ID   LIG_PHLRA      STANDARD;      PRT;   361 AA.
AC   P20010;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   04-APR-2006, entry version 46.
DE   Ligninase-3 precursor (EC 1.11.1.14) (Ligninase III) (Diarylpropane
DE   peroxidase) (Lignin peroxidase).
OS   Phlebia radiata (White-rot fungus).
OC   Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Homobasidiomycetes;
OC   Aphyllophorales; Corticiaceae; Phlebia.
OX   NCBI_TaxID=5308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=79;
RX   MEDLINE=90185208; PubMed=2628172; DOI=10.1016/0378-1119(89)90427-7;
RA   Saloheimo M., Barajas V., Niku-Paavola M.L., Knowles J.K.C.;
RT   "A lignin peroxidase-encoding cDNA from the white-rot fungus Phlebia
RT   radiata: characterization and expression in Trichoderma reesei.";
RL   Gene 85:343-351(1989).
CC   -!- FUNCTION: Depolymerization of lignin. Catalyzes the C(alpha)-
CC       C(beta) cleavage of the propyl side chains of lignin.
CC   -!- CATALYTIC ACTIVITY: 1,2-bis-(3,4-dimethoxyphenyl)propane-1,3-diol
CC       + H(2)O(2) = veratraldehyde +
CC       1-(3,4-dimethylphenyl)ethane-1,2-diol + 4 H(2)O.
CC   -!- COFACTOR: Binds 2 calcium ions per subunit (By similarity).
CC   -!- PATHWAY: Lignin degradation; first step.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
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DR   PIR; JQ0374; JQ0374.
DR   HSSP; P06181; 1B85.
DR   InterPro; IPR001621; Ligninase.
DR   InterPro; IPR002016; Peroxidase.
DR   InterPro; IPR010255; Peroxidase_super.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00462; LIGNINASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   PROSITE; PS00435; PEROXIDASE_1; FALSE_NEG.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
KW   Calcium; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW   Lignin degradation; Metal-binding; Oxidoreductase; Peroxidase; Signal.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    361       Ligninase-3.
FT                                /FTId=PRO_0000023776.
FT   ACT_SITE     70     70       Proton acceptor (By similarity).
FT   METAL        71     71       Calcium 1 (By similarity).
FT   METAL        89     89       Calcium 1 (via carbonyl oxygen) (By
FT                                similarity).
FT   METAL        91     91       Calcium 1 (By similarity).
FT   METAL        93     93       Calcium 1 (By similarity).
FT   METAL       199    199       Iron (heme axial ligand) (By similarity).
FT   METAL       200    200       Calcium 2 (By similarity).
FT   METAL       217    217       Calcium 2 (By similarity).
FT   METAL       219    219       Calcium 2 (By similarity).
FT   METAL       222    222       Calcium 2 (via carbonyl oxygen) (By
FT                                similarity).
FT   METAL       224    224       Calcium 2 (By similarity).
FT   SITE         66     66       Transition state stabilizer (By
FT                                similarity).
FT   CARBOHYD    268    268       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   361 AA;  38439 MW;  A353806643242974 CRC64;
     MAFKQLLSAV TLALAASAAS VTRRATCPDG TQLMNAECCA LLAVRDDLQN NMFNNECGDE
     AHEALRLTFH DAIAISPAME ATGQFGGGGA DGSIMIFSDI ETKFHPNIGL DEVVESFRPF
     QQRSGMGVAD FIQFSGAVGT SNCPGAPTLN AFIGRKDATQ AAPDGLVPEP FHDVNTILAR
     FNDAGDFDEL ETVWFLIAHS VAAQNDIDPA VSHAPFDSTP SVMDGQFFIE TQLRGVEFIG
     SGGIEGVAES PVKGEFRLMS DQQIARDNRT ACEWQSFGTD QAKLQNRFQF IFEAMGQLGT
     DPTTLIDCSD VLPVPPPLST VPHFPAGITI NDVEPACAET PFPTLPTDPG PATAVAAVPR
     D
//