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Reviewed, UniProtKB/Swiss-Prot P85347 (PER2_CYCRE)

Last modified November 25, 2008. Version 4. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peroxidase 2
    EC=1.11.1.7
OrganismCycas revoluta (Sago palm)
Taxonomic identifier3396 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaCycadophytaCycadalesCycadaceaeCycas

Protein attributes

Sequence length15 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Removal of H(2)O(2), 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

Donor + H(2)O(2) = oxidized donor + 2 H(2)O.

Cofactor

Binds 2 calcium ions per subunit By similarity.

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

Subcellular location

SecretedBy similarity.

Sequence similarities

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

Ontologies

Keywords

   Biological processHydrogen peroxide
   Cellular componentSecreted
   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

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

heme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peroxidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›15›15Peroxidase 2
PRO_0000315884

Sites

Metal binding91Iron (heme axial ligand) By similarity
Metal binding101Calcium 2 By similarity

Experimental info

Non-terminal residue11
Non-terminal residue151

Sequences

Sequence LengthMass (Da)Tools
P85347-1 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: D6D047F4379189B9

FASTA151,509
        10 
DLVALSGAHT IGQAR 

« Hide

References

[1]Novo Uzal E., Gomez Ros L.V., Ros Barcelo A.
Submitted (NOV-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE.
Tissue: Callus.

Cross-references

3D structure databases

ModBaseSearch...

Family and domain databases

InterProIPR002016. Haem_peroxidase_pln/fun/bac.
[Graphical view]
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. Partial match.
PS50873. PEROXIDASE_4. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePER2_CYCRE
AccessionPrimary (citable) accession number: P85347
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: November 25, 2008
This is version 4 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents