PEM3_PHACH
ID PEM3_PHACH Reviewed; 380 AA.
AC P78733; Q01666;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Manganese peroxidase H3;
DE EC=1.11.1.13;
DE AltName: Full=Peroxidase manganese-dependent H3;
DE Flags: Precursor;
OS Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerodontia.
OX NCBI_TaxID=2822231;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM
RC F-1767;
RX PubMed=7926830; DOI=10.1016/0378-1119(94)90251-8;
RA Orth A.B., Rzhetskaya M., Cullen D., Tien M.;
RT "Characterization of a cDNA encoding a manganese peroxidase from
RT Phanerochaete chrysosporium: genomic organization of lignin and manganese
RT peroxidase-encoding genes.";
RL Gene 148:161-165(1994).
RN [2]
RP PROTEIN SEQUENCE OF 26-45.
RX PubMed=1592808; DOI=10.1128/jb.174.11.3532-3540.1992;
RA Pease E.A., Tien M.;
RT "Heterogeneity and regulation of manganese peroxidases from Phanerochaete
RT chrysosporium.";
RL J. Bacteriol. 174:3532-3540(1992).
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.
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 -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
CC {ECO:0000305}.
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DR EMBL; U10306; AAA62243.1; -; mRNA.
DR PIR; JC2579; JC2579.
DR AlphaFoldDB; P78733; -.
DR SMR; P78733; -.
DR CAZy; AA2; Auxiliary Activities 2.
DR CLAE; MPO2C_PHACH; -.
DR PeroxiBase; 2382; PcMnP03_ATCC24725.
DR VEuPathDB; FungiDB:AGR57_1292; -.
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..25
FT /evidence="ECO:0000269|PubMed:1592808"
FT CHAIN 26..380
FT /note="Manganese peroxidase H3"
FT /id="PRO_0000023779"
FT ACT_SITE 71
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 60
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 72
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 220
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 67
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 39..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 58..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 277..342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 364..371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ 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
