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Q02567 (PEM1_PHACH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Manganese peroxidase 1
Short name=MnP-1
Short name=MnP1
EC=1.11.1.13
Alternative name(s):
Manganese peroxidase isozyme 1
Peroxidase manganese-dependent 1
Peroxidase manganese-dependent I
Gene names
Name:MNP1
OrganismPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Taxonomic identifier5306 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Agaricomycetes › Corticiales › Corticiaceae › Phanerochaete

Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of Mn2+ to Mn3+. The latter, acting as a diffusible redox mediator, is capable of oxidizing a variety of lignin compounds.

Catalytic activity

2 Mn2+ + 2 H+ + H2O2 = 2 Mn3+ + 2 H2O.

Cofactor

Binds 2 calcium ions per subunit.

Binds 1 heme B (iron-protoporphyrin IX) group per subunit.

Subcellular location

Secreted.

Induction

During wound-healing and by factors which induce suberization.

Sequence similarities

Belongs to the peroxidase family. Ligninase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Ref.2
Chain22 – 378357Manganese peroxidase 1
PRO_0000023778

Sites

Active site671Proton acceptor
Metal binding561Manganese
Metal binding601Manganese
Metal binding681Calcium 1
Metal binding831Calcium 1; via carbonyl oxygen
Metal binding851Calcium 1
Metal binding871Calcium 1
Metal binding1941Iron (heme axial ligand)
Metal binding1951Calcium 2
Metal binding2001Manganese
Metal binding2121Calcium 2
Metal binding2141Calcium 2
Metal binding2171Calcium 2; via carbonyl oxygen
Metal binding2191Calcium 2
Site631Transition state stabilizer

Amino acid modifications

Glycosylation971N-linked (GlcNAc...) Potential
Glycosylation1521N-linked (GlcNAc...)
Glycosylation2381N-linked (GlcNAc...) Potential
Disulfide bond24 ↔ 36
Disulfide bond35 ↔ 310
Disulfide bond54 ↔ 138
Disulfide bond274 ↔ 340
Disulfide bond362 ↔ 369

Experimental info

Sequence conflict751S → L in AAA33742. Ref.2

Secondary structure

1 ....................................................... 378
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02567 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 17A9A8F642441F27

FASTA37839,557
        10         20         30         40         50         60 
MAFKSLIAFV ALAAAVRAAP TAVCPDGTRV SHAACCAFIP LAQDLQETIF QNECGEDAHE 

        70         80         90        100        110        120 
VIRLTFHDAI AISRSQGPKA GGGADGSMLL FPTVEPNFSA NNGIDDSVNN LIPFMQKHNT 

       130        140        150        160        170        180 
ISAADLVQFA GAVALSNCPG APRLEFLAGR PNKTIAAVDG LIPEPQDSVT KILQRFEDAG 

       190        200        210        220        230        240 
GFTPFEVVSL LASHSVARAD KVDQTIDAAP FDSTPFTFDT QVFLEVLLKG VGFPGSANNT 

       250        260        270        280        290        300 
GEVASPLPLG SGSDTGEMRL QSDFALAHDP RTACIWQGFV NEQAFMAASF RAAMSKLAVL 

       310        320        330        340        350        360 
GHNRNSLIDC SDVVPVPKPA TGQPAMFPAS TGPQDLELSC PSERFPTLTT QPGASQSLIA 

       370 
HCPDGSMSCP GVQFNGPA

« Hide

References

[1]"Characterization of a gene encoding a manganese peroxidase from Phanerochaete chrysosporium."
Godfrey B.J., Mayfield M.B., Brown J.A., Gold M.H.
Gene 93:119-124(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 201542 / OGC101.
[2]"Characterization of a cDNA encoding a manganese peroxidase, from the lignin-degrading basidiomycete Phanerochaete chrysosporium."
Pribnow D., Mayfield M.B., Nipper V.J., Brown J.A., Gold M.H.
J. Biol. Chem. 264:5036-5040(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-41.
Strain: ATCC 201542 / OGC101.
[3]"Characterization of manganese(II) binding site mutants of manganese peroxidase."
Kishi K., Kusters-van Someren M., Mayfield M.B., Sun J., Loehr T.M., Gold M.H.
Biochemistry 35:8986-8994(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: METAL-BINDING.
[4]"The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-A resolution."
Sundaramoorthy M., Kishi K., Gold M.H., Poulos T.L.
J. Biol. Chem. 269:32759-32767(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS).
[5]"Crystal structures of substrate binding site mutants of manganese peroxidase."
Sundaramoorthy M., Kishi K., Gold M.H., Poulos T.L.
J. Biol. Chem. 272:17574-17580(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M60672 Genomic DNA. Translation: AAA33744.1.
M77513 Genomic DNA. Translation: AAA33743.1.
J04624 mRNA. Translation: AAA33742.1.
PIRA33271. JN0092.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MN1X-ray2.00A22-378[»]
1MN2X-ray2.00A22-378[»]
1MNPX-ray2.00A22-378[»]
1YYDX-ray1.45A22-378[»]
1YYGX-ray1.60A22-378[»]
1YZPX-ray1.60A22-378[»]
1YZRX-ray1.60A22-378[»]
3M5QX-ray0.93A22-378[»]
3M8MX-ray1.05A22-378[»]
ProteinModelPortalQ02567.
SMRQ02567. Positions 22-378.
ModBaseSearch...

Protein family/group databases

mycoCLAPMnPA_PHACH.
PeroxiBase3866. PcMnP01_OGC101.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGeuNOG20355.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14335.
SABIO-RKQ02567.

Family and domain databases

InterProIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamPF11895. DUF3415. 1 hit.
PF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSPR00462. LIGNINASE.
PR00458. PEROXIDASE.
SUPFAMSSF48113. Peroxidase_super. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ02567.

Entry information

Entry namePEM1_PHACH
AccessionPrimary (citable) accession number: Q02567
Secondary accession number(s): Q01788
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1996
Last modified: April 3, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents