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Protein

Peroxidase N

Gene

HRPN

Organism
Armoracia rusticana (Horseradish) (Armoracia laphatifolia)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 2 calcium ions per subunit.
  • heme bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei66Transition state stabilizerPROSITE-ProRule annotation1
Active sitei70Proton acceptorPROSITE-ProRule annotation1
Metal bindingi71Calcium 1PROSITE-ProRule annotation1
Metal bindingi74Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi76Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi78Calcium 1PROSITE-ProRule annotation1
Metal bindingi80Calcium 1PROSITE-ProRule annotation1
Binding sitei163Substrate; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi193Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi194Calcium 2PROSITE-ProRule annotation1
Metal bindingi245Calcium 2PROSITE-ProRule annotation1
Metal bindingi248Calcium 2PROSITE-ProRule annotation1
Metal bindingi253Calcium 2PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Enzyme and pathway databases

SABIO-RKQ42517.

Protein family/group databases

PeroxiBasei87. AruPrx06.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase N (EC:1.11.1.7)
Alternative name(s):
Neutral peroxidase
Gene namesi
Name:HRPN
OrganismiArmoracia rusticana (Horseradish) (Armoracia laphatifolia)
Taxonomic identifieri3704 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCardamineaeArmoracia

Subcellular locationi

  • Secreted PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
ChainiPRO_000002374529 – 327Peroxidase NAdd BLAST299

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei29Pyrrolidone carboxylic acidBy similarity1
Disulfide bondi39 ↔ 116PROSITE-ProRule annotation
Disulfide bondi72 ↔ 77PROSITE-ProRule annotation
Disulfide bondi122 ↔ 323PROSITE-ProRule annotation
Glycosylationi155N-linked (GlcNAc...)Sequence analysis1
Glycosylationi182N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi200 ↔ 232PROSITE-ProRule annotation
Glycosylationi209N-linked (GlcNAc...)Sequence analysis1
Glycosylationi239N-linked (GlcNAc...)Sequence analysis1
Glycosylationi247N-linked (GlcNAc...)Sequence analysis1
Glycosylationi281N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PRIDEiQ42517.

Structurei

3D structure databases

ProteinModelPortaliQ42517.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

CDDicd00693. secretory_peroxidase. 1 hit.
InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
IPR033905. Secretory_peroxidase.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00458. PEROXIDASE.
PR00461. PLPEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q42517-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTQTKVMGG HVLLTVFTLC MLCSAVRAQL SPDIYAKSCP NLLQIVRDQV
60 70 80 90 100
KIALKAEIRM AASLIRLHFH DCFVNGCDAS VLLDGTNSEK LAIPNVNSVR
110 120 130 140 150
GFEVIDTIKA AVENACPGVV SCADILTLAA RDSVYLSGGP QWRVALGRKD
160 170 180 190 200
GLVANQSSAN NLPSPFEPLD AIIAKFAAVG LNVTDVVALS GAHTFGQAKC
210 220 230 240 250
DLFSNRLFNF TGAGTPDSTL ETTLLSDLQT VCPIGGNGNK TAPLDRNSTD
260 270 280 290 300
AFDNNYFKNL LEGKGLLSSD QILFSSDLAV NTTKRLVEAY SRSQYLFFRD
310 320
FTCSMIRMGS LVNGASGEVR TNCRVIN
Length:327
Mass (Da):35,126
Last modified:November 1, 1996 - v1
Checksum:i5C427EBDD0A2CCDF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57564 mRNA. Translation: CAA40796.1.
PIRiS14268.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57564 mRNA. Translation: CAA40796.1.
PIRiS14268.

3D structure databases

ProteinModelPortaliQ42517.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei87. AruPrx06.

Proteomic databases

PRIDEiQ42517.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ42517.

Miscellaneous databases

PROiQ42517.

Family and domain databases

CDDicd00693. secretory_peroxidase. 1 hit.
InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
IPR033905. Secretory_peroxidase.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00458. PEROXIDASE.
PR00461. PLPEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPERN_ARMRU
AccessioniPrimary (citable) accession number: Q42517
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.