LNP_TAICA
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 03-AUG-2022, entry version 36.
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 camphorata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporales incertae sedis; Taiwanofungus.
OX NCBI_TaxID=2696576;
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 peroxidase
RT gene from poroid brown-rot fungus Antrodia cinnamomea.";
RL Microbiology 155:424-433(2009).
CC -!- FUNCTION: Can oxidize the lignin redox mediator veratryl alcohol to
CC veratryl aldehyde. May be involved in oxidation of lignocellulose
CC substrates. {ECO:0000269|PubMed:19202090}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
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:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00297};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.1 uM for veratryl alcohol {ECO:0000269|PubMed:19202090};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297,
CC ECO:0000269|PubMed:19202090}.
CC -!- MISCELLANEOUS: In comparison to other ligninolytic peroxidases, lacks a
CC Mn(2+)-oxidation site (as in manganese peroxidases (MnP) and versatile
CC peroxidase (VP)) and an exposed tryptophan responsible for high redox-
CC potential substrate oxidation (as in lignin peroxidase (LiP) and VP).
CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
CC {ECO:0000305}.
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DR EMBL; EU289404; ACA48489.1; -; mRNA.
DR EMBL; EU526903; ACD44888.1; -; Genomic_DNA.
DR AlphaFoldDB; C0IW58; -.
DR SMR; C0IW58; -.
DR CAZy; AA2; Auxiliary Activities 2.
DR CLAE; 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:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
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; 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; 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
FT /evidence="ECO:0000255"
FT CHAIN 25..330
FT /note="Low-redox potential peroxidase"
FT /id="PRO_0000393299"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 178
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 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 54..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 251..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CONFLICT 184
FT /note="N -> K (in Ref. 1; ACA48489)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="P -> L (in Ref. 1; ACA48489)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="S -> P (in Ref. 1; ACA48489)"
FT /evidence="ECO:0000305"
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
