LAC1_TRAMX
ID LAC1_TRAMX Reviewed; 499 AA.
AC D0VWU3;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Laccase {ECO:0000303|PubMed:16944230, ECO:0000303|PubMed:17012782, ECO:0000312|PDB:3DIV};
DE EC=1.10.3.2 {ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782};
DE AltName: Full=Benzenediol:oxygen oxidoreductase {ECO:0000250|UniProtKB:Q12718};
DE AltName: Full=Diphenol oxidase {ECO:0000250|UniProtKB:Q12718};
DE AltName: Full=Urishiol oxidase {ECO:0000250|UniProtKB:Q12718};
OS Trametes maxima (White-rot fungus) (Cerrena maxima).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=259368;
RN [1] {ECO:0000305}
RP CRYSTALLIZATION, PRELIMINARY X-RAY CRYSTALLOGRAPHY, CATALYTIC ACTIVITY,
RP COFACTOR, SUBCELLULAR LOCATION, NITRATION AT TYR-196 AND TYR-372,
RP GLYCOSYLATION AT ASN-54; ASN-217 AND ASN-436, AND DISULFIDE BONDS.
RC STRAIN=0275 {ECO:0000269|PubMed:17012782};
RX PubMed=17012782; DOI=10.1107/s1744309106036578;
RA Lyashenko A.V., Zhukhlistova N.E., Gabdoulkhakov A.G., Zhukova Y.N.,
RA Voelter W., Zaitsev V.N., Bento I., Stepanova E.V., Kachalova G.S.,
RA Koroleva O.V., Cherkashyn E.A., Tishkov V.I., Lamzin V.S., Schirwitz K.,
RA Morgunova E.Y., Betzel C., Lindley P.F., Mikhailov A.M.;
RT "Purification, crystallization and preliminary X-ray study of the fungal
RT laccase from Cerrena maxima.";
RL Acta Crystallogr. F 62:954-957(2006).
RN [2] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBCELLULAR LOCATION, NITRATION AT TYR-196 AND TYR-372,
RP GLYCOSYLATION AT ASN-54; ASN-217; ASN-333 AND ASN-436, COPPER-BINDING
RP SITES, AND DISULFIDE BONDS.
RC STRAIN=0275 {ECO:0000269|PubMed:16944230};
RX PubMed=16944230; DOI=10.1007/s00775-006-0158-x;
RA Lyashenko A.V., Bento I., Zaitsev V.N., Zhukhlistova N.E., Zhukova Y.N.,
RA Gabdoulkhakov A.G., Morgunova E.Y., Voelter W., Kachalova G.S.,
RA Stepanova E.V., Koroleva O.V., Lamzin V.S., Tishkov V.I., Betzel C.,
RA Lindley P.F., Mikhailov A.M.;
RT "X-ray structural studies of the fungal laccase from Cerrena maxima.";
RL J. Biol. Inorg. Chem. 11:963-973(2006).
RN [3] {ECO:0000305, ECO:0000312|PDB:3DIV}
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS), COPPER-BINDING SITES, NITRATION AT
RP TYR-196 AND TYR-372, GLYCOSYLATION AT ASN-54 AND ASN-217, AND DISULFIDE
RP BONDS.
RA Lyashenko A.V., Zhukova Y.N., Mikhailov A.M.;
RL Submitted (JUN-2008) to the PDB data bank.
CC -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC products. {ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782,
CC ECO:0000305}.
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:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000269|PubMed:16944230,
CC ECO:0000269|PubMed:17012782};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16944230,
CC ECO:0000269|PubMed:17012782}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000255}.
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DR PDB; 2H5U; X-ray; 1.90 A; A=2-499.
DR PDB; 3DIV; X-ray; 1.76 A; A=1-499.
DR PDBsum; 2H5U; -.
DR PDBsum; 3DIV; -.
DR AlphaFoldDB; D0VWU3; -.
DR SMR; D0VWU3; -.
DR iPTMnet; D0VWU3; -.
DR EvolutionaryTrace; D0VWU3; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0052716; F:hydroquinone:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0046274; P:lignin catabolic process; TAS:UniProtKB.
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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Disulfide bond; Glycoprotein; Lignin degradation;
KW Metal-binding; Nitration; Oxidoreductase; Repeat; Secreted.
FT CHAIN 1..499
FT /note="Laccase"
FT /id="PRO_0000401149"
FT DOMAIN 2..127
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 139..281
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 348..470
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT BINDING 64
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"
FT BINDING 66
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"
FT BINDING 109
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"
FT BINDING 111
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"
FT BINDING 395
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"
FT BINDING 398
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"
FT BINDING 400
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"
FT BINDING 452
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"
FT BINDING 453
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"
FT BINDING 454
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"
FT BINDING 458
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"
FT MOD_RES 196
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000269|PubMed:16944230,
FT ECO:0000269|PubMed:17012782, ECO:0000269|Ref.3"
FT MOD_RES 372
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000269|PubMed:16944230,
FT ECO:0000269|PubMed:17012782, ECO:0000269|Ref.3"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944230,
FT ECO:0000269|PubMed:17012782, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2H5U"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944230,
FT ECO:0000269|PubMed:17012782, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944230,
FT ECO:0007744|PDB:2H5U"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944230,
FT ECO:0000269|PubMed:17012782, ECO:0007744|PDB:2H5U"
FT DISULFID 85..488
FT /evidence="ECO:0000269|PubMed:16944230,
FT ECO:0000269|PubMed:17012782, ECO:0007744|PDB:2H5U,
FT ECO:0007744|PDB:3DIV"
FT DISULFID 117..205
FT /evidence="ECO:0000269|PubMed:16944230,
FT ECO:0000269|PubMed:17012782, ECO:0007744|PDB:2H5U,
FT ECO:0007744|PDB:3DIV"
FT STRAND 4..15
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:3DIV"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:3DIV"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:3DIV"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:3DIV"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:3DIV"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:3DIV"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:3DIV"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 226..238
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 254..267
FT /evidence="ECO:0007829|PDB:3DIV"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:3DIV"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:3DIV"
FT HELIX 351..356
FT /evidence="ECO:0007829|PDB:3DIV"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 379..385
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:2H5U"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:3DIV"
FT TURN 431..434
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 436..442
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 447..455
FT /evidence="ECO:0007829|PDB:3DIV"
FT HELIX 456..460
FT /evidence="ECO:0007829|PDB:3DIV"
FT STRAND 464..470
FT /evidence="ECO:0007829|PDB:3DIV"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:3DIV"
FT HELIX 474..477
FT /evidence="ECO:0007829|PDB:3DIV"
FT HELIX 482..485
FT /evidence="ECO:0007829|PDB:3DIV"
FT HELIX 487..492
FT /evidence="ECO:0007829|PDB:3DIV"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:3DIV"
SQ SEQUENCE 499 AA; 53451 MW; F018B0357333CF33 CRC64;
AVGPVADNTI TDAATSPDGF SRQAVVVNGV TPGPLVAGNI GDRFQLNVID NLTNHTMLKT
TSVHWHGFFQ QGTNWADGPA FINQCPISPG HSFLYDFQVP NQAGTFWYHS HLSTQYCDGL
RGPFVVYDPN DPHASRYDVD NDDTVITLAD WYHTAAKLGP RFPAGADATL INGKGRAPSD
TSAELSVIKV TKGKRYRFRL VSLSCDPNFT FSIDGHNLTI IEVDSSNSQP LSVDSIQIFA
AQRYSFVLNA NQAVDNYWIR ANPNFGNVGF NGGINSAILR YDGAPAVEPT TNQTTSVKPL
NEVNLHPLVS TPVPGSPSSG GVDKAINMAF NFNGSNFFIN GASFVPPSVP VLLQILSGAQ
TAQDLLPSGS VYVLPSNASI EISFPATAAA PGAPHPFHLH GHTFAVVRSA GSTVYNYSNP
IFRDVVSTGT PAAGDNVTIR FLTNNPGPWF LHCHIDFHLE GGFAVVQAED VPDVKATNPV
PQAWSDLCPT YDANAPSDQ
