LIG5_PHACH
ID LIG5_PHACH Reviewed; 371 AA.
AC P11543;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Ligninase LG5;
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=GLG5; Synonyms=LIP6;
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].
RX PubMed=3440521; DOI=10.1016/0378-1119(87)90217-4;
RA de Boer H.A., Zhang Y.Z., Collins C., Reddy C.A.;
RT "Analysis of nucleotide sequences of two ligninase cDNAs from a white-rot
RT filamentous fungus, Phanerochaete chrysosporium.";
RL Gene 60:93-102(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM
RC F-1767;
RX PubMed=2011531; DOI=10.1093/nar/19.3.599;
RA Gaskell J., Dieperink E., Cullen D.;
RT "Genomic organization of lignin peroxidase genes of Phanerochaete
RT chrysosporium.";
RL Nucleic Acids Res. 19:599-603(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM
RC F-1767;
RX PubMed=1999283; DOI=10.1016/0378-1119(91)90051-c;
RA Zhang Y.Z., Reddy C.A., Rasooly A.;
RT "Cloning of several lignin peroxidase (LIP)-encoding genes: sequence
RT analysis of the LIP6 gene from the white-rot basidiomycete, Phanerochaete
RT chrysosporium.";
RL Gene 97:191-198(1991).
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 EMBL; M18794; AAA33734.1; -; mRNA.
DR EMBL; X55343; CAA39033.1; -; Genomic_DNA.
DR EMBL; M63496; AAA33739.1; -; Genomic_DNA.
DR PIR; JN0117; OPJGG5.
DR AlphaFoldDB; P11543; -.
DR SMR; P11543; -.
DR CAZy; AA2; Auxiliary Activities 2.
DR PeroxiBase; 2411; PcLiP03_BKMF1767.
DR VEuPathDB; FungiDB:AGR57_14174; -.
DR BioCyc; MetaCyc:MON-14339; -.
DR BRENDA; 1.11.1.14; 1380.
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..27
FT /evidence="ECO:0000255"
FT /id="PRO_0000023768"
FT CHAIN 28..371
FT /note="Ligninase LG5"
FT /id="PRO_0000023769"
FT REGION 349..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 74
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 92
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 202
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 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 220
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 225
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 SITE 70
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 41..311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 61..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 275..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ SEQUENCE 371 AA; 39418 MW; F0AE30C69D7EF5C2 CRC64;
MAFKKLLAVL TAALSLRAAQ GAAVEKRATC SNGKVVPAAS CCTWFNVLSD IQENLFNGGQ
CGAEAHESIR LVFHDAIAIS PAMEPQASSV RGADGSIMIF DEIETNFHPN IGLDEIVRLQ
KPFVQKHGVT PGDFIAFAGA VALSNCPGAP QMNFFTGRAP ATQPAPDGLV PEPFHSVDQI
IDRVFDAGEF DELELVWMLS AHSVAAANDI DPNIQGLPFD STPGIFDSQF FVETQLAGTG
FTGGSNNQGE VSSPLPGEMR LQSDFLIARD ARTACEWQSF VNNQSKLVSD FQFIFLALTQ
LGQDPDAMTD CSAVIPISKP APNNTPGFSF FPPGMTMDDV EQACAETPFP TLSTLPGPAT
SVARIPPPPG A
