LAC4_THACU
ID LAC4_THACU Reviewed; 531 AA.
AC Q02081;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Laccase-4;
DE EC=1.10.3.2 {ECO:0000250|UniProtKB:Q70KY3};
DE AltName: Full=Benzenediol:oxygen oxidoreductase 4;
DE AltName: Full=Diphenol oxidase 4;
DE AltName: Full=Urishiol oxidase 4;
DE Flags: Precursor;
GN Name=LCC4;
OS Thanatephorus cucumeris (Black scurf of potato) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Thanatephorus.
OX NCBI_TaxID=107832;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC STRAIN=R22 / IMI 358730 / AG-6;
RX PubMed=8598061; DOI=10.1007/bf02208621;
RA Wahleithner J.A., Xu F., Brown K.M., Brown S.H., Golightly E.J.,
RA Halkier T., Kauppinen S., Pederson A., Schneider P.;
RT "The identification and characterization of four laccases from the plant
RT pathogenic fungus Rhizoctonia solani.";
RL Curr. Genet. 29:395-403(1996).
CC -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC products. {ECO:0000250|UniProtKB:Q70KY3}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:8598061};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q99046}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q70KY3}.
CC -!- TISSUE SPECIFICITY: In mycelia, at a higher level than LCC1, LCC2 and
CC LCC3. {ECO:0000269|PubMed:8598061}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; Z54277; CAA91042.1; -; Genomic_DNA.
DR PIR; S68120; S68120.
DR AlphaFoldDB; Q02081; -.
DR SMR; Q02081; -.
DR CAZy; AA1; Auxiliary Activities 1.
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; IEA:UniProtKB-EC.
DR GO; GO:0046274; P:lignin catabolic process; 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; 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.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Lignin degradation; Metal-binding; Oxidoreductase; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..19
FT CHAIN 20..531
FT /note="Laccase-4"
FT /id="PRO_0000002938"
FT DOMAIN 23..146
FT /note="Plastocyanin-like 1"
FT DOMAIN 158..315
FT /note="Plastocyanin-like 2"
FT DOMAIN 384..507
FT /note="Plastocyanin-like 3"
FT BINDING 83
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 85
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 128
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 130
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 427
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 430
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 432
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 479
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 480
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 481
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 CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..528
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT VARIANT 42
FT /note="P -> S"
FT VARIANT 119
FT /note="H -> R"
FT VARIANT 246
FT /note="R -> S"
FT VARIANT 256
FT /note="P -> L"
FT VARIANT 261
FT /note="P -> A"
SQ SEQUENCE 531 AA; 57545 MW; 737339803F75AB19 CRC64;
MLSSITLLPL LAAVSTPAFA AVRNYKFDIK NVNVAPDGFQ RPIVSVNGLV PGTLITANKG
DTLRINVTNQ LTDPSMRRAT TIHWHGLFQA TTADEDGPAF VTQCPIAQNL SYTYEIPLHG
QTGTMWYHAH LASQYVDGLR GPLVIYDPND PHKSRYDVDD ASTVVMLEDW YHTPAPVLEK
QMFSTNNTAL LSPVPDSGLI NGKGRYVGGP AVPRSVINVK RGKRYRLRVI NASAIGSFTF
SIEGHRLTVI EADGIPHQPL PVDSFQIYAG QRYSVIVEAN QTAANYWIRA PMTVAGAGTN
ANLDPTNVFA VLHYEGAPNA EPTTEQGSAI GTALVEENLH ALINPGAPGG SAPADVSLNL
AIGRSTVDGI LRFTFNNIKY EAPSLPTLLK ILANNASNDA DFTPNEHTIV LPHNKVIGAQ
HHRGADHPIH LHGHVFDIVK SLGGTPNYVN PPRRDVVRVG GTGVVLRFKA DNPGPWFVHC
HIDCTWRLGS HLSLPRPPAR FARVSSRSSP TMPGTSSAPS TRLFLPICSK W
