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Protein

Versatile peroxidase VPS1

Gene

vps1

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:
  • 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

<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=48 µM for manganese1 Publication
  2. KM=9 µM for H2O2 (in manganese oxidation)1 Publication
  3. KM=2 µM for H2O2 (in manganese-independent oxidations)1 Publication
  4. KM=17 µM for methoxyhydroquinone1 Publication
  5. KM=200 µM for syringol1 Publication
  6. KM=3500 µM for veratryl alcohol1 Publication
  7. KM=2 µM for reactive black 51 Publication

    pH dependencei

    Optimum pH is 5 for manganese oxidation reaction, and around 3 for all the manganese-independent reactions.1 Publication

    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 bindingi67ManganeseBy similarity1
    Metal bindingi71ManganeseBy 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>Sitei74Transition 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 sitei78Proton acceptorPROSITE-ProRule annotation1
    Metal bindingi79Calcium 1PROSITE-ProRule annotation1
    Metal bindingi97Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation1
    Metal bindingi99Calcium 1PROSITE-ProRule annotation1
    Metal bindingi101Calcium 1PROSITE-ProRule annotation1
    Active sitei201Tryptophan radical intermediateBy similarity1
    Metal bindingi206Iron (heme axial ligand)PROSITE-ProRule annotation1
    Metal bindingi207Calcium 2PROSITE-ProRule annotation1
    Metal bindingi212ManganeseBy similarity1
    Metal bindingi224Calcium 2PROSITE-ProRule annotation1
    Metal bindingi226Calcium 2PROSITE-ProRule annotation1
    Metal bindingi229Calcium 2; via carbonyl oxygen1
    Metal bindingi231Calcium 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

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.11.1.16 4910

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q9UVP6

    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
    VPO2C_PLEER

    PeroxiBase, a peroxidase database

    More...
    PeroxiBasei
    2302 PerVP02

    <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 VPS1 (EC:1.11.1.161 Publication)
    Alternative name(s):
    Versatile solid phase peroxidase 1
    <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:vps1
    Synonyms:ps1
    <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

    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 – 20Sequence analysisAdd BLAST20
    <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_000030816921 – 312 PublicationsAdd BLAST11
    <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_500005698132 – 370Versatile peroxidase VPS1Add BLAST339

    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 bondi34 ↔ 46PROSITE-ProRule annotation
    Disulfide bondi45 ↔ 315PROSITE-ProRule annotation
    Disulfide bondi65 ↔ 151PROSITE-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>Glycosylationi133N-linked (GlcNAc...) asparagineSequence analysis1
    Disulfide bondi279 ↔ 344PROSITE-ProRule annotation

    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

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    Q9UVP6

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

    More...
    SMRi
    Q9UVP6

    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

    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>Regioni210 – 214Heme bindingBy similarity5

    <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

    KEGG Orthology (KO)

    More...
    KOi
    K20205

    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.

    Q9UVP6-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAFAKLSAFV LALGATVALG ESPTHRCLNK RVTCATGQTT ANEACCALFP
    60 70 80 90 100
    ILDDIQTNLF DGAQCGEEVH ESLRLTFHDA IAFSPALTNA GQFGGGGADG
    110 120 130 140 150
    SMIIFSDTEP NFHANLGIDE IVEAQKPFIA RHNISAADFI QFAGAIGVSN
    160 170 180 190 200
    CAGAPRLNFF LGRPDATQIP PDGLVPEPFD DVTKILSRMG DAGFSTVEVV
    210 220 230 240 250
    WLLASHTIAA ADHVDPSIPG TPFDSTPSTF DSQFFLETML QGTAFPGTPG
    260 270 280 290 300
    NQGEVESPLA GEMRLQSDFL LARDSRSACE WQSMVNNMPK IQNRFTQVMK
    310 320 330 340 350
    KLSLLGHNQA DLIDCSDVIP VPKTLTKAAT FPAGKSQADV EIVCNAAATP
    360 370
    FPALASDPGP VTAVPPVPPS
    Length:370
    Mass (Da):39,046
    Last modified:May 1, 2000 - 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:i86DA6F99C79D08B9
    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
    AF175710 Genomic DNA Translation: AAD54310.1

    Genome annotation databases

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ag:AAD54310

    <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
    AF175710 Genomic DNA Translation: AAD54310.1

    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
    1BQWmodel-A32-318[»]
    1QJRmodel-A32-370[»]
    ProteinModelPortaliQ9UVP6
    SMRiQ9UVP6
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiAA2 Auxiliary Activities 2
    mycoCLAPiVPO2C_PLEER
    PeroxiBasei2302 PerVP02

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAD54310

    Phylogenomic databases

    KOiK20205

    Enzyme and pathway databases

    BRENDAi1.11.1.16 4910
    SABIO-RKiQ9UVP6

    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 nameiVPS1_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: Q9UVP6
    <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, 2000
    Last modified: December 5, 2018
    This is version 82 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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