Reviewed, UniProtKB/Swiss-Prot P27337 (PER1_HORVU)

Names and origin

Protein names	Recommended name:     Peroxidase 1     EC=1.11.1.7
Organism	Hordeum vulgare (Barley)
Taxonomic identifier	4513 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum

Protein attributes

Sequence length	315 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 H2O2, 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 + H2O2 = oxidized donor + 2 H2O.
Cofactor	Binds 2 calcium ions per subunit. Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
Subcellular location	Secreted By similarity.
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	Disulfide bond 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-SubCell
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 peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 315	294	Peroxidase 1		PRO_0000023748
Sites
	Active site	63	1	Proton acceptor By similarity
	Metal binding	64	1	Calcium 1 By similarity
	Metal binding	67	1	Calcium 1; via carbonyl oxygen 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	186	1	Iron (heme axial ligand) By similarity
	Metal binding	187	1	Calcium 2 By similarity
	Metal binding	234	1	Calcium 2 By similarity
	Metal binding	237	1	Calcium 2 By similarity
	Metal binding	242	1	Calcium 2 By similarity
	Binding site	155	1	Substrate; via carbonyl oxygen By similarity
	Site	59	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	22	1	Pyrrolidone carboxylic acid By similarity
	Glycosylation	158	1	N-linked (GlcNAc...) Potential
	Glycosylation	265	1	N-linked (GlcNAc...) Potential
	Disulfide bond	32 ↔ 107		By similarity
	Disulfide bond	65 ↔ 70		By similarity
	Disulfide bond	113 ↔ 310		By similarity
	Disulfide bond	193 ↔ 219		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P27337-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 4867179BD0296172	FASTA	315	32,976
	10 20 30 40 50 60 MASSSYTSLL VLVALVTAAS AQLSPTFYDT SCPRALATIK SGVMAAVTSD PRMGASLLRL 70 80 90 100 110 120 HFHDCFVQGC DASVLLSGME QNAIPNAGSL RGFGVIDSIK TQIEAICKQT VSCADILTVA 130 140 150 160 170 180 ARDSVVALGG PSWTVPLGRR DSIDANENEA NTDLPGFNSS RAELEAAFLK KGGLNTVDMV 190 200 210 220 230 240 ALSGAHTIGQ AQCSTFRARI YGGDTNINAA YAASLRANCP QTVGSGDGSL ANLDTTTANT 250 260 270 280 290 300 FDNAYYTNLM SQKGLLHSDQ VLFNNDTTDN TVRNFASNPA AFSSSFTTAM IKMGNIAPKT 310 GTQGQIRLSC SRVNS

References

[1]

"cDNA cloning and characterization of two barley peroxidase transcripts induced differentially by the powdery mildew fungus Erysiphe graminis." Thordal-Christensen H., Brandt J., Cho B.H., Rasmussen S.K., Gregersen P.L., Smedegaard-Petersen V., Collinge D.B. Physiol. Mol. Plant Pathol. 40:395-409(1992) [Agricola: IND93004675] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Pallas / P-01. Tissue: Seedling leaf.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X58396 mRNA. Translation: CAA41294.1.
PIR	S14611. T06164.
UniGene	Hv.23479
3D structure databases
HSSP	HSSP built from PDB template 1SCH based on UniProtKB P22195.
ModBase	Search...
Protein family/group databases
PeroxiBase	69. HVPEROXI.
Organism-specific databases
Gramene	P27337.
Enzyme and pathway databases
BRENDA	1.11.1.7. 283.
Family and domain databases
InterPro	IPR002016. Haem_peroxidase_pln/fun/bac. IPR000823. Peroxidase_pln. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [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_HORVU

Accession

Primary (citable) accession number: P27337

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)