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Protein

Ligninase H2

Gene

GLG4

Organism
Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O.
2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O.

Cofactori

Protein has several cofactor binding sites:
  • heme bPROSITE-ProRule annotationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.PROSITE-ProRule annotation
  • Ca2+Note: Binds 2 calcium ions per subunit.

Pathwayi: lignin degradation

This protein is involved in the pathway lignin degradation, which is part of Secondary metabolite metabolism.
View all proteins of this organism that are known to be involved in the pathway lignin degradation and in Secondary metabolite metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei72 – 721Transition state stabilizer
Active sitei76 – 761Proton acceptor
Metal bindingi77 – 771Calcium 1
Metal bindingi95 – 951Calcium 1; via carbonyl oxygen
Metal bindingi97 – 971Calcium 1
Metal bindingi99 – 991Calcium 1
Metal bindingi205 – 2051Iron (heme axial ligand)
Metal bindingi206 – 2061Calcium 2
Metal bindingi223 – 2231Calcium 2
Metal bindingi225 – 2251Calcium 2
Metal bindingi228 – 2281Calcium 2; via carbonyl oxygen
Metal bindingi230 – 2301Calcium 2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide, Lignin degradation

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14340.
UniPathwayiUPA00892.

Protein family/group databases

mycoCLAPiLPO2B_PHACH.
PeroxiBasei2414. PcLiP04_BKMF1767.

Names & Taxonomyi

Protein namesi
Recommended name:
Ligninase H2 (EC:1.11.1.14)
Alternative name(s):
Diarylpropane peroxidase
LG4
Lignin peroxidase
Gene namesi
Name:GLG4
Synonyms:LIP2
OrganismiPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Taxonomic identifieri5306 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesPhanerochaetaceaePhanerochaete

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Propeptidei22 – 2871 PublicationPRO_0000023766
Chaini29 – 372344Ligninase H2PRO_0000023767Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 44
Disulfide bondi43 ↔ 314
Disulfide bondi63 ↔ 149
Disulfide bondi278 ↔ 344
Glycosylationi286 – 2861N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Expressioni

Developmental stagei

Ligninases are expressed during secondary metabolism, and are triggered by nutrient limitation.

Structurei

Secondary structure

1
372
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi41 – 466Combined sources
Helixi47 – 5610Combined sources
Turni59 – 613Combined sources
Helixi65 – 7814Combined sources
Helixi83 – 875Combined sources
Beta strandi95 – 984Combined sources
Helixi99 – 1024Combined sources
Helixi104 – 1074Combined sources
Helixi111 – 1133Combined sources
Helixi116 – 13015Combined sources
Helixi134 – 14714Combined sources
Helixi180 – 19112Combined sources
Helixi195 – 2017Combined sources
Helixi202 – 2065Combined sources
Beta strandi209 – 2146Combined sources
Beta strandi220 – 2245Combined sources
Helixi232 – 2365Combined sources
Beta strandi245 – 2473Combined sources
Beta strandi256 – 2594Combined sources
Helixi265 – 2728Combined sources
Turni274 – 2763Combined sources
Helixi277 – 2815Combined sources
Turni282 – 2854Combined sources
Helixi287 – 30216Combined sources
Turni303 – 3053Combined sources
Helixi308 – 3103Combined sources
Beta strandi311 – 3133Combined sources
Helixi315 – 3173Combined sources
Helixi337 – 3393Combined sources
Beta strandi345 – 3473Combined sources
Beta strandi356 – 3594Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QPAX-ray1.80A/B29-372[»]
ProteinModelPortaliP11542.
SMRiP11542. Positions 29-372.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11542.

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Ligninase subfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410II1B. Eukaryota.
ENOG410ZS1R. LUCA.

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF11895. DUF3415. 1 hit.
PF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00462. LIGNINASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11542-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFKQLLAAL SVALTLQVTQ AAPNLDKRVA CPDGVHTASN AACCAWFPVL
60 70 80 90 100
DDIQQNLFHG GQCGAEAHEA LRMVFHDSIA ISPKLQSQGK FGGGGADGSI
110 120 130 140 150
ITFSSIETTY HPNIGLDEVV AIQKPFIAKH GVTRGDFIAF AGAVGVSNCP
160 170 180 190 200
GAPQMQFFLG RPEATQAAPD GLVPEPFHTI DQVLARMLDA GGFDEIETVW
210 220 230 240 250
LLSAHSIAAA NDVDPTISGL PFDSTPGQFD SQFFVETQLR GTAFPGKTGI
260 270 280 290 300
QGTVMSPLKG EMRLQTDHLF ARDSRTACEW QSFVNNQTKL QEDFQFIFTA
310 320 330 340 350
LSTLGHDMNA MTDCSEVIPA PKPVNFGPSF FPAGKTHADI EQACASTPFP
360 370
TLITAPGPSA SVARIPPPPS PN
Length:372
Mass (Da):39,523
Last modified:February 1, 1991 - v2
Checksum:iA17AD0AB5FE1A290
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti312 – 3121T → I in AAA33733 (PubMed:3440521).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15599 Genomic DNA. Translation: CAA33621.1.
M18743 mRNA. Translation: AAA33733.1.
PIRiS06043. OPJGH2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15599 Genomic DNA. Translation: CAA33621.1.
M18743 mRNA. Translation: AAA33733.1.
PIRiS06043. OPJGH2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QPAX-ray1.80A/B29-372[»]
ProteinModelPortaliP11542.
SMRiP11542. Positions 29-372.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

mycoCLAPiLPO2B_PHACH.
PeroxiBasei2414. PcLiP04_BKMF1767.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410II1B. Eukaryota.
ENOG410ZS1R. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00892.
BioCyciMetaCyc:MONOMER-14340.

Miscellaneous databases

EvolutionaryTraceiP11542.

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF11895. DUF3415. 1 hit.
PF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00462. LIGNINASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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 / DSM 6909 / CBS 481.73 / BCRC 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-59.
    Strain: ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 29-372, GLYCOSYLATION AT ASN-286.

Entry informationi

Entry nameiLIG4_PHACH
AccessioniPrimary (citable) accession number: P11542
Secondary accession number(s): P14153
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: February 1, 1991
Last modified: May 11, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.