P85333 (PER2_BETPN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Peroxidase 2 EC=1.11.1.7
Organism	Betula pendula (European white birch) (Betula verrucosa)
Taxonomic identifier	3505 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fagales › Betulaceae › Betula

Protein attributes

Sequence length	13 AA.
Sequence status	Fragment.
Protein existence	Evidence 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 P84516 Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. UniProtKB P84516
Subcellular location	Secreted By similarity UniProtKB P84516.
Sequence similarities	Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Secreted
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›13	›13	Peroxidase 2		PRO_0000314639
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	13	1

Sequences

	Sequence		Length	Mass (Da)
	P85333 [UniParc]. Last modified January 15, 2008. Version 1. Checksum: 905A145F0159205A	FASTA	13	1,288
	10 VVSCADILAV AAR

References

[1]

"The presence of sinapyl lignin in Ginkgo biloba cell cultures changes our views of the evolution of lignin biosynthesis." Novo Uzal E., Gomez Ros L.V., Pomar F., Bernal M.A., Paradela A., Albar J.P., Ros Barcelo A. Physiol. Plantarum 135:196-213(2009) [PubMed: 19055540] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: PC-1121. Tissue: Callus.

Cross-references

3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
PROSITE	PS00435. PEROXIDASE_1. Partial match. PS00436. PEROXIDASE_2. Partial match. PS50873. PEROXIDASE_4. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PER2_BETPN

Accession

Primary (citable) accession number: P85333

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 15, 2008
Last modified:	June 28, 2011
This is version 13 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program