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Protein

Peroxidase 65

Gene

PER65

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 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
Sitei69 – 691Transition state stabilizerPROSITE-ProRule annotation
Active sitei73 – 731Proton acceptorPROSITE-ProRule annotation
Metal bindingi74 – 741Calcium 1PROSITE-ProRule annotation
Metal bindingi79 – 791Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi81 – 811Calcium 1PROSITE-ProRule annotation
Metal bindingi83 – 831Calcium 1PROSITE-ProRule annotation
Binding sitei171 – 1711Substrate; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi201 – 2011Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi202 – 2021Calcium 2PROSITE-ProRule annotation
Metal bindingi250 – 2501Calcium 2PROSITE-ProRule annotation
Metal bindingi253 – 2531Calcium 2PROSITE-ProRule annotation
Metal bindingi258 – 2581Calcium 2PROSITE-ProRule annotation

GO - Molecular functioni

  • heme binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW
  • peroxidase activity Source: UniProtKB-KW
  • xylan 1,4-beta-xylosidase activity Source: TAIR

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:AT5G47000-MONOMER.

Protein family/group databases

PeroxiBasei231. AtPrx65.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase 65 (EC:1.11.1.7)
Short name:
Atperox P65
Alternative name(s):
ATP43
Gene namesi
Name:PER65
Synonyms:P65
Ordered Locus Names:At5g47000
ORF Names:MQD22.14
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G47000.

Subcellular locationi

  • Secreted PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Chaini29 – 334306Peroxidase 65PRO_0000023730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 123PROSITE-ProRule annotation
Disulfide bondi75 ↔ 80PROSITE-ProRule annotation
Disulfide bondi129 ↔ 326PROSITE-ProRule annotation
Glycosylationi174 – 1741N-linked (GlcNAc...)Sequence analysis
Disulfide bondi208 ↔ 236PROSITE-ProRule annotation
Glycosylationi238 – 2381N-linked (GlcNAc...)Sequence analysis
Glycosylationi282 – 2821N-linked (GlcNAc...)Sequence analysis
Glycosylationi294 – 2941N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9FJR1.
PRIDEiQ9FJR1.

Expressioni

Gene expression databases

GenevisibleiQ9FJR1. AT.

Interactioni

Protein-protein interaction databases

BioGridi19994. 1 interaction.
STRINGi3702.AT5G47000.1.

Structurei

3D structure databases

ProteinModelPortaliQ9FJR1.
SMRiQ9FJR1. Positions 33-330.
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

eggNOGiENOG410IH5P. Eukaryota.
ENOG410YA7M. LUCA.
HOGENOMiHOG000237556.
InParanoidiQ9FJR1.
KOiK00430.
OMAiVVQSKQM.
PhylomeDBiQ9FJR1.

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.

Q9FJR1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNMQFSRGF NPFVILFCLA VVAPIISADV AILRTDYYQK TCPDFHKIVR
60 70 80 90 100
EAVTTKQVQQ PTTAAGTLRL FFHDCFLEGC DASVLIATNS FNKAERDDDL
110 120 130 140 150
NDSLPGDAFD IVTRIKTALE LSCPGVVSCA DILAQATRDL VTMVGGPYFD
160 170 180 190 200
VKLGRKDGFE SKAHKVRGNV PMANQTVPDI HGIFKKNGFS LREMVALSGA
210 220 230 240 250
HTIGFSHCKE FSDRLYGSRA DKEINPRFAA ALKDLCKNHT VDDTIAAFND
260 270 280 290 300
VMTPGKFDNM YFKNLKRGLG LLASDHILIK DNSTKPFVDL YATNETAFFE
310 320 330
DFARAMEKLG TVGVKGDKDG EVRRRCDHFN NLNV
Length:334
Mass (Da):37,014
Last modified:December 6, 2002 - v2
Checksum:iDC07C78864450E44
GO

Sequence cautioni

The sequence BAB10239.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161L → F in AAM65654 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013394 Genomic DNA. Translation: BAB10239.1. Different initiation.
CP002688 Genomic DNA. Translation: AED95456.1.
AY093131 mRNA. Translation: AAM13130.1.
BT008821 mRNA. Translation: AAP68260.1.
AY088108 mRNA. Translation: AAM65654.1.
RefSeqiNP_568674.1. NM_124071.2.
UniGeneiAt.29916.
At.74143.

Genome annotation databases

EnsemblPlantsiAT5G47000.1; AT5G47000.1; AT5G47000.
GeneIDi834746.
GrameneiAT5G47000.1; AT5G47000.1; AT5G47000.
KEGGiath:AT5G47000.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013394 Genomic DNA. Translation: BAB10239.1. Different initiation.
CP002688 Genomic DNA. Translation: AED95456.1.
AY093131 mRNA. Translation: AAM13130.1.
BT008821 mRNA. Translation: AAP68260.1.
AY088108 mRNA. Translation: AAM65654.1.
RefSeqiNP_568674.1. NM_124071.2.
UniGeneiAt.29916.
At.74143.

3D structure databases

ProteinModelPortaliQ9FJR1.
SMRiQ9FJR1. Positions 33-330.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi19994. 1 interaction.
STRINGi3702.AT5G47000.1.

Protein family/group databases

PeroxiBasei231. AtPrx65.

Proteomic databases

PaxDbiQ9FJR1.
PRIDEiQ9FJR1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G47000.1; AT5G47000.1; AT5G47000.
GeneIDi834746.
GrameneiAT5G47000.1; AT5G47000.1; AT5G47000.
KEGGiath:AT5G47000.

Organism-specific databases

TAIRiAT5G47000.

Phylogenomic databases

eggNOGiENOG410IH5P. Eukaryota.
ENOG410YA7M. LUCA.
HOGENOMiHOG000237556.
InParanoidiQ9FJR1.
KOiK00430.
OMAiVVQSKQM.
PhylomeDBiQ9FJR1.

Enzyme and pathway databases

BioCyciARA:AT5G47000-MONOMER.

Miscellaneous databases

PROiQ9FJR1.

Gene expression databases

GenevisibleiQ9FJR1. 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 analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones."
    Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S.
    DNA Res. 5:203-216(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "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.
  4. "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].
  5. "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 nameiPER65_ARATH
AccessioniPrimary (citable) accession number: Q9FJR1
Secondary accession number(s): Q8RWF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: December 6, 2002
Last modified: February 17, 2016
This is version 118 of the entry and version 2 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.