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Protein

Peroxidase 3

Gene
N/A
Organism
Vitis vinifera (Grape)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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.Curated

Catalytic activityi

2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.

Cofactori

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase 3By similarity (EC:1.11.1.7)
OrganismiVitis vinifera (Grape)
Taxonomic identifieri29760 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsVitalesVitaceaeVitis

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; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000352653‹1 – ›41Peroxidase 3Add BLAST›41

Proteomic databases

PRIDEiP86015

Structurei

3D structure databases

SMRiP86015
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.PROSITE-ProRule annotation

Sequencei

Sequence statusi: Fragments.

P86015-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40 
QTFVTIPGTL RDHPDNLSLA GDGFDTVIKV SCADILTMAT R
Length:41
Mass (Da):4,391
Last modified:October 14, 2008 - v1
Checksum:iD5442744DC68035C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence uncertaintyi1Q or K1
Non-terminal residuei11
Sequence uncertaintyi3F or M1
Sequence uncertaintyi6I or L1
Sequence uncertaintyi10L or I1
Non-adjacent residuesi11 – 12Curated2
Sequence uncertaintyi17L or I1
Sequence uncertaintyi19L or I1
Sequence uncertaintyi24F or M1
Sequence uncertaintyi29K or Q1
Non-adjacent residuesi30 – 31Curated2
Sequence uncertaintyi35I or L1
Sequence uncertaintyi36L or I1
Sequence uncertaintyi38M or F1
Non-terminal residuei411

Cross-referencesi

3D structure databases

SMRiP86015
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP86015

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiPER3_VITVI
AccessioniPrimary (citable) accession number: P86015
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: October 14, 2008
Last modified: May 10, 2017
This is version 19 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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Main funding by: National Institutes of Health

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