Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P15233 (PER1C_ARMRU)

Last modified June 16, 2009. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

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 › eurosids II › Brassicales › Brassicaceae › Armoracia

Hide | Top

Protein attributes

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

Hide | Top

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

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 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.

Hide | Top

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

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P15233-1 [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

Hide | Top

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].

Hide | Top

Cross-references

Sequence databases

M60729 Genomic DNA. Translation: AAA33379.1.
PIRS00627.

3D structure databases

HSSPHSSP built from PDB template 2ATJ based on UniProtKB P00433.
SMRP15233. Positions 10-315.
ModBaseSearch...

Protein family/group databases

PeroxiBase88. AruPrx01c.

Enzyme and pathway databases

BRENDA1.11.1.7. 141069.

Family and domain databases

InterProIPR002016. 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.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

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 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Hide | Top

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents