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P15233 (PER1C_ARMRU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 82. 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 C1C
EC=1.11.1.7
Gene names
Name:PRXC1C
Synonyms:HRPC3
OrganismArmoracia rusticana (Horseradish) (Armoracia laphatifolia)
Taxonomic identifier3704 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Cardamineae › Armoracia

Protein attributes

Sequence length332 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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.

Subcellular location

Secreted Probable. Vacuole Probable. Note: Carboxy-terminal extension appears to target the protein to vacuoles.

Sequence similarities

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

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentSecreted
Vacuole
   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

vacuole

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 peptide‹1 – 9›9
Chain10 – 332323Peroxidase C1C
PRO_0000023742

Sites

Active site511Proton acceptor By similarity
Metal binding521Calcium 1 By similarity
Metal binding551Calcium 1; via carbonyl oxygen By similarity
Metal binding571Calcium 1; via carbonyl oxygen By similarity
Metal binding591Calcium 1 By similarity
Metal binding611Calcium 1 By similarity
Metal binding1791Iron (heme axial ligand) By similarity
Metal binding1801Calcium 2 By similarity
Metal binding2311Calcium 2 By similarity
Metal binding2341Calcium 2 By similarity
Metal binding2391Calcium 2 By similarity
Binding site1481Substrate; via carbonyl oxygen By similarity
Site471Transition state stabilizer By similarity

Amino acid modifications

Modified residue101Pyrrolidone carboxylic acid By similarity
Glycosylation221N-linked (GlcNAc...) Potential
Glycosylation661N-linked (GlcNAc...) Potential
Glycosylation1951N-linked (GlcNAc...) Potential
Glycosylation2071N-linked (GlcNAc...) Potential
Glycosylation2231N-linked (GlcNAc...) Potential
Glycosylation2641N-linked (GlcNAc...) Potential
Disulfide bond20 ↔ 100 By similarity
Disulfide bond53 ↔ 58 By similarity
Disulfide bond106 ↔ 310 By similarity
Disulfide bond186 ↔ 218 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P15233 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 1938A450D595DFBE

FASTA33236,548
        10         20         30         40         50         60 
MLHASFSNAQ LTPTFYDNSC PNVSNIVRDI IINELRSDPS IAASILRLHF HDCFVNGCDA 

        70         80         90        100        110        120 
SILLDNTTSF RTEKDAFGNA NSARGFPVVD RIKAAVERAC PRTVSCADVL TIAAQQSVNL 

       130        140        150        160        170        180 
AGGPSWRVPL GRRDSRQAFL DLANANLPAP SFTLPELKAA FANVGLNRPS DLVALSGGHT 

       190        200        210        220        230        240 
FGKNQCRFIM DRLYNFSNTG LPDPTLNTTY LQTLRQQCPR NGNQSVLVDF DLRTPTVFDN 

       250        260        270        280        290        300 
KYYVNLKEQK GLIQSDQELF SSPNATDTIP LVRSYADGTQ TFFNAFVEAM NRMGNITPLT 

       310        320        330 
GTQGEIRLNC RVVNSNSLLH DIVEVVDFVS SM

« Hide

References

[1]"Structure of the horseradish peroxidase isozyme C genes."
Fujiyama K., Takemura H., Shibayama S., Kobayashi K., Choi J.K., Shinmyo A., Takano M., Yamada Y., Okada H.
Eur. J. Biochem. 173:681-687(1988) [PubMed: 3371352] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M60729 Genomic DNA. Translation: AAA33379.1.
PIRS00627.

3D structure databases

ProteinModelPortalP15233.
SMRP15233. Positions 10-316.
ModBaseSearch...

Protein family/group databases

PeroxiBase88. AruPrx01c.

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 namePER1C_ARMRU
AccessionPrimary (citable) accession number: P15233
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 28, 2011
This is version 82 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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