[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767; DOI=10.1038/326520a0; PubMed=3561490 [NCBI, ExPASy, EBI, Israel, Japan] Tien M., Tu C.-P.D.; "Cloning and sequencing of a cDNA for a ligninase from Phanerochaete chrysosporium."; Nature 326:520-523(1987).
[2]	ERRATUM, AND SEQUENCE REVISION. Tien M., Tu C.-P.D.; Nature 328:742-742(1987).
[3]	NUCLEOTIDE SEQUENCE. DOI=10.1016/0378-1119(88)90111-4; PubMed=3240864 [NCBI, ExPASy, EBI, Israel, Japan] Walther L., Kaelin M., Reiser J., Suter F., Fritsche B., Saloheimo M., Leisola M., Teeri T., Knowles J.K.C., Fiechter A.; "Molecular analysis of a Phanerochaete chrysosporium lignin peroxidase gene."; Gene 70:127-137(1988).
[4]	NUCLEOTIDE SEQUENCE. DOI=10.1093/nar/16.3.1219; PubMed=3344218 [NCBI, ExPASy, EBI, Israel, Japan] Smith T.L., Schalch H., Gaskell J., Covert S., Cullan D.; "Nucleotide sequence of a ligninase gene from Phanerochaete chrysosporium."; Nucleic Acids Res. 16:1219-1219(1988).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0006-291X(89)92363-2; PubMed=2474293 [NCBI, ExPASy, EBI, Israel, Japan] Andrawis A., Pease E.A., Kuan I., Holzbaur E., Tien M.; "Characterization of two lignin peroxidase clones from Phanerochaete chrysosporium."; Biochem. Biophys. Res. Commun. 162:673-680(1989).
[6]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-1. DOI=10.1016/S0006-291X(88)80541-2; PubMed=2844176 [NCBI, ExPASy, EBI, Israel, Japan] Holzbaur E.L.F., Tien M.; "Structure and regulation of a lignin peroxidase gene from Phanerochaete chrysosporium."; Biochem. Biophys. Res. Commun. 155:626-633(1988).
[7]	PROTEIN SEQUENCE OF 29-58. STRAIN=ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767; PubMed=2303054 [NCBI, ExPASy, EBI, Israel, Japan] Glumoff T., Harvey P.J., Molinari S., Goble M., Frank G., Palmer J.M., Smit J.D.G., Leisola M.S.A.; "Lignin peroxidase from Phanerochaete chrysosporium. Molecular and kinetic characterization of isozymes."; Eur. J. Biochem. 187:515-520(1990).
[8]	CHARACTERIZATION. PubMed=16593451 [NCBI, ExPASy, EBI, Israel, Japan] Tien M., Kirk T.K.; "Lignin-degrading enzyme from Phanerochaete chrysosporium: purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase."; Proc. Natl. Acad. Sci. U.S.A. 81:2280-2284(1984).
[9]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). PubMed=11607355 [NCBI, ExPASy, EBI, Israel, Japan] Edwards S.L., Raag R., Wariishi H., Gold M.H., Poulos T.L.; "Crystal structure of lignin peroxidase."; Proc. Natl. Acad. Sci. U.S.A. 90:750-754(1993).
[10]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). STRAIN=ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767; DOI=10.1021/bi9727186; PubMed=9636023 [NCBI, ExPASy, EBI, Israel, Japan] Blodig W., Doyle W.A., Smith A.T., Winterhalter K.H., Choinowski T., Piontek K.; "Autocatalytic formation of a hydroxy group at C beta of Trp171 in lignin peroxidase."; Biochemistry 37:8832-8838(1998).

Comments

FUNCTION: Depolymerization of lignin. Catalyzes the C(alpha)-C(beta) cleavage of the propyl side chains of lignin.
CATALYTIC ACTIVITY: 1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + H₂O₂ = 3,4-dimethoxybenzaldehyde + 1-(3,4-dimethoxyphenyl)ethane-1,2-diol + H₂O.
COFACTOR: Binds 2 calcium ions per subunit.
COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
PATHWAY: Secondary metabolite metabolism; lignin degradation .
DEVELOPMENTAL STAGE: Ligninases are expressed during secondary metabolism, and are triggered by nutrient limitation.
SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.

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

M37701; AAA33740.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y00262; CAA68373.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M21913; -; NOT_ANNOTATED_CDS; mRNA.	[EMBL / GenBank / DDBJ]
M27401; AAA53109.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M27884; AAB00798.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A27817; A27817.
A32322; A32322.
A43638; A43638.
B32322; B32322.
JT0402; JT0402.
PS0010; PS0010.
S01028; S01028.
S08202; S08202.
S69246; S69246.

3D structure databases

PDB

1B80; X-ray; 1.73 A; A/B=22-372.	[ExPASy / RCSB / EBI]
1B82; X-ray; 1.80 A; A/B=22-372.	[ExPASy / RCSB / EBI]
1B85; X-ray; 1.85 A; A/B=22-372.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1B80; -.
1B82; -.
1B85; -.

ModBase

P06181.

Protein family/group databases

PeroxiBase

2412; PcLiPA.

Ontologies

GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016690;	Molecular function: diarylpropane peroxidase activity (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0042744;	Biological process: hydrogen peroxide catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0046274;	Biological process: lignin catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002016; Haem_peroxidase_pln/fun/bac.
IPR001621; Ligninase.
Graphical view of domain structure.

Pfam

PF00141; peroxidase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00462; LIGNINASE.
PR00458; PEROXIDASE.

PROSITE

PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

3D-structure; Calcium; Cleavage on pair of basic residues; Direct protein sequencing; Glycoprotein; Heme; Hydrogen peroxide; Iron; Lignin degradation; Metal-binding; Oxidoreductase; Peroxidase; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`	`Potential.`
`PROPEP`	`22 28`	`7`		`PRO_0000023760`
`CHAIN`	`29 372`	`344`	`Ligninase H8.`	`PRO_0000023761`
`ACT_SITE`	`75 75`		`Proton acceptor.`
`METAL`	`76 76`		`Calcium 1.`
`METAL`	`94 94`		`Calcium 1; via carbonyl oxygen.`
`METAL`	`96 96`		`Calcium 1.`
`METAL`	`98 98`		`Calcium 1.`
`METAL`	`204 204`		`Iron (heme axial ligand).`
`METAL`	`205 205`		`Calcium 2.`
`METAL`	`222 222`		`Calcium 2.`
`METAL`	`224 224`		`Calcium 2.`
`METAL`	`227 227`		`Calcium 2; via carbonyl oxygen.`
`METAL`	`229 229`		`Calcium 2.`
`SITE`	`71 71`	`1`	`Transition state stabilizer.`
`CARBOHYD`	`285 285`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`31 43`
`DISULFID`	`42 313`
`DISULFID`	`62 148`
`DISULFID`	`277 345`
`VARIANT`	`15 15`	`1`	`L -> S.`
`VARIANT`	`142 142`	`1`	`R -> A.`
`STRAND`	`36 39`	`4`
`HELIX`	`40 44`	`5`
`HELIX`	`45 55`	`11`
`TURN`	`58 60`	`3`
`HELIX`	`64 77`	`14`
`HELIX`	`82 86`	`5`
`STRAND`	`94 97`	`4`
`HELIX`	`98 101`	`4`
`HELIX`	`103 106`	`4`
`HELIX`	`110 112`	`3`
`TURN`	`113 115`	`3`
`HELIX`	`116 129`	`14`
`HELIX`	`133 146`	`14`
`HELIX`	`179 190`	`12`
`HELIX`	`194 200`	`7`
`HELIX`	`201 206`	`6`
`STRAND`	`208 213`	`6`
`STRAND`	`219 223`	`5`
`HELIX`	`231 235`	`5`
`STRAND`	`244 247`	`4`
`STRAND`	`255 257`	`3`
`HELIX`	`264 269`	`6`
`TURN`	`273 275`	`3`
`HELIX`	`276 281`	`6`
`TURN`	`282 284`	`3`
`HELIX`	`286 301`	`16`
`TURN`	`302 304`	`3`
`HELIX`	`307 309`	`3`
`STRAND`	`310 312`	`3`
`HELIX`	`314 316`	`3`
`STRAND`	`325 327`	`3`
`HELIX`	`338 340`	`3`
`STRAND`	`357 359`	`3`

Sequence information

Length: 372 AA [This is the length of the unprocessed precursor]

Molecular weight: 39686 Da [This is the MW of the unprocessed precursor]

CRC64: E6ABA9FD48428FCC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAFKQLFAAI SLALLLSAAN AAAVIEKRAT CSNGKTVGDA SCCAWFDVLD DIQQNLFHGG 

        70         80         90        100        110        120 
QCGAEAHESI RLVFHDSIAI SPAMEAQGKF GGGGADGSIM IFDDIETAFH PNIGLDEIVK 

       130        140        150        160        170        180 
LQKPFVQKHG VTPGDFIAFA GRVALSNCPG APQMNFFTGR APATQPAPDG LVPEPFHTVD 

       190        200        210        220        230        240 
QIINRVNDAG EFDELELVWM LSAHSVAAVN DVDPTVQGLP FDSTPGIFDS QFFVETQLRG 

       250        260        270        280        290        300 
TAFPGSGGNQ GEVESPLPGE IRIQSDHTIA RDSRTACEWQ SFVNNQSKLV DDFQFIFLAL 

       310        320        330        340        350        360 
TQLGQDPNAM TDCSDVIPQS KPIPGNLPFS FFPAGKTIKD VEQACAETPF PTLTTLPGPE 

       370 
TSVQRIPPPP GA

P06181 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