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P19136 (PEM4_PHACH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Manganese peroxidase H4
EC=1.11.1.13
Alternative name(s):
MP-I
Peroxidase manganese-dependent H4
OrganismPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Taxonomic identifier5306 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Corticiales › Corticiaceae › Phanerochaete

Protein attributes

Sequence length382 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. Ref.1

Catalytic activity

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

Cofactor

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

Binds 2 calcium ions per subunit By similarity.

Subcellular location

Secreted Ref.1.

Induction

During wound-healing and by factors which induce suberization. Ref.1

Sequence similarities

Belongs to the peroxidase family. Ligninase subfamily.

Ontologies

Keywords
   Biological processHydrogen peroxide
Lignin degradation
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Heme
Iron
Manganese
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

lignin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionheme binding

Inferred from electronic annotation. Source: InterPro

manganese peroxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.1 Ref.2
Chain25 – 382358Manganese peroxidase H4
PRO_0000023780

Sites

Active site701Proton acceptor By similarity
Metal binding591Manganese By similarity
Metal binding631Manganese By similarity
Metal binding711Calcium 1 By similarity
Metal binding861Calcium 1; via carbonyl oxygen By similarity
Metal binding881Calcium 1 By similarity
Metal binding901Calcium 1 By similarity
Metal binding1971Iron (heme axial ligand) By similarity
Metal binding1981Calcium 2 By similarity
Metal binding2031Manganese By similarity
Metal binding2151Calcium 2 By similarity
Metal binding2171Calcium 2 By similarity
Metal binding2201Calcium 2; via carbonyl oxygen By similarity
Metal binding2221Calcium 2 By similarity
Site661Transition state stabilizer By similarity

Amino acid modifications

Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation1551N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Disulfide bond27 ↔ 39 Ref.1
Disulfide bond38 ↔ 313 Ref.1
Disulfide bond57 ↔ 141 Ref.1
Disulfide bond277 ↔ 344 Ref.1
Disulfide bond366 ↔ 373 Ref.1

Sequences

Sequence LengthMass (Da)Tools
P19136 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 75E2A6B762867E3D

FASTA38240,115
        10         20         30         40         50         60 
MAFGSLLAFV ALAAITRAAP TAESAVCPDG TRVTNAACCA FIPLAQDLQE TLFQGDCGED 

        70         80         90        100        110        120 
AHEVIRLTFH DAIAISQSLG PQAGGGADGS MLHFPTIEPN FSANSGIDDS VNNLLPFMQK 

       130        140        150        160        170        180 
HDTISAADLV QFAGAVALSN CPGAPRLEFM AGRPNTTIPA VEGLIPEPQD SVTKILQRFE 

       190        200        210        220        230        240 
DAGNFSPFEV VSLLASHTVA RADKVDETID AAPFDSTPFT FDTQVFLEVL LKGTGFPGSN 

       250        260        270        280        290        300 
NNTGEVMSPL PLGSGSDTGE MRLQSDFALA RDERTACFWQ SFVNEQEFMA ASFKAAMAKL 

       310        320        330        340        350        360 
AILGHSRSSL IDCSDVVPVP KPAVNKPATF PATKGPKDLD TLTCKALKFP TLTSDPGATE 

       370        380 
TLIPHCSNGG MSCPGVQFDG PA

« Hide

References

[1]"Manganese-dependent peroxidase from Phanerochaete chrysosporium. Primary structure deduced from cDNA sequence."
Pease E.A., Andrawis A., Tien M.
J. Biol. Chem. 264:13531-13535(1989) [PubMed: 2760033] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-45, FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DISULFIDE BONDS.
Strain: ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM F-1767.
[2]"Heterogeneity and regulation of manganese peroxidases from Phanerochaete chrysosporium."
Pease E.A., Tien M.
J. Bacteriol. 174:3532-3540(1992) [PubMed: 1592808] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-44.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J04980 mRNA. Translation: AAA33746.1.
PIRA32630.

3D structure databases

ProteinModelPortalP19136.
SMRP19136. Positions 25-382.
ModBaseSearch...

Protein family/group databases

PeroxiBase2383. PcMnP02_RP78.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

PhylomeDBP19136.

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...

Entry information

Entry namePEM4_PHACH
AccessionPrimary (citable) accession number: P19136
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: December 14, 2011
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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