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P85346 (PER1_CYCRE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 15. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peroxidase 1

EC=1.11.1.7
OrganismCycas revoluta (Sago palm)
Taxonomic identifier3396 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaCycadophytaCycadalesCycadaceaeCycas

Protein attributes

Sequence length9 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Cofactor

Binds 2 calcium ions per subunit By similarity. UniProtKB P22195

Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. UniProtKB P22195

Subcellular location

Secreted By similarity. Secretedcell wall Ref.1 UniProtKB P84516.

Sequence similarities

Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentCell wall
Secreted
   LigandCalcium
Heme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›9›9Peroxidase 1
PRO_0000315883

Experimental info

Non-terminal residue11
Non-terminal residue91

Sequences

Sequence LengthMass (Da)Tools
P85346 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: DAAB544AB2D2CAA9

FASTA91,006
GFDVVDNIK 

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References

[1]"Analysis of the soluble cell wall proteome of gymnosperms."
Uzal E.N., Gomez-Ros L.V., Hernandez J.A., Pedreno M.A., Cuello J., Ros Barcelo A.
J. Plant Physiol. 166:831-843(2009) [PubMed: 19157640] [Abstract]
Cited for: PROTEIN SEQUENCE, SUBCELLULAR LOCATION.
Tissue: Callus.

Cross-references

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

PROSITEPS00435. PEROXIDASE_1. Partial match.
PS00436. PEROXIDASE_2. Partial match.
PS50873. PEROXIDASE_4. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePER1_CYCRE
AccessionPrimary (citable) accession number: P85346
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: June 28, 2011
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families