NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2247460 [NCBI, ExPASy, EBI, Israel, Japan]
Buffard D., Breda C., van Huystee R.B., Asemota O., Pierre M., Dang Ha D.B., Esnault R.;
"Molecular cloning of complementary DNAs encoding two cationic peroxidases from cultivated peanut cells.";
Proc. Natl. Acad. Sci. U.S.A. 87:8874-8878(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 (By similarity).
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

M37637; AAA32676.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B38265; B38265.

3D structure databases

HSSP

Q42578; 1PA2. [HSSP ENTRY / PDB]

ModBase

P22196.

Protein family/group databases

PeroxiBase

103; AhPrx05.

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; Secreted; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`	`Potential.`
`CHAIN`	`24 330`	`307`	`Cationic peroxidase 2.`	`PRO_0000023747`
`ACT_SITE`	`72 72`		`Proton acceptor (By similarity).`
`METAL`	`73 73`		`Calcium 1 (By similarity).`
`METAL`	`76 76`		`Calcium 1 (via carbonyl oxygen) (By similarity).`
`METAL`	`78 78`		`Calcium 1 (via carbonyl oxygen) (By similarity).`
`METAL`	`80 80`		`Calcium 1 (By similarity).`
`METAL`	`82 82`		`Calcium 1 (By similarity).`
`METAL`	`194 194`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`195 195`		`Calcium 2 (By similarity).`
`METAL`	`246 246`		`Calcium 2 (By similarity).`
`METAL`	`249 249`		`Calcium 2 (By similarity).`
`METAL`	`254 254`		`Calcium 2 (By similarity).`
`BINDING`	`164 164`		`Substrate; via carbonyl oxygen (By similarity).`
`SITE`	`68 68`	`1`	`Transition state stabilizer (By similarity).`
`CARBOHYD`	`212 212`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`41 117`		`By similarity.`
`DISULFID`	`74 79`		`By similarity.`
`DISULFID`	`123 326`		`By similarity.`
`DISULFID`	`201 233`		`By similarity.`

Sequence information

Length: 330 AA [This is the length of the unprocessed precursor]

Molecular weight: 35556 Da [This is the MW of the unprocessed precursor]

CRC64: A751978FDD9B63D2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEGVFNNKKF ILVFVFMLGL CIGITTVHGQ GTRVGFYSRT CPRAESIVRS TVRSHVNSDP 

        70         80         90        100        110        120 
TLAAKILRMH FHDCFVQGCD GSILISGPAT EKTAFANLGL RGYEIIDDAK TQLEAACPGV 

       130        140        150        160        170        180 
VSCADILALA ARDSVVLSGG LSWQVPTGRR DGRVSQASDV SNLPAPSDSV DVQKQKFAAK 

       190        200        210        220        230        240 
GLNTQDLVTL VGGHTIGTSE CQFFSNRLFN FNGTAAADPA IDPSFVSNLQ ALCPQNTGAA 

       250        260        270        280        290        300 
NRVALDTGSQ FKFDTSYFSN LRNRRGVLQS DQALWNDPST KSFVQRYLGL RGFLGLTFNV 

       310        320        330 
EFGKSMVKMS NIGVKTGTDG EIRKICSAFN

P22196 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