LIG6_PHACH
ID LIG6_PHACH Reviewed; 372 AA.
AC P50622;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Ligninase LG6;
DE EC=1.11.1.14 {ECO:0000250|UniProtKB:P06181};
DE AltName: Full=Diarylpropane peroxidase;
DE AltName: Full=Lignin peroxidase;
DE Flags: Precursor;
GN Name=GLG6;
OS Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerodontia.
OX NCBI_TaxID=2822231;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM
RC F-1767;
RX PubMed=2268360; DOI=10.1016/s0006-291x(05)80884-8;
RA Naidu P.S., Zhang Y.Z., Reddy C.A.;
RT "Characterization of a new lignin peroxidase gene (GLG6) from Phanerochaete
RT chrysosporium.";
RL Biochem. Biophys. Res. Commun. 173:994-1000(1990).
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=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00297};
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 -!- PATHWAY: Secondary metabolite metabolism; lignin degradation.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
CC {ECO:0000305}.
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DR EMBL; M80213; AAA33737.1; -; mRNA.
DR AlphaFoldDB; P50622; -.
DR SMR; P50622; -.
DR CAZy; AA2; Auxiliary Activities 2.
DR PeroxiBase; 2415; PcLiP06.
DR VEuPathDB; FungiDB:AGR57_14201; -.
DR BioCyc; MetaCyc:MON-14342; -.
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 InterPro; IPR019793; Peroxidases_heam-ligand_BS.
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; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW Heme; Hydrogen peroxide; Iron; Lignin degradation; Metal-binding;
KW Oxidoreductase; Peroxidase; Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..28
FT /evidence="ECO:0000255"
FT /id="PRO_0000023770"
FT CHAIN 29..372
FT /note="Ligninase LG6"
FT /id="PRO_0000023771"
FT REGION 352..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 75
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 204
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 205
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 BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 71
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..43
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 62..148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 277..345
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ SEQUENCE 372 AA; 39259 MW; B192A93351F8CC16 CRC64;
MALKQLAAAV ALALSIQAAQ GAAVKEKRAT CSNGATVGDA SSCAWFDVLD DIQQNLFNGA
QCGAEAHESI RLVFHDAIAI SPALESQGKF GGGGADGSII LFDDIETNFH PNIGLDEIVN
LQKPFIQKHG VTPGDFIAFA GAVAMSNCPG APQMNFFTGR APATQAAPDG LVPEPFHTVD
QIISRVNDAG EFDELELVWM LSAHSVAAAN DVDPTIQGLA FDSTPGVFDS QFFVETQLRG
TAFPGSGGNQ GEVESPLPGE MRLQSDSSIA RDSRTACEWQ SFVNNQSKLV SDFQFIFLAL
TQLGENPDAM TDCSDVIPIS KPVPNNVPFS FFPAGKTMAD VEQACAETPF PTLTTLPGPE
TSVQRIQPPP GA
