PEM3_PHLRA
ID PEM3_PHLRA Reviewed; 362 AA.
AC Q96TS6;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Manganese peroxidase 3;
DE Short=MnP3;
DE EC=1.11.1.13;
DE AltName: Full=Manganese peroxidase isozyme 3;
DE Flags: Precursor;
GN Name=mnp3;
OS Phlebia radiata (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Meruliaceae; Phlebia.
OX NCBI_TaxID=5308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=ATCC 64658 / 79;
RX PubMed=15809005; DOI=10.1016/j.fgb.2005.01.008;
RA Hilden K., Martinez A.T., Hatakka A., Lundell T.;
RT "The two manganese peroxidases Pr-MnP2 and Pr-MnP3 of Phlebia radiata, a
RT lignin-degrading basidiomycete, are phylogenetically and structurally
RT divergent.";
RL Fungal Genet. Biol. 42:403-419(2005).
RN [2]
RP FUNCTION, AND INDUCTION.
RX DOI=10.1007/s002530050764;
RA Moilanen A.-M., Lundell T., Vares T., Hatakka A.;
RT "Manganese and malonate are individual regulators for the production of
RT lignin and manganese peroxidase isozymes and in the degradation of lignin
RT by Phlebia radiata.";
RL Appl. Microbiol. Biotechnol. 45:792-799(1996).
CC -!- FUNCTION: Catalyzes the oxidation of Mn(2+) to Mn(3+). The latter,
CC acting as a diffusible redox mediator, is capable of oxidizing a
CC variety of lignin compounds. This isozyme is also able to oxidize
CC phenols and amines in the absence of Mn(2+), similar to versatile
CC peroxidases. {ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + H2O2 + 2 Mn(2+) = 2 H2O + 2 Mn(3+);
CC Xref=Rhea:RHEA:22776, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:29035, ChEBI:CHEBI:29041;
CC EC=1.11.1.13;
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 Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00297};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- INDUCTION: By a combination of high manganese and malonate levels.
CC {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ310930; CAC84573.1; -; mRNA.
DR EMBL; AJ566200; CAD92855.1; -; Genomic_DNA.
DR AlphaFoldDB; Q96TS6; -.
DR SMR; Q96TS6; -.
DR CAZy; AA2; Auxiliary Activities 2.
DR PeroxiBase; 2294; PrCIIBB03.
DR KEGG; ag:CAC84573; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016689; F:manganese peroxidase activity; IEA:UniProtKB-EC.
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-KW.
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 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW Lignin degradation; Manganese; Metal-binding; Oxidoreductase; Peroxidase;
KW Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..23
FT /evidence="ECO:0000250"
FT /id="PRO_0000391465"
FT CHAIN 24..362
FT /note="Manganese peroxidase 3"
FT /id="PRO_5000067443"
FT REGION 341..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 71
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 60
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 200
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 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 206
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 67
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..39
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 38..309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 58..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 273..338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ SEQUENCE 362 AA; 37815 MW; 996683DB86F6741B CRC64;
MAFKQLLTAI SIVSVANAAL TRRVACPDGV NTATNAVCCS LFAVRDLIQD QLFDGGECGE
EVHESLRLTF HDAIGISPTI ASTGVFGGGG ADGSIAIFAE IETNFHANNG VDEIIGEQAP
FIQMTNMTTA DFIQFAGAVG VSNCPGAPAL PVFVGRPDAT QPAPDKTVPE PFDTVDSILA
RFADAGGFSS AEVVALLASH TIAAADHVDP SIPGTPFDST PEIFDTQFFI ETQLRGILFP
GTGGNQGEVE SPLHGEIRLQ SDSELARDSR TACEWQSFVN NQAKIQSAFK AAFRKMTILG
HSESSLIECS EVIQTPPALE GNAHLPAGQT MNDIEQACAT TPFPSLSADP GPATSVAPVP
PS
