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P27337 (PER1_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peroxidase 1
EC=1.11.1.7
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum

Protein attributes

Sequence length315 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

2 phenolic donor + H2O2 = 2 phenoxyl radical of the 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 processHydrogen peroxide
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Heme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   PTMDisulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionheme binding

Inferred from electronic annotation. Source: InterPro

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 315294Peroxidase 1
PRO_0000023748

Sites

Active site631Proton acceptor By similarity
Metal binding641Calcium 1 By similarity
Metal binding671Calcium 1; via carbonyl oxygen By similarity
Metal binding691Calcium 1; via carbonyl oxygen By similarity
Metal binding711Calcium 1 By similarity
Metal binding731Calcium 1 By similarity
Metal binding1861Iron (heme axial ligand) By similarity
Metal binding1871Calcium 2 By similarity
Metal binding2341Calcium 2 By similarity
Metal binding2371Calcium 2 By similarity
Metal binding2421Calcium 2 By similarity
Binding site1551Substrate; via carbonyl oxygen By similarity
Site591Transition state stabilizer By similarity

Amino acid modifications

Modified residue221Pyrrolidone carboxylic acid By similarity
Glycosylation1581N-linked (GlcNAc...) Potential
Glycosylation2651N-linked (GlcNAc...) Potential
Disulfide bond32 ↔ 107 By similarity
Disulfide bond65 ↔ 70 By similarity
Disulfide bond113 ↔ 310 By similarity
Disulfide bond193 ↔ 219 By similarity

Sequences

Sequence LengthMass (Da)Tools
P27337 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 4867179BD0296172

FASTA31532,976
        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

« Hide

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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X58396 mRNA. Translation: CAA41294.1.
PIRS14611.
T06164.
UniGeneHv.23479.

3D structure databases

ProteinModelPortalP27337.
SMRP27337. Positions 22-314.
ModBaseSearch...

Protein family/group databases

PeroxiBase69. HVPEROXI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP27337.

Gene expression databases

GenevestigatorP27337.

Family and domain databases

InterProIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSPR00458. PEROXIDASE.
PR00461. PLPEROXIDASE.
SUPFAMSSF48113. Peroxidase_super. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePER1_HORVU
AccessionPrimary (citable) accession number: P27337
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 28, 2011
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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