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Protein

Ligninase-3

Gene
N/A
Organism
Phlebia radiata (White-rot fungus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Cofactori

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

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)DescriptionActionsGraphical viewLength
Sitei66Transition state stabilizerPROSITE-ProRule annotation1
Active sitei70Proton acceptorPROSITE-ProRule annotation1
Metal bindingi71Calcium 1PROSITE-ProRule annotation1
Metal bindingi89Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi91Calcium 1PROSITE-ProRule annotation1
Metal bindingi93Calcium 1PROSITE-ProRule annotation1
Metal bindingi199Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi200Calcium 2PROSITE-ProRule annotation1
Metal bindingi217Calcium 2PROSITE-ProRule annotation1
Metal bindingi219Calcium 2PROSITE-ProRule annotation1
Metal bindingi222Calcium 2; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi224Calcium 2PROSITE-ProRule annotation1

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

UniPathwayiUPA00892.

Protein family/group databases

PeroxiBasei2297. PrLiP03.

Names & Taxonomyi

Protein namesi
Recommended name:
Ligninase-3 (EC:1.11.1.14By similarity)
Alternative name(s):
Diarylpropane peroxidase
Lignin peroxidase
Ligninase III
OrganismiPhlebia radiata (White-rot fungus)
Taxonomic identifieri5308 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesCorticialesCorticiaceaePhlebia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000002377621 – 361Ligninase-3Add BLAST341

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi268N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliP20010.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Ligninase subfamily.Curated

Keywords - Domaini

Signal

Family and domain databases

CDDicd00692. ligninase. 1 hit.
InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
PF11895. Peroxidase_ext. 1 hit.
[Graphical view]
PRINTSiPR00462. LIGNINASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00436. 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.

P20010-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFKQLLSAV TLALAASAAS VTRRATCPDG TQLMNAECCA LLAVRDDLQN
60 70 80 90 100
NMFNNECGDE AHEALRLTFH DAIAISPAME ATGQFGGGGA DGSIMIFSDI
110 120 130 140 150
ETKFHPNIGL DEVVESFRPF QQRSGMGVAD FIQFSGAVGT SNCPGAPTLN
160 170 180 190 200
AFIGRKDATQ AAPDGLVPEP FHDVNTILAR FNDAGDFDEL ETVWFLIAHS
210 220 230 240 250
VAAQNDIDPA VSHAPFDSTP SVMDGQFFIE TQLRGVEFIG SGGIEGVAES
260 270 280 290 300
PVKGEFRLMS DQQIARDNRT ACEWQSFGTD QAKLQNRFQF IFEAMGQLGT
310 320 330 340 350
DPTTLIDCSD VLPVPPPLST VPHFPAGITI NDVEPACAET PFPTLPTDPG
360
PATAVAAVPR D
Length:361
Mass (Da):38,439
Last modified:February 1, 1991 - v1
Checksum:iA353806643242974
GO

Sequence databases

PIRiJQ0374.

Cross-referencesi

Sequence databases

PIRiJQ0374.

3D structure databases

ProteinModelPortaliP20010.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei2297. PrLiP03.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00892.

Family and domain databases

CDDicd00692. ligninase. 1 hit.
InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
PF11895. Peroxidase_ext. 1 hit.
[Graphical view]
PRINTSiPR00462. LIGNINASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLIG_PHLRA
AccessioniPrimary (citable) accession number: P20010
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 30, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.