Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Manganese peroxidase H3

Gene
N/A
Organism
Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Protein has several cofactor binding sites:
  • heme bPROSITE-ProRule annotationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.PROSITE-ProRule annotation
  • Ca2+PROSITE-ProRule annotationNote: Binds 2 calcium ions per subunit.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi60 – 601ManganeseBy similarity
Metal bindingi64 – 641ManganeseBy similarity
Sitei67 – 671Transition state stabilizerPROSITE-ProRule annotation
Active sitei71 – 711Proton acceptorPROSITE-ProRule annotation
Metal bindingi72 – 721Calcium 1PROSITE-ProRule annotation
Metal bindingi86 – 861Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi88 – 881Calcium 1PROSITE-ProRule annotation
Metal bindingi90 – 901Calcium 1PROSITE-ProRule annotation
Metal bindingi197 – 1971Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi198 – 1981Calcium 2PROSITE-ProRule annotation
Metal bindingi203 – 2031ManganeseBy similarity
Metal bindingi215 – 2151Calcium 2PROSITE-ProRule annotation
Metal bindingi217 – 2171Calcium 2PROSITE-ProRule annotation
Metal bindingi220 – 2201Calcium 2; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi222 – 2221Calcium 2PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide, Lignin degradation

Keywords - Ligandi

Calcium, Heme, Iron, Manganese, Metal-binding

Protein family/group databases

mycoCLAPiMPO2C_PHACH.
PeroxiBasei2382. PcMnP03_.

Names & Taxonomyi

Protein namesi
Recommended name:
Manganese peroxidase H3 (EC:1.11.1.13)
Alternative name(s):
Peroxidase manganese-dependent H3
OrganismiPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Taxonomic identifieri5306 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesPhanerochaetaceaePhanerochaete

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 PublicationAdd
BLAST
Chaini26 – 380355Manganese peroxidase H3PRO_0000023779Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 40PROSITE-ProRule annotation
Disulfide bondi39 ↔ 312PROSITE-ProRule annotation
Disulfide bondi58 ↔ 141PROSITE-ProRule annotation
Glycosylationi100 – 1001N-linked (GlcNAc...)Sequence analysis
Glycosylationi155 – 1551N-linked (GlcNAc...)Sequence analysis
Disulfide bondi277 ↔ 342PROSITE-ProRule annotation
Disulfide bondi364 ↔ 371PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliP78733.
SMRiP78733. Positions 26-380.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Ligninase subfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IZ9A. Eukaryota.
ENOG410YEPY. LUCA.

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF11895. DUF3415. 1 hit.
PF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00462. LIGNINASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P78733-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFASSLLAL VALAAVTSAA PATTQATCPD GTKVNNAACC AFIPLAQDLQ
60 70 80 90 100
ETIFQNDCGE DAHEVIRLTF HDAIAISQSK GPSAGGADGS MLLFPTIEPN
110 120 130 140 150
FSANNGIDDS VNNLIPFMQK HNTISAGDIV QFTGAVALTN CPGAPQLEFL
160 170 180 190 200
ARRPNKTIPA IDGLIPEPQD SVTSILERFK DAGNFSPFEV VSLLASHSVA
210 220 230 240 250
RADKVDETID AAPFDTTPFV FDTQIFLEVL LKGVGFPGTR TTRGEVASPL
260 270 280 290 300
PLTSGSDTGE LRLQSDFALA RDERTACIWQ GFVNEQALMA SFKAAMRKLA
310 320 330 340 350
VLGQHRNTLI DCSDVVPAPK PAVNKPASFP ATTGPQDLEL SCNTKPFPSL
360 370 380
SVDAGAQQTL IPHCSDGDMT CQSVQFNGPA
Length:380
Mass (Da):40,078
Last modified:July 5, 2004 - v2
Checksum:i4C8931EA3940BBA6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10306 mRNA. Translation: AAA62243.1.
PIRiJC2579.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10306 mRNA. Translation: AAA62243.1.
PIRiJC2579.

3D structure databases

ProteinModelPortaliP78733.
SMRiP78733. Positions 26-380.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

mycoCLAPiMPO2C_PHACH.
PeroxiBasei2382. PcMnP03_.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IZ9A. Eukaryota.
ENOG410YEPY. LUCA.

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF11895. DUF3415. 1 hit.
PF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00462. LIGNINASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of a cDNA encoding a manganese peroxidase from Phanerochaete chrysosporium: genomic organization of lignin and manganese peroxidase-encoding genes."
    Orth A.B., Rzhetskaya M., Cullen D., Tien M.
    Gene 148:161-165(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-45.

Entry informationi

Entry nameiPEM3_PHACH
AccessioniPrimary (citable) accession number: P78733
Secondary accession number(s): Q01666
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: July 5, 2004
Last modified: November 11, 2015
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.