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Reviewed, UniProtKB/Swiss-Prot P11542 (LIG4_PHACH)

Last modified June 16, 2009. Version 87. 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

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Names and origin

Protein namesRecommended name:
    Ligninase H2
    EC=1.11.1.14
Alternative name(s):
    Diarylpropane peroxidase
    Lignin peroxidase
    LG4
Gene names
Name: GLG4
Synonyms: LIP2
OrganismPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Taxonomic identifier5306 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Corticiales › Corticiaceae › Phanerochaete

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Protein attributes

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

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

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.

Sequence similarities

Belongs to the peroxidase family. Ligninase subfamily.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 287 Ref.3
PRO_0000023766
Chain29 – 372344Ligninase H2
PRO_0000023767

Sites

Active site761Proton acceptor
Metal binding771Calcium 1
Metal binding951Calcium 1; via carbonyl oxygen
Metal binding971Calcium 1
Metal binding991Calcium 1
Metal binding2051Iron (heme axial ligand)
Metal binding2061Calcium 2
Metal binding2231Calcium 2
Metal binding2251Calcium 2
Metal binding2281Calcium 2; via carbonyl oxygen
Metal binding2301Calcium 2
Site721Transition state stabilizer

Amino acid modifications

Glycosylation2861N-linked (GlcNAc...) Ref.4
Disulfide bond31 ↔ 44
Disulfide bond43 ↔ 314
Disulfide bond63 ↔ 149
Disulfide bond278 ↔ 344

Experimental info

Sequence conflict3121T → I in AAA33733. Ref.2

Secondary structure

1 ........................................................ 372
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P11542-1 [UniParc].

Last modified February 1, 1991. Version 2.
Checksum: A17AD0AB5FE1A290

FASTA37239,523
        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

« Hide

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References

[1]Naidu P.S., Zhang Y.Z., Reddy C.A.
Submitted (JUN-1989) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767.
[2]"Analysis of nucleotide sequences of two ligninase cDNAs from a white-rot filamentous fungus, Phanerochaete chrysosporium."
de Boer H.A., Zhang Y.Z., Collins C., Reddy C.A.
Gene 60:93-102(1987) [PubMed: 3440521] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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 29-59.
Strain: ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767.
[4]"Do carbohydrates play a role in the lignin peroxidase cycle? Redox catalysis in the endergonic region of the driving force."
Schoemaker H.E., Lundell T.K., Floris R., Glumoff T., Winterhalter K.H., Piontek K.
Bioorg. Med. Chem. 2:509-519(1994) [PubMed: 8000874] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 29-372, GLYCOSYLATION AT ASN-286.

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Cross-references

Sequence databases

X15599 Genomic DNA. Translation: CAA33621.1.
M18743 mRNA. Translation: AAA33733.1.
PIROPJGH2. S06043.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1QPAX-ray1.80A/B29-372[»]
ModBaseSearch...

Protein family/group databases

PeroxiBase2414. PcLiPD.

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...

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Entry information

Entry nameLIG4_PHACH
AccessionPrimary (citable) accession number: P11542
Secondary accession number(s): P14153
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: February 1, 1991
Last modified: June 16, 2009
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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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