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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi60ManganeseBy similarity1
Metal bindingi64ManganeseBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei67Transition state stabilizerPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei71Proton acceptorPROSITE-ProRule annotation1
Metal bindingi72Calcium 1PROSITE-ProRule annotation1
Metal bindingi86Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi88Calcium 1PROSITE-ProRule annotation1
Metal bindingi90Calcium 1PROSITE-ProRule annotation1
Metal bindingi197Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi198Calcium 2PROSITE-ProRule annotation1
Metal bindingi203ManganeseBy similarity1
Metal bindingi215Calcium 2PROSITE-ProRule annotation1
Metal bindingi217Calcium 2PROSITE-ProRule annotation1
Metal bindingi220Calcium 2; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi222Calcium 2PROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase, Peroxidase
Biological processHydrogen peroxide, Lignin degradation
LigandCalcium, Heme, Iron, Manganese, Metal-binding

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
AA2 Auxiliary Activities 2

mycoCLAP, a database of fungal genes encoding lignocellulose-active proteins

More...
mycoCLAPi
MPO2C_PHACH

PeroxiBase, a peroxidase database

More...
PeroxiBasei
2382 PcMnP03_ATCC24725

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Manganese peroxidase H3 (EC:1.11.1.13)
Alternative name(s):
Peroxidase manganese-dependent H3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri5306 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesPhanerochaetaceaePhanerochaete

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 251 PublicationAdd BLAST25
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002377926 – 380Manganese peroxidase H3Add BLAST355

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi28 ↔ 40PROSITE-ProRule annotation
Disulfide bondi39 ↔ 312PROSITE-ProRule annotation
Disulfide bondi58 ↔ 141PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi100N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi155N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi277 ↔ 342PROSITE-ProRule annotation
Disulfide bondi364 ↔ 371PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P78733

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P78733

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peroxidase family. Ligninase subfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IZ9A Eukaryota
ENOG410YEPY LUCA

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00692 ligninase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR010255 Haem_peroxidase
IPR002016 Haem_peroxidase_pln/fun/bac
IPR001621 Ligninase
IPR024589 Ligninase_C
IPR019794 Peroxidases_AS
IPR019793 Peroxidases_heam-ligand_BS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00141 peroxidase, 1 hit
PF11895 Peroxidase_ext, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00462 LIGNINASE
PR00458 PEROXIDASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48113 SSF48113, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00435 PEROXIDASE_1, 1 hit
PS00436 PEROXIDASE_2, 1 hit
PS50873 PEROXIDASE_4, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4C8931EA3940BBA6
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U10306 mRNA Translation: AAA62243.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JC2579

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliP78733
SMRiP78733
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA2 Auxiliary Activities 2
mycoCLAPiMPO2C_PHACH
PeroxiBasei2382 PcMnP03_ATCC24725

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IZ9A Eukaryota
ENOG410YEPY LUCA

Family and domain databases

CDDicd00692 ligninase, 1 hit
InterProiView protein in InterPro
IPR010255 Haem_peroxidase
IPR002016 Haem_peroxidase_pln/fun/bac
IPR001621 Ligninase
IPR024589 Ligninase_C
IPR019794 Peroxidases_AS
IPR019793 Peroxidases_heam-ligand_BS
PfamiView protein in Pfam
PF00141 peroxidase, 1 hit
PF11895 Peroxidase_ext, 1 hit
PRINTSiPR00462 LIGNINASE
PR00458 PEROXIDASE
SUPFAMiSSF48113 SSF48113, 1 hit
PROSITEiView protein in PROSITE
PS00435 PEROXIDASE_1, 1 hit
PS00436 PEROXIDASE_2, 1 hit
PS50873 PEROXIDASE_4, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPEM3_PHACH
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P78733
Secondary accession number(s): Q01666
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: July 5, 2004
Last modified: December 5, 2018
This is version 88 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again