Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P00433 (PER1A_ARMRU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxidase C1A

EC=1.11.1.7
Gene names
Name:PRXC1A
Synonyms:HPRC1
OrganismArmoracia rusticana (Horseradish) (Armoracia laphatifolia)
Taxonomic identifier3704 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCardamineaeArmoracia

Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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 ineach 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.

Subunit structure

Monomer.

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
   Technical term3D-structure
Direct protein sequencing
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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

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 – 3030 Ref.2
Chain31 – 338308Peroxidase C1A Ref.2
PRO_0000023739
Propeptide339 – 35315
PRO_0000023740

Sites

Active site721Proton acceptor
Metal binding731Calcium 1
Metal binding761Calcium 1; via carbonyl oxygen
Metal binding781Calcium 1; via carbonyl oxygen
Metal binding801Calcium 1
Metal binding821Calcium 1
Metal binding941Calcium 1
Metal binding2001Iron (heme axial ligand)
Metal binding2011Calcium 2
Metal binding2521Calcium 2
Metal binding2551Calcium 2
Metal binding2601Calcium 2
Binding site1691Substrate; via carbonyl oxygen
Site681Transition state stabilizer

Amino acid modifications

Modified residue311Pyrrolidone carboxylic acid Ref.2
Glycosylation431N-linked (GlcNAc...) Ref.2
Glycosylation871N-linked (GlcNAc...) Ref.2
Glycosylation1881N-linked (GlcNAc...)
Glycosylation2161N-linked (GlcNAc...)
Glycosylation2281N-linked (GlcNAc...)
Glycosylation2441N-linked (GlcNAc...)
Glycosylation2851N-linked (GlcNAc...)
Glycosylation2981N-linked (GlcNAc...)
Disulfide bond41 ↔ 121 Ref.2
Disulfide bond74 ↔ 79 Ref.2
Disulfide bond127 ↔ 331
Disulfide bond207 ↔ 239

Secondary structure

..................................................... 353
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00433 [UniParc].

Last modified April 1, 1990. Version 2.
Checksum: AC916C03C4A24D27

FASTA35338,825
        10         20         30         40         50         60 
MHFSSSSTLF TCITLIPLVC LILHASLSDA QLTPTFYDNS CPNVSNIVRD TIVNELRSDP 

        70         80         90        100        110        120 
RIAASILRLH FHDCFVNGCD ASILLDNTTS FRTEKDAFGN ANSARGFPVI DRMKAAVESA 

       130        140        150        160        170        180 
CPRTVSCADL LTIAAQQSVT LAGGPSWRVP LGRRDSLQAF LDLANANLPA PFFTLPQLKD 

       190        200        210        220        230        240 
SFRNVGLNRS SDLVALSGGH TFGKNQCRFI MDRLYNFSNT GLPDPTLNTT YLQTLRGLCP 

       250        260        270        280        290        300 
LNGNLSALVD FDLRTPTIFD NKYYVNLEEQ KGLIQSDQEL FSSPNATDTI PLVRSFANST 

       310        320        330        340        350 
QTFFNAFVEA MDRMGNITPL TGTQGQIRLN CRVVNSNSLL HDMVEVVDFV SSM 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Covalent structure of the glycoprotein horseradish peroxidase (EC 1.11.1.7)."
Welinder K.G.
FEBS Lett. 72:19-23(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-338.
[3]"Crystal structure of horseradish peroxidase C at 2.15-A resolution."
Gajhede M., Schuller D.J., Henriksen A., Smith A.T., Poulos T.L.
Nat. Struct. Biol. 4:1032-1038(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
[4]"Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by X-ray crystallography."
Henriksen A., Schuller D.J., Meno K., Welinder K.G., Smith A.T., Gajhede M.
Biochemistry 37:8054-8060(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[5]Meno K., White C.G., Smith A.T., Gajhede M.
Submitted (DEC-1998) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M37156 Genomic DNA. Translation: AAA33377.1.
PIROPRHC. S00625.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ATJX-ray2.15A/B/C/D/E/F31-336[»]
1GW2X-ray2.15A31-338[»]
1GWOX-ray2.07A31-338[»]
1GWTX-ray1.70A31-338[»]
1GWUX-ray1.31A31-338[»]
1GX2X-ray2.20A/B31-338[»]
1H55X-ray1.61A31-338[»]
1H57X-ray1.60A31-338[»]
1H58X-ray1.70A31-338[»]
1H5AX-ray1.60A31-338[»]
1H5CX-ray1.62A31-338[»]
1H5DX-ray1.60A31-338[»]
1H5EX-ray1.60A31-338[»]
1H5FX-ray1.60A31-338[»]
1H5GX-ray1.57A31-338[»]
1H5HX-ray1.60A31-338[»]
1H5IX-ray1.60A31-338[»]
1H5JX-ray1.60A31-338[»]
1H5KX-ray1.60A31-338[»]
1H5LX-ray1.60A31-338[»]
1H5MX-ray1.57A31-338[»]
1HCHX-ray1.57A31-336[»]
1KZMX-ray2.00A31-338[»]
1W4WX-ray1.55A31-353[»]
1W4YX-ray1.60A31-353[»]
2ATJX-ray2.00A/B31-337[»]
2YLJX-ray1.69A31-336[»]
3ATJX-ray2.20A/B31-338[»]
4ATJX-ray2.50A/B31-338[»]
6ATJX-ray2.00A31-338[»]
7ATJX-ray1.47A31-338[»]
ProteinModelPortalP00433.
SMRP00433. Positions 31-337.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

PeroxiBase90. AruPrx01-1.

PTM databases

UniCarbKBP00433.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP00433.

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. SSF48113. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00433.

Entry information

Entry namePER1A_ARMRU
AccessionPrimary (citable) accession number: P00433
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1990
Last modified: February 19, 2014
This is version 112 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references