PEM4_PHACH
ID PEM4_PHACH Reviewed; 382 AA.
AC P19136;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Manganese peroxidase H4;
DE EC=1.11.1.13;
DE AltName: Full=MP-I;
DE AltName: Full=Peroxidase manganese-dependent H4;
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], PROTEIN SEQUENCE OF 25-45, FUNCTION,
RP SUBCELLULAR LOCATION, INDUCTION, AND DISULFIDE BONDS.
RC STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM
RC F-1767;
RX PubMed=2760033; DOI=10.1016/s0021-9258(18)80029-1;
RA Pease E.A., Andrawis A., Tien M.;
RT "Manganese-dependent peroxidase from Phanerochaete chrysosporium. Primary
RT structure deduced from cDNA sequence.";
RL J. Biol. Chem. 264:13531-13535(1989).
RN [2]
RP PROTEIN SEQUENCE OF 25-44.
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. {ECO:0000269|PubMed:2760033}.
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 {ECO:0000255|PROSITE-ProRule:PRU00297,
CC ECO:0000269|PubMed:2760033}.
CC -!- INDUCTION: During wound-healing and by factors which induce
CC suberization. {ECO:0000269|PubMed:2760033}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
CC {ECO:0000305}.
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DR EMBL; J04980; AAA33746.1; -; mRNA.
DR PIR; A32630; A32630.
DR AlphaFoldDB; P19136; -.
DR SMR; P19136; -.
DR CAZy; AA2; Auxiliary Activities 2.
DR CLAE; MPO2D_PHACH; -.
DR PeroxiBase; 2383; PcMnP02_RP78.
DR VEuPathDB; FungiDB:AGR57_5338; -.
DR OMA; IACHARA; -.
DR SABIO-RK; P19136; -.
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..24
FT /evidence="ECO:0000269|PubMed:1592808,
FT ECO:0000269|PubMed:2760033"
FT CHAIN 25..382
FT /note="Manganese peroxidase H4"
FT /id="PRO_0000023780"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 59
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 71
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 66
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 CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..39
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:2760033"
FT DISULFID 38..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:2760033"
FT DISULFID 57..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:2760033"
FT DISULFID 277..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:2760033"
FT DISULFID 366..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:2760033"
SQ 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
