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P85439 (PER1_CATRO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 14. 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 attributes

Sequence length46 AA.
Sequence statusFragments.
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 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. UniProtKB P22195

Binds 2 calcium ions per subunit By similarity. UniProtKB P22195

Subcellular location

Secreted By similarity UniProtKB P84516.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentSecreted
   LigandCalcium
Heme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular componentextracellular 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 – ›46›46Peroxidase 1
PRO_0000324678

Experimental info

Non-adjacent residues24 – 252
Non-terminal residue11
Non-terminal residue461

Sequences

Sequence LengthMass (Da)Tools
P85439 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: 95DE73C8F37F8DEB

FASTA464,764
        10         20         30         40 
LVCFVVVVFM AAAAAMAGAD RELKYLSHGG VDFPVPAGRL DGVVSR 

« Hide

References

[1]Varman P.A.M., Ranjitha Kumari B.D.
Submitted (JAN-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE.

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_CATRO
AccessionPrimary (citable) accession number: P85439
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: June 28, 2011
This is version 14 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