[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1128/AEM.70.1.137-144.2004; PubMed=14711635 [NCBI, ExPASy, EBI, Israel, Japan] Kiiskinen L.-L., Saloheimo M.; "Molecular cloning and expression in Saccharomyces cerevisiae of a laccase gene from the ascomycete Melanocarpus albomyces."; Appl. Environ. Microbiol. 70:137-144(2004).
[2]	PROTEIN SEQUENCE OF 51-78; 214-228 AND 507-517, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY. STRAIN=VTT D-96490; DOI=10.1007/s00253-002-1012-x; PubMed=12111146 [NCBI, ExPASy, EBI, Israel, Japan] Kiiskinen L.-L., Viikari L., Kruus K.; "Purification and characterisation of a novel laccase from the ascomycete Melanocarpus albomyces."; Appl. Microbiol. Biotechnol. 59:198-204(2002).
[3]	PROBABLE FUNCTION. DOI=10.1016/j.febslet.2004.08.040; PubMed=15474046 [NCBI, ExPASy, EBI, Israel, Japan] Kiiskinen L.-L., Palonen H., Linder M., Viikari L., Kruus K.; "Laccase from Melanocarpus albomyces binds effectively to cellulose."; FEBS Lett. 576:251-255(2004).
[4]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 51-609 IN COMPLEX WITH COFACTOR AND OXYGEN, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GLYCOSYLATION AT ASN-89; ASN-138; ASN-251; ASN-266; ASN-294; ASN-339; ASN-426 AND ASN-446, AND DISULFIDE BONDS. DOI=10.1038/nsb823; PubMed=12118243 [NCBI, ExPASy, EBI, Israel, Japan] Hakulinen N., Kiiskinen L.-L., Kruus K., Saloheimo M., Paananen A., Koivula A., Rouvinen J.; "Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site."; Nat. Struct. Biol. 9:601-605(2002).

Comments

FUNCTION: Lignin degradation and detoxification of lignin-derived products (Probable).
CATALYTIC ACTIVITY: 4 benzenediol + O₂ = 4 benzosemiquinone + 2 H₂O.
COFACTOR: Binds 4 copper ions per monomer.

BIOPHYSICOCHEMICAL PROPERTIES:

Absorption:	Abs(max)=280 nm;
Absorption:	Note=Exhibits a shoulder at 360 nm, a smaller absorption peak at 450 nm, and a second, larger peak at 590 nm;
pH dependence:	Optimum pH is 3.5 with 2,2'-azinobis-(3-ethylbenzthiazoline-6- sulphonate) as substrate, 5.0-7.5 with guiacol as substrate, and 6.0-7.0 with syringaldazine as substrate;
Temperature dependence:	Optimum temperature is 60-70 degrees Celsius;

SUBUNIT: Monomer.
TISSUE SPECIFICITY: Secreted protein; extracellular space.
SIMILARITY: Belongs to the multicopper oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ571698; CAE00180.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1GW0; X-ray; 2.40 A; A/B=51-609.	[ExPASy / RCSB / EBI]
2IH8; X-ray; 2.00 A; A/B=51-609.	[ExPASy / RCSB / EBI]
2IH9; X-ray; 2.00 A; A/B=51-609.	[ExPASy / RCSB / EBI]
2Q9O; X-ray; 1.30 A; A/B=51-609.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1GW0; -.
2IH8; -.
2IH9; -.
2Q9O; -.

ModBase

Q70KY3.

Ontologies

GO:0043245;	Cellular component: extraorganismal space (inferred from direct assay from UniProtKB).
GO:0005507;	Molecular function: copper ion binding (inferred from direct assay from UniProtKB).
GO:0008471;	Molecular function: laccase activity (inferred from direct assay from UniProtKB).
GO:0030245;	Biological process: cellulose catabolic process (traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR001117; Cu-oxidase.
IPR011706; Cu-oxidase_2.
IPR011707; Cu-oxidase_3.
IPR002355; Cu_oxidase_Cu_BS.
IPR008972; Cupredoxin.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.420; Cupredoxin; 3.

Pfam

PF00394; Cu-oxidase; 1.
PF07731; Cu-oxidase_2; 1.
PF07732; Cu-oxidase_3; 1.
Pfam graphical view of domain structure.

PROSITE

PS00079; MULTICOPPER_OXIDASE1; 1.
PS00080; MULTICOPPER_OXIDASE2; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Copper; Direct protein sequencing; Glycoprotein; Lignin degradation; Metal-binding; Oxidoreductase; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 22`	`22`	`Potential.`
`PROPEP`	`23 50`	`28`		`PRO_0000235826`
`CHAIN`	`51 609`	`559`	`Laccase-1.`	`PRO_0000235827`
`PROPEP`	`610 623`	`14`		`PRO_0000235828`
`METAL`	`143 143`		`Copper 1.`
`METAL`	`145 145`		`Copper 2.`
`METAL`	`188 188`		`Copper 2.`
`METAL`	`190 190`		`Copper 3.`
`METAL`	`481 481`		`Copper 4.`
`METAL`	`484 484`		`Copper 1.`
`METAL`	`486 486`		`Copper 3.`
`METAL`	`552 552`		`Copper 3.`
`METAL`	`553 553`		`Copper 4.`
`METAL`	`554 554`		`Copper 2.`
`METAL`	`558 558`		`Copper 4.`
`CARBOHYD`	`89 89`		`N-linked (GlcNAc...).`
`CARBOHYD`	`138 138`		`N-linked (GlcNAc...).`
`CARBOHYD`	`251 251`		`N-linked (GlcNAc...).`
`CARBOHYD`	`266 266`		`N-linked (GlcNAc...).`
`CARBOHYD`	`294 294`		`N-linked (GlcNAc...).`
`CARBOHYD`	`339 339`		`N-linked (GlcNAc...).`
`CARBOHYD`	`426 426`		`N-linked (GlcNAc...).`
`CARBOHYD`	`446 446`		`N-linked (GlcNAc...).`
`DISULFID`	`54 62`
`DISULFID`	`164 590`
`DISULFID`	`348 382`
`STRAND`	`62 64`	`3`
`TURN`	`73 75`	`3`
`STRAND`	`83 97`	`15`
`STRAND`	`103 110`	`8`
`STRAND`	`113 115`	`3`
`STRAND`	`119 122`	`4`
`STRAND`	`126 134`	`9`
`STRAND`	`142 145`	`4`
`HELIX`	`153 155`	`3`
`TURN`	`159 161`	`3`
`STRAND`	`171 178`	`8`
`STRAND`	`183 189`	`7`
`HELIX`	`194 196`	`3`
`STRAND`	`200 206`	`7`
`STRAND`	`214 225`	`12`
`HELIX`	`230 236`	`7`
`TURN`	`237 239`	`3`
`STRAND`	`245 250`	`6`
`TURN`	`257 259`	`3`
`STRAND`	`266 269`	`4`
`STRAND`	`274 281`	`8`
`STRAND`	`288 292`	`5`
`STRAND`	`297 302`	`6`
`STRAND`	`305 313`	`9`
`STRAND`	`315 317`	`3`
`STRAND`	`322 328`	`7`
`STRAND`	`333 341`	`9`
`TURN`	`345 348`	`4`
`STRAND`	`351 354`	`4`
`STRAND`	`357 362`	`6`
`STRAND`	`390 392`	`3`
`HELIX`	`405 407`	`3`
`STRAND`	`408 414`	`7`
`STRAND`	`416 420`	`5`
`STRAND`	`422 425`	`4`
`HELIX`	`438 443`	`6`
`HELIX`	`451 453`	`3`
`STRAND`	`455 458`	`4`
`STRAND`	`464 471`	`8`
`STRAND`	`481 485`	`5`
`STRAND`	`490 496`	`7`
`HELIX`	`511 514`	`4`
`TURN`	`515 517`	`3`
`STRAND`	`525 531`	`7`
`STRAND`	`535 542`	`8`
`STRAND`	`547 553`	`7`
`HELIX`	`556 561`	`6`
`STRAND`	`564 570`	`7`
`HELIX`	`571 576`	`6`
`HELIX`	`580 596`	`17`
`HELIX`	`597 599`	`3`

Sequence information

Length: 623 AA [This is the length of the unprocessed precursor]

Molecular weight: 68958 Da [This is the MW of the unprocessed precursor]

CRC64: A322F89B438784E1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKTFTSALAL VVGMLAPGAV VAAPPSTPAQ RDLVELREAR QEGGKDLRPR EPTCNTPSNR 

        70         80         90        100        110        120 
ACWSDGFDIN TDYEVSTPDT GVTQSYVFNL TEVDNWMGPD GVVKEKVMLI NGNIMGPNIV 

       130        140        150        160        170        180 
ANWGDTVEVT VINNLVTNGT SIHWHGIHQK DTNLHDGANG VTECPIPPKG GQRTYRWRAR 

       190        200        210        220        230        240 
QYGTSWYHSH FSAQYGNGVV GTIQINGPAS LPYDIDLGVF PITDYYYRAA DDLVHFTQNN 

       250        260        270        280        290        300 
APPFSDNVLI NGTAVNPNTG EGQYANVTLT PGKRHRLRIL NTSTENHFQV SLVNHTMTVI 

       310        320        330        340        350        360 
AADMVPVNAM TVDSLFLAVG QRYDVVIDAS RAPDNYWFNV TFGGQAACGG SLNPHPAAIF 

       370        380        390        400        410        420 
HYAGAPGGLP TDEGTPPVDH QCLDTLDVRP VVPRSVPVNS FVKRPDNTLP VALDLTGTPL 

       430        440        450        460        470        480 
FVWKVNGSDI NVDWGKPIID YILTGNTSYP VSDNIVQVDA VDQWTYWLIE NDPEGPFSLP 

       490        500        510        520        530        540 
HPMHLHGHDF LVLGRSPDVP AASQQRFVFD PAVDLARLNG DNPPRRDTTM LPAGGWLLLA 

       550        560        570        580        590        600 
FRTDNPGAWL FHCHIAWHVS GGLSVDFLER PADLRQRISQ EDEDDFNRVC DEWRAYWPTN 

       610        620 
PYPKIDSGLK RRRWVEESEW LVR

Q70KY3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools