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Manganese peroxidase 2 (MnP2) (EC 1.11.1.13) (Manganese peroxidase isozyme 2)

 PEM2_PHLRA              Reviewed;         390 AA.
Q70LM3; Q96TS5;
09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
10-MAY-2017, entry version 55.
RecName: Full=Manganese peroxidase 2;
Short=MnP2;
EC=1.11.1.13;
AltName: Full=Manganese peroxidase isozyme 2;
Flags: Precursor;
Name=mnp2;
Phlebia radiata (White-rot fungus).
Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
Agaricomycetes; Polyporales; Meruliaceae; Phlebia.
NCBI_TaxID=5308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PROTEIN SEQUENCE OF
N-TERMINUS.
STRAIN=ATCC 64658 / 79;
PubMed=15809005; DOI=10.1016/j.fgb.2005.01.008;
Hilden K., Martinez A.T., Hatakka A., Lundell T.;
"The two manganese peroxidases Pr-MnP2 and Pr-MnP3 of Phlebia radiata,
a lignin-degrading basidiomycete, are phylogenetically and
structurally divergent.";
Fungal Genet. Biol. 42:403-419(2005).
[2]
FUNCTION, AND INDUCTION.
DOI=10.1007/s002530050764;
Moilanen A.-M., Lundell T., Vares T., Hatakka A.;
"Manganese and malonate are individual regulators for the production
of lignin and manganese peroxidase isozymes and in the degradation of
lignin by Phlebia radiata.";
Appl. Microbiol. Biotechnol. 45:792-799(1996).
-!- FUNCTION: Catalyzes the oxidation of Mn(2+) to Mn(3+). The latter,
acting as a diffusible redox mediator, is capable of oxidizing a
variety of lignin compounds. {ECO:0000269|Ref.2}.
-!- CATALYTIC ACTIVITY: 2 Mn(2+) + 2 H(+) + H(2)O(2) = 2 Mn(3+) + 2
H(2)O.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
subunit. {ECO:0000255|PROSITE-ProRule:PRU00297};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE-
ProRule:PRU00297};
-!- SUBCELLULAR LOCATION: Secreted.
-!- INDUCTION: By a combination of high manganese and malonate levels.
{ECO:0000269|Ref.2}.
-!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
{ECO:0000305}.
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EMBL; AJ315701; CAC85963.1; -; mRNA.
EMBL; AJ566199; CAD92854.1; -; Genomic_DNA.
ProteinModelPortal; Q70LM3; -.
SMR; Q70LM3; -.
CAZy; AA2; Auxiliary Activities 2.
PeroxiBase; 2296; PrMnP02.
KEGG; ag:CAC85963; -.
KO; K20205; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0016689; F:manganese peroxidase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
CDD; cd00692; ligninase; 1.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
InterPro; IPR001621; Ligninase.
InterPro; IPR024589; Ligninase_C.
InterPro; IPR019794; Peroxidases_AS.
InterPro; IPR019793; Peroxidases_heam-ligand_BS.
Pfam; PF00141; peroxidase; 1.
Pfam; PF11895; Peroxidase_ext; 1.
PRINTS; PR00462; LIGNINASE.
PRINTS; PR00458; PEROXIDASE.
SUPFAM; SSF48113; SSF48113; 1.
PROSITE; PS00435; PEROXIDASE_1; 1.
PROSITE; PS00436; PEROXIDASE_2; 1.
PROSITE; PS50873; PEROXIDASE_4; 1.
1: Evidence at protein level;
Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein;
Heme; Hydrogen peroxide; Iron; Lignin degradation; Manganese;
Metal-binding; Oxidoreductase; Peroxidase; Secreted; Signal.
SIGNAL 1 23 {ECO:0000269|PubMed:15809005}.
CHAIN 24 390 Manganese peroxidase 2.
/FTId=PRO_5000071417.
ACT_SITE 70 70 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00297, ECO:0000255|PROSITE-
ProRule:PRU10012}.
METAL 59 59 Manganese. {ECO:0000250}.
METAL 63 63 Manganese. {ECO:0000250}.
METAL 71 71 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 86 86 Calcium 1; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 88 88 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 90 90 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 197 197 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 198 198 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 203 203 Manganese. {ECO:0000250}.
METAL 215 215 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 217 217 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 222 222 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
SITE 66 66 Transition state stabilizer.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
CARBOHYD 155 155 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 27 39 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 38 313 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 57 141 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 277 343 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 365 372 {ECO:0000255|PROSITE-ProRule:PRU00297}.
CONFLICT 131 131 Q -> H (in Ref. 1; CAC85963).
{ECO:0000305}.
CONFLICT 225 225 I -> V (in Ref. 1; CAC85963).
{ECO:0000305}.
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


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