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Reviewed, UniProtKB/Swiss-Prot P06181 (LIG8_PHACH)

Last modified May 26, 2009. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaHomobasidiomycetesCorticialesCorticiaceaePhanerochaete

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

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.

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 Ref.7
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
P06181-1 [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: 3561490] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ATCC 24725 / CBS 481.73 / CCRC 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: 3240864] [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: 3344218] [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: 2474293] [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: 2844176] [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: 2303054] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-58.
Strain: ATCC 24725 / CBS 481.73 / CCRC 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: 16593451] [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: 11607355] [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: 9636023] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Strain: ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767.
+Additional computationally mapped references.

Cross-references

Sequence databases

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

EntryMethodResolution (Å)ChainPositionsPDBsum
1B80X-ray1.73A/B24-372[»]
1B82X-ray1.80A/B22-372[»]
1B85X-ray1.85A/B24-372[»]
ModBaseSearch...

Protein family/group databases

PeroxiBase2412. PcLiPA.

Enzyme and pathway databases

BRENDA1.11.1.14. 16698.

Family and domain databases

InterProIPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSPR00462. LIGNINASE.
PR00458. PEROXIDASE.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

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: May 26, 2009
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents