LIGA_PHACH
ID LIGA_PHACH Reviewed; 372 AA.
AC P31837;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Ligninase A;
DE EC=1.11.1.14 {ECO:0000269|PubMed:3240864};
DE AltName: Full=Diarylpropane peroxidase;
DE AltName: Full=Lignin peroxidase;
DE Flags: Precursor;
GN Name=LIPA; Synonyms=LPOB;
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 [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 [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=2373364; DOI=10.1016/0378-1119(90)90218-g;
RA Huoponen K., Ollikka P., Kaelin M., Walther I., Maentsaelae P., Reiser J.;
RT "Characterization of lignin peroxidase-encoding genes from lignin-degrading
RT basidiomycetes.";
RL Gene 89:145-150(1990).
RN [3]
RP PROTEIN SEQUENCE OF 29-58, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=3240864; DOI=10.1016/0378-1119(88)90111-4;
RA Walther L., Kaelin M., Reiser J., Suter F., Fritsche B., Saloheimo M.,
RA Leisola M., Teeri T., Knowles J.K.C., Fiechter A.;
RT "Molecular analysis of a Phanerochaete chrysosporium lignin peroxidase
RT gene.";
RL Gene 70:127-137(1988).
CC -!- FUNCTION: Depolymerization of lignin. Catalyzes the C(alpha)-C(beta)
CC cleavage of the propyl side chains of lignin.
CC {ECO:0000269|PubMed:3240864}.
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:3240864};
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:3240864};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=140 uM for H(2)O(2) {ECO:0000269|PubMed:3240864};
CC KM=200 uM for (3,4-dimethoxyphenyl)methanol
CC {ECO:0000269|PubMed:3240864};
CC pH dependence:
CC Optimum pH is 2.5. {ECO:0000269|PubMed:3240864};
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; X54257; CAA38177.1; -; Genomic_DNA.
DR EMBL; M37701; AAA33741.1; -; Genomic_DNA.
DR PIR; JH0156; JH0156.
DR PIR; PS0011; PS0011.
DR PIR; S13563; OPJGAP.
DR AlphaFoldDB; P31837; -.
DR SMR; P31837; -.
DR CAZy; AA2; Auxiliary Activities 2.
DR PeroxiBase; 2413; PcLiP02_RP78.
DR VEuPathDB; FungiDB:AGR57_14164; -.
DR BioCyc; MetaCyc:MON-14336; -.
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 1: Evidence at protein level;
KW Calcium; Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW Lignin degradation; Metal-binding; Oxidoreductase; Peroxidase; Signal;
KW Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..28
FT /evidence="ECO:0000269|PubMed:3240864"
FT /id="PRO_0000023772"
FT CHAIN 29..372
FT /note="Ligninase A"
FT /id="PRO_0000023773"
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 42..313
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"
FT CONFLICT 135
FT /note="A -> D (in Ref. 2; AAA33741)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="A -> R (in Ref. 2; AAA33741)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="L -> H (in Ref. 2; AAA33741)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 39394 MW; 04CE4598D6D6F09B CRC64;
MAFKQLVAAI SLALSLTTAN AAVVKEKRAT CSNGATVGDA SCCAWFDVLD DIQQNLFQGG
QCGAEAHESI RLVFHDAIAI SPAMEAQGKF GGGGADGSIM IFDDIEPNFH PNIGLDEIIN
LQKPFVQKHG VTPGAFIAFA GAVALSNCPG APQMNFFTGR APATQPAPDG LVPEPFHTVD
QIIARVNDAG EFDELELVWM LSAHSVAAVN DVDPTVQGLP FDSTPGIFDS QFFVETQFRG
ILFPGSGGNQ GEVESGMAGE IRIQTDHTLA RDSRTACEWQ SFVNNQSKLV SDFQFIFLAL
TQLGQDPNAM TDCSDVIPIS KPIPGNLPFS FFPPGKSMKD VEQACAETPF PSLVTLPGPA
TSVARIPPPP GA
