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Protein

Peroxidase 32

Gene

PER32

Organism
Arabidopsis thaliana (Mouse-ear cress)
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.
Exhibits a Ca2+-pectate binding affinity which could be interpreted in vivo as a specificity to interact with the pectic structure of the cell wall.

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei67Transition state stabilizerPROSITE-ProRule annotation1
Active sitei71Proton acceptor1
Metal bindingi72Calcium 1PROSITE-ProRule annotation1
Metal bindingi75Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi77Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi79Calcium 1PROSITE-ProRule annotation1
Metal bindingi81Calcium 1PROSITE-ProRule annotation1
Binding sitei168Substrate; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi199Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi200Calcium 2PROSITE-ProRule annotation1
Metal bindingi251Calcium 2PROSITE-ProRule annotation1
Metal bindingi254Calcium 2PROSITE-ProRule annotation1
Metal bindingi259Calcium 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

BioCyciARA:AT3G32980-MONOMER.

Protein family/group databases

PeroxiBasei198. AtPrx32.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase 32 (EC:1.11.1.7)
Short name:
Atperox P32
Alternative name(s):
ATP16a
PRXR3
Gene namesi
Name:PER32
Synonyms:P32
Ordered Locus Names:At3g32980
ORF Names:T15D2.7, T15D2.9
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G32980.

Subcellular locationi

  • Secreted Curated
  • Vacuole Curated

  • Note: Carboxy-terminal extension appears to target the protein to vacuoles.

GO - Cellular componenti

  • cell wall Source: TAIR
  • extracellular region Source: UniProtKB-SubCell
  • membrane Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Secreted, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Sequence analysisAdd BLAST29
ChainiPRO_000002369830 – 352Peroxidase 32Add BLAST323

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei30Pyrrolidone carboxylic acidPROSITE-ProRule annotationBy similarity1
Disulfide bondi40 ↔ 120PROSITE-ProRule annotation
Disulfide bondi73 ↔ 78PROSITE-ProRule annotation
Glycosylationi86N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi126 ↔ 330PROSITE-ProRule annotation
Disulfide bondi206 ↔ 238PROSITE-ProRule annotation
Glycosylationi215N-linked (GlcNAc...)Sequence analysis1
Glycosylationi227N-linked (GlcNAc...)Sequence analysis1
Glycosylationi243N-linked (GlcNAc...)Sequence analysis1
Glycosylationi284N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiQ9LHB9.
PRIDEiQ9LHB9.

Expressioni

Tissue specificityi

Strongly expressed in roots.2 Publications

Inductioni

Late induced by infection with an incompatible bacterial plant pathogen.1 Publication

Gene expression databases

ExpressionAtlasiQ9LHB9. baseline and differential.

Interactioni

Protein-protein interaction databases

BioGridi8393. 1 interactor.
IntActiQ9LHB9. 1 interactor.
STRINGi3702.AT3G32980.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LHB9.
SMRiQ9LHB9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410JAWC. Eukaryota.
ENOG41119N5. LUCA.
HOGENOMiHOG000237557.
InParanoidiQ9LHB9.
KOiK00430.
OMAiGTQKFFN.
OrthoDBiEOG09360FST.
PhylomeDBiQ9LHB9.

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.

Q9LHB9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNFSYSSLST WTTLMTLGCL LLHSSISSAQ LTPTFYDNTC PSVFTIVRDT
60 70 80 90 100
IVNELRSDPR IAASILRLHF HDCFVNGCDA SILLDNTTSF RTEKDAAPNA
110 120 130 140 150
NSARGFPVID RMKAAVETAC PRTVSCADIL TIAAQQAVNL AGGPSWRVPL
160 170 180 190 200
GRRDSLQAFF ALANTNLPAP FFTLPQLKAS FQNVGLDRPS DLVALSGGHT
210 220 230 240 250
FGKNQCQFIM DRLYNFSNTG LPDPTLNTTY LQTLRGQCPR NGNQTVLVDF
260 270 280 290 300
DLRTPTVFDN KYYVNLKELK GLIQTDQELF SSPNATDTIP LVREYADGTQ
310 320 330 340 350
KFFNAFVEAM NRMGNITPLT GTQGQIRQNC RVVNSNSLLH DVVEIVDFVS

SM
Length:352
Mass (Da):38,847
Last modified:February 5, 2008 - v3
Checksum:i765696B3869BA1DB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti24S → L (Ref. 1) Curated1
Sequence conflicti24S → L (Ref. 2) Curated1
Sequence conflicti24S → L (Ref. 3) Curated1
Sequence conflicti24S → L (Ref. 7) Curated1
Sequence conflicti145S → Y in AAM64838 (Ref. 7) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98315 mRNA. Translation: CAA66959.1.
X98777 mRNA. Translation: CAA67313.1.
AJ133036 Genomic DNA. Translation: CAB37193.1.
AP002054 Genomic DNA. Translation: BAB02631.1.
CP002686 Genomic DNA. Translation: AEE77707.1.
AY080608 mRNA. Translation: AAL86292.1.
AY133730 mRNA. Translation: AAM91664.1.
AY087285 mRNA. Translation: AAM64838.1.
RefSeqiNP_850652.1. NM_180321.4.
UniGeneiAt.47588.
At.67710.
At.71576.

Genome annotation databases

EnsemblPlantsiAT3G32980.1; AT3G32980.1; AT3G32980.
GeneIDi823067.
GrameneiAT3G32980.1; AT3G32980.1; AT3G32980.
KEGGiath:AT3G32980.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98315 mRNA. Translation: CAA66959.1.
X98777 mRNA. Translation: CAA67313.1.
AJ133036 Genomic DNA. Translation: CAB37193.1.
AP002054 Genomic DNA. Translation: BAB02631.1.
CP002686 Genomic DNA. Translation: AEE77707.1.
AY080608 mRNA. Translation: AAL86292.1.
AY133730 mRNA. Translation: AAM91664.1.
AY087285 mRNA. Translation: AAM64838.1.
RefSeqiNP_850652.1. NM_180321.4.
UniGeneiAt.47588.
At.67710.
At.71576.

3D structure databases

ProteinModelPortaliQ9LHB9.
SMRiQ9LHB9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi8393. 1 interactor.
IntActiQ9LHB9. 1 interactor.
STRINGi3702.AT3G32980.1.

Protein family/group databases

PeroxiBasei198. AtPrx32.

Proteomic databases

PaxDbiQ9LHB9.
PRIDEiQ9LHB9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G32980.1; AT3G32980.1; AT3G32980.
GeneIDi823067.
GrameneiAT3G32980.1; AT3G32980.1; AT3G32980.
KEGGiath:AT3G32980.

Organism-specific databases

TAIRiAT3G32980.

Phylogenomic databases

eggNOGiENOG410JAWC. Eukaryota.
ENOG41119N5. LUCA.
HOGENOMiHOG000237557.
InParanoidiQ9LHB9.
KOiK00430.
OMAiGTQKFFN.
OrthoDBiEOG09360FST.
PhylomeDBiQ9LHB9.

Enzyme and pathway databases

BioCyciARA:AT3G32980-MONOMER.

Miscellaneous databases

PROiQ9LHB9.

Gene expression databases

ExpressionAtlasiQ9LHB9. baseline and differential.

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 nameiPER32_ARATH
AccessioniPrimary (citable) accession number: Q9LHB9
Secondary accession number(s): Q43732, Q6K1J2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: February 5, 2008
Last modified: November 30, 2016
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

There are 73 peroxidase genes in A.thaliana.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.