LAC2_TRAVE
ID LAC2_TRAVE Reviewed; 519 AA.
AC Q12718; Q12716;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Laccase-2;
DE EC=1.10.3.2 {ECO:0000250|UniProtKB:Q70KY3};
DE AltName: Full=Benzenediol:oxygen oxidoreductase 2;
DE AltName: Full=Diphenol oxidase 2;
DE AltName: Full=Laccase I;
DE AltName: Full=Urishiol oxidase 2;
DE Flags: Precursor;
GN Name=LCC2; Synonyms=LCCI;
OS Trametes versicolor (White-rot fungus) (Coriolus versicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5325;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 20869 / PAP 52 / 52J;
RX PubMed=9322748; DOI=10.1016/s0378-1119(97)00215-1;
RA Ong E., Pollock W.B., Smith M.;
RT "Cloning and sequence analysis of two laccase complementary DNAs from the
RT ligninolytic basidiomycete Trametes versicolor.";
RL Gene 196:113-119(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 21-519, COFACTOR, SUBCELLULAR
RP LOCATION, COPPER-BINDING SITES, GLYCOSYLATION AT ASN-74; ASN-237; ASN-271;
RP ASN-353; ASN-361 AND ASN-456, AND DISULFIDE BONDS.
RX PubMed=12163489; DOI=10.1074/jbc.m204571200;
RA Piontek K., Antorini M., Choinowski T.;
RT "Crystal structure of a laccase from the fungus Trametes versicolor at
RT 1.90-A resolution containing a full complement of coppers.";
RL J. Biol. Chem. 277:37663-37669(2002).
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:0000269|PubMed:12163489};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000269|PubMed:12163489};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12163489}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; U44851; AAA86659.1; -; Genomic_DNA.
DR EMBL; U44430; AAC49828.1; -; mRNA.
DR PDB; 1GYC; X-ray; 1.90 A; A=21-519.
DR PDBsum; 1GYC; -.
DR AlphaFoldDB; Q12718; -.
DR SMR; Q12718; -.
DR CAZy; AA1; Auxiliary Activities 1.
DR iPTMnet; Q12718; -.
DR BioCyc; MetaCyc:MON-17211; -.
DR BRENDA; 1.10.3.2; 1626.
DR SABIO-RK; Q12718; -.
DR EvolutionaryTrace; Q12718; -.
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; 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; Oxidoreductase; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..519
FT /note="Laccase-2"
FT /id="PRO_0000002940"
FT DOMAIN 22..147
FT /note="Plastocyanin-like 1"
FT DOMAIN 159..301
FT /note="Plastocyanin-like 2"
FT DOMAIN 368..490
FT /note="Plastocyanin-like 3"
FT BINDING 84
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:12163489,
FT ECO:0007744|PDB:1GYC"
FT BINDING 86
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:12163489,
FT ECO:0007744|PDB:1GYC"
FT BINDING 129
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:12163489,
FT ECO:0007744|PDB:1GYC"
FT BINDING 131
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:12163489,
FT ECO:0007744|PDB:1GYC"
FT BINDING 415
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:12163489,
FT ECO:0007744|PDB:1GYC"
FT BINDING 418
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:12163489,
FT ECO:0007744|PDB:1GYC"
FT BINDING 420
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:12163489,
FT ECO:0007744|PDB:1GYC"
FT BINDING 472
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:12163489,
FT ECO:0007744|PDB:1GYC"
FT BINDING 473
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:12163489,
FT ECO:0007744|PDB:1GYC"
FT BINDING 474
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:12163489,
FT ECO:0007744|PDB:1GYC"
FT BINDING 478
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:12163489,
FT ECO:0007744|PDB:1GYC"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12163489,
FT ECO:0007744|PDB:1GYC"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12163489,
FT ECO:0007744|PDB:1GYC"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12163489,
FT ECO:0007744|PDB:1GYC"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12163489,
FT ECO:0007744|PDB:1GYC"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12163489,
FT ECO:0007744|PDB:1GYC"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12163489,
FT ECO:0007744|PDB:1GYC"
FT DISULFID 105..508
FT /evidence="ECO:0000269|PubMed:12163489,
FT ECO:0007744|PDB:1GYC"
FT DISULFID 137..225
FT /evidence="ECO:0000269|PubMed:12163489,
FT ECO:0007744|PDB:1GYC"
FT CONFLICT 69
FT /note="D -> V (in Ref. 1; AAC49828)"
FT /evidence="ECO:0000305"
FT STRAND 24..35
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:1GYC"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:1GYC"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1GYC"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:1GYC"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:1GYC"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1GYC"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:1GYC"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 246..258
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 274..287
FT /evidence="ECO:0007829|PDB:1GYC"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:1GYC"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:1GYC"
FT HELIX 371..376
FT /evidence="ECO:0007829|PDB:1GYC"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 390..394
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 399..405
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 416..419
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 442..447
FT /evidence="ECO:0007829|PDB:1GYC"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 456..462
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 467..475
FT /evidence="ECO:0007829|PDB:1GYC"
FT HELIX 476..480
FT /evidence="ECO:0007829|PDB:1GYC"
FT STRAND 484..489
FT /evidence="ECO:0007829|PDB:1GYC"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:1GYC"
FT HELIX 494..497
FT /evidence="ECO:0007829|PDB:1GYC"
FT HELIX 502..512
FT /evidence="ECO:0007829|PDB:1GYC"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:1GYC"
SQ SEQUENCE 519 AA; 55811 MW; BFFB5B4CD0007702 CRC64;
MGLQRFSFFV TLALVARSLA AIGPVASLVV ANAPVSPDGF LRDAIVVNGV VPSPLITGKK
GDRFQLNVDD TLTNHSMLKS TSIHWHGFFQ AGTNWADGPA FVNQCPIASG HSFLYDFHVP
DQAGTFWYHS HLSTQYCDGL RGPFVVYDPK DPHASRYDVD NESTVITLTD WYHTAARLGP
RFPLGADATL INGLGRSAST PTAALAVINV QHGKRYRFRL VSISCDPNYT FSIDGHNLTV
IEVDGINSQP LLVDSIQIFA AQRYSFVLNA NQTVGNYWVR ANPNFGTVGF AGGINSAILR
YQGAPVAEPT TTQTTSVIPL IETNLHPLAR MPVPGSPTPG GVDKALNLAF NFNGTNFFIN
NATFTPPTVP VLLQILSGAQ TAQDLLPAGS VYPLPAHSTI EITLPATALA PGAPHPFHLH
GHAFAVVRSA GSTTYNYNDP IFRDVVSTGT PAAGDNVTIR FQTDNPGPWF LHCHIDFHLD
AGFAIVFAED VADVKAANPV PKAWSDLCPI YDGLSEANQ
