Reviewed, UniProtKB/Swiss-Prot Q70KY3 (LAC1_MELAO)

Names and origin

Protein names

Recommended name:
    Laccase-1
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 1
    Urishiol oxidase 1
    Diphenol oxidase 1
    Ligninolytic phenoloxidase

Gene names

Name:

LAC1

Organism

Melanocarpus albomyces

Taxonomic identifier

204285 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariales incertae sedis › Melanocarpus

Protein attributes

Sequence length	623 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Lignin degradation and detoxification of lignin-derived products Probable.
Catalytic activity	4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O.
Cofactor	Binds 4 copper ions per monomer.
Subunit structure	Monomer.
Tissue specificity	Secreted protein; extracellular space.
Sequence similarities	Belongs to the multicopper oxidase family.
Biophysicochemical properties	Absorption: Exhibits a shoulder at 360 nm, a smaller absorption peak at 450 nm, and a second, larger peak at 590 nm. Abs(max)=280 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.

Ontologies

Keywords
Biological process	Lignin degradation
Domain	Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cellulose catabolic process Ref.3 Traceable author statement. Source: UniProtKB lignin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extraorganismal space Ref.2 Inferred from direct assay. Source: UniProtKB
Molecular function	copper ion binding Ref.4 Inferred from direct assay. Source: UniProtKB laccase activity Ref.2 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Potential

Propeptide

23 – 50

28

PRO_0000235826

Chain

51 – 609

559

Laccase-1

PRO_0000235827

Propeptide

610 – 623

14

PRO_0000235828

Sites

Metal binding

143

1

Copper 1

Metal binding

145

1

Copper 2

Metal binding

188

1

Copper 2

Metal binding

190

1

Copper 3

Metal binding

481

1

Copper 4

Metal binding

484

1

Copper 1

Metal binding

486

1

Copper 3

Metal binding

552

1

Copper 3

Metal binding

553

1

Copper 4

Metal binding

554

1

Copper 2

Metal binding

558

1

Copper 4

Amino acid modifications

Glycosylation

89

1

N-linked (GlcNAc...)

Glycosylation

138

1

N-linked (GlcNAc...)

Glycosylation

251

1

N-linked (GlcNAc...)

Glycosylation

266

1

N-linked (GlcNAc...)

Glycosylation

294

1

N-linked (GlcNAc...)

Glycosylation

339

1

N-linked (GlcNAc...)

Glycosylation

426

1

N-linked (GlcNAc...)

Glycosylation

446

1

N-linked (GlcNAc...)

Disulfide bond

54 ↔ 62

Disulfide bond

164 ↔ 590

Disulfide bond

348 ↔ 382

Secondary structure

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623

Helix Strand Turn

Details...

Beta strand

62 – 64

3

Turn

73 – 75

3

Beta strand

83 – 97

15

Beta strand

103 – 110

8

Beta strand

113 – 115

3

Beta strand

119 – 122

4

Beta strand

126 – 134

9

Beta strand

142 – 145

4

Helix

153 – 155

3

Turn

159 – 161

3

Beta strand

171 – 178

8

Beta strand

183 – 189

7

Helix

194 – 196

3

Beta strand

200 – 206

7

Beta strand

214 – 225

12

Helix

230 – 236

7

Turn

237 – 239

3

Beta strand

245 – 250

6

Turn

257 – 259

3

Beta strand

266 – 269

4

Beta strand

274 – 281

8

Beta strand

288 – 292

5

Beta strand

297 – 302

6

Beta strand

305 – 313

9

Beta strand

315 – 317

3

Beta strand

322 – 328

7

Beta strand

333 – 341

9

Turn

345 – 348

4

Beta strand

351 – 354

4

Beta strand

357 – 362

6

Beta strand

390 – 392

3

Helix

405 – 407

3

Beta strand

408 – 414

7

Beta strand

416 – 420

5

Beta strand

422 – 425

4

Helix

438 – 443

6

Helix

451 – 453

3

Beta strand

455 – 458

4

Beta strand

464 – 471

8

Beta strand

481 – 485

5

Beta strand

490 – 496

7

Helix

511 – 514

4

Turn

515 – 517

3

Beta strand

525 – 531

7

Beta strand

535 – 542

8

Beta strand

547 – 553

7

Helix

556 – 561

6

Beta strand

564 – 570

7

Helix

571 – 576

6

Helix

580 – 596

17

Helix

597 – 599

3

Sequences

	Sequence		Length	Mass (Da)
	Q70KY3-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: A322F89B438784E1	FASTA	623	68,958
	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

References

[1]	"Molecular cloning and expression in Saccharomyces cerevisiae of a laccase gene from the ascomycete Melanocarpus albomyces." Kiiskinen L.-L., Saloheimo M. Appl. Environ. Microbiol. 70:137-144(2004) [PubMed: 14711635] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Purification and characterisation of a novel laccase from the ascomycete Melanocarpus albomyces." Kiiskinen L.-L., Viikari L., Kruus K. Appl. Microbiol. Biotechnol. 59:198-204(2002) [PubMed: 12111146] [Abstract] Cited for: PROTEIN SEQUENCE OF 51-78; 214-228 AND 507-517, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY. Strain: VTT D-96490.
[3]	"Laccase from Melanocarpus albomyces binds effectively to cellulose." Kiiskinen L.-L., Palonen H., Linder M., Viikari L., Kruus K. FEBS Lett. 576:251-255(2004) [PubMed: 15474046] [Abstract] Cited for: PROBABLE FUNCTION.
[4]	"Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site." Hakulinen N., Kiiskinen L.-L., Kruus K., Saloheimo M., Paananen A., Koivula A., Rouvinen J. Nat. Struct. Biol. 9:601-605(2002) [PubMed: 12118243] [Abstract] Cited for: 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, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases