LIG_PHLRA
ID LIG_PHLRA Reviewed; 361 AA.
AC P20010;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Ligninase-3;
DE EC=1.11.1.14 {ECO:0000250|UniProtKB:P06181};
DE AltName: Full=Diarylpropane peroxidase;
DE AltName: Full=Lignin peroxidase;
DE AltName: Full=Ligninase III;
DE Flags: Precursor;
OS Phlebia radiata (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Meruliaceae; Phlebia.
OX NCBI_TaxID=5308;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64658 / 79;
RX PubMed=2628172; DOI=10.1016/0378-1119(89)90427-7;
RA Saloheimo M., Barajas V., Niku-Paavola M.L., Knowles J.K.C.;
RT "A lignin peroxidase-encoding cDNA from the white-rot fungus Phlebia
RT radiata: characterization and expression in Trichoderma reesei.";
RL Gene 85:343-351(1989).
CC -!- FUNCTION: Depolymerization of lignin. Catalyzes the C(alpha)-C(beta)
CC cleavage of the propyl side chains of lignin.
CC {ECO:0000250|UniProtKB:P06181}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol +
CC H2O2 = 3,4-dimethoxybenzaldehyde + glycolaldehyde + guaiacol + H2O;
CC Xref=Rhea:RHEA:48004, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17071, ChEBI:CHEBI:17098, ChEBI:CHEBI:28591,
CC ChEBI:CHEBI:86963; EC=1.11.1.14;
CC Evidence={ECO:0000250|UniProtKB:P06181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-
CC dimethoxyphenyl)methanol radical + 2 H2O; Xref=Rhea:RHEA:30271,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:62150,
CC ChEBI:CHEBI:88143; EC=1.11.1.14;
CC Evidence={ECO:0000250|UniProtKB:P06181};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00297};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:P06181};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000250|UniProtKB:P06181};
CC -!- PATHWAY: Secondary metabolite metabolism; lignin degradation.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
CC {ECO:0000305}.
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DR PIR; JQ0374; JQ0374.
DR AlphaFoldDB; P20010; -.
DR SMR; P20010; -.
DR PeroxiBase; 2297; PrLiP03.
DR UniPathway; UPA00892; -.
DR GO; GO:0016690; F:diarylpropane peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00692; ligninase; 1.
DR InterPro; IPR044831; Ccp1-like.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR001621; Ligninase.
DR InterPro; IPR024589; Ligninase_C.
DR InterPro; IPR019794; Peroxidases_AS.
DR PANTHER; PTHR31356; PTHR31356; 1.
DR Pfam; PF00141; peroxidase; 1.
DR Pfam; PF11895; Peroxidase_ext; 1.
DR PRINTS; PR00462; LIGNINASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Calcium; Glycoprotein; Heme; Hydrogen peroxide; Iron; Lignin degradation;
KW Metal-binding; Oxidoreductase; Peroxidase; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..361
FT /note="Ligninase-3"
FT /id="PRO_0000023776"
FT REGION 341..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 199
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 66
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 361 AA; 38439 MW; A353806643242974 CRC64;
MAFKQLLSAV TLALAASAAS VTRRATCPDG TQLMNAECCA LLAVRDDLQN NMFNNECGDE
AHEALRLTFH DAIAISPAME ATGQFGGGGA DGSIMIFSDI ETKFHPNIGL DEVVESFRPF
QQRSGMGVAD FIQFSGAVGT SNCPGAPTLN AFIGRKDATQ AAPDGLVPEP FHDVNTILAR
FNDAGDFDEL ETVWFLIAHS VAAQNDIDPA VSHAPFDSTP SVMDGQFFIE TQLRGVEFIG
SGGIEGVAES PVKGEFRLMS DQQIARDNRT ACEWQSFGTD QAKLQNRFQF IFEAMGQLGT
DPTTLIDCSD VLPVPPPLST VPHFPAGITI NDVEPACAET PFPTLPTDPG PATAVAAVPR
D
