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P06181 (LIG8_PHACH) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ligninase H8

EC=1.11.1.14
Alternative name(s):
Diarylpropane peroxidase
Lignin peroxidase
Gene names
Name:LPOA
OrganismPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Taxonomic identifier5306 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesCorticialesCorticiaceaePhanerochaete

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Depolymerization of lignin. Catalyzes the C(alpha)-C(beta) cleavage of the propyl side chains of lignin.

Catalytic activity

(3,4-dimethoxyphenyl)methanol + H2O2 = 3,4-dimethoxybenzaldehyde + 2 H2O.

Cofactor

Binds 2 calcium ions per subunit.

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.

Sequence similarities

Belongs to the peroxidase family. Ligninase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 287
PRO_0000023760
Chain29 – 372344Ligninase H8
PRO_0000023761

Sites

Active site751Proton acceptor
Metal binding761Calcium 1
Metal binding941Calcium 1; via carbonyl oxygen
Metal binding961Calcium 1
Metal binding981Calcium 1
Metal binding2041Iron (heme axial ligand)
Metal binding2051Calcium 2
Metal binding2221Calcium 2
Metal binding2241Calcium 2
Metal binding2271Calcium 2; via carbonyl oxygen
Metal binding2291Calcium 2
Site711Transition state stabilizer

Amino acid modifications

Glycosylation2851N-linked (GlcNAc...) Potential
Disulfide bond31 ↔ 43
Disulfide bond42 ↔ 313
Disulfide bond62 ↔ 148
Disulfide bond277 ↔ 345

Natural variations

Natural variant151L → S.
Natural variant1421R → A.

Secondary structure

........................................................... 372
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06181 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: E6ABA9FD48428FCC

FASTA37239,686
        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 

« Hide

References

[1]"Cloning and sequencing of a cDNA for a ligninase from Phanerochaete chrysosporium."
Tien M., Tu C.-P.D.
Nature 326:520-523(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM F-1767.
[2]Erratum
Tien M., Tu C.-P.D.
Nature 328:742-742(1987)
Cited for: SEQUENCE REVISION.
[3]"Molecular analysis of a Phanerochaete chrysosporium lignin peroxidase gene."
Walther L., Kaelin M., Reiser J., Suter F., Fritsche B., Saloheimo M., Leisola M., Teeri T., Knowles J.K.C., Fiechter A.
Gene 70:127-137(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[4]"Nucleotide sequence of a ligninase gene from Phanerochaete chrysosporium."
Smith T.L., Schalch H., Gaskell J., Covert S., Cullan D.
Nucleic Acids Res. 16:1219-1219(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[5]"Characterization of two lignin peroxidase clones from Phanerochaete chrysosporium."
Andrawis A., Pease E.A., Kuan I., Holzbaur E., Tien M.
Biochem. Biophys. Res. Commun. 162:673-680(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Structure and regulation of a lignin peroxidase gene from Phanerochaete chrysosporium."
Holzbaur E.L.F., Tien M.
Biochem. Biophys. Res. Commun. 155:626-633(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1.
[7]"Lignin peroxidase from Phanerochaete chrysosporium. Molecular and kinetic characterization of isozymes."
Glumoff T., Harvey P.J., Molinari S., Goble M., Frank G., Palmer J.M., Smit J.D.G., Leisola M.S.A.
Eur. J. Biochem. 187:515-520(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-58.
Strain: ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM F-1767.
[8]"Lignin-degrading enzyme from Phanerochaete chrysosporium: purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase."
Tien M., Kirk T.K.
Proc. Natl. Acad. Sci. U.S.A. 81:2280-2284(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[9]"Crystal structure of lignin peroxidase."
Edwards S.L., Raag R., Wariishi H., Gold M.H., Poulos T.L.
Proc. Natl. Acad. Sci. U.S.A. 90:750-754(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[10]"Autocatalytic formation of a hydroxy group at C beta of Trp171 in lignin peroxidase."
Blodig W., Doyle W.A., Smith A.T., Winterhalter K.H., Choinowski T., Piontek K.
Biochemistry 37:8832-8838(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Strain: ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM F-1767.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M37701 Genomic DNA. Translation: AAA33740.1. Sequence problems.
Y00262 mRNA. Translation: CAA68373.1. Sequence problems.
M21913 mRNA. No translation available.
M27401 Genomic DNA. Translation: AAA53109.1.
M27884 Genomic DNA. Translation: AAB00798.1.
PIRA27817.
A32322.
A43638.
B32322.
JT0402.
PS0010.
S01028.
S08202.
S69246.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B80X-ray1.73A/B24-372[»]
1B82X-ray1.80A/B22-372[»]
1B85X-ray1.85A/B22-372[»]
ProteinModelPortalP06181.
SMRP06181. Positions 24-372.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

mycoCLAPLPO2H_PHACH.
PeroxiBase2412. PcLiP01_RP78.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG250742.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14338.
BRENDA1.11.1.14. 4722.
UniPathwayUPA00892.

Family and domain databases

InterProIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamPF11895. DUF3415. 1 hit.
PF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSPR00462. LIGNINASE.
PR00458. PEROXIDASE.
SUPFAMSSF48113. SSF48113. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06181.

Entry information

Entry nameLIG8_PHACH
AccessionPrimary (citable) accession number: P06181
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: April 1, 1988
Last modified: October 16, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways