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Manganese peroxidase 3 (MnP3) (EC 1.11.1.13) (Manganese peroxidase isozyme 3)

 PEM3_PHLRA              Reviewed;         362 AA.
Q96TS6;
09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
10-MAY-2017, entry version 71.
RecName: Full=Manganese peroxidase 3;
Short=MnP3;
EC=1.11.1.13;
AltName: Full=Manganese peroxidase isozyme 3;
Flags: Precursor;
Name=mnp3;
Phlebia radiata (White-rot fungus).
Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
Agaricomycetes; Polyporales; Meruliaceae; Phlebia.
NCBI_TaxID=5308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
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. This isozyme is also able to oxidize
phenols and amines in the absence of Mn(2+), similar to versatile
peroxidases. {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; AJ310930; CAC84573.1; -; mRNA.
EMBL; AJ566200; CAD92855.1; -; Genomic_DNA.
ProteinModelPortal; Q96TS6; -.
SMR; Q96TS6; -.
CAZy; AA2; Auxiliary Activities 2.
PeroxiBase; 2294; PrCIIBB03.
PRIDE; Q96TS6; -.
KEGG; ag:CAC84573; -.
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.
2: Evidence at transcript level;
Calcium; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
Lignin degradation; Manganese; Metal-binding; Oxidoreductase;
Peroxidase; Secreted; Signal.
SIGNAL 1 18 {ECO:0000255}.
PROPEP 19 23 {ECO:0000250}.
/FTId=PRO_0000391465.
CHAIN 24 362 Manganese peroxidase 3.
/FTId=PRO_5000067443.
ACT_SITE 71 71 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00297, ECO:0000255|PROSITE-
ProRule:PRU10012}.
METAL 60 60 Manganese. {ECO:0000250}.
METAL 64 64 Manganese. {ECO:0000250}.
METAL 72 72 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 90 90 Calcium 1; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 92 92 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 94 94 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 200 200 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 201 201 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 206 206 Manganese. {ECO:0000250}.
METAL 218 218 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 220 220 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 223 223 Calcium 2; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 225 225 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
SITE 67 67 Transition state stabilizer.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
CARBOHYD 126 126 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 26 39 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 38 309 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 58 144 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 273 338 {ECO:0000255|PROSITE-ProRule:PRU00297}.
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


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