Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P15232 (PER1B_ARMRU)

Last modified June 16, 2009. Version 71. 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 C1B
    EC=1.11.1.7
Gene names
Name: PRXC1B
Synonyms: HRPC2
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 length351 AA.
Sequence statusComplete.
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 peptide1 – 2828
Chain29 – 351323Peroxidase C1B
PRO_0000023741

Sites

Active site701Proton acceptor By similarity
Metal binding711Calcium 1 By similarity
Metal binding741Calcium 1; via carbonyl oxygen By similarity
Metal binding761Calcium 1; via carbonyl oxygen By similarity
Metal binding781Calcium 1 By similarity
Metal binding801Calcium 1 By similarity
Metal binding1981Iron (heme axial ligand) By similarity
Metal binding1991Calcium 2 By similarity
Metal binding2501Calcium 2 By similarity
Metal binding2531Calcium 2 By similarity
Metal binding2581Calcium 2 By similarity
Binding site1671Substrate; via carbonyl oxygen By similarity
Site661Transition state stabilizer By similarity

Amino acid modifications

Modified residue291Pyrrolidone carboxylic acid By similarity
Glycosylation411N-linked (GlcNAc...) Potential
Glycosylation851N-linked (GlcNAc...) Potential
Glycosylation2141N-linked (GlcNAc...) Potential
Glycosylation2261N-linked (GlcNAc...) Potential
Glycosylation2421N-linked (GlcNAc...) Potential
Glycosylation2831N-linked (GlcNAc...) Potential
Disulfide bond39 ↔ 119 By similarity
Disulfide bond72 ↔ 77 By similarity
Disulfide bond125 ↔ 329 By similarity
Disulfide bond205 ↔ 237 By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P15232-1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 7A8C606A3928950B

FASTA35138,646
        10         20         30         40         50         60 
MHSPSSTSFT WILITLGCLA FYASLSDAQL TPTFYDTSCP NVSNIVRDII INELRSDPRI 

        70         80         90        100        110        120 
TASILRLHFH DCFVNGCDAS ILLDNTTSFL TEKDALGNAN SARGFPTVDR IKAAVERACP 

       130        140        150        160        170        180 
RTVSCADVLT IAAQQSVNLA GGPSWRVPLG RRDSLQAFLD LANANLPAPF FTLPQLKDAF 

       190        200        210        220        230        240 
AKVGLDRPSD LVALSGGHTF GKNQCRFIMD RLYNFSNTGL PDPTLNTTYL QTLRQQCPLN 

       250        260        270        280        290        300 
GNQSVLVDFD LRTPTVFDNK YYVNLKEQKG LIQSDQELFS SPNATDTIPL VRSFADGTQK 

       310        320        330        340        350 
FFNAFVEAMN RMGNITPLTG TQGEIRLNCR VVNSNSLLHD IVEVVDFVSS M

« 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

M37157 Genomic DNA. Translation: AAA33378.1.
PIRS00626.

3D structure databases

HSSPHSSP built from PDB template 2ATJ based on UniProtKB P00433.
SMRP15232. Positions 29-334.
ModBaseSearch...

Protein family/group databases

PeroxiBase89. AruPrx01b.

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 namePER1B_ARMRU
AccessionPrimary (citable) accession number: P15232
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 16, 2009
This is version 71 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