PEM1_PHACH
ID PEM1_PHACH Reviewed; 378 AA.
AC Q02567; Q01788;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Manganese peroxidase 1;
DE Short=MnP-1;
DE Short=MnP1;
DE EC=1.11.1.13;
DE AltName: Full=Manganese peroxidase isozyme 1;
DE AltName: Full=Peroxidase manganese-dependent 1;
DE AltName: Full=Peroxidase manganese-dependent I;
DE Flags: Precursor;
GN Name=MNP1;
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 [GENOMIC DNA].
RC STRAIN=ATCC 201542 / OGC101;
RX PubMed=2227420; DOI=10.1016/0378-1119(90)90144-g;
RA Godfrey B.J., Mayfield M.B., Brown J.A., Gold M.H.;
RT "Characterization of a gene encoding a manganese peroxidase from
RT Phanerochaete chrysosporium.";
RL Gene 93:119-124(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-41.
RC STRAIN=ATCC 201542 / OGC101;
RX PubMed=2925681; DOI=10.1016/s0021-9258(18)83695-x;
RA Pribnow D., Mayfield M.B., Nipper V.J., Brown J.A., Gold M.H.;
RT "Characterization of a cDNA encoding a manganese peroxidase, from the
RT lignin-degrading basidiomycete Phanerochaete chrysosporium.";
RL J. Biol. Chem. 264:5036-5040(1989).
RN [3]
RP METAL-BINDING.
RX PubMed=8688436; DOI=10.1021/bi960679c;
RA Kishi K., Kusters-van Someren M., Mayfield M.B., Sun J., Loehr T.M.,
RA Gold M.H.;
RT "Characterization of manganese(II) binding site mutants of manganese
RT peroxidase.";
RL Biochemistry 35:8986-8994(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS).
RX PubMed=7806497; DOI=10.1016/s0021-9258(20)30056-9;
RA Sundaramoorthy M., Kishi K., Gold M.H., Poulos T.L.;
RT "The crystal structure of manganese peroxidase from Phanerochaete
RT chrysosporium at 2.06-A resolution.";
RL J. Biol. Chem. 269:32759-32767(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS.
RX PubMed=9211904; DOI=10.1074/jbc.272.28.17574;
RA Sundaramoorthy M., Kishi K., Gold M.H., Poulos T.L.;
RT "Crystal structures of substrate binding site mutants of manganese
RT peroxidase.";
RL J. Biol. Chem. 272:17574-17580(1997).
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=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 2 calcium ions per subunit.;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- INDUCTION: During wound-healing and by factors which induce
CC suberization.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
CC {ECO:0000305}.
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DR EMBL; M60672; AAA33744.1; -; Genomic_DNA.
DR EMBL; M77513; AAA33743.1; -; Genomic_DNA.
DR EMBL; J04624; AAA33742.1; -; mRNA.
DR PIR; JN0092; A33271.
DR PDB; 1MN1; X-ray; 2.00 A; A=22-378.
DR PDB; 1MN2; X-ray; 2.00 A; A=22-378.
DR PDB; 1MNP; X-ray; 2.00 A; A=22-378.
DR PDB; 1YYD; X-ray; 1.45 A; A=22-378.
DR PDB; 1YYG; X-ray; 1.60 A; A=22-378.
DR PDB; 1YZP; X-ray; 1.60 A; A=22-378.
DR PDB; 1YZR; X-ray; 1.60 A; A=22-378.
DR PDB; 3M5Q; X-ray; 0.93 A; A=22-378.
DR PDB; 3M8M; X-ray; 1.05 A; A=22-378.
DR PDBsum; 1MN1; -.
DR PDBsum; 1MN2; -.
DR PDBsum; 1MNP; -.
DR PDBsum; 1YYD; -.
DR PDBsum; 1YYG; -.
DR PDBsum; 1YZP; -.
DR PDBsum; 1YZR; -.
DR PDBsum; 3M5Q; -.
DR PDBsum; 3M8M; -.
DR AlphaFoldDB; Q02567; -.
DR SMR; Q02567; -.
DR CAZy; AA2; Auxiliary Activities 2.
DR CLAE; MPO2A_PHACH; -.
DR PeroxiBase; 2379; PcMnP01-1A_RP78.
DR PeroxiBase; 3866; PcMnP01_OGC101.
DR VEuPathDB; FungiDB:AGR57_13026; -.
DR OMA; PEFHAND; -.
DR BioCyc; MetaCyc:MON-14335; -.
DR BRENDA; 1.11.1.13; 1380.
DR SABIO-RK; Q02567; -.
DR EvolutionaryTrace; Q02567; -.
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 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Heme; Hydrogen peroxide; Iron; Lignin degradation; Manganese;
KW Metal-binding; Oxidoreductase; Peroxidase; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:2925681"
FT CHAIN 22..378
FT /note="Manganese peroxidase 1"
FT /id="PRO_0000023778"
FT ACT_SITE 67
FT /note="Proton acceptor"
FT BINDING 56
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 60
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 194
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 BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT SITE 63
FT /note="Transition state stabilizer"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..36
FT DISULFID 35..310
FT DISULFID 54..138
FT DISULFID 274..340
FT DISULFID 362..369
FT CONFLICT 75
FT /note="S -> L (in Ref. 2; AAA33742)"
FT /evidence="ECO:0000305"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:3M5Q"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:3M5Q"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:3M5Q"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:3M5Q"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1YYD"
FT HELIX 56..70
FT /evidence="ECO:0007829|PDB:3M5Q"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:3M5Q"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:3M5Q"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:3M5Q"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:3M5Q"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:3M5Q"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3M5Q"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:3M5Q"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:3M5Q"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:3M5Q"
FT HELIX 123..136
FT /evidence="ECO:0007829|PDB:3M5Q"
FT HELIX 169..180
FT /evidence="ECO:0007829|PDB:3M5Q"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:3M5Q"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:3M5Q"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:3M5Q"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:3M5Q"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:3M5Q"
FT HELIX 261..268
FT /evidence="ECO:0007829|PDB:3M5Q"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:3M5Q"
FT HELIX 273..278
FT /evidence="ECO:0007829|PDB:3M5Q"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:3M5Q"
FT HELIX 283..297
FT /evidence="ECO:0007829|PDB:3M5Q"
FT TURN 298..301
FT /evidence="ECO:0007829|PDB:3M5Q"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:3M5Q"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:3M5Q"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:3M5Q"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:3M5Q"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:3M5Q"
SQ SEQUENCE 378 AA; 39557 MW; 17A9A8F642441F27 CRC64;
MAFKSLIAFV ALAAAVRAAP TAVCPDGTRV SHAACCAFIP LAQDLQETIF QNECGEDAHE
VIRLTFHDAI AISRSQGPKA GGGADGSMLL FPTVEPNFSA NNGIDDSVNN LIPFMQKHNT
ISAADLVQFA GAVALSNCPG APRLEFLAGR PNKTIAAVDG LIPEPQDSVT KILQRFEDAG
GFTPFEVVSL LASHSVARAD KVDQTIDAAP FDSTPFTFDT QVFLEVLLKG VGFPGSANNT
GEVASPLPLG SGSDTGEMRL QSDFALAHDP RTACIWQGFV NEQAFMAASF RAAMSKLAVL
GHNRNSLIDC SDVVPVPKPA TGQPAMFPAS TGPQDLELSC PSERFPTLTT QPGASQSLIA
HCPDGSMSCP GVQFNGPA
