LIG2_PHACH
ID LIG2_PHACH Reviewed; 371 AA.
AC P49012;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Ligninase LG2;
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=GLG2; Synonyms=LIP2;
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], AND PROTEIN SEQUENCE OF 29-48.
RC STRAIN=ATCC 201542 / OGC101;
RX PubMed=1743510; DOI=10.1016/0378-1119(91)90304-t;
RA Ritch T.G. Jr., Nipper V.J., Akileswaran L., Smith A.J., Pribnow D.G.,
RA Gold M.H.;
RT "Lignin peroxidase from the basidiomycete Phanerochaete chrysosporium is
RT synthesized as a preproenzyme.";
RL Gene 107:119-126(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 201542 / OGC101;
RX PubMed=1511887; DOI=10.1016/0378-1119(92)90250-s;
RA Ritch T.G. Jr., Gold M.H.;
RT "Characterization of a highly expressed lignin peroxidase-encoding gene
RT from the basidiomycete Phanerochaete chrysosporium.";
RL Gene 118:73-80(1992).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=8440725; DOI=10.2210/pdb1lga/pdb;
RA Poulos T.L., Edwards S.L., Wariishi H., Gold M.H.;
RT "Crystallographic refinement of lignin peroxidase at 2 A.";
RL J. Biol. Chem. 268:4429-4440(1993).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND HYDROXYLATION AT TRP-199.
RC STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM
RC F-1767;
RX PubMed=10024453; DOI=10.1006/jmbi.1998.2507;
RA Choinowski T., Blodig W., Winterhalter K.H., Piontek K.;
RT "The crystal structure of lignin peroxidase at 1.70-A resolution reveals a
RT hydroxy group on the cbeta of tryptophan 171: a novel radical site formed
RT during the redox cycle.";
RL J. Mol. Biol. 286:809-827(1999).
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 Note=Binds 2 calcium ions per subunit.;
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 -!- DEVELOPMENTAL STAGE: Ligninases are expressed during secondary
CC metabolism, and are triggered by nutrient limitation.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
CC {ECO:0000305}.
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DR EMBL; M74229; AAA33735.1; -; mRNA.
DR EMBL; M92644; AAA33738.1; -; Genomic_DNA.
DR PIR; JC1268; JC1268.
DR PDB; 1LGA; X-ray; 2.03 A; A/B=29-371.
DR PDB; 1LLP; X-ray; 1.70 A; A=29-371.
DR PDBsum; 1LGA; -.
DR PDBsum; 1LLP; -.
DR AlphaFoldDB; P49012; -.
DR SMR; P49012; -.
DR CAZy; AA2; Auxiliary Activities 2.
DR PeroxiBase; 2409; PcLiP05_RP78.
DR VEuPathDB; FungiDB:AGR57_14158; -.
DR OMA; IMIFDTI; -.
DR BRENDA; 1.11.1.14; 1380.
DR UniPathway; UPA00892; -.
DR EvolutionaryTrace; P49012; -.
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: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 1: Evidence at protein level;
KW 3D-structure; Calcium; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Heme;
KW Hydroxylation; Iron; Lignin degradation; Metal-binding; Oxidoreductase;
KW Peroxidase; Signal; Zymogen.
FT SIGNAL 1..21
FT PROPEP 22..28
FT /evidence="ECO:0000269|PubMed:1743510"
FT /id="PRO_0000023762"
FT CHAIN 29..371
FT /note="Ligninase LG2"
FT /id="PRO_0000023763"
FT ACT_SITE 75
FT /note="Proton acceptor"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT SITE 71
FT /note="Transition state stabilizer"
FT MOD_RES 199
FT /note="3-hydroxytryptophan"
FT /evidence="ECO:0000269|PubMed:10024453"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..43
FT DISULFID 42..313
FT DISULFID 62..148
FT DISULFID 277..345
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:1LLP"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:1LLP"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:1LLP"
FT HELIX 64..77
FT /evidence="ECO:0007829|PDB:1LLP"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:1LLP"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1LGA"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:1LLP"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:1LLP"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:1LLP"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1LLP"
FT HELIX 115..129
FT /evidence="ECO:0007829|PDB:1LLP"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:1LLP"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:1LLP"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:1LLP"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:1LLP"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:1LLP"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:1LLP"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:1LLP"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:1LLP"
FT HELIX 264..269
FT /evidence="ECO:0007829|PDB:1LLP"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:1LLP"
FT HELIX 276..280
FT /evidence="ECO:0007829|PDB:1LLP"
FT TURN 281..284
FT /evidence="ECO:0007829|PDB:1LLP"
FT HELIX 286..301
FT /evidence="ECO:0007829|PDB:1LLP"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:1LLP"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:1LLP"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:1LLP"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:1LLP"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:1LLP"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:1LLP"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:1LLP"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:1LLP"
SQ SEQUENCE 371 AA; 39329 MW; F6AAB123EDC92123 CRC64;
MAFKQLFAAI TVALSLTAAN AAVVKEKRAT CANGKTVGDA SCCAWFDVLD DIQANMFHGG
QCGAEAHESI RLVFHDSIAI SPAMEAKGKF GGGGADGSIM IFDTIETAFH PNIGLDEVVA
MQKPFVQKHG VTPGDFIAFA GAVALSNCPG APQMNFFTGR KPATQPAPDG LVPEPFHTVD
QIIARVNDAG EFDELELVWM LSAHSVAAVN DVDPTVQGLP FDSTPGIFDS QFFVETQFRG
TLFPGSGGNQ GEVESGMAGE IRIQTDHTLA RDSRTACEWQ SFVGNQSKLV DDFQFIFLAL
TQLGQDPNAM TDCSDVIPLS KPIPGNGPFS FFPPGKSHSD IEQACAETPF PSLVTLPGPA
TSVARIPPHK A
