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Protein

Peroxidase 23

Gene

PER23

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 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:
  • 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 acceptorPROSITE-ProRule annotation
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:AT2G38390-MONOMER.

Protein family/group databases

PeroxiBasei116. AtPrx23.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase 23 (EC:1.11.1.7)
Short name:
Atperox P23
Alternative name(s):
ATP34
Gene namesi
Name:PER23
Synonyms:P23
Ordered Locus Names:At2g38390
ORF Names:T19C21.12
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G38390.

Subcellular locationi

  • Secreted Curated
  • Vacuole Curated

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence analysisAdd
BLAST
Chaini30 – 349320Peroxidase 23PRO_0000023689Add
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 ↔ 329PROSITE-ProRule annotation
Disulfide bondi206 ↔ 238PROSITE-ProRule annotation
Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence analysis
Glycosylationi243 – 2431N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiO80912.
PRIDEiO80912.

Expressioni

Inductioni

By methyl jasmonate, a plant defense-related signaling molecule.1 Publication

Gene expression databases

GenevisibleiO80912. AT.

Interactioni

Protein-protein interaction databases

IntActiO80912. 1 interaction.
STRINGi3702.AT2G38390.1.

Structurei

3D structure databases

ProteinModelPortaliO80912.
SMRiO80912. Positions 30-333.
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

eggNOGiENOG410JT8V. Eukaryota.
ENOG411082W. LUCA.
HOGENOMiHOG000237557.
InParanoidiO80912.
KOiK00430.
OMAiQYSSNTF.
PhylomeDBiO80912.

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.

O80912-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFSSSLSCS AMGALIVGCL LLQASNSNAQ LRPDFYFRTC PPIFNIIGDT
60 70 80 90 100
IVNELRTDPR IAASLLRLHF HDCFVRGCDA SILLDNSTSF RTEKDAAPNK
110 120 130 140 150
NSVRGFDVID RMKAAIERAC PRTVSCADII TIASQISVLL SGGPWWPVPL
160 170 180 190 200
GRRDSVEAFF ALANTALPSP FSTLTQLKTA FADVGLNRPS DLVALSGGHT
210 220 230 240 250
FGKAQCQFVT PRLYNFNGTN RPDPSLNPTY LVELRRLCPQ NGNGTVLVNF
260 270 280 290 300
DSVTPTTFDR QYYTNLLNGK GLIQSDQVLF STPGADTIPL VNQYSSNTFV
310 320 330 340
FFGAFVDAMI RMGNLKPLTG TQGEIRQNCR VVNPRIRVVE NDDGVVSSI
Length:349
Mass (Da):38,100
Last modified:November 1, 1998 - v1
Checksum:i74A1C6F71A415169
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF452385 mRNA. Translation: AAL40849.1.
AC004683 Genomic DNA. Translation: AAC28765.1.
CP002685 Genomic DNA. Translation: AEC09531.1.
AY099555 mRNA. Translation: AAM20407.1.
BT001238 mRNA. Translation: AAN65125.1.
PIRiT02506.
RefSeqiNP_181373.1. NM_129395.2.
UniGeneiAt.28466.

Genome annotation databases

EnsemblPlantsiAT2G38390.1; AT2G38390.1; AT2G38390.
GeneIDi818420.
GrameneiAT2G38390.1; AT2G38390.1; AT2G38390.
KEGGiath:AT2G38390.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF452385 mRNA. Translation: AAL40849.1.
AC004683 Genomic DNA. Translation: AAC28765.1.
CP002685 Genomic DNA. Translation: AEC09531.1.
AY099555 mRNA. Translation: AAM20407.1.
BT001238 mRNA. Translation: AAN65125.1.
PIRiT02506.
RefSeqiNP_181373.1. NM_129395.2.
UniGeneiAt.28466.

3D structure databases

ProteinModelPortaliO80912.
SMRiO80912. Positions 30-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO80912. 1 interaction.
STRINGi3702.AT2G38390.1.

Protein family/group databases

PeroxiBasei116. AtPrx23.

Proteomic databases

PaxDbiO80912.
PRIDEiO80912.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G38390.1; AT2G38390.1; AT2G38390.
GeneIDi818420.
GrameneiAT2G38390.1; AT2G38390.1; AT2G38390.
KEGGiath:AT2G38390.

Organism-specific databases

TAIRiAT2G38390.

Phylogenomic databases

eggNOGiENOG410JT8V. Eukaryota.
ENOG411082W. LUCA.
HOGENOMiHOG000237557.
InParanoidiO80912.
KOiK00430.
OMAiQYSSNTF.
PhylomeDBiO80912.

Enzyme and pathway databases

BioCyciARA:AT2G38390-MONOMER.

Miscellaneous databases

PROiO80912.

Gene expression databases

GenevisibleiO80912. AT.

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. "Structural diversity and transcription of class III peroxidases from Arabidopsis thaliana."
    Welinder K.G., Justesen A.F., Kjaersgaard I.V.H., Jensen R.B., Rasmussen S.K., Jespersen H.M., Duroux L.
    Eur. J. Biochem. 269:6063-6081(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
    Tissue: Root.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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.
  5. "Coordinated plant defense responses in Arabidopsis revealed by microarray analysis."
    Schenk P.M., Kazan K., Wilson I., Anderson J.P., Richmond T., Somerville S.C., Manners J.M.
    Proc. Natl. Acad. Sci. U.S.A. 97:11655-11660(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: cv. Columbia.
  6. "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 nameiPER23_ARATH
AccessioniPrimary (citable) accession number: O80912
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: November 1, 1998
Last modified: February 17, 2016
This is version 123 of the entry and version 1 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.