[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767; Naidu P.S., Zhang Y.Z., Reddy C.A.; Submitted (JUN-1989) to the EMBL/GenBank/DDBJ databases.
[2]	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).
[3]	PROTEIN SEQUENCE OF 29-59. 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).
[4]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 29-372, AND GLYCOSYLATION AT ASN-286. DOI=10.1016/0968-0896(94)80021-9; PubMed=8000874 [NCBI, ExPASy, EBI, Israel, Japan] Schoemaker H.E., Lundell T.K., Floris R., Glumoff T., Winterhalter K.H., Piontek K.; "Do carbohydrates play a role in the lignin peroxidase cycle? Redox catalysis in the endergonic region of the driving force."; Bioorg. Med. Chem. 2:509-519(1994).

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.
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

X15599; CAA33621.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M18743; AAA33733.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S06043; OPJGH2.

3D structure databases

PDB

1QPA; X-ray; 1.80 A; A/B=29-372.

[ExPASy / RCSB / EBI]

PDBsum

1QPA; -.

ModBase

P11542.

Protein family/group databases

PeroxiBase

2414; PcLiPD.

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

P11542; -.

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_0000023766`
`CHAIN`	`29 372`	`344`	`Ligninase H2.`	`PRO_0000023767`
`ACT_SITE`	`76 76`		`Proton acceptor.`
`METAL`	`77 77`		`Calcium 1.`
`METAL`	`95 95`		`Calcium 1; via carbonyl oxygen.`
`METAL`	`97 97`		`Calcium 1.`
`METAL`	`99 99`		`Calcium 1.`
`METAL`	`205 205`		`Iron (heme axial ligand).`
`METAL`	`206 206`		`Calcium 2.`
`METAL`	`223 223`		`Calcium 2.`
`METAL`	`225 225`		`Calcium 2.`
`METAL`	`228 228`		`Calcium 2; via carbonyl oxygen.`
`METAL`	`230 230`		`Calcium 2.`
`SITE`	`72 72`	`1`	`Transition state stabilizer.`
`CARBOHYD`	`286 286`		`N-linked (GlcNAc...).`
`DISULFID`	`31 44`
`DISULFID`	`43 314`
`DISULFID`	`63 149`
`DISULFID`	`278 344`
`CONFLICT`	`312 312`		`T -> I (in Ref. 2; AAA33733).`
`HELIX`	`41 46`	`6`
`HELIX`	`47 56`	`10`
`TURN`	`59 61`	`3`
`HELIX`	`65 78`	`14`
`HELIX`	`83 87`	`5`
`STRAND`	`95 98`	`4`
`HELIX`	`99 102`	`4`
`HELIX`	`104 107`	`4`
`HELIX`	`111 113`	`3`
`HELIX`	`116 130`	`15`
`HELIX`	`134 147`	`14`
`HELIX`	`180 191`	`12`
`HELIX`	`195 201`	`7`
`HELIX`	`202 206`	`5`
`STRAND`	`209 214`	`6`
`STRAND`	`220 224`	`5`
`HELIX`	`232 236`	`5`
`STRAND`	`245 247`	`3`
`STRAND`	`256 259`	`4`
`HELIX`	`265 272`	`8`
`TURN`	`274 276`	`3`
`HELIX`	`277 281`	`5`
`TURN`	`282 285`	`4`
`HELIX`	`287 302`	`16`
`TURN`	`303 305`	`3`
`HELIX`	`308 310`	`3`
`STRAND`	`311 313`	`3`
`HELIX`	`315 317`	`3`
`HELIX`	`337 339`	`3`
`STRAND`	`345 347`	`3`
`STRAND`	`356 359`	`4`

Sequence information

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

Molecular weight: 39523 Da [This is the MW of the unprocessed precursor]

CRC64: A17AD0AB5FE1A290 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAFKQLLAAL SVALTLQVTQ AAPNLDKRVA CPDGVHTASN AACCAWFPVL DDIQQNLFHG 

        70         80         90        100        110        120 
GQCGAEAHEA LRMVFHDSIA ISPKLQSQGK FGGGGADGSI ITFSSIETTY HPNIGLDEVV 

       130        140        150        160        170        180 
AIQKPFIAKH GVTRGDFIAF AGAVGVSNCP GAPQMQFFLG RPEATQAAPD GLVPEPFHTI 

       190        200        210        220        230        240 
DQVLARMLDA GGFDEIETVW LLSAHSIAAA NDVDPTISGL PFDSTPGQFD SQFFVETQLR 

       250        260        270        280        290        300 
GTAFPGKTGI QGTVMSPLKG EMRLQTDHLF ARDSRTACEW QSFVNNQTKL QEDFQFIFTA 

       310        320        330        340        350        360 
LSTLGHDMNA MTDCSEVIPA PKPVNFGPSF FPAGKTHADI EQACASTPFP TLITAPGPSA 

       370 
SVARIPPPPS PN

P11542 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