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Database: UniProt
Entry: C0IW58
LinkDB: C0IW58
Original site: C0IW58 
ID   LNP_TAICA               Reviewed;         330 AA.
AC   C0IW58; C0IMT9;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   19-FEB-2014, entry version 18.
DE   RecName: Full=Low-redox potential peroxidase;
DE            EC=1.11.1.7;
DE   AltName: Full=Putative ligninolytic peroxidase;
DE   Flags: Precursor;
GN   Name=LnP;
OS   Taiwanofungus camphoratus (Poroid brown-rot fungus) (Antrodia
OS   camphorata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Taiwanofungus.
OX   NCBI_TaxID=196114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBCELLULAR LOCATION.
RC   STRAIN=ACT1;
RX   PubMed=19202090; DOI=10.1099/mic.0.022459-0;
RA   Huang S.T., Tzean S.S., Tsai B.Y., Hsieh H.J.;
RT   "Cloning and heterologous expression of a novel ligninolytic
RT   peroxidase gene from poroid brown-rot fungus Antrodia cinnamomea.";
RL   Microbiology 155:424-433(2009).
CC   -!- FUNCTION: Can oxidize the lignin redox mediator veratryl alcohol
CC       to veratryl aldehyde. May be involved in oxidation of
CC       lignocellulose substrates.
CC   -!- CATALYTIC ACTIVITY: 2 phenolic donor + H(2)O(2) = 2 phenoxyl
CC       radical of the donor + 2 H(2)O.
CC   -!- COFACTOR: Binds 2 calcium ions per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per
CC       subunit (By similarity).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=13.1 uM for veratryl alcohol;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: In comparison to other ligninolytic peroxidases,
CC       lacks a Mn(2+)-oxidation site (as in manganese peroxidases (MnP)
CC       and versatile peroxidase (VP)) and an exposed tryptophan
CC       responsible for high redox-potential substrate oxidation (as in
CC       lignin peroxidase (LiP) and VP).
CC   -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
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DR   EMBL; EU289404; ACA48489.1; -; mRNA.
DR   EMBL; EU526903; ACD44888.1; -; Genomic_DNA.
DR   mycoCLAP; LPO2A_TAICA; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR010255; Haem_peroxidase.
DR   InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
DR   InterPro; IPR001621; Ligninase.
DR   InterPro; IPR024589; Ligninase_C.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   Pfam; PF11895; DUF3415; 1.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00462; LIGNINASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; SSF48113; 1.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   1: Evidence at protein level;
KW   Calcium; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW   Metal-binding; Oxidoreductase; Peroxidase; Secreted; Signal.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25    330       Low-redox potential peroxidase.
FT                                /FTId=PRO_0000393299.
FT   METAL        69     69       Calcium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        71     71       Calcium 1 (By similarity).
FT   METAL        73     73       Calcium 1 (By similarity).
FT   METAL       178    178       Iron (heme axial ligand) (By similarity).
FT   METAL       179    179       Calcium 2 (By similarity).
FT   METAL       196    196       Calcium 2 (By similarity).
FT   METAL       198    198       Calcium 2 (By similarity).
FT   METAL       203    203       Calcium 2 (By similarity).
FT   CARBOHYD     27     27       N-linked (GlcNAc...) (Potential).
FT   DISULFID     34    285       By similarity.
FT   DISULFID     54    123       By similarity.
FT   DISULFID    251    314       By similarity.
FT   CONFLICT    184    184       N -> K (in Ref. 1; ACA48489).
FT   CONFLICT    230    230       P -> L (in Ref. 1; ACA48489).
FT   CONFLICT    313    313       S -> P (in Ref. 1; ACA48489).
SQ   SEQUENCE   330 AA;  35770 MW;  8F7D76BACF5CE1B3 CRC64;
     MRSSTHIFVS FVVYCGVFVT SAIALSNHTN AYQCDRWSNV LNELQANLFH EGQCRSAALR
     ASGTFGGGGA DGSIIQFAHT ELAYPANEGL EEMVYTLKHF ADGHEVSYGD MIQFAGAVAL
     SNCPGSPRLR FYAGRPEAIA PSPPNLLPLP TDPVEKILSR MADAGFNAGD TVALLAAHSI
     AVQNTIDPSI PDSPLDSTPR IFDTQFYLET LLRGTRYPGK GRGPAQSKSP IEHEFRLASD
     AAIARHTSTA CEWQSFIDNQ EGLRSAFRNA MVKLANQGHD NLVDCSFVIP VPPPWNLPVE
     YPSGKSRSDV EQSCSDVPFP TISLNSDVHD
//
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