates fungal
CC conidiation by controlling the conidiation regulatory pathway, and that
CC all three pigmentation genes Pks1, EthD and Mlac1 exercise feedback
CC regulation of conidiation (PubMed:28447400).
CC {ECO:0000269|PubMed:28447400}.
CC -!- DISRUPTION PHENOTYPE: Reduces significantly the conidial yields.
CC {ECO:0000269|PubMed:28447400}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; ADNJ02000010; EFY96686.2; -; Genomic_DNA.
DR RefSeq; XP_007823936.2; XM_007825745.2.
DR AlphaFoldDB; E9F648; -.
DR SMR; E9F648; -.
DR EnsemblFungi; EFY96686; EFY96686; MAA_07747.
DR GeneID; 19262033; -.
DR KEGG; maj:MAA_07747; -.
DR HOGENOM; CLU_006504_5_0_1; -.
DR Proteomes; UP000002498; 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..613
FT /note="Laccase 1"
FT /id="PRO_5003239663"
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; 69133 MW; 92B7A95B3A0724A1 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
ATTAQITFSV DSHEFWLYEI DGNYVNPRKF VSAVMSAGET FSVMIKLDQE PGKYTMRIPN
SGASQVLGGF AEMVYKGCER EEKAGKAYLS YGGNPTSPDV EKNSFFPWQL DTDHMSPWPP
NKPRPGNADE EHLLVLGRVG APYNYTMNTK YLYPVDFQND DPLLFYPNAT RDTENDGLVL
RTKNGSWVDL ILQVSTLPGD TASFEHFMHK HGSKTWRIGF GTGVWNYTSV EEAIQERPQD
FNLETPGLRD TWITAFSIGG EAYWSVFRYF VDNPGPWLFH CHIELHLMGG MGIAILDGVD
AWPEHIPEEY QLR
