NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Cheyenne;
DOI=10.1007/BF00017928; PubMed=1653627 [NCBI, ExPASy, EBI, Israel, Japan]
Hertig C., Rebmann G., Bull J., Mauch F., Dudler R.;
"Sequence and tissue-specific expression of a putative peroxidase gene from wheat (Triticum aestivum L.).";
Plant Mol. Biol. 16:171-174(1991).

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.
FUNCTION: Involved in defense response to powdery meldew fungus.
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).
TISSUE SPECIFICITY: Root.
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

X53675; CAA37713.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S13325; S13325.

UniGene

Ta.56782

3D structure databases

HSSP

P22195; 1SCH. [HSSP ENTRY / PDB]

ModBase

Q05855.

Protein family/group databases

PeroxiBase

468; TaPrx02-3.

Organism-specific databases

Gramene

Q05855; -.

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.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`	`Potential.`
`CHAIN`	`24 312`	`289`	`Peroxidase.`	`PRO_0000023757`
`ACT_SITE`	`65 65`		`Proton acceptor (By similarity).`
`METAL`	`66 66`		`Calcium 1 (By similarity).`
`METAL`	`69 69`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`71 71`		`Calcium 1 (By similarity).`
`METAL`	`73 73`		`Calcium 1 (By similarity).`
`METAL`	`185 185`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`186 186`		`Calcium 2 (By similarity).`
`METAL`	`231 231`		`Calcium 2 (By similarity).`
`METAL`	`234 234`		`Calcium 2 (By similarity).`
`METAL`	`239 239`		`Calcium 2 (By similarity).`
`BINDING`	`155 155`		`Substrate; via carbonyl oxygen (By similarity).`
`SITE`	`61 61`	`1`	`Transition state stabilizer (By similarity).`
`MOD_RES`	`24 24`		`Pyrrolidone carboxylic acid (By similarity).`
`CARBOHYD`	`262 262`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`34 107`		`By similarity.`
`DISULFID`	`67 70`		`By similarity.`
`DISULFID`	`113 307`		`By similarity.`
`DISULFID`	`192 218`		`By similarity.`

Sequence information

Length: 312 AA [This is the length of the unprocessed precursor]

Molecular weight: 32382 Da [This is the MW of the unprocessed precursor]

CRC64: FF468A33F3DC68F7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAMGSASCIS LVVLVALATA ASGQLSSTFY DTSCPRALVA IKSGVAAAVS SDPRMGASLL 

        70         80         90        100        110        120 
RLHFHDCFGC DASVLLTGME QNAGPNVGSL RGFGVIDNIK TQLESVCKQT VSCADILTVA 

       130        140        150        160        170        180 
ARDSVVALGG PSWTVPLGRR DSTTASASLA NSDLPGPSSS RSQLEAAFLK KNLNTVDMVA 

       190        200        210        220        230        240 
LSGAHTIGKA QCSNFRTRIY GGDTNINTAF ATSLKANCPQ SGGNTNLANL DTMTPNAFDN 

       250        260        270        280        290        300 
AYYTNLLSQK GLLHSDQVLF NNETTDNTVR NFASNAAAFS SAFTTAMIKM GNIAPLTGTQ 

       310 
GQIRLSCSKV NS

Q05855 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