LAC1_MELAO
ID LAC1_MELAO Reviewed; 623 AA.
AC Q70KY3; Q7SIE6;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Laccase-1;
DE EC=1.10.3.2 {ECO:0000269|PubMed:12111146};
DE AltName: Full=Benzenediol:oxygen oxidoreductase 1;
DE AltName: Full=Diphenol oxidase 1;
DE AltName: Full=Ligninolytic phenoloxidase;
DE AltName: Full=Urishiol oxidase 1;
DE Flags: Precursor;
GN Name=LAC1;
OS Melanocarpus albomyces.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Melanocarpus.
OX NCBI_TaxID=204285;
RN [1] {ECO:0000312|EMBL:CAE00180.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14711635; DOI=10.1128/aem.70.1.137-144.2004;
RA Kiiskinen L.-L., Saloheimo M.;
RT "Molecular cloning and expression in Saccharomyces cerevisiae of a laccase
RT gene from the ascomycete Melanocarpus albomyces.";
RL Appl. Environ. Microbiol. 70:137-144(2004).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 51-78; 214-228 AND 507-517, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC STRAIN=VTT D-96490 {ECO:0000269|PubMed:12111146};
RX PubMed=12111146; DOI=10.1007/s00253-002-1012-x;
RA Kiiskinen L.-L., Viikari L., Kruus K.;
RT "Purification and characterisation of a novel laccase from the ascomycete
RT Melanocarpus albomyces.";
RL Appl. Microbiol. Biotechnol. 59:198-204(2002).
RN [3] {ECO:0000305}
RP PROBABLE FUNCTION.
RX PubMed=15474046; DOI=10.1016/j.febslet.2004.08.040;
RA Kiiskinen L.-L., Palonen H., Linder M., Viikari L., Kruus K.;
RT "Laccase from Melanocarpus albomyces binds effectively to cellulose.";
RL FEBS Lett. 576:251-255(2004).
RN [4] {ECO:0000305, ECO:0000312|EMBL:CAE00180.1}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 51-609 IN COMPLEX WITH COFACTOR
RP AND OXYGEN, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GLYCOSYLATION AT
RP ASN-89; ASN-138; ASN-251; ASN-266; ASN-294; ASN-339; ASN-426 AND ASN-446,
RP AND DISULFIDE BONDS.
RX PubMed=12118243; DOI=10.1038/nsb823;
RA Hakulinen N., Kiiskinen L.-L., Kruus K., Saloheimo M., Paananen A.,
RA Koivula A., Rouvinen J.;
RT "Crystal structure of a laccase from Melanocarpus albomyces with an intact
RT trinuclear copper site.";
RL Nat. Struct. Biol. 9:601-605(2002).
CC -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC products. {ECO:0000269|PubMed:15474046, 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:12111146};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:12111146, ECO:0000269|PubMed:12118243};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000269|PubMed:12111146,
CC ECO:0000269|PubMed:12118243};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=280 nm {ECO:0000269|PubMed:12111146,
CC ECO:0000269|PubMed:12118243};
CC Note=Exhibits a shoulder at 360 nm, a smaller absorption peak at 450
CC nm, and a second, larger peak at 590 nm.
CC {ECO:0000269|PubMed:12118243};
CC pH dependence:
CC Optimum pH is 3.5 with 2,2'-azinobis-(3-ethylbenzthiazoline-6-
CC sulphonate) as substrate, 5.0-7.5 with guiacol as substrate, and 6.0-
CC 7.0 with syringaldazine as substrate. {ECO:0000269|PubMed:12111146,
CC ECO:0000269|PubMed:12118243};
CC Temperature dependence:
CC Optimum temperature is 60-70 degrees Celsius.
CC {ECO:0000269|PubMed:12111146, ECO:0000269|PubMed:12118243};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12118243}.
CC -!- TISSUE SPECIFICITY: Secreted protein; extracellular space.
CC {ECO:0000269|PubMed:12111146}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000255}.
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DR EMBL; AJ571698; CAE00180.1; -; Genomic_DNA.
DR PDB; 1GW0; X-ray; 2.40 A; A/B=51-609.
DR PDB; 2IH8; X-ray; 2.00 A; A/B=51-609.
DR PDB; 2IH9; X-ray; 2.00 A; A/B=51-609.
DR PDB; 2Q9O; X-ray; 1.30 A; A/B=51-609.
DR PDB; 3DKH; X-ray; 2.40 A; A/B=51-609.
DR PDB; 3FU7; X-ray; 1.67 A; A/B=51-609.
DR PDB; 3FU8; X-ray; 1.80 A; A/B=51-609.
DR PDB; 3FU9; X-ray; 2.00 A; A/B=51-609.
DR PDB; 3QPK; X-ray; 1.90 A; A/B=51-609.
DR PDBsum; 1GW0; -.
DR PDBsum; 2IH8; -.
DR PDBsum; 2IH9; -.
DR PDBsum; 2Q9O; -.
DR PDBsum; 3DKH; -.
DR PDBsum; 3FU7; -.
DR PDBsum; 3FU8; -.
DR PDBsum; 3FU9; -.
DR PDBsum; 3QPK; -.
DR AlphaFoldDB; Q70KY3; -.
DR SMR; Q70KY3; -.
DR CAZy; AA1; Auxiliary Activities 1.
DR iPTMnet; Q70KY3; -.
DR BRENDA; 1.10.3.2; 3208.
DR EvolutionaryTrace; Q70KY3; -.
DR GO; GO:0043245; C:extraorganismal space; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0052716; F:hydroquinone:oxygen oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0030245; P:cellulose catabolic process; TAS:UniProtKB.
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; 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 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Lignin degradation; Metal-binding; Oxidoreductase; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..50
FT /evidence="ECO:0000255, ECO:0000269|PubMed:12111146"
FT /id="PRO_0000235826"
FT CHAIN 51..609
FT /note="Laccase-1"
FT /evidence="ECO:0000269|PubMed:12118243"
FT /id="PRO_0000235827"
FT PROPEP 610..623
FT /evidence="ECO:0000269|PubMed:12118243"
FT /id="PRO_0000235828"
FT BINDING 143
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:12118243"
FT BINDING 145
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:12118243"
FT BINDING 188
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:12118243"
FT BINDING 190
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:12118243"
FT BINDING 481
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:12118243"
FT BINDING 484
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:12118243"
FT BINDING 486
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:12118243"
FT BINDING 552
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:12118243"
FT BINDING 553
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:12118243"
FT BINDING 554
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:12118243"
FT BINDING 558
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:12118243"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12118243"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12118243"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12118243"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12118243"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12118243"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12118243"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12118243"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12118243"
FT DISULFID 54..62
FT /evidence="ECO:0000269|PubMed:12118243"
FT DISULFID 164..590
FT /evidence="ECO:0000269|PubMed:12118243"
FT DISULFID 348..382
FT /evidence="ECO:0000269|PubMed:12118243"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:2Q9O"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 83..97
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2Q9O"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:2Q9O"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:2Q9O"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:2Q9O"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 214..225
FT /evidence="ECO:0007829|PDB:2Q9O"
FT HELIX 230..237
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:2Q9O"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 274..281
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 333..341
FT /evidence="ECO:0007829|PDB:2Q9O"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 357..362
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:3FU9"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 408..414
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:3DKH"
FT HELIX 438..444
FT /evidence="ECO:0007829|PDB:2Q9O"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 455..458
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 464..471
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 481..488
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 490..496
FT /evidence="ECO:0007829|PDB:2Q9O"
FT HELIX 511..514
FT /evidence="ECO:0007829|PDB:2Q9O"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 525..531
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 535..542
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 547..553
FT /evidence="ECO:0007829|PDB:2Q9O"
FT HELIX 556..560
FT /evidence="ECO:0007829|PDB:2Q9O"
FT STRAND 564..569
FT /evidence="ECO:0007829|PDB:2Q9O"
FT HELIX 571..574
FT /evidence="ECO:0007829|PDB:2Q9O"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:2Q9O"
FT HELIX 580..596
FT /evidence="ECO:0007829|PDB:2Q9O"
FT HELIX 597..599
FT /evidence="ECO:0007829|PDB:2Q9O"
SQ SEQUENCE 623 AA; 68958 MW; A322F89B438784E1 CRC64;
MKTFTSALAL VVGMLAPGAV VAAPPSTPAQ RDLVELREAR QEGGKDLRPR EPTCNTPSNR
ACWSDGFDIN TDYEVSTPDT GVTQSYVFNL TEVDNWMGPD GVVKEKVMLI NGNIMGPNIV
ANWGDTVEVT VINNLVTNGT SIHWHGIHQK DTNLHDGANG VTECPIPPKG GQRTYRWRAR
QYGTSWYHSH FSAQYGNGVV GTIQINGPAS LPYDIDLGVF PITDYYYRAA DDLVHFTQNN
APPFSDNVLI NGTAVNPNTG EGQYANVTLT PGKRHRLRIL NTSTENHFQV SLVNHTMTVI
AADMVPVNAM TVDSLFLAVG QRYDVVIDAS RAPDNYWFNV TFGGQAACGG SLNPHPAAIF
HYAGAPGGLP TDEGTPPVDH QCLDTLDVRP VVPRSVPVNS FVKRPDNTLP VALDLTGTPL
FVWKVNGSDI NVDWGKPIID YILTGNTSYP VSDNIVQVDA VDQWTYWLIE NDPEGPFSLP
HPMHLHGHDF LVLGRSPDVP AASQQRFVFD PAVDLARLNG DNPPRRDTTM LPAGGWLLLA
FRTDNPGAWL FHCHIAWHVS GGLSVDFLER PADLRQRISQ EDEDDFNRVC DEWRAYWPTN
PYPKIDSGLK RRRWVEESEW LVR
