Reviewed, UniProtKB/Swiss-Prot P17180 (PER3_ARMRU)

Names and origin

Protein names

Recommended name:
    Peroxidase C3
    EC=1.11.1.7

Gene names

Name:

PRXC3

Organism

Armoracia rusticana (Horseradish) (Armoracia laphatifolia)

Taxonomic identifier

3704 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Armoracia

Protein attributes

Sequence length	349 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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	Donor + H2O2 = oxidized donor + 2 H2O.
Cofactor	Binds 2 calcium ions per subunit. Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
Subcellular location	Secreted Probable. Vacuole Probable. Note: Carboxy-terminal extension appears to target the protein to vacuoles.
Sequence similarities	Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Secreted Vacuole
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell vacuole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro 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
	Signal peptide	1 – 29	29
	Chain	30 – 349	320	Peroxidase C3		PRO_0000023744
Sites
	Active site	71	1	Proton acceptor By similarity
	Metal binding	72	1	Calcium 1 By similarity
	Metal binding	75	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	77	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	79	1	Calcium 1 By similarity
	Metal binding	81	1	Calcium 1 By similarity
	Metal binding	199	1	Iron (heme axial ligand) By similarity
	Metal binding	200	1	Calcium 2 By similarity
	Metal binding	251	1	Calcium 2 By similarity
	Metal binding	254	1	Calcium 2 By similarity
	Metal binding	259	1	Calcium 2 By similarity
	Binding site	168	1	Substrate; via carbonyl oxygen By similarity
	Site	67	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	30	1	Pyrrolidone carboxylic acid By similarity
	Glycosylation	86	1	N-linked (GlcNAc...) Potential
	Glycosylation	217	1	N-linked (GlcNAc...) Potential
	Glycosylation	243	1	N-linked (GlcNAc...) Potential
	Disulfide bond	40 ↔ 120		By similarity
	Disulfide bond	73 ↔ 78		By similarity
	Disulfide bond	126 ↔ 329		By similarity
	Disulfide bond	206 ↔ 238		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P17180-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 6563EB3880B75EC3	FASTA	349	38,180
	10 20 30 40 50 60 MGFSPLISCS AMGALILSCL LLQASNSNAQ LRPDFYFRTC PSVFNIIGDI IVDELRTDPR 70 80 90 100 110 120 IAASLLRLHF HDCFVRGCDA SILLDNSTSF RTEKDAAPNA NSARGFGVID RMKTSLERAC 130 140 150 160 170 180 PRTVSCADVL TIASQISVLL SGGPWWPVPL GRRDSVEAFF DLANTALPSP FFTLAQLKKA 190 200 210 220 230 240 FADVGLNRPS DLVALSGGHT FGRAQCQFVT PRLYNFNGTN RPDPTLDPTY LVQLRALCPQ 250 260 270 280 290 300 NGNGTVLVNF DVVTPNTFDR QYYTNLRNGK GLIQSDQELF STPGADTIPL VNLYSSNTFA 310 320 330 340 FFGAFVDAMI RMGNLRPLTG TQGEIRQNCR VVNSRIRGME NDDGVVSSI

References

[1]	"Genomic DNA structure of two new horseradish-peroxidase-encoding genes." Fujiyama K., Takemura H., Shinmyo A., Okada H., Takano M. Gene 89:163-169(1990) [PubMed: 2373366] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	D90116 Genomic DNA. Translation: BAA14144.1.
PIR	JH0150.
3D structure databases
HSSP	HSSP built from PDB template 1HCH based on UniProtKB P00433.
SMR	P17180. Positions 30-334.
ModBase	Search...
Protein family/group databases
PeroxiBase	56. AruPrx03.
Enzyme and pathway databases
BRENDA	1.11.1.7. 141069.
Family and domain databases
InterPro	IPR002016. Haem_peroxidase_pln/fun/bac. IPR000823. Peroxidase_pln. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00458. PEROXIDASE. PR00461. PLPEROXIDASE.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PER3_ARMRU

Accession

Primary (citable) accession number: P17180

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)