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

Peroxidase

Gene
N/A
Organism
Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus)
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

Miscellaneous

On the 2D-gel the determined pI of this protein is: 9.3, its MW is: 38249 kDa.1 Publication

Catalytic activityi

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

Cofactori

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BRENDAi1.11.1.7 1789

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase (EC:1.11.1.7)
OrganismiCynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus)
Taxonomic identifieri59895 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeCarduoideaeCardueaeCarduinaeCynara

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000055606‹1 – ›43PeroxidaseAdd BLAST›43

Proteomic databases

PRIDEiP84714

Structurei

3D structure databases

ProteinModelPortaliP84714
SMRiP84714
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Sequencei

Sequence statusi: Fragments.

P84714-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40 
VVSCADITAL AARQGLFTSD QDLYTDSRMG QLNVLTGTQG EIR
Length:43
Mass (Da):4,616
Last modified:December 20, 2005 - v1
Checksum:iC93CBF95846E20CC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11 Publication1
Non-adjacent residuesi13 – 141 Publication2
Non-adjacent residuesi28 – 291 Publication2
Non-terminal residuei431 Publication1

Cross-referencesi

3D structure databases

ProteinModelPortaliP84714
SMRiP84714
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP84714

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.11.1.7 1789

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiPER_CYNCS
AccessioniPrimary (citable) accession number: P84714
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: May 10, 2017
This is version 35 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
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