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P19135 (PER2_CUCSA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 73. 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 2
EC=1.11.1.7
Alternative name(s):
CUP2
OrganismCucumis sativus (Cucumber)
Taxonomic identifier3659 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Cucurbitales › Cucurbitaceae › Benincaseae › Cucumis

Protein attributes

Sequence length292 AA.
Sequence statusFragment.
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.

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.

Sequence similarities

Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

Ontologies

Keywords
   Biological processHydrogen peroxide
   LigandCalcium
Heme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   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

Chain‹1 – 292›292Peroxidase 2
PRO_0000055610

Sites

Active site381Proton acceptor By similarity
Metal binding391Calcium 1 By similarity
Metal binding421Calcium 1; via carbonyl oxygen By similarity
Metal binding441Calcium 1; via carbonyl oxygen By similarity
Metal binding461Calcium 1 By similarity
Metal binding481Calcium 1 By similarity
Metal binding1641Iron (heme axial ligand) By similarity
Metal binding1651Calcium 2 By similarity
Metal binding2101Calcium 2 By similarity
Metal binding2131Calcium 2 By similarity
Metal binding2181Calcium 2 By similarity
Binding site1341Substrate; via carbonyl oxygen By similarity
Site341Transition state stabilizer By similarity

Amino acid modifications

Glycosylation681N-linked (GlcNAc...) Potential
Glycosylation1391N-linked (GlcNAc...) Potential
Glycosylation1791N-linked (GlcNAc...) Potential
Disulfide bond7 ↔ 86 By similarity
Disulfide bond40 ↔ 45 By similarity
Disulfide bond92 ↔ 288 By similarity
Disulfide bond171 ↔ 199 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P19135 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 98FD89EF01CE6888

FASTA29231,857
        10         20         30         40         50         60 
TFYDESCPDV SNIVRRVVQQ ALVSDERAGA RLIRLHFHDC FVNGCDGSVL LEDQPGVVSE 

        70         80         90        100        110        120 
LAAPGNANIT GFNIVNNIKA AVEKACPGVV SCADILAIAS VGSVNLAGGP CWEVQLGRRD 

       130        140        150        160        170        180 
SRRANLQGAI DGLPSPFENV TQLKRKFDRV DLDSTDLVAL SGAHTFGKSR CQFFDRRLNV 

       190        200        210        220        230        240 
SNPDSTLNPR YAQQLRQACS SGRDTFVNLD PTTPNKFDKN YYTNLQSNTG PLTSDQVLHS 

       250        260        270        280        290 
TPGEDTVKIV NLFAASQNQF FESFGQSMIN MGNIQPLTGN QGEIRSNCRR LN

« Hide

References

[1]"Isolation and sequencing of cDNA clones encoding ethylene-induced putative peroxidases from cucumber cotyledons."
Morgens P.H., Callahan A.M., Dunn L.J., Abeles F.B.
Plant Mol. Biol. 14:715-725(1990) [PubMed: 2102850] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M32742 mRNA. Translation: AAA33121.1.
PIRS11870.

3D structure databases

ProteinModelPortalP19135.
SMRP19135. Positions 1-292.
ModBaseSearch...

Protein family/group databases

PeroxiBase23. CsaPrx07.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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 namePER2_CUCSA
AccessionPrimary (citable) accession number: P19135
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: June 28, 2011
This is version 73 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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