[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0378-1119(90)90002-9; PubMed=2373366 [NCBI, ExPASy, EBI, Israel, Japan] Fujiyama K., Takemura H., Shinmyo A., Okada H., Takano M.; "Genomic DNA structure of two new horseradish-peroxidase-encoding genes."; Gene 89:163-169(1990).

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 + H₂O₂ = oxidized donor + 2 H₂O.
COFACTOR: Binds 2 calcium ions per subunit.
COFACTOR: 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.
SIMILARITY: Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D90116; BAA14144.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JH0150; JH0150.

3D structure databases

HSSP

P00433; 1HCH. [HSSP ENTRY / PDB]

SMR

P17180; 30-334.

ModBase

P17180.

Protein family/group databases

PeroxiBase

56; AruPrx03.

Family and domain databases

InterPro

IPR002016; Haem_peroxidase_pln/fun/bac.
IPR000823; Peroxidase_pln.
Graphical view of domain structure.

Pfam

PF00141; peroxidase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00458; PEROXIDASE.
PR00461; PLPEROXIDASE.

PROSITE

PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calcium; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid; Secreted; Signal; Vacuole.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 29`	`29`
`CHAIN`	`30 349`	`320`	`Peroxidase C3.`	`PRO_0000023744`
`ACT_SITE`	`71 71`		`Proton acceptor (By similarity).`
`METAL`	`72 72`		`Calcium 1 (By similarity).`
`METAL`	`75 75`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`77 77`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`79 79`		`Calcium 1 (By similarity).`
`METAL`	`81 81`		`Calcium 1 (By similarity).`
`METAL`	`199 199`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`200 200`		`Calcium 2 (By similarity).`
`METAL`	`251 251`		`Calcium 2 (By similarity).`
`METAL`	`254 254`		`Calcium 2 (By similarity).`
`METAL`	`259 259`		`Calcium 2 (By similarity).`
`BINDING`	`168 168`		`Substrate; via carbonyl oxygen (By similarity).`
`SITE`	`67 67`	`1`	`Transition state stabilizer (By similarity).`
`MOD_RES`	`30 30`		`Pyrrolidone carboxylic acid (By similarity).`
`CARBOHYD`	`86 86`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`217 217`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`243 243`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`40 120`		`By similarity.`
`DISULFID`	`73 78`		`By similarity.`
`DISULFID`	`126 329`		`By similarity.`
`DISULFID`	`206 238`		`By similarity.`

Sequence information

Length: 349 AA [This is the length of the unprocessed precursor]

Molecular weight: 38180 Da [This is the MW of the unprocessed precursor]

CRC64: 6563EB3880B75EC3 [This is a checksum on the sequence]

        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

P17180 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools