[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0378-1119(87)90217-4; PubMed=3440521 [NCBI, ExPASy, EBI, Israel, Japan] de Boer H.A., Zhang Y.Z., Collins C., Reddy C.A.; "Analysis of nucleotide sequences of two ligninase cDNAs from a white-rot filamentous fungus, Phanerochaete chrysosporium."; Gene 60:93-102(1987).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767; DOI=10.1093/nar/19.3.599; PubMed=2011531 [NCBI, ExPASy, EBI, Israel, Japan] Gaskell J., Dieperink E., Cullen D.; "Genomic organization of lignin peroxidase genes of Phanerochaete chrysosporium."; Nucleic Acids Res. 19:599-603(1991).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767; DOI=10.1016/0378-1119(91)90051-C; PubMed=1999283 [NCBI, ExPASy, EBI, Israel, Japan] Zhang Y.Z., Reddy C.A., Rasooly A.; "Cloning of several lignin peroxidase (LIP)-encoding genes: sequence analysis of the LIP6 gene from the white-rot basidiomycete, Phanerochaete chrysosporium."; Gene 97:191-198(1991).

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 (By similarity).
PATHWAY: Secondary metabolite metabolism; lignin degradation .
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

M18794; AAA33734.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X55343; CAA39033.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M63496; AAA33739.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JN0117; OPJGG5.

3D structure databases

HSSP

P06181; 1B85. [HSSP ENTRY / PDB]

SMR

P11543; 24-371.

ModBase

P11543.

Protein family/group databases

PeroxiBase

2411; PcLiPC.

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

Calcium; Cleavage on pair of basic residues; 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 27`	`6`	`Potential.`	`PRO_0000023768`
`CHAIN`	`28 371`	`344`	`Ligninase LG5.`	`PRO_0000023769`
`ACT_SITE`	`74 74`		`Proton acceptor (By similarity).`
`METAL`	`75 75`		`Calcium 1 (By similarity).`
`METAL`	`92 92`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`94 94`		`Calcium 1 (By similarity).`
`METAL`	`96 96`		`Calcium 1 (By similarity).`
`METAL`	`202 202`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`203 203`		`Calcium 2 (By similarity).`
`METAL`	`220 220`		`Calcium 2 (By similarity).`
`METAL`	`222 222`		`Calcium 2 (By similarity).`
`METAL`	`225 225`		`Calcium 2; via carbonyl oxygen (By similarity).`
`METAL`	`227 227`		`Calcium 2 (By similarity).`
`SITE`	`70 70`	`1`	`Transition state stabilizer (By similarity).`
`CARBOHYD`	`283 283`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`30 42`		`By similarity.`
`DISULFID`	`41 311`		`By similarity.`
`DISULFID`	`61 146`		`By similarity.`
`DISULFID`	`275 344`		`By similarity.`

Sequence information

Length: 371 AA [This is the length of the unprocessed precursor]

Molecular weight: 39418 Da [This is the MW of the unprocessed precursor]

CRC64: F0AE30C69D7EF5C2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAFKKLLAVL TAALSLRAAQ GAAVEKRATC SNGKVVPAAS CCTWFNVLSD IQENLFNGGQ 

        70         80         90        100        110        120 
CGAEAHESIR LVFHDAIAIS PAMEPQASSV RGADGSIMIF DEIETNFHPN IGLDEIVRLQ 

       130        140        150        160        170        180 
KPFVQKHGVT PGDFIAFAGA VALSNCPGAP QMNFFTGRAP ATQPAPDGLV PEPFHSVDQI 

       190        200        210        220        230        240 
IDRVFDAGEF DELELVWMLS AHSVAAANDI DPNIQGLPFD STPGIFDSQF FVETQLAGTG 

       250        260        270        280        290        300 
FTGGSNNQGE VSSPLPGEMR LQSDFLIARD ARTACEWQSF VNNQSKLVSD FQFIFLALTQ 

       310        320        330        340        350        360 
LGQDPDAMTD CSAVIPISKP APNNTPGFSF FPPGMTMDDV EQACAETPFP TLSTLPGPAT 

       370 
SVARIPPPPG A

P11543 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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