[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3371352 [NCBI, ExPASy, EBI, Israel, Japan] Fujiyama K., Takemura H., Shibayama S., Kobayashi K., Choi J.K., Shinmyo A., Takano M., Yamada Y., Okada H.; "Structure of the horseradish peroxidase isozyme C genes."; Eur. J. Biochem. 173:681-687(1988).
[2]	PROTEIN SEQUENCE OF 31-338. DOI=10.1016/0014-5793(76)80804-6; PubMed=1001465 [NCBI, ExPASy, EBI, Israel, Japan] Welinder K.G.; "Covalent structure of the glycoprotein horseradish peroxidase (EC 1.11.1.7)."; FEBS Lett. 72:19-23(1976).
[3]	X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS). DOI=10.1038/nsb1297-1032; PubMed=9406554 [NCBI, ExPASy, EBI, Israel, Japan] Gajhede M., Schuller D.J., Henriksen A., Smith A.T., Poulos T.L.; "Crystal structure of horseradish peroxidase C at 2.15-A resolution."; Nat. Struct. Biol. 4:1032-1038(1997).
[4]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). DOI=10.1021/bi980234j; PubMed=9609699 [NCBI, ExPASy, EBI, Israel, Japan] Henriksen A., Schuller D.J., Meno K., Welinder K.G., Smith A.T., Gajhede M.; "Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by X-ray crystallography."; Biochemistry 37:8054-8060(1998).
[5]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). Meno K., White C.G., Smith A.T., Gajhede M.; Submitted (DEC-1998) to the PDB data bank.

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.
SUBUNIT: Monomer.
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

M37156; AAA33377.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S00625; OPRHC.

3D structure databases

PDB

1ATJ; X-ray; 2.15 A; A/B/C/D/E/F=31-336.	[ExPASy / RCSB / EBI]
1GW2; X-ray; 2.15 A; A=31-338.	[ExPASy / RCSB / EBI]
1GWO; X-ray; 2.07 A; A=31-338.	[ExPASy / RCSB / EBI]
1GWT; X-ray; 1.70 A; A=31-338.	[ExPASy / RCSB / EBI]
1GWU; X-ray; 1.31 A; A=31-338.	[ExPASy / RCSB / EBI]
1GX2; X-ray; 2.20 A; A/B=31-338.	[ExPASy / RCSB / EBI]
1H55; X-ray; 1.61 A; A=31-338.	[ExPASy / RCSB / EBI]
1H57; X-ray; 1.60 A; A=31-338.	[ExPASy / RCSB / EBI]
1H58; X-ray; 1.70 A; A=31-338.	[ExPASy / RCSB / EBI]
1H5A; X-ray; 1.60 A; A=31-338.	[ExPASy / RCSB / EBI]
1H5C; X-ray; 1.62 A; A=31-338.	[ExPASy / RCSB / EBI]
1H5D; X-ray; 1.60 A; A=31-338.	[ExPASy / RCSB / EBI]
1H5E; X-ray; 1.60 A; A=31-338.	[ExPASy / RCSB / EBI]
1H5F; X-ray; 1.60 A; A=31-338.	[ExPASy / RCSB / EBI]
1H5G; X-ray; 1.60 A; A=31-338.	[ExPASy / RCSB / EBI]
1H5H; X-ray; 1.60 A; A=31-338.	[ExPASy / RCSB / EBI]
1H5I; X-ray; 1.60 A; A=31-338.	[ExPASy / RCSB / EBI]
1H5J; X-ray; 1.60 A; A=31-338.	[ExPASy / RCSB / EBI]
1H5K; X-ray; 1.60 A; A=31-338.	[ExPASy / RCSB / EBI]
1H5L; X-ray; 1.60 A; A=31-338.	[ExPASy / RCSB / EBI]
1H5M; X-ray; 1.60 A; A=31-338.	[ExPASy / RCSB / EBI]
1HCH; X-ray; 1.57 A; A=31-336.	[ExPASy / RCSB / EBI]
1KZM; X-ray; 2.00 A; A=31-338.	[ExPASy / RCSB / EBI]
1W4W; X-ray; 1.55 A; A=31-353.	[ExPASy / RCSB / EBI]
1W4Y; X-ray; 1.60 A; A=31-353.	[ExPASy / RCSB / EBI]
2ATJ; X-ray; 2.00 A; A/B=31-337.	[ExPASy / RCSB / EBI]
3ATJ; X-ray; 2.20 A; A/B=31-338.	[ExPASy / RCSB / EBI]
4ATJ; X-ray; 2.50 A; A/B=31-338.	[ExPASy / RCSB / EBI]
6ATJ; X-ray; 2.00 A; A=31-338.	[ExPASy / RCSB / EBI]
7ATJ; X-ray; 1.47 A; A=31-338.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1ATJ; -.
1GW2; -.
1GWO; -.
1GWT; -.
1GWU; -.
1GX2; -.
1H55; -.
1H57; -.
1H58; -.
1H5A; -.
1H5C; -.
1H5D; -.
1H5E; -.
1H5F; -.
1H5G; -.
1H5H; -.
1H5I; -.
1H5J; -.
1H5K; -.
1H5L; -.
1H5M; -.
1HCH; -.
1KZM; -.
1W4W; -.
1W4Y; -.
2ATJ; -.
3ATJ; -.
4ATJ; -.
6ATJ; -.
7ATJ; -.

ModBase

P00433.

Protein family/group databases

PeroxiBase

90; AruPrx01a.

PTM databases

GlycoSuiteDB

P00433; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005773;	Cellular component: vacuole (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004601;	Molecular function: peroxidase activity (inferred from electronic annotation from InterPro).
GO:0042744;	Biological process: hydrogen peroxide catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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

P00433; -.

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

Keywords

3D-structure; Calcium; Direct protein sequencing; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid; Secreted; Signal; Vacuole.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 30`	`30`
`CHAIN`	`31 338`	`308`	`Peroxidase C1A.`	`PRO_0000023739`
`PROPEP`	`339 353`	`15`		`PRO_0000023740`
`ACT_SITE`	`72 72`		`Proton acceptor.`
`METAL`	`73 73`		`Calcium 1.`
`METAL`	`76 76`		`Calcium 1; via carbonyl oxygen.`
`METAL`	`78 78`		`Calcium 1; via carbonyl oxygen.`
`METAL`	`80 80`		`Calcium 1.`
`METAL`	`82 82`		`Calcium 1.`
`METAL`	`94 94`		`Calcium 1.`
`METAL`	`200 200`		`Iron (heme axial ligand).`
`METAL`	`201 201`		`Calcium 2.`
`METAL`	`252 252`		`Calcium 2.`
`METAL`	`255 255`		`Calcium 2.`
`METAL`	`260 260`		`Calcium 2.`
`BINDING`	`169 169`		`Substrate; via carbonyl oxygen.`
`SITE`	`68 68`	`1`	`Transition state stabilizer.`
`MOD_RES`	`31 31`		`Pyrrolidone carboxylic acid.`
`CARBOHYD`	`43 43`		`N-linked (GlcNAc...).`
`CARBOHYD`	`87 87`		`N-linked (GlcNAc...).`
`CARBOHYD`	`188 188`		`N-linked (GlcNAc...).`
`CARBOHYD`	`216 216`		`N-linked (GlcNAc...).`
`CARBOHYD`	`228 228`		`N-linked (GlcNAc...).`
`CARBOHYD`	`244 244`		`N-linked (GlcNAc...).`
`CARBOHYD`	`285 285`		`N-linked (GlcNAc...).`
`CARBOHYD`	`298 298`		`N-linked (GlcNAc...).`
`DISULFID`	`41 121`
`DISULFID`	`74 79`
`DISULFID`	`127 331`
`DISULFID`	`207 239`
`TURN`	`34 40`	`7`
`HELIX`	`44 58`	`15`
`HELIX`	`62 74`	`13`
`TURN`	`75 77`	`3`
`STRAND`	`78 81`	`4`
`HELIX`	`82 84`	`3`
`STRAND`	`89 91`	`3`
`HELIX`	`94 96`	`3`
`TURN`	`98 103`	`6`
`HELIX`	`107 120`	`14`
`TURN`	`122 124`	`3`
`HELIX`	`127 141`	`15`
`HELIX`	`161 167`	`7`
`HELIX`	`175 184`	`10`
`HELIX`	`190 197`	`8`
`HELIX`	`198 201`	`4`
`STRAND`	`204 206`	`3`
`HELIX`	`207 210`	`4`
`HELIX`	`211 215`	`5`
`HELIX`	`217 219`	`3`
`STRAND`	`220 222`	`3`
`HELIX`	`229 238`	`10`
`STRAND`	`248 251`	`4`
`HELIX`	`262 268`	`7`
`HELIX`	`275 282`	`8`
`TURN`	`284 288`	`5`
`HELIX`	`289 298`	`10`
`HELIX`	`300 314`	`15`
`STRAND`	`324 326`	`3`

Sequence information

Length: 353 AA [This is the length of the unprocessed precursor]

Molecular weight: 38825 Da [This is the MW of the unprocessed precursor]

CRC64: AC916C03C4A24D27 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHFSSSSTLF TCITLIPLVC LILHASLSDA QLTPTFYDNS CPNVSNIVRD TIVNELRSDP 

        70         80         90        100        110        120 
RIAASILRLH FHDCFVNGCD ASILLDNTTS FRTEKDAFGN ANSARGFPVI DRMKAAVESA 

       130        140        150        160        170        180 
CPRTVSCADL LTIAAQQSVT LAGGPSWRVP LGRRDSLQAF LDLANANLPA PFFTLPQLKD 

       190        200        210        220        230        240 
SFRNVGLNRS SDLVALSGGH TFGKNQCRFI MDRLYNFSNT GLPDPTLNTT YLQTLRGLCP 

       250        260        270        280        290        300 
LNGNLSALVD FDLRTPTIFD NKYYVNLEEQ KGLIQSDQEL FSSPNATDTI PLVRSFANST 

       310        320        330        340        350 
QTFFNAFVEA MDRMGNITPL TGTQGQIRLN CRVVNSNSLL HDMVEVVDFV SSM

P00433 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