LAC1_EMENI
ID LAC1_EMENI Reviewed; 609 AA.
AC P17489; C8V1C0; Q5AYJ5;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Laccase-1;
DE EC=1.10.3.2 {ECO:0000250|UniProtKB:Q70KY3};
DE AltName: Full=Benzenediol:oxygen oxidoreductase 1;
DE AltName: Full=Conidial laccase;
DE AltName: Full=Diphenol oxidase 1;
DE AltName: Full=Laccase I;
DE AltName: Full=Urishiol oxidase 1;
DE Flags: Precursor;
GN Name=yA; ORFNames=AN6635;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139, and Winter;
RX PubMed=2192364; DOI=10.1093/nar/18.11.3415;
RA Aramayo R., Timberlake W.E.;
RT "Sequence and molecular structure of the Aspergillus nidulans yA (laccase
RT I) gene.";
RL Nucleic Acids Res. 18:3415-3415(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=2659435; DOI=10.1093/genetics/121.2.249;
RA O'Hara E.B., Timberlake W.E.;
RT "Molecular characterization of the Aspergillus nidulans yA locus.";
RL Genetics 121:249-254(1989).
CC -!- FUNCTION: Required for the conversion of the yellow polyketide pigment
CC synthesized by wA to the conidial green pigment.
CC {ECO:0000269|PubMed:2659435}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O;
CC Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2;
CC Evidence={ECO:0000250|UniProtKB:Q70KY3};
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q70KY3}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed late during asexual
CC development. {ECO:0000269|PubMed:2659435}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; X52552; CAA36787.1; -; Genomic_DNA.
DR EMBL; AACD01000110; EAA58164.1; -; Genomic_DNA.
DR EMBL; BN001301; CBF71142.1; -; Genomic_DNA.
DR PIR; S10149; KSASL1.
DR RefSeq; XP_664239.1; XM_659147.1.
DR AlphaFoldDB; P17489; -.
DR SMR; P17489; -.
DR STRING; 162425.CADANIAP00007416; -.
DR EnsemblFungi; CBF71142; CBF71142; ANIA_06635.
DR EnsemblFungi; EAA58164; EAA58164; AN6635.2.
DR GeneID; 2870381; -.
DR KEGG; ani:AN6635.2; -.
DR VEuPathDB; FungiDB:AN6635; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_5_0_1; -.
DR InParanoid; P17489; -.
DR OMA; HITTHQE; -.
DR OrthoDB; 454773at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0052716; F:hydroquinone:oxygen oxidoreductase activity; IDA:AspGD.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0048315; P:conidium formation; IMP:AspGD.
DR GO; GO:0043324; P:pigment metabolic process involved in developmental pigmentation; IMP:AspGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; 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; 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; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 2: Evidence at transcript level;
KW Conidiation; Copper; Glycoprotein; Metal-binding; Oxidoreductase;
KW Reference proteome; Repeat; Secreted; Signal; Sporulation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..609
FT /note="Laccase-1"
FT /id="PRO_0000002927"
FT DOMAIN 45..141
FT /note="Plastocyanin-like 1"
FT DOMAIN 270..372
FT /note="Plastocyanin-like 2"
FT DOMAIN 463..602
FT /note="Plastocyanin-like 3"
FT BINDING 79
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 81
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 123
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 125
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 508
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 511
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 513
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 585
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 586
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 587
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 591
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 225..229
FT /note="DGLTA -> TALLS (in Ref. 1; CAA36787)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="G -> A (in Ref. 1; CAA36787)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="G -> A (in Ref. 1; CAA36787)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 609 AA; 67981 MW; 529A20B2DD9AA73E CRC64;
MYLSTVLFPL LALNLGLSHA RFVRETLELT WEYGSPNGGT PREMVFTNGE YPGPDLIFDE
DDDVEVLVIN NLPFNTTVHW HGLEMRETPE ADGVPGLTQT PIEPGATFTY RFRAYPAGTF
WYHSHYKGLM QDGQVGAMYI RRKPDALRPY AVITEDPREL AEIQYAEDNP YLMLATDWTY
LTSAEYHNIE VESGYNVFCV DSLLINGRGS VYCPGYQYLE EVSDDGLTAV LEGTHLTEKG
CLQPDLHNVQ GDYGPWNLSA VPTEVVFNCT PSSVEPPVIY VDPEFNGWVS LNFIGGAAQK
AITFSVDNHP MWVYEVDGQF VEPREVEMVG VYSGARYAVM IKLDQTPGDY AIRIAVNGGD
QVMSVYAILS YVNQDWIHRE NVPKAAIGPH TDTVGYMNYG GGNTSADVRQ LLFTENLPAF
GVPPPPPSSE VSTTLRTGMI RVNNSYSWSL GNNVLYEPEM TSSTPLLFEP DPLAVIAPKY
ALTTENNTWV DIVLEITADP RDLIHPPHPI HKHGNRAYII GNGVGKFRWE NVSAAEAEVP
DLFYVNETAA LRDTFVTDFF DSRLMDGAWI VIRYFVQDKF PSILHCHIAS HQMGGMALAL
LDGVDVWDS
