LIG4_PHACH
ID LIG4_PHACH Reviewed; 372 AA.
AC P11542; P14153;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Ligninase H2;
DE EC=1.11.1.14 {ECO:0000269|PubMed:3240864};
DE AltName: Full=Diarylpropane peroxidase;
DE AltName: Full=LG4;
DE AltName: Full=Lignin peroxidase;
DE Flags: Precursor;
GN Name=GLG4; 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 [GENOMIC DNA].
RC STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM
RC F-1767;
RA Naidu P.S., Zhang Y.Z., Reddy C.A.;
RL Submitted (JUN-1989) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 29-60, 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).
RN [4]
RP PROTEIN SEQUENCE OF 29-59.
RC STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM
RC F-1767;
RX PubMed=2303054; DOI=10.1111/j.1432-1033.1990.tb15333.x;
RA Glumoff T., Harvey P.J., Molinari S., Goble M., Frank G., Palmer J.M.,
RA Smit J.D.G., Leisola M.S.A.;
RT "Lignin peroxidase from Phanerochaete chrysosporium. Molecular and kinetic
RT characterization of isozymes.";
RL Eur. J. Biochem. 187:515-520(1990).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 29-372, AND GLYCOSYLATION AT
RP ASN-286.
RX PubMed=8000874; DOI=10.1016/0968-0896(94)80021-9;
RA Schoemaker H.E., Lundell T.K., Floris R., Glumoff T., Winterhalter K.H.,
RA Piontek K.;
RT "Do carbohydrates play a role in the lignin peroxidase cycle? Redox
RT catalysis in the endergonic region of the driving force.";
RL Bioorg. Med. Chem. 2:509-519(1994).
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 Note=Binds 2 calcium ions per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=85 uM for H(2)O(2) {ECO:0000269|PubMed:3240864};
CC KM=171 uM for (3,4-dimethoxyphenyl)methanol
CC {ECO:0000269|PubMed:3240864};
CC pH dependence:
CC Optimum pH is 2.3. {ECO:0000269|PubMed:3240864};
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; X15599; CAA33621.1; -; Genomic_DNA.
DR EMBL; M18743; AAA33733.1; -; mRNA.
DR PIR; S06043; OPJGH2.
DR PDB; 1QPA; X-ray; 1.80 A; A/B=29-372.
DR PDBsum; 1QPA; -.
DR AlphaFoldDB; P11542; -.
DR SMR; P11542; -.
DR CAZy; AA2; Auxiliary Activities 2.
DR CLAE; LPO2B_PHACH; -.
DR PeroxiBase; 2414; PcLiP04_BKMF1767.
DR iPTMnet; P11542; -.
DR VEuPathDB; FungiDB:AGR57_11042; -.
DR BioCyc; MetaCyc:MON-14340; -.
DR BRENDA; 1.11.1.14; 1380.
DR UniPathway; UPA00892; -.
DR EvolutionaryTrace; P11542; -.
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 3D-structure; Calcium; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Heme;
KW Hydrogen peroxide; Iron; Lignin degradation; Metal-binding; Oxidoreductase;
KW Peroxidase; Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..28
FT /evidence="ECO:0000269|PubMed:2303054,
FT ECO:0000269|PubMed:3240864"
FT /id="PRO_0000023766"
FT CHAIN 29..372
FT /note="Ligninase H2"
FT /id="PRO_0000023767"
FT ACT_SITE 76
FT /note="Proton acceptor"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT SITE 72
FT /note="Transition state stabilizer"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8000874"
FT DISULFID 31..44
FT DISULFID 43..314
FT DISULFID 63..149
FT DISULFID 278..344
FT CONFLICT 312
FT /note="T -> I (in Ref. 2; AAA33733)"
FT /evidence="ECO:0000305"
FT HELIX 41..46
FT /evidence="ECO:0007829|PDB:1QPA"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:1QPA"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1QPA"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:1QPA"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:1QPA"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1QPA"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:1QPA"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:1QPA"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1QPA"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:1QPA"
FT HELIX 134..147
FT /evidence="ECO:0007829|PDB:1QPA"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:1QPA"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:1QPA"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:1QPA"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:1QPA"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:1QPA"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:1QPA"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:1QPA"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:1QPA"
FT HELIX 265..272
FT /evidence="ECO:0007829|PDB:1QPA"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:1QPA"
FT HELIX 277..281
FT /evidence="ECO:0007829|PDB:1QPA"
FT TURN 282..285
FT /evidence="ECO:0007829|PDB:1QPA"
FT HELIX 287..302
FT /evidence="ECO:0007829|PDB:1QPA"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:1QPA"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:1QPA"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:1QPA"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:1QPA"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:1QPA"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:1QPA"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:1QPA"
SQ SEQUENCE 372 AA; 39523 MW; A17AD0AB5FE1A290 CRC64;
MAFKQLLAAL SVALTLQVTQ AAPNLDKRVA CPDGVHTASN AACCAWFPVL DDIQQNLFHG
GQCGAEAHEA LRMVFHDSIA ISPKLQSQGK FGGGGADGSI ITFSSIETTY HPNIGLDEVV
AIQKPFIAKH GVTRGDFIAF AGAVGVSNCP GAPQMQFFLG RPEATQAAPD GLVPEPFHTI
DQVLARMLDA GGFDEIETVW LLSAHSIAAA NDVDPTISGL PFDSTPGQFD SQFFVETQLR
GTAFPGKTGI QGTVMSPLKG EMRLQTDHLF ARDSRTACEW QSFVNNQTKL QEDFQFIFTA
LSTLGHDMNA MTDCSEVIPA PKPVNFGPSF FPAGKTHADI EQACASTPFP TLITAPGPSA
SVARIPPPPS PN
