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Entry version 101 (29 Sep 2021)
Sequence version 1 (01 May 1999)
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Protein

Versatile peroxidase VPL2

Gene

vpl2

Organism
Pleurotus eryngii (Boletus of the steppes)
Status
Reviewed-Annotation score:

Annotation score:5 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

A versatile ligninolytic peroxidase that combines the substrate specificity characteristics of the two other ligninolytic peroxidases, manganese peroxidase and lignin peroxidase.

1 Publication

<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:

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=19 µM for manganese1 Publication
  2. KM=3000 µM for veratryl alcohol1 Publication
  3. KM=4 µM for reactive black 51 Publication
  4. KM=3 µM for 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonate) (ABTS)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi66Manganese1 Publication1
Metal bindingi70ManganeseBy 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>Sitei73Transition state stabilizerPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei77Proton acceptorPROSITE-ProRule annotation1
Metal bindingi78Calcium 11
Metal bindingi90Calcium 1; via carbonyl oxygen1
Metal bindingi92Calcium 11
Metal bindingi94Calcium 11
Active sitei194Tryptophan radical intermediate1 Publication1
Metal bindingi199Iron (heme axial ligand)1
Metal bindingi200Calcium 21
Metal bindingi205Manganese1 Publication1
Metal bindingi217Calcium 21
Metal bindingi219Calcium 21
Metal bindingi222Calcium 2; via carbonyl oxygen1
Metal bindingi224Calcium 21

<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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-14479

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.11.1.16, 4910
1.11.1.7, 4910

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
O94753

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
AA2, Auxiliary Activities 2

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

More...
CLAEi
VPO2B_PLEER

PeroxiBase, a peroxidase database

More...
PeroxiBasei
2299, PerVP05-2_CBS613

<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:
Versatile peroxidase VPL2 (EC:1.11.1.163 Publications)
Alternative name(s):
Versatile liquid phase peroxidase 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:vpl2
<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>OrganismiPleurotus eryngii (Boletus of the steppes)
<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 identifieri5323 [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 lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesPleurotaceaePleurotus

<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

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi106P → H: Minor effects on activity. 1 Publication1
Mutagenesisi194W → H or S: Complete loss of activity toward veratryl alcohol and reactive black 5. No effect on manganese oxidation. 1 Publication1
Mutagenesisi205D → A: Complete loss of oxidation activity toward manganese. 1 Publication1
Mutagenesisi262H → F: Minor effects on activity. 1 Publication1

<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 – 22Sequence analysisAdd BLAST22
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000030817123 – 301 Publication8
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_500005324731 – 361Versatile peroxidase VPL2Add BLAST331

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 bondi33 ↔ 45PROSITE-ProRule annotation1 Publication
Disulfide bondi44 ↔ 308PROSITE-ProRule annotation1 Publication
Disulfide bondi64 ↔ 144PROSITE-ProRule annotation1 Publication
<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>Glycosylationi126N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi272 ↔ 337PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Organic radical, Zymogen

<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

Secondary structure

1361
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
O94753

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O94753

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni203 – 207Heme binding5

<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

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
IPR044831, Ccp1-like
IPR002016, Haem_peroxidase
IPR010255, Haem_peroxidase_sf
IPR001621, Ligninase
IPR024589, Ligninase_C
IPR019794, Peroxidases_AS
IPR019793, Peroxidases_heam-ligand_BS

The PANTHER Classification System

More...
PANTHERi
PTHR31356, PTHR31356, 1 hit

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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

O94753-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSFKTLSALA LALGAAVQFA SAAVPLVQKR ATCDDGRTTA NAACCILFPI
60 70 80 90 100
LDDIQENLFD GAQCGEEVHE SLRLTFHDAI GFSPTLGGGG ADGSIIAFDT
110 120 130 140 150
IETNFPANAG IDEIVSAQKP FVAKHNISAG DFIQFAGAVG VSNCPGGVRI
160 170 180 190 200
PFFLGRPDAV AASPDHLVPE PFDSVDSILA RMGDAGFSPV EVVWLLASHS
210 220 230 240 250
IAAADKVDPS IPGTPFDSTP GVFDSQFFIE TQLKGRLFPG TADNKGEAQS
260 270 280 290 300
PLQGEIRLQS DHLLARDPQT ACEWQSMVNN QPKIQNRFAA TMSKMALLGQ
310 320 330 340 350
DKTKLIDCSD VIPTPPALVG AAHLPAGFSL SDVEQACAAT PFPALTADPG
360
PVTSVPPVPG S
Length:361
Mass (Da):37,624
Last modified:May 1, 1999 - v1
<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:i18C4C6900F22A1E5
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF007222 mRNA Translation: AAD01402.1
AF007224 Genomic DNA Translation: AAD01404.1

<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
AF007222 mRNA Translation: AAD01402.1
AF007224 Genomic DNA Translation: AAD01404.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BOQX-ray1.33A31-361[»]
2VKAX-ray2.00A31-347[»]
2W23X-ray1.94A31-346[»]
3FJWX-ray2.80A/B31-361[»]
3FKGX-ray1.81A31-361[»]
3FM1X-ray1.78A31-361[»]
3FM4X-ray2.11A31-361[»]
3FM6X-ray1.13A31-361[»]
3FMUX-ray1.04A31-361[»]
4FCNX-ray1.70A31-349[»]
4FCSX-ray1.50A31-345[»]
4FDQX-ray1.60A31-345[»]
4FEFX-ray2.00A31-345[»]
4G05X-ray2.35A31-347[»]
5ABNX-ray2.19A31-361[»]
5ABOX-ray1.09A33-361[»]
5ABQX-ray2.29A33-361[»]
5FNBX-ray1.79A/B31-359[»]
5FNEX-ray1.50A31-359[»]
SMRiO94753
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

CAZyiAA2, Auxiliary Activities 2
CLAEiVPO2B_PLEER
PeroxiBasei2299, PerVP05-2_CBS613

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14479
BRENDAi1.11.1.16, 4910
1.11.1.7, 4910
SABIO-RKiO94753

Miscellaneous databases

EvolutionaryTraceiO94753

Family and domain databases

CDDicd00692, ligninase, 1 hit
InterProiView protein in InterPro
IPR044831, Ccp1-like
IPR002016, Haem_peroxidase
IPR010255, Haem_peroxidase_sf
IPR001621, Ligninase
IPR024589, Ligninase_C
IPR019794, Peroxidases_AS
IPR019793, Peroxidases_heam-ligand_BS
PANTHERiPTHR31356, PTHR31356, 1 hit
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

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiVPL2_PLEER
<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: O94753
<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: October 23, 2007
Last sequence update: May 1, 1999
Last modified: September 29, 2021
This is version 101 of the entry and version 1 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

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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