Reviewed, UniProtKB/Swiss-Prot Q02497 (LAC1_TRAHI)

Names and origin

Protein names	Recommended name:     Laccase     EC=1.10.3.2 Alternative name(s):     Benzenediol:oxygen oxidoreductase     Urishiol oxidase     Diphenol oxidase     Ligninolytic phenoloxidase
Organism	Trametes hirsuta (White-rot fungus) (Coriolus hirsutus)
Taxonomic identifier	5327 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Aphyllophorales › Trametes

Protein attributes

Sequence length	520 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	Most probably plays an important role in lignin degradation. Cleaves the C-C and C-O bonds of some phenolic lignin model compounds (such as O- and P-quinols, aminophenols and phenylenediamine).
Catalytic activity	4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.
Cofactor	Binds 4 copper ions per monomer By similarity.
Subcellular location	Secreted.
Polymorphism	2 allelic forms exist in position 111.
Sequence similarities	Belongs to the multicopper oxidase family. Contains 3 plastocyanin-like domains.

Ontologies

Keywords
Biological process	Lignin degradation
Cellular component	Secreted
Domain	Repeat Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	lignin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW laccase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21
	Chain	22 – 520	499	Laccase		PRO_0000002939
Regions
	Domain	23 – 148	126	Plastocyanin-like 1
	Domain	160 – 302	143	Plastocyanin-like 2
	Domain	369 – 491	123	Plastocyanin-like 3
Sites
	Metal binding	85	1	Copper 1; type 2 By similarity
	Metal binding	87	1	Copper 2; type 3 By similarity
	Metal binding	130	1	Copper 2; type 3 By similarity
	Metal binding	132	1	Copper 3; type 3 By similarity
	Metal binding	416	1	Copper 4; type 1 By similarity
	Metal binding	419	1	Copper 1; type 2 By similarity
	Metal binding	421	1	Copper 3; type 3 By similarity
	Metal binding	473	1	Copper 3; type 3 By similarity
	Metal binding	474	1	Copper 4; type 1 By similarity
	Metal binding	475	1	Copper 2; type 3 By similarity
	Metal binding	479	1	Copper 4; type 1 By similarity
Amino acid modifications
	Glycosylation	50	1	N-linked (GlcNAc...) Potential
	Glycosylation	72	1	N-linked (GlcNAc...) Potential
	Glycosylation	75	1	N-linked (GlcNAc...) Potential
	Glycosylation	210	1	N-linked (GlcNAc...) Potential
	Glycosylation	229	1	N-linked (GlcNAc...) Potential
	Glycosylation	354	1	N-linked (GlcNAc...) Potential
	Glycosylation	457	1	N-linked (GlcNAc...) Potential
	Disulfide bond	106 ↔ 509		Potential
	Disulfide bond	138 ↔ 226		Potential
Natural variations
	Natural variant	411	1	A → P
Experimental info
	Sequence conflict	378 – 379	2	SG → RR in AAA33104. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q02497-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 977D8DFA551F7929	FASTA	520	55,688
	10 20 30 40 50 60 MSRFQSLLAF VVASLAAVAH AAIGPTADLT ISNAEVSPDG FARQAVVVNN VTPGPLVAGN 70 80 90 100 110 120 KGDRFQLNVI DNLTNHTMLK STSIHWHGFF QKGTNWADGP AFVNQCPISS GHSFLYDFQV 130 140 150 160 170 180 PDQAGTFWYH SHLSTQYCDG LRGPFVVYDP NDPHASLYDV DNDDTVITLA DWYHTAAKLG 190 200 210 220 230 240 PAFPLGADAT LINGLGRSPS TTAADLAVIN VTKGKRYRFR LVSLSCDPNH TFSIDGHDLT 250 260 270 280 290 300 IIEVDSINSQ PLVVDSIQIF AAQRYSFVLN ADQDVGNYWI RANPNFGNVG FAGGINSAIL 310 320 330 340 350 360 RYDGADPVEP TTTQTTPTKP LNEVDLHPLA TMAVPGSPVA GGVDTAINMA FNFNGTNFFI 370 380 390 400 410 420 NGASFVPPTV PVLLQIISGA QNAQDLLPSG SVYSLPSNAD IEISFPATAA APGAPHPFHL 430 440 450 460 470 480 HGHAFAVVRS AGSTVYNYDN PIFRDVVSTG TPAAGDNVTI RFRTDNPGPW FLHCHIDFHL 490 500 510 520 EAGFAVVFAE DIPDVASANP VPQAWSDLCP IYDALDVNDQ

References

[1]

"Cloning, sequence analysis, and expression of ligninolytic phenoloxidase genes of the white-rot basidiomycete Coriolus hirsutus." Kojima Y., Tsukuda Y., Kawai Y., Tsukamoto A., Sugiura J., Sakaino M., Kita Y. J. Biol. Chem. 265:15224-15230(1990) [PubMed: 2394718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, VARIANT PRO-411. Strain: IFO 4917.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M60560 Genomic DNA. Translation: AAA33103.1. M60561 Genomic DNA. Translation: AAA33104.1.
PIR	A35883.
3D structure databases
HSSP	HSSP built from PDB template 1KYA based on UniProtKB Q96UT7.
SMR	Q02497. Positions 22-520.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.10.3.2. 119234.
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]
Gene3D	G3DSA:2.60.40.420. Cupredoxin. 3 hits.
Pfam	PF00394. Cu-oxidase. 1 hit. PF07731. Cu-oxidase_2. 1 hit. PF07732. Cu-oxidase_3. 1 hit. [Graphical view]
PROSITE	PS00079. MULTICOPPER_OXIDASE1. 1 hit. PS00080. MULTICOPPER_OXIDASE2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LAC1_TRAHI

Accession

Primary (citable) accession number: Q02497

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)