Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Neutral peroxidase

Gene
N/A
Organism
Ipomoea batatas (Sweet potato) (Convolvulus batatas)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.
May contribute to protection against cold-induced oxidative stress.

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei96 – 961Transition state stabilizerPROSITE-ProRule annotation
Active sitei100 – 1001Proton acceptorPROSITE-ProRule annotation
Metal bindingi101 – 1011Calcium 1PROSITE-ProRule annotation
Metal bindingi104 – 1041Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi106 – 1061Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi108 – 1081Calcium 1PROSITE-ProRule annotation
Binding sitei198 – 1981Substrate; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi228 – 2281Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi229 – 2291Calcium 2PROSITE-ProRule annotation
Metal bindingi269 – 2691Calcium 2PROSITE-ProRule annotation
Metal bindingi271 – 2711Calcium 2PROSITE-ProRule annotation
Metal bindingi276 – 2761Calcium 2PROSITE-ProRule annotation

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

Protein family/group databases

PeroxiBasei65. IbPrx09.

Names & Taxonomyi

Protein namesi
Recommended name:
Neutral peroxidase (EC:1.11.1.7)
Alternative name(s):
SwPN1
OrganismiIpomoea batatas (Sweet potato) (Convolvulus batatas)
Taxonomic identifieri4120 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesConvolvulaceaeIpomoeeaeIpomoea

Subcellular locationi

  • Secreted PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – 67471 PublicationPRO_0000023751Add
BLAST
Chaini68 – 348281Neutral peroxidasePRO_0000023752Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi71 ↔ 149PROSITE-ProRule annotation
Disulfide bondi102 ↔ 107PROSITE-ProRule annotation
Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence analysis
Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence analysis
Disulfide bondi156 ↔ 344PROSITE-ProRule annotation
Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence analysis
Glycosylationi177 – 1771N-linked (GlcNAc...)Sequence analysis
Glycosylationi189 – 1891N-linked (GlcNAc...)Sequence analysis
Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence analysis
Disulfide bondi235 ↔ 256PROSITE-ProRule annotation
Glycosylationi247 – 2471N-linked (GlcNAc...)Sequence analysis
Glycosylationi261 – 2611N-linked (GlcNAc...)Sequence analysis
Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Highly expressed in suspension cultured cells. Weak expression also found in the stems of intact plants. No expression in leaf, tuberous root and non-tuberous root.

Developmental stagei

Very low expression level 0.5 days after subculture (DAS).

Inductioni

By wounding and cold stress. Induced by acclimation and repressed by chilling.

Structurei

3D structure databases

ProteinModelPortaliO04796.
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

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[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.

O04796-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASFVARLTL ALSFIALALA GYSLVQNTLS SPTHTRLNLI PTWLDSTFDS
60 70 80 90 100
ADVLSYLGFG KSSGRLSDSN CVFSAVKEIV DAAITAETRM GASLIRLHFH
110 120 130 140 150
DCFVDGCDGG ILLNDTANFT GEQGAPANSN SVRGFSVIDQ AKRNAQTKCA
160 170 180 190 200
DTPVSCADVL AIAARDAFRK FTNQTYNITL GRQDARTANL TGANTQLPAP
210 220 230 240 250
FDNLSIQTAK FADKGFNQRE MVVLAGAHTV GFSRCAVLCT STNLNQNRSA
260 270 280 290 300
TLQCTCPASA NDTGLVGLDP SPGTFDKKYF EELVKGQGLL FSDQELMQSN
310 320 330 340
ATVTAVRRYR DATGAFLTDF AAAMVKMSNL PPSAGVQLEI RNVCSRVN
Length:348
Mass (Da):37,186
Last modified:July 1, 1997 - v1
Checksum:i3FA8C361B72CD383
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z84473 mRNA. Translation: CAB06478.1.
PIRiT10946.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z84473 mRNA. Translation: CAB06478.1.
PIRiT10946.

3D structure databases

ProteinModelPortaliO04796.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei65. IbPrx09.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[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_IPOBA
AccessioniPrimary (citable) accession number: O04796
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 4, 2003
Last sequence update: July 1, 1997
Last modified: March 4, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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.