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Entry version 60 (08 May 2019)
Sequence version 1 (05 Jul 2005)
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Protein

Basic peroxidase

Gene

POD3

more
Organism
Zinnia violacea (Garden zinnia) (Zinnia elegans)
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

Removal of H2O2, oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. Involved in the synthesis of highly polymerized lignins.

Caution

Four genes are encoding the same mature protein that may have different glycosylation degree. The two precursors produced differ by only one amino acid located in the signal peptide.Curated

<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

The full glycosylation reduces the affinity of the enzyme for both p-coumaryl and coniferyl, but not sinapyl, alcohol.
  1. KM=241 µM for p-coumaryl alcohol (in the presence of 10.2 µM H2O2, for a partially glycosylated enzyme)1 Publication
  2. KM=432 µM for p-coumaryl alcohol (in the presence of 10.2 µM H2O2, for a fully glycosylated enzyme)1 Publication
  3. KM=83 µM for coniferyl alcohol (in the presence of 10.2 µM H2O2, for a partially glycosylated enzyme)1 Publication
  4. KM=124 µM for coniferyl alcohol (in the presence of 10.2 µM H2O2, for a fully glycosylated enzyme)1 Publication
  5. KM=15 µM for sinapyl alcohol (in the presence of 10.2 µM H2O2, for a partially glycosylated enzyme)1 Publication
  6. KM=13 µM for sinapyl alcohol (in the presence of 10.2 µM H2O2, for a fully glycosylated enzyme)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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>Sitei68Transition 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 sitei72Proton acceptor1
    <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 bindingi73Calcium 1PROSITE-ProRule annotation1
    Metal bindingi76Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation1
    Metal bindingi78Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation1
    Metal bindingi80Calcium 1PROSITE-ProRule annotation1
    Metal bindingi82Calcium 1PROSITE-ProRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei165Substrate; via carbonyl oxygenPROSITE-ProRule annotation1
    Metal bindingi195Iron (heme axial ligand)1
    Metal bindingi196Calcium 2PROSITE-ProRule annotation1
    Metal bindingi241Calcium 2PROSITE-ProRule annotation1
    Metal bindingi244Calcium 2PROSITE-ProRule annotation1
    Metal bindingi249Calcium 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
    LigandCalcium, Heme, Iron, Metal-binding

    Protein family/group databases

    PeroxiBase, a peroxidase database

    More...
    PeroxiBasei
    2625 ZePrx14

    <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:
    Basic peroxidase (EC:1.11.1.7)
    Alternative name(s):
    ZePrx33.44
    ZePrx34.70
    <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:POD3
    AND
    Name:POD4
    <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>OrganismiZinnia violacea (Garden zinnia) (Zinnia elegans)
    <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 identifieri34245 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeAsteroideaeHeliantheae allianceHeliantheaeZinnia

    <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 Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; 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 – 301 PublicationAdd BLAST30
    <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_000004269731 – 321Basic peroxidaseAdd BLAST291

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei31Pyrrolidone carboxylic acidPROSITE-ProRule annotation1 Publication1
    <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 bondi41 ↔ 117PROSITE-ProRule annotation
    Disulfide bondi74 ↔ 79PROSITE-ProRule annotation
    Disulfide bondi123 ↔ 317PROSITE-ProRule annotation
    Disulfide bondi202 ↔ 228PROSITE-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>Glycosylationi211N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi221N-linked (GlcNAc...) asparagineSequence analysis1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    N-glycosylated.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Expressed in tracheary elements, roots, young and old hypocotyls, and stems in the partially glycosylated form and in roots and young hypocotyls in the fully glycosylated form. None of the isoforms is significantly expressed in leaves or cotyledons.1 Publication

    <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

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

    More...
    SMRi
    Q4W1I9

    Database of comparative protein structure models

    More...
    ModBasei
    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. Classical plant (class III) peroxidase subfamily.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00693 secretory_peroxidase, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002016 Haem_peroxidase
    IPR010255 Haem_peroxidase_sf
    IPR000823 Peroxidase_pln
    IPR019794 Peroxidases_AS
    IPR019793 Peroxidases_heam-ligand_BS
    IPR033905 Secretory_peroxidase

    Pfam protein domain database

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

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00458 PEROXIDASE
    PR00461 PLPEROXIDASE

    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.

    Q4W1I9-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSYHKSSGTT LMVPLFMLLI SVNYFMSCNA QLSTTFYDTT CPTALSTIRT
    60 70 80 90 100
    SIRSSVSSNR RNAALVIRLL FHDCFVQGCD ASLLLSGAGS ERASPANDGV
    110 120 130 140 150
    LGYEVIDAAK AAVERVCPGV VSCADILAVA ARDASVAVGG PSWTVRLGRR
    160 170 180 190 200
    DSTTSNAAQA ATDLPRGNMV LSQLISNFAN KGLNTREMVA LSGSHTLGQA
    210 220 230 240 250
    RCIRFRGRIY NSTLRIEPNF NRSLSQACPP TGNDATLRPL DLVTPNSFDN
    260 270 280 290 300
    NYYRNLVTSR GLLISDQVLF NADSTDSIVT EYVNNPATFA ADFAAAMVKM
    310 320
    SEIGVVTGTS GIVRTLCGNP S
    Length:321
    Mass (Da):34,233
    Last modified:July 5, 2005 - 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:i620A21D02479F7F3
    GO

    <p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

    Molecular mass is 31460 Da from positions 30 - 321. Determined by MALDI. Deglycosylated form.1 Publication
    Molecular mass is 33440 Da from positions 30 - 321. Determined by MALDI. Partially glycosylated form.1 Publication
    Molecular mass is 34700 Da from positions 30 - 321. Determined by MALDI. Fully glycosylated form.1 Publication

    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
    AJ880394 mRNA Translation: CAI54301.1
    AJ880392 mRNA Translation: CAI54299.1

    <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
    AJ880394 mRNA Translation: CAI54301.1
    AJ880392 mRNA Translation: CAI54299.1

    3D structure databases

    SMRiQ4W1I9
    ModBaseiSearch...

    Protein family/group databases

    PeroxiBasei2625 ZePrx14

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Family and domain databases

    CDDicd00693 secretory_peroxidase, 1 hit
    InterProiView protein in InterPro
    IPR002016 Haem_peroxidase
    IPR010255 Haem_peroxidase_sf
    IPR000823 Peroxidase_pln
    IPR019794 Peroxidases_AS
    IPR019793 Peroxidases_heam-ligand_BS
    IPR033905 Secretory_peroxidase
    PfamiView protein in Pfam
    PF00141 peroxidase, 1 hit
    PRINTSiPR00458 PEROXIDASE
    PR00461 PLPEROXIDASE
    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...

    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 nameiPER2_ZINVI
    <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: Q4W1I9
    Secondary accession number(s): P84332, P84333
    <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: November 8, 2005
    Last sequence update: July 5, 2005
    Last modified: May 8, 2019
    This is version 60 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 programPlant 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
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