Reviewed, UniProtKB/Swiss-Prot Q05855 (PER1_WHEAT)

Names and origin

Protein names	Recommended name:     Peroxidase     EC=1.11.1.7 Alternative name(s):     WP2
Organism	Triticum aestivum (Wheat)
Taxonomic identifier	4565 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Triticum

Protein attributes

Sequence length	312 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (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. Involved in defense response to powdery meldew fungus.
Catalytic activity	Donor + H(2)O(2) = oxidized donor + 2 H(2)O.
Cofactor	Binds 2 calcium ions per subunit. Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
Subcellular location	SecretedBy similarity.
Tissue specificity	Root.
Sequence similarities	Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	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-KW
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 iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW peroxidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 312	289	Peroxidase		PRO_0000023757
Sites
	Active site	65	1	Proton acceptor By similarity
	Metal binding	66	1	Calcium 1 By similarity
	Metal binding	69	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	71	1	Calcium 1 By similarity
	Metal binding	73	1	Calcium 1 By similarity
	Metal binding	185	1	Iron (heme axial ligand) By similarity
	Metal binding	186	1	Calcium 2 By similarity
	Metal binding	231	1	Calcium 2 By similarity
	Metal binding	234	1	Calcium 2 By similarity
	Metal binding	239	1	Calcium 2 By similarity
	Binding site	155	1	Substrate; via carbonyl oxygen By similarity
	Site	61	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	24	1	Pyrrolidone carboxylic acid By similarity
	Glycosylation	262	1	N-linked (GlcNAc...) Potential
	Disulfide bond	34 ↔ 107		By similarity
	Disulfide bond	67 ↔ 70		By similarity
	Disulfide bond	113 ↔ 307		By similarity
	Disulfide bond	192 ↔ 218		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q05855-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: FF468A33F3DC68F7	FASTA	312	32,382
	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

References

[1]	"Sequence and tissue-specific expression of a putative peroxidase gene from wheat (Triticum aestivum L.)." Hertig C., Rebmann G., Bull J., Mauch F., Dudler R. Plant Mol. Biol. 16:171-174(1991) [PubMed: 1653627] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Cheyenne.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X53675 mRNA. Translation: CAA37713.1.
PIR	S13325.
UniGene	Ta.56782
3D structure databases
HSSP	HSSP built from PDB template 1SCH based on UniProtKB P22195.
ModBase	Search...
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]
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

PER1_WHEAT

Accession

Primary (citable) accession number: Q05855

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	November 25, 2008
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)