LIGC_TRAVE
ID LIGC_TRAVE Reviewed; 372 AA.
AC P20013;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ligninase C;
DE EC=1.11.1.14 {ECO:0000269|PubMed:2707445};
DE AltName: Full=Diarylpropane peroxidase;
DE AltName: Full=Lignin peroxidase;
DE Flags: Precursor;
OS Trametes versicolor (White-rot fungus) (Coriolus versicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5325;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PRL 572;
RX PubMed=1581393; DOI=10.1016/0300-9084(92)90043-e;
RA Joensson L.J., Nyman P.O.;
RT "Characterization of a lignin peroxidase gene from the white-rot fungus
RT Trametes versicolor.";
RL Biochimie 74:177-182(1992).
RN [2]
RP PROTEIN SEQUENCE OF 27-38, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=2707445; DOI=10.1016/0014-5793(89)81258-x;
RA Joensson L.J., Karlsson O., Lundquist K., Nyman P.O.;
RT "Trametes versicolor ligninase: isozyme sequence homology and substrate
RT specificity.";
RL FEBS Lett. 247:143-146(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:0000269|PubMed:2707445};
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:0000269|PubMed:2707445};
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 -!- 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; M64993; AAA34049.1; -; Genomic_DNA.
DR PIR; S32581; S32581.
DR AlphaFoldDB; P20013; -.
DR SMR; P20013; -.
DR CAZy; AA2; Auxiliary Activities 2.
DR CLAE; LPO2C_TRAVE; -.
DR PeroxiBase; 2420; TvLiP12_PRL572.
DR OMA; YDHTCPH; -.
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 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Glycoprotein; Heme; Hydrogen peroxide;
KW Iron; Lignin degradation; Metal-binding; Oxidoreductase; Peroxidase;
KW Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:2707445"
FT CHAIN 27..372
FT /note="Ligninase C"
FT /id="PRO_0000023777"
FT REGION 346..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..372
FT /note="Pro residues"
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 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 205
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 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 223
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 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 230
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 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 372 AA; 39625 MW; 9F7A06AABAA9B25A CRC64;
MAFKSLLSFV SVIGALQGAN AALTRRVACP DGVNTATNAA CCQLFAVRED LQQNLFHGGL
CTAEAHESLR LTFHDAIAIS PALEAQGIFG GGGADGSIAI FPEIETNFHP NIGLDEIIEL
QKPFIARHNI SVADFIQFAG AIGASNCAGA PQLAAFVGRK DATQPAPDGL VPEPFHTPDQ
IFDRLADASQ GEFDPILTVW LLTAHTVAAA NDVDPTKSGL PFDSTPELWD TQFFLETQLR
GTSFPGSGGN QGEVESPLAG EMRLQSDHTI ARDSRTACEW QSFVDNQPKA QQMFQFVFHD
LSIFGQDINT LVDCTEVVPI PADPQGHTHF PAGLSNADIE QACAETPFPT FPTDPGPKTA
VAPVPKPPAA RK
