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Manganese peroxidase H4 (EC 1.11.1.13) (MP-I) (Peroxidase manganese-dependent H4)

 PEM4_PHACH              Reviewed;         382 AA.
P19136;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
07-JUN-2017, entry version 110.
RecName: Full=Manganese peroxidase H4;
EC=1.11.1.13;
AltName: Full=MP-I;
AltName: Full=Peroxidase manganese-dependent H4;
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], PROTEIN SEQUENCE OF 25-45, FUNCTION,
SUBCELLULAR LOCATION, INDUCTION, AND DISULFIDE BONDS.
STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 /
VKM F-1767;
PubMed=2760033;
Pease E.A., Andrawis A., Tien M.;
"Manganese-dependent peroxidase from Phanerochaete chrysosporium.
Primary structure deduced from cDNA sequence.";
J. Biol. Chem. 264:13531-13535(1989).
[2]
PROTEIN SEQUENCE OF 25-44.
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. {ECO:0000269|PubMed:2760033}.
-!- 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 {ECO:0000255|PROSITE-
ProRule:PRU00297, ECO:0000269|PubMed:2760033}.
-!- INDUCTION: During wound-healing and by factors which induce
suberization. {ECO:0000269|PubMed:2760033}.
-!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
{ECO:0000305}.
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EMBL; J04980; AAA33746.1; -; mRNA.
PIR; A32630; A32630.
ProteinModelPortal; P19136; -.
SMR; P19136; -.
CAZy; AA2; Auxiliary Activities 2.
mycoCLAP; MPO2D_PHACH; -.
PeroxiBase; 2383; PcMnP02_RP78.
eggNOG; ENOG410IZ9A; Eukaryota.
eggNOG; ENOG410YEPY; LUCA.
OMA; CITHAGR; -.
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 24 {ECO:0000269|PubMed:1592808,
ECO:0000269|PubMed:2760033}.
CHAIN 25 382 Manganese peroxidase H4.
/FTId=PRO_0000023780.
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 220 220 Calcium 2; via carbonyl oxygen.
{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 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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,
ECO:0000269|PubMed:2760033}.
DISULFID 38 313 {ECO:0000255|PROSITE-ProRule:PRU00297,
ECO:0000269|PubMed:2760033}.
DISULFID 57 141 {ECO:0000255|PROSITE-ProRule:PRU00297,
ECO:0000269|PubMed:2760033}.
DISULFID 277 344 {ECO:0000255|PROSITE-ProRule:PRU00297,
ECO:0000269|PubMed:2760033}.
DISULFID 366 373 {ECO:0000255|PROSITE-ProRule:PRU00297,
ECO:0000269|PubMed:2760033}.
SEQUENCE 382 AA; 40115 MW; 75E2A6B762867E3D CRC64;
MAFGSLLAFV ALAAITRAAP TAESAVCPDG TRVTNAACCA FIPLAQDLQE TLFQGDCGED
AHEVIRLTFH DAIAISQSLG PQAGGGADGS MLHFPTIEPN FSANSGIDDS VNNLLPFMQK
HDTISAADLV QFAGAVALSN CPGAPRLEFM AGRPNTTIPA VEGLIPEPQD SVTKILQRFE
DAGNFSPFEV VSLLASHTVA RADKVDETID AAPFDSTPFT FDTQVFLEVL LKGTGFPGSN
NNTGEVMSPL PLGSGSDTGE MRLQSDFALA RDERTACFWQ SFVNEQEFMA ASFKAAMAKL
AILGHSRSSL IDCSDVVPVP KPAVNKPATF PATKGPKDLD TLTCKALKFP TLTSDPGATE
TLIPHCSNGG MSCPGVQFDG PA


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