[1]	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).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767; DOI=10.1016/0378-1119(90)90218-G; PubMed=2373364 [NCBI, ExPASy, EBI, Israel, Japan] Huoponen K., Ollikka P., Kaelin M., Walther I., Maentsaelae P., Reiser J.; "Characterization of lignin peroxidase-encoding genes from lignin-degrading basidiomycetes."; Gene 89:145-150(1990).

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 1 heme B (iron-protoporphyrin IX) group per subunit (By similarity).
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

X54257; CAA38177.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M37701; AAA33741.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JH0156; JH0156.
PS0011; PS0011.
S13563; OPJGAP.

3D structure databases

HSSP

P49012; 1LLP. [HSSP ENTRY / PDB]

SMR

P31837; 24-372.

ModBase

P31837.

Protein family/group databases

PeroxiBase

2413; PcLiPB.

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 28`	`7`	`Potential.`	`PRO_0000023772`
`CHAIN`	`29 372`	`344`	`Ligninase A.`	`PRO_0000023773`
`ACT_SITE`	`75 75`		`Proton acceptor (By similarity).`
`METAL`	`76 76`		`Calcium 1 (By similarity).`
`METAL`	`94 94`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`96 96`		`Calcium 1 (By similarity).`
`METAL`	`98 98`		`Calcium 1 (By similarity).`
`METAL`	`204 204`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`205 205`		`Calcium 2 (By similarity).`
`METAL`	`222 222`		`Calcium 2 (By similarity).`
`METAL`	`224 224`		`Calcium 2 (By similarity).`
`METAL`	`227 227`		`Calcium 2; via carbonyl oxygen (By similarity).`
`METAL`	`229 229`		`Calcium 2 (By similarity).`
`SITE`	`71 71`	`1`	`Transition state stabilizer (By similarity).`
`CARBOHYD`	`285 285`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`31 43`		`By similarity.`
`DISULFID`	`42 313`		`By similarity.`
`DISULFID`	`62 148`		`By similarity.`
`DISULFID`	`277 345`		`By similarity.`
`CONFLICT`	`135 135`		`A -> D (in Ref. 2; AAA33741).`
`CONFLICT`	`161 161`		`A -> R (in Ref. 2; AAA33741).`
`CONFLICT`	`298 298`		`L -> H (in Ref. 2; AAA33741).`

Sequence information

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

Molecular weight: 39394 Da [This is the MW of the unprocessed precursor]

CRC64: 04CE4598D6D6F09B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAFKQLVAAI SLALSLTTAN AAVVKEKRAT CSNGATVGDA SCCAWFDVLD DIQQNLFQGG 

        70         80         90        100        110        120 
QCGAEAHESI RLVFHDAIAI SPAMEAQGKF GGGGADGSIM IFDDIEPNFH PNIGLDEIIN 

       130        140        150        160        170        180 
LQKPFVQKHG VTPGAFIAFA GAVALSNCPG APQMNFFTGR APATQPAPDG LVPEPFHTVD 

       190        200        210        220        230        240 
QIIARVNDAG EFDELELVWM LSAHSVAAVN DVDPTVQGLP FDSTPGIFDS QFFVETQFRG 

       250        260        270        280        290        300 
ILFPGSGGNQ GEVESGMAGE IRIQTDHTLA RDSRTACEWQ SFVNNQSKLV SDFQFIFLAL 

       310        320        330        340        350        360 
TQLGQDPNAM TDCSDVIPIS KPIPGNLPFS FFPPGKSMKD VEQACAETPF PSLVTLPGPA 

       370 
TSVARIPPPP GA

P31837 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