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Protein

Peroxidase 57

Gene

PER57

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.

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
Sitei60Transition state stabilizerPROSITE-ProRule annotation1
Active sitei64Proton acceptorPROSITE-ProRule annotation1
Metal bindingi65Calcium 1PROSITE-ProRule annotation1
Metal bindingi68Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi70Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi72Calcium 1PROSITE-ProRule annotation1
Metal bindingi74Calcium 1PROSITE-ProRule annotation1
Binding sitei155Substrate; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi185Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi186Calcium 2PROSITE-ProRule annotation1
Metal bindingi233Calcium 2PROSITE-ProRule annotation1
Metal bindingi236Calcium 2PROSITE-ProRule annotation1
Metal bindingi241Calcium 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

Protein family/group databases

PeroxiBasei223. AtPrx57.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase 57 (EC:1.11.1.7)
Short name:
Atperox P57
Alternative name(s):
ATP13a
PRXR10
Gene namesi
Name:PER57
Synonyms:P57
Ordered Locus Names:At5g17820
ORF Names:MVA3.170, MVA3.18
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G17820.

Subcellular locationi

  • Secreted PROSITE-ProRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000002372223 – 313Peroxidase 57Add BLAST291

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi33 ↔ 109PROSITE-ProRule annotation
Disulfide bondi66 ↔ 71PROSITE-ProRule annotation
Disulfide bondi115 ↔ 309PROSITE-ProRule annotation
Disulfide bondi192 ↔ 224PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ43729.
PRIDEiQ43729.

PTM databases

iPTMnetiQ43729.

Expressioni

Tissue specificityi

Mainly expressed in roots.1 Publication

Inductioni

Positively light-regulated during the firt stage of development. Up-regulated transiently by a cold treatment. Induced in shoots of plants subjected to a long Fe deficiency stress. Down-regulated by salicylic acid, a plant defense-related signaling molecule.4 Publications

Gene expression databases

ExpressionAtlasiQ43729. baseline and differential.
GenevisibleiQ43729. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT5G17820.1.

Structurei

3D structure databases

ProteinModelPortaliQ43729.
SMRiQ43729.
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

eggNOGiENOG410IEWY. Eukaryota.
ENOG4110UVG. LUCA.
HOGENOMiHOG000237556.
InParanoidiQ43729.
KOiK00430.
OMAiNTCRNSA.
OrthoDBiEOG09360MRF.
PhylomeDBiQ43729.

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.

Q43729-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMKGAKFSSL LVLFFIFPIA FAQLRVGFYS QSCPQAETIV RNLVRQRFGV
60 70 80 90 100
TPTVTAALLR MHFHDCFVKG CDASLLIDST NSEKTAGPNG SVREFDLIDR
110 120 130 140 150
IKAQLEAACP STVSCADIVT LATRDSVALA GGPSYSIPTG RRDGRVSNNL
160 170 180 190 200
DVTLPGPTIS VSGAVSLFTN KGMNTFDAVA LLGAHTVGQG NCGLFSDRIT
210 220 230 240 250
SFQGTGRPDP SMDPALVTSL RNTCRNSATA ALDQSSPLRF DNQFFKQIRK
260 270 280 290 300
RRGVLQVDQR LASDPQTRGI VARYANNNAF FKRQFVRAMV KMGAVDVLTG
310
RNGEIRRNCR RFN
Length:313
Mass (Da):34,098
Last modified:November 1, 1996 - v1
Checksum:iBFD2855EC45DFF26
GO

Sequence cautioni

The sequence AAM65434 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98322 mRNA. Translation: CAA66966.1.
X98776 mRNA. Translation: CAA67312.1.
AB006706 Genomic DNA. Translation: BAB09581.1.
CP002688 Genomic DNA. Translation: AED92474.1.
BT002958 mRNA. Translation: AAO22769.2.
AY087882 mRNA. Translation: AAM65434.1. Different initiation.
RefSeqiNP_197284.1. NM_121788.4.
UniGeneiAt.25535.

Genome annotation databases

EnsemblPlantsiAT5G17820.1; AT5G17820.1; AT5G17820.
GeneIDi831650.
GrameneiAT5G17820.1; AT5G17820.1; AT5G17820.
KEGGiath:AT5G17820.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98322 mRNA. Translation: CAA66966.1.
X98776 mRNA. Translation: CAA67312.1.
AB006706 Genomic DNA. Translation: BAB09581.1.
CP002688 Genomic DNA. Translation: AED92474.1.
BT002958 mRNA. Translation: AAO22769.2.
AY087882 mRNA. Translation: AAM65434.1. Different initiation.
RefSeqiNP_197284.1. NM_121788.4.
UniGeneiAt.25535.

3D structure databases

ProteinModelPortaliQ43729.
SMRiQ43729.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT5G17820.1.

Protein family/group databases

PeroxiBasei223. AtPrx57.

PTM databases

iPTMnetiQ43729.

Proteomic databases

PaxDbiQ43729.
PRIDEiQ43729.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G17820.1; AT5G17820.1; AT5G17820.
GeneIDi831650.
GrameneiAT5G17820.1; AT5G17820.1; AT5G17820.
KEGGiath:AT5G17820.

Organism-specific databases

TAIRiAT5G17820.

Phylogenomic databases

eggNOGiENOG410IEWY. Eukaryota.
ENOG4110UVG. LUCA.
HOGENOMiHOG000237556.
InParanoidiQ43729.
KOiK00430.
OMAiNTCRNSA.
OrthoDBiEOG09360MRF.
PhylomeDBiQ43729.

Miscellaneous databases

PROiQ43729.

Gene expression databases

ExpressionAtlasiQ43729. baseline and differential.
GenevisibleiQ43729. AT.

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 nameiPER57_ARATH
AccessioniPrimary (citable) accession number: Q43729
Secondary accession number(s): Q84WN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 135 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.