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Manganese peroxidase 1 (MnP-1) (MnP1) (EC 1.11.1.13) (Manganese peroxidase isozyme 1) (Peroxidase manganese-dependent 1) (Peroxidase manganese-dependent I)

 PEM1_PHACH              Reviewed;         378 AA.
Q02567; Q01788;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
07-JUN-2017, entry version 123.
RecName: Full=Manganese peroxidase 1;
Short=MnP-1;
Short=MnP1;
EC=1.11.1.13;
AltName: Full=Manganese peroxidase isozyme 1;
AltName: Full=Peroxidase manganese-dependent 1;
AltName: Full=Peroxidase manganese-dependent I;
Flags: Precursor;
Name=MNP1;
Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum
pruinosum).
Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
Agaricomycetes; Polyporales; Phanerochaetaceae; Phanerochaete.
NCBI_TaxID=5306;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 201542 / OGC101;
PubMed=2227420; DOI=10.1016/0378-1119(90)90144-G;
Godfrey B.J., Mayfield M.B., Brown J.A., Gold M.H.;
"Characterization of a gene encoding a manganese peroxidase from
Phanerochaete chrysosporium.";
Gene 93:119-124(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-41.
STRAIN=ATCC 201542 / OGC101;
PubMed=2925681;
Pribnow D., Mayfield M.B., Nipper V.J., Brown J.A., Gold M.H.;
"Characterization of a cDNA encoding a manganese peroxidase, from the
lignin-degrading basidiomycete Phanerochaete chrysosporium.";
J. Biol. Chem. 264:5036-5040(1989).
[3]
METAL-BINDING.
PubMed=8688436; DOI=10.1021/bi960679c;
Kishi K., Kusters-van Someren M., Mayfield M.B., Sun J., Loehr T.M.,
Gold M.H.;
"Characterization of manganese(II) binding site mutants of manganese
peroxidase.";
Biochemistry 35:8986-8994(1996).
[4]
X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS).
PubMed=7806497;
Sundaramoorthy M., Kishi K., Gold M.H., Poulos T.L.;
"The crystal structure of manganese peroxidase from Phanerochaete
chrysosporium at 2.06-A resolution.";
J. Biol. Chem. 269:32759-32767(1994).
[5]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS.
PubMed=9211904; DOI=10.1074/jbc.272.28.17574;
Sundaramoorthy M., Kishi K., Gold M.H., Poulos T.L.;
"Crystal structures of substrate binding site mutants of manganese
peroxidase.";
J. Biol. Chem. 272:17574-17580(1997).
-!- 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=Ca(2+); Xref=ChEBI:CHEBI:29108;
Note=Binds 2 calcium ions per subunit.;
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
subunit.;
-!- SUBCELLULAR LOCATION: Secreted.
-!- INDUCTION: During wound-healing and by factors which induce
suberization.
-!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
{ECO:0000305}.
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EMBL; M60672; AAA33744.1; -; Genomic_DNA.
EMBL; M77513; AAA33743.1; -; Genomic_DNA.
EMBL; J04624; AAA33742.1; -; mRNA.
PIR; JN0092; A33271.
PDB; 1MN1; X-ray; 2.00 A; A=22-378.
PDB; 1MN2; X-ray; 2.00 A; A=22-378.
PDB; 1MNP; X-ray; 2.00 A; A=22-378.
PDB; 1YYD; X-ray; 1.45 A; A=22-378.
PDB; 1YYG; X-ray; 1.60 A; A=22-378.
PDB; 1YZP; X-ray; 1.60 A; A=22-378.
PDB; 1YZR; X-ray; 1.60 A; A=22-378.
PDB; 3M5Q; X-ray; 0.93 A; A=22-378.
PDB; 3M8M; X-ray; 1.05 A; A=22-378.
PDBsum; 1MN1; -.
PDBsum; 1MN2; -.
PDBsum; 1MNP; -.
PDBsum; 1YYD; -.
PDBsum; 1YYG; -.
PDBsum; 1YZP; -.
PDBsum; 1YZR; -.
PDBsum; 3M5Q; -.
PDBsum; 3M8M; -.
ProteinModelPortal; Q02567; -.
SMR; Q02567; -.
CAZy; AA2; Auxiliary Activities 2.
mycoCLAP; MPO2A_PHACH; -.
PeroxiBase; 3866; PcMnP01_OGC101.
eggNOG; ENOG410IZ9A; Eukaryota.
eggNOG; ENOG410YEPY; LUCA.
OMA; FRTACEW; -.
BioCyc; MetaCyc:MONOMER-14335; -.
BRENDA; 1.11.1.13; 1380.
SABIO-RK; Q02567; -.
EvolutionaryTrace; Q02567; -.
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;
3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
Glycoprotein; Heme; Hydrogen peroxide; Iron; Lignin degradation;
Manganese; Metal-binding; Oxidoreductase; Peroxidase; Secreted;
Signal.
SIGNAL 1 21 {ECO:0000269|PubMed:2925681}.
CHAIN 22 378 Manganese peroxidase 1.
/FTId=PRO_0000023778.
ACT_SITE 67 67 Proton acceptor.
METAL 56 56 Manganese.
METAL 60 60 Manganese.
METAL 68 68 Calcium 1.
METAL 83 83 Calcium 1; via carbonyl oxygen.
METAL 85 85 Calcium 1.
METAL 87 87 Calcium 1.
METAL 194 194 Iron (heme axial ligand).
METAL 195 195 Calcium 2.
METAL 200 200 Manganese.
METAL 212 212 Calcium 2.
METAL 214 214 Calcium 2.
METAL 217 217 Calcium 2; via carbonyl oxygen.
METAL 219 219 Calcium 2.
SITE 63 63 Transition state stabilizer.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 152 152 N-linked (GlcNAc...) asparagine.
CARBOHYD 238 238 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 24 36
DISULFID 35 310
DISULFID 54 138
DISULFID 274 340
DISULFID 362 369
CONFLICT 75 75 S -> L (in Ref. 2; AAA33742).
{ECO:0000305}.
STRAND 25 27 {ECO:0000244|PDB:3M5Q}.
HELIX 33 37 {ECO:0000244|PDB:3M5Q}.
HELIX 38 48 {ECO:0000244|PDB:3M5Q}.
TURN 49 52 {ECO:0000244|PDB:3M5Q}.
STRAND 53 55 {ECO:0000244|PDB:1YYD}.
HELIX 56 70 {ECO:0000244|PDB:3M5Q}.
TURN 74 76 {ECO:0000244|PDB:3M5Q}.
HELIX 78 80 {ECO:0000244|PDB:3M5Q}.
STRAND 83 85 {ECO:0000244|PDB:3M5Q}.
HELIX 87 90 {ECO:0000244|PDB:3M5Q}.
TURN 92 94 {ECO:0000244|PDB:3M5Q}.
HELIX 95 97 {ECO:0000244|PDB:3M5Q}.
HELIX 99 101 {ECO:0000244|PDB:3M5Q}.
TURN 102 104 {ECO:0000244|PDB:3M5Q}.
HELIX 105 117 {ECO:0000244|PDB:3M5Q}.
HELIX 123 136 {ECO:0000244|PDB:3M5Q}.
HELIX 169 180 {ECO:0000244|PDB:3M5Q}.
HELIX 184 190 {ECO:0000244|PDB:3M5Q}.
HELIX 191 196 {ECO:0000244|PDB:3M5Q}.
STRAND 198 203 {ECO:0000244|PDB:3M5Q}.
STRAND 209 213 {ECO:0000244|PDB:3M5Q}.
HELIX 221 226 {ECO:0000244|PDB:3M5Q}.
HELIX 261 268 {ECO:0000244|PDB:3M5Q}.
TURN 270 272 {ECO:0000244|PDB:3M5Q}.
HELIX 273 278 {ECO:0000244|PDB:3M5Q}.
TURN 279 281 {ECO:0000244|PDB:3M5Q}.
HELIX 283 297 {ECO:0000244|PDB:3M5Q}.
TURN 298 301 {ECO:0000244|PDB:3M5Q}.
HELIX 304 306 {ECO:0000244|PDB:3M5Q}.
STRAND 307 309 {ECO:0000244|PDB:3M5Q}.
HELIX 311 313 {ECO:0000244|PDB:3M5Q}.
HELIX 333 335 {ECO:0000244|PDB:3M5Q}.
STRAND 365 367 {ECO:0000244|PDB:3M5Q}.
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


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