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Manganese peroxidase H3 (EC 1.11.1.13) (Peroxidase manganese-dependent H3)

 PEM3_PHACH              Reviewed;         380 AA.
P78733; Q01666;
01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 2.
10-MAY-2017, entry version 86.
RecName: Full=Manganese peroxidase H3;
EC=1.11.1.13;
AltName: Full=Peroxidase manganese-dependent H3;
Flags: Precursor;
Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum
pruinosum).
Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
Agaricomycetes; Polyporales; Phanerochaetaceae; Phanerochaete.
NCBI_TaxID=5306;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 /
VKM F-1767;
PubMed=7926830; DOI=10.1016/0378-1119(94)90251-8;
Orth A.B., Rzhetskaya M., Cullen D., Tien M.;
"Characterization of a cDNA encoding a manganese peroxidase from
Phanerochaete chrysosporium: genomic organization of lignin and
manganese peroxidase-encoding genes.";
Gene 148:161-165(1994).
[2]
PROTEIN SEQUENCE OF 26-45.
PubMed=1592808; DOI=10.1128/jb.174.11.3532-3540.1992;
Pease E.A., Tien M.;
"Heterogeneity and regulation of manganese peroxidases from
Phanerochaete chrysosporium.";
J. Bacteriol. 174:3532-3540(1992).
-!- 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.
-!- 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.
-!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
{ECO:0000305}.
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EMBL; U10306; AAA62243.1; -; mRNA.
PIR; JC2579; JC2579.
ProteinModelPortal; P78733; -.
SMR; P78733; -.
CAZy; AA2; Auxiliary Activities 2.
mycoCLAP; MPO2C_PHACH; -.
PeroxiBase; 2382; PcMnP03_.
eggNOG; ENOG410IZ9A; Eukaryota.
eggNOG; ENOG410YEPY; LUCA.
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 25 {ECO:0000269|PubMed:1592808}.
CHAIN 26 380 Manganese peroxidase H3.
/FTId=PRO_0000023779.
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 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 220 220 Calcium 2; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 222 222 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
SITE 67 67 Transition state stabilizer.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 155 155 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 40 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 39 312 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 58 141 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 277 342 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 364 371 {ECO:0000255|PROSITE-ProRule:PRU00297}.
SEQUENCE 380 AA; 40078 MW; 4C8931EA3940BBA6 CRC64;
MAFASSLLAL VALAAVTSAA PATTQATCPD GTKVNNAACC AFIPLAQDLQ ETIFQNDCGE
DAHEVIRLTF HDAIAISQSK GPSAGGADGS MLLFPTIEPN FSANNGIDDS VNNLIPFMQK
HNTISAGDIV QFTGAVALTN CPGAPQLEFL ARRPNKTIPA IDGLIPEPQD SVTSILERFK
DAGNFSPFEV VSLLASHSVA RADKVDETID AAPFDTTPFV FDTQIFLEVL LKGVGFPGTR
TTRGEVASPL PLTSGSDTGE LRLQSDFALA RDERTACIWQ GFVNEQALMA SFKAAMRKLA
VLGQHRNTLI DCSDVVPAPK PAVNKPASFP ATTGPQDLEL SCNTKPFPSL SVDAGAQQTL
IPHCSDGDMT CQSVQFNGPA


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