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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)LengthDescriptionGraphical viewFeature identifierActions
Sitei67 – 671Transition state stabilizerPROSITE-ProRule annotation
Active sitei71 – 711Proton acceptor
Metal bindingi72 – 721Calcium 1PROSITE-ProRule annotation
Metal bindingi75 – 751Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi77 – 771Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi79 – 791Calcium 1PROSITE-ProRule annotation
Metal bindingi81 – 811Calcium 1PROSITE-ProRule annotation
Binding sitei168 – 1681Substrate; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi199 – 1991Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi200 – 2001Calcium 2PROSITE-ProRule annotation
Metal bindingi251 – 2511Calcium 2PROSITE-ProRule annotation
Metal bindingi254 – 2541Calcium 2PROSITE-ProRule annotation
Metal bindingi259 – 2591Calcium 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

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence analysisAdd
BLAST
Chaini30 – 352323Peroxidase 32PRO_0000023698Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301Pyrrolidone carboxylic acidPROSITE-ProRule annotationBy similarity
Disulfide bondi40 ↔ 120PROSITE-ProRule annotation
Disulfide bondi73 ↔ 78PROSITE-ProRule annotation
Glycosylationi86 – 861N-linked (GlcNAc...)Sequence analysis
Disulfide bondi126 ↔ 330PROSITE-ProRule annotation
Disulfide bondi206 ↔ 238PROSITE-ProRule annotation
Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence analysis
Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence analysis
Glycosylationi243 – 2431N-linked (GlcNAc...)Sequence analysis
Glycosylationi284 – 2841N-linked (GlcNAc...)Sequence analysis

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 interaction.
IntActiQ9LHB9. 1 interaction.
STRINGi3702.AT3G32980.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LHB9.
SMRiQ9LHB9. Positions 30-335.
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.
OMAiQGQIRQN.
PhylomeDBiQ9LHB9.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241S → L (Ref. 1) Curated
Sequence conflicti24 – 241S → L (Ref. 2) Curated
Sequence conflicti24 – 241S → L (Ref. 3) Curated
Sequence conflicti24 – 241S → L (Ref. 7) Curated
Sequence conflicti145 – 1451S → Y in AAM64838 (Ref. 7) Curated

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_180321.3.
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_180321.3.
UniGeneiAt.47588.
At.67710.
At.71576.

3D structure databases

ProteinModelPortaliQ9LHB9.
SMRiQ9LHB9. Positions 30-335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi8393. 1 interaction.
IntActiQ9LHB9. 1 interaction.
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.
OMAiQGQIRQN.
PhylomeDBiQ9LHB9.

Enzyme and pathway databases

BioCyciARA:AT3G32980-MONOMER.

Miscellaneous databases

PROiQ9LHB9.

Gene expression databases

ExpressionAtlasiQ9LHB9. baseline and differential.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Eleven cDNA clones from Arabidopsis thaliana encoding isoperoxidases."
    Capelli N., Tognolli M., Flach J., Overney S., Penel C., Greppin H., Simon P.
    Plant Gene Register PGR96-066
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "From expressed sequence tags to structure, function, evolution and expression of 28 ER-targeted Arabidopsis peroxidases."
    Welinder K.G., Jespersen H.M., Kjaersgaard I.V.H., Justesen A.F., Oestergaard L., Abelskov A.K., Jensen R.B., Hansen L.N., Rasmussen S.K.
    Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  3. "Structure of the gene encoding Arabidopsis thaliana PRXR3 peroxidase."
    Tognolli M., Greppin H., Simon P.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Columbia.
  4. "Structural analysis of Arabidopsis thaliana chromosome 3. III."
    Nakamura Y.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  7. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. "Computational analyses and annotations of the Arabidopsis peroxidase gene family."
    Oestergaard L., Pedersen A.G., Jespersen H.M., Brunak S., Welinder K.G.
    FEBS Lett. 433:98-102(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: cv. Columbia.
  9. "Identification and characterization of Ca(2+)-pectate binding peroxidases in Arabidopsis thaliana."
    Dunand C., Tognolli M., Overney S., von Tobel L., de Meyer M., Simon P., Penel C.
    J. Plant Physiol. 159:1165-1171(2002)
    Cited for: CHARACTERIZATION.
    Strain: cv. Columbia.
  10. "Towards Arabidopsis genome analysis: monitoring expression profiles of 1400 genes using cDNA microarrays."
    Ruan Y., Gilmore J., Conner T.
    Plant J. 15:821-833(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
    Strain: cv. Columbia.
  11. "Toward elucidating the global gene expression patterns of developing Arabidopsis: parallel analysis of 8300 genes by a high-density oligonucleotide probe array."
    Zhu T., Budworth P., Han B., Brown D., Chang H.-S., Zou G., Wang X.
    Plant Physiol. Biochem. 39:221-242(2001)
    Cited for: TISSUE SPECIFICITY.
    Strain: cv. Columbia.
  12. "Monitoring the switch from housekeeping to pathogen defense metabolism in Arabidopsis thaliana using cDNA arrays."
    Scheideler M., Schlaich N.L., Fellenberg K., Beissbarth T., Hauser N.C., Vingron M., Slusarenko A.J., Hoheisel J.D.
    J. Biol. Chem. 277:10555-10561(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: cv. Columbia.
  13. "Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana."
    Tognolli M., Penel C., Greppin H., Simon P.
    Gene 288:129-138(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE.
    Strain: cv. Columbia.

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: February 17, 2016
This is version 124 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.