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Protein

Peroxidase 69

Gene

PER69

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei73 – 731Transition state stabilizerPROSITE-ProRule annotation
Active sitei77 – 771Proton acceptorPROSITE-ProRule annotation
Metal bindingi78 – 781Calcium 1PROSITE-ProRule annotation
Metal bindingi81 – 811Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi83 – 831Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi85 – 851Calcium 1PROSITE-ProRule annotation
Metal bindingi87 – 871Calcium 1PROSITE-ProRule annotation
Binding sitei168 – 1681Substrate; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi198 – 1981Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi199 – 1991Calcium 2PROSITE-ProRule annotation
Metal bindingi248 – 2481Calcium 2PROSITE-ProRule annotation
Metal bindingi251 – 2511Calcium 2PROSITE-ProRule annotation
Metal bindingi256 – 2561Calcium 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:AT5G64100-MONOMER.

Protein family/group databases

PeroxiBasei235. AtPrx69.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase 69 (EC:1.11.1.7)
Short name:
Atperox P69
Alternative name(s):
ATP3a
Gene namesi
Name:PER69
Synonyms:P69
Ordered Locus Names:At5g64100
ORF Names:MHJ24.8
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G64100.

Subcellular locationi

  • Secreted PROSITE-ProRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 331308Peroxidase 69PRO_0000023734Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 122PROSITE-ProRule annotation
Disulfide bondi79 ↔ 84PROSITE-ProRule annotation
Glycosylationi93 – 931N-linked (GlcNAc...)Sequence analysis
Disulfide bondi128 ↔ 327PROSITE-ProRule annotation
Disulfide bondi205 ↔ 237PROSITE-ProRule annotation
Glycosylationi216 – 2161N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ96511.
PRIDEiQ96511.

PTM databases

iPTMnetiQ96511.

Expressioni

Tissue specificityi

Mainly expressed in roots and slightly in leaves.2 Publications

Gene expression databases

GenevisibleiQ96511. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT5G64100.1.

Structurei

3D structure databases

ProteinModelPortaliQ96511.
SMRiQ96511. Positions 38-331.
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

eggNOGiENOG410JX47. Eukaryota.
ENOG41104B9. LUCA.
HOGENOMiHOG000237556.
InParanoidiQ96511.
KOiK00430.
OMAiTAQGNRG.
PhylomeDBiQ96511.

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.

Q96511-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRGYNLLFV LVTFLVLVAA VTAQGNRGSN SGGGRRPHVG FYGNRCRNVE
60 70 80 90 100
SIVRSVVQSH VRSIPANAPG ILRMHFHDCF VHGCDGSVLL AGNTSERTAV
110 120 130 140 150
PNRSLRGFEV IEEAKARLEK ACPRTVSCAD ILTLAARDAV VLTGGQRWEV
160 170 180 190 200
PLGRLDGRIS QASDVNLPGP SDSVAKQKQD FAAKTLNTLD LVTLVGGHTI
210 220 230 240 250
GTAGCGLVRG RFVNFNGTGQ PDPSIDPSFV PLILAQCPQN GGTRVELDEG
260 270 280 290 300
SVDKFDTSFL RKVTSSRVVL QSDLVLWKDP ETRAIIERLL GLRRPSLRFG
310 320 330
TEFGKSMVKM SLIEVKTGSD GEIRRVCSAI N
Length:331
Mass (Da):35,679
Last modified:February 1, 1997 - v1
Checksum:i4906CDF9648BD060
GO

Sequence cautioni

The sequence AAM13011.1 differs from that shown. Reason: Erroneous termination at position 169. Translated as Gly.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98808 mRNA. Translation: CAA67340.1.
AB008266 Genomic DNA. Translation: BAB10278.1.
CP002688 Genomic DNA. Translation: AED97840.1.
AY093012 mRNA. Translation: AAM13011.1. Sequence problems.
RefSeqiNP_201215.1. NM_125806.2.
UniGeneiAt.25608.

Genome annotation databases

EnsemblPlantsiAT5G64100.1; AT5G64100.1; AT5G64100.
GeneIDi836531.
GrameneiAT5G64100.1; AT5G64100.1; AT5G64100.
KEGGiath:AT5G64100.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98808 mRNA. Translation: CAA67340.1.
AB008266 Genomic DNA. Translation: BAB10278.1.
CP002688 Genomic DNA. Translation: AED97840.1.
AY093012 mRNA. Translation: AAM13011.1. Sequence problems.
RefSeqiNP_201215.1. NM_125806.2.
UniGeneiAt.25608.

3D structure databases

ProteinModelPortaliQ96511.
SMRiQ96511. Positions 38-331.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT5G64100.1.

Protein family/group databases

PeroxiBasei235. AtPrx69.

PTM databases

iPTMnetiQ96511.

Proteomic databases

PaxDbiQ96511.
PRIDEiQ96511.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G64100.1; AT5G64100.1; AT5G64100.
GeneIDi836531.
GrameneiAT5G64100.1; AT5G64100.1; AT5G64100.
KEGGiath:AT5G64100.

Organism-specific databases

TAIRiAT5G64100.

Phylogenomic databases

eggNOGiENOG410JX47. Eukaryota.
ENOG41104B9. LUCA.
HOGENOMiHOG000237556.
InParanoidiQ96511.
KOiK00430.
OMAiTAQGNRG.
PhylomeDBiQ96511.

Enzyme and pathway databases

BioCyciARA:AT5G64100-MONOMER.

Miscellaneous databases

PROiQ96511.

Gene expression databases

GenevisibleiQ96511. 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. "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., Hansen L.N., Rasmussen S.K.
    Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones."
    Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S.
    DNA Res. 4:401-414(1997) [PubMed] [Europe PMC] [Abstract]
    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. "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.
  6. "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.
  7. "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.
  8. "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 nameiPER69_ARATH
AccessioniPrimary (citable) accession number: Q96511
Secondary accession number(s): Q8RWL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: February 1, 1997
Last modified: July 6, 2016
This is version 127 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.