[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 29-48. STRAIN=ATCC 201542 / OGC101; DOI=10.1016/0378-1119(91)90304-T; PubMed=1743510 [NCBI, ExPASy, EBI, Israel, Japan] Ritch T.G. Jr., Nipper V.J., Akileswaran L., Smith A.J., Pribnow D.G., Gold M.H.; "Lignin peroxidase from the basidiomycete Phanerochaete chrysosporium is synthesized as a preproenzyme."; Gene 107:119-126(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 201542 / OGC101; DOI=10.1016/0378-1119(92)90250-S; PubMed=1511887 [NCBI, ExPASy, EBI, Israel, Japan] Ritch T.G. Jr., Gold M.H.; "Characterization of a highly expressed lignin peroxidase-encoding gene from the basidiomycete Phanerochaete chrysosporium."; Gene 118:73-80(1992).
[3]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). PubMed=8440725 [NCBI, ExPASy, EBI, Israel, Japan] Poulos T.L., Edwards S.L., Wariishi H., Gold M.H.; "Crystallographic refinement of lignin peroxidase at 2 A."; J. Biol. Chem. 268:4429-4440(1993).
[4]	X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND HYDROXYLATION AT TRP-199. STRAIN=ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767; DOI=10.1006/jmbi.1998.2507; PubMed=10024453 [NCBI, ExPASy, EBI, Israel, Japan] Choinowski T., Blodig W., Winterhalter K.H., Piontek K.; "The crystal structure of lignin peroxidase at 1.70-A resolution reveals a hydroxy group on the cbeta of tryptophan 171: a novel radical site formed during the redox cycle."; J. Mol. Biol. 286:809-827(1999).

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

M74229; AAA33735.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M92644; AAA33738.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC1268; JC1268.

3D structure databases

PDB

1LGA; X-ray; 2.03 A; A/B=29-371.	[ExPASy / RCSB / EBI]
1LLP; X-ray; 1.70 A; A=29-371.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1LGA; -.
1LLP; -.

ModBase

P49012.

Protein family/group databases

PeroxiBase

2409; PcLiPE_OGC101.

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

P49012; -.

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; Hydroxylation; 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`
`PROPEP`	`22 28`	`7`		`PRO_0000023762`
`CHAIN`	`29 371`	`343`	`Ligninase LG2.`	`PRO_0000023763`
`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.`
`MOD_RES`	`199 199`		`3-hydroxytryptophan.`
`CARBOHYD`	`285 285`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`31 43`
`DISULFID`	`42 313`
`DISULFID`	`62 148`
`DISULFID`	`277 345`
`HELIX`	`40 43`	`4`
`HELIX`	`44 55`	`12`
`TURN`	`58 60`	`3`
`HELIX`	`64 77`	`14`
`HELIX`	`82 85`	`4`
`STRAND`	`87 89`	`3`
`STRAND`	`94 97`	`4`
`HELIX`	`98 101`	`4`
`HELIX`	`103 106`	`4`
`HELIX`	`110 112`	`3`
`HELIX`	`115 129`	`15`
`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`	`255 258`	`4`
`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`	`346 348`	`3`
`STRAND`	`357 359`	`3`

Sequence information

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

Molecular weight: 39329 Da [This is the MW of the unprocessed precursor]

CRC64: F6AAB123EDC92123 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAFKQLFAAI TVALSLTAAN AAVVKEKRAT CANGKTVGDA SCCAWFDVLD DIQANMFHGG 

        70         80         90        100        110        120 
QCGAEAHESI RLVFHDSIAI SPAMEAKGKF GGGGADGSIM IFDTIETAFH PNIGLDEVVA 

       130        140        150        160        170        180 
MQKPFVQKHG VTPGDFIAFA GAVALSNCPG APQMNFFTGR KPATQPAPDG LVPEPFHTVD 

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

       250        260        270        280        290        300 
TLFPGSGGNQ GEVESGMAGE IRIQTDHTLA RDSRTACEWQ SFVGNQSKLV DDFQFIFLAL 

       310        320        330        340        350        360 
TQLGQDPNAM TDCSDVIPLS KPIPGNGPFS FFPPGKSHSD IEQACAETPF PSLVTLPGPA 

       370 
TSVARIPPHK A

P49012 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