PEM2_PHLRA
ID PEM2_PHLRA Reviewed; 390 AA.
AC Q70LM3; Q96TS5;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Manganese peroxidase 2;
DE Short=MnP2;
DE EC=1.11.1.13;
DE AltName: Full=Manganese peroxidase isozyme 2;
DE Flags: Precursor;
GN Name=mnp2;
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], AND PROTEIN SEQUENCE OF
RP N-TERMINUS.
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. {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; AJ315701; CAC85963.1; -; mRNA.
DR EMBL; AJ566199; CAD92854.1; -; Genomic_DNA.
DR AlphaFoldDB; Q70LM3; -.
DR SMR; Q70LM3; -.
DR CAZy; AA2; Auxiliary Activities 2.
DR PeroxiBase; 2296; PrMnP02.
DR KEGG; ag:CAC85963; -.
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 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein; Heme;
KW Hydrogen peroxide; Iron; Lignin degradation; Manganese; Metal-binding;
KW Oxidoreductase; Peroxidase; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:15809005"
FT CHAIN 24..390
FT /note="Manganese peroxidase 2"
FT /id="PRO_5000071417"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 59
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
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 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 88
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 197
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 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="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 66
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..39
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 38..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 57..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 277..343
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 365..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CONFLICT 131
FT /note="Q -> H (in Ref. 1; CAC85963)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="I -> V (in Ref. 1; CAC85963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 40326 MW; 270D7F2C36A99E50 CRC64;
MAFNFAAILA FVSLAAVTSA APSKTTCSNG VVVPDAVCCD FVPLASALQS EVLMGDCGED
AHELVRLIFH DAIAISQSMG PSAGGGADGS MLIFPTVEPA FFPNLGIADS VNNLIPFLSQ
FPTISAGDLV QFAGAVAISN CPGAPQLEFL AGRPNATAPA IDGLIPEPQD DVTKILARFK
DAGNFSPAEV VALLASHSIA RADHVDPTLD AAPFDSTPFD FDTQIFLEVL LKGVGFPGLA
NNTGEVSSPL PVTDGTDVGE LRLQSDFALA RDERTACAWQ SFVNEQEAMA TAFKNAVKKL
AVLGHNRNDL VDCSAVVPVP KPATGTPATF PASTGPQDLE LTCTTEPFPT LSTAPGAQQT
LIPHCSDGTM TCNSVQFDGP ATNFGGADDS
