ID A0A1M2W425_TRAPU Unreviewed; 365 AA.
AC A0A1M2W425;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051};
DE EC=1.11.1.- {ECO:0000256|RuleBase:RU363051};
GN ORFNames=TRAPUB_8933 {ECO:0000313|EMBL:OJT14530.1};
OS Trametes pubescens (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=154538 {ECO:0000313|EMBL:OJT14530.1, ECO:0000313|Proteomes:UP000184267};
RN [1] {ECO:0000313|EMBL:OJT14530.1, ECO:0000313|Proteomes:UP000184267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBCC735 {ECO:0000313|EMBL:OJT14530.1,
RC ECO:0000313|Proteomes:UP000184267};
RA Makela M.R., Granchi Z., Peng M., De Vries R.P., Grigoriev I., Riley R.,
RA Hilden K.;
RT "Genome sequence of the basidiomycete white-rot fungus Trametes
RT pubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR601621-2,
CC ECO:0000256|RuleBase:RU363051};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR601621-
CC 2, ECO:0000256|RuleBase:RU363051};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|PIRSR:PIRSR601621-2};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000256|PIRSR:PIRSR601621-2};
CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
CC {ECO:0000256|ARBA:ARBA00006089, ECO:0000256|RuleBase:RU363051}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJT14530.1}.
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DR EMBL; MNAD01000280; OJT14530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M2W425; -.
DR STRING; 154538.A0A1M2W425; -.
DR OMA; HACAETP; -.
DR OrthoDB; 1010072at2759; -.
DR Proteomes; UP000184267; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00692; ligninase; 1.
DR Gene3D; 1.10.520.10; -; 1.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 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 PANTHER; PTHR31356:SF8; L-ASCORBATE PEROXIDASE 6-RELATED; 1.
DR PANTHER; PTHR31356; THYLAKOID LUMENAL 29 KDA PROTEIN, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00141; peroxidase; 1.
DR Pfam; PF11895; Peroxidase_ext; 1.
DR PRINTS; PR00462; LIGNINASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR601621-2, ECO:0000256|RuleBase:RU363051};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601621-4};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR601621-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR601621-2};
KW Lignin degradation {ECO:0000256|ARBA:ARBA00023185};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601621-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU363051};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU363051};
KW Reference proteome {ECO:0000313|Proteomes:UP000184267};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU363051}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU363051"
FT CHAIN 22..365
FT /note="Peroxidase"
FT /evidence="ECO:0000256|RuleBase:RU363051"
FT /id="PRO_5011819951"
FT DOMAIN 48..287
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|Pfam:PF00141"
FT DOMAIN 291..365
FT /note="Fungal ligninase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11895"
FT ACT_SITE 75
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-1"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 206
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:0000256|PIRSR:PIRSR601621-2"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT SITE 71
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-3"
FT DISULFID 30..43
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
FT DISULFID 42..315
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
FT DISULFID 62..148
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
FT DISULFID 279..344
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
SQ SEQUENCE 365 AA; 39303 MW; 6EA06C56E364690B CRC64;
MAFKLLSSFV ALAAALQGVS AAALNRRVAC PDGVHTASNE ACCQLFAVRE DLQKNLFDGA
QCNAEAHESL RLTFHDAIAI SPALEAQGTF GGGGADGSIA IFSHIETAFH PNIGLDEIVE
KQRPFIERHN LGVADFIQFA GALGASNCPG APQLSAFVGR KDATRPAPDG LVPEPFHTPD
MIFDRLADAS QGEFDPILTV WLLTAHTVAA ANDVDPTIPG SPFDSTPGEF DSQFFLETQL
KGTLFPGDGP NQGEVESPMR GEFRLQSDFA IARDERTACE WQSFVNNQTK VQQMFQFVFH
DLSLFGQNIT DLVDCTEVIP VPKPLRQATH FPAGFTVRDI EHACAETPFP TLPTQPGPKT
SVAPV
//
