Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peroxidase 64

Gene

PER64

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
Sitei59 – 591Transition state stabilizerPROSITE-ProRule annotation
Active sitei63 – 631Proton acceptorPROSITE-ProRule annotation
Metal bindingi64 – 641Calcium 1PROSITE-ProRule annotation
Metal bindingi67 – 671Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi69 – 691Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi71 – 711Calcium 1PROSITE-ProRule annotation
Metal bindingi73 – 731Calcium 1PROSITE-ProRule annotation
Binding sitei158 – 1581Substrate; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi188 – 1881Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi189 – 1891Calcium 2PROSITE-ProRule annotation
Metal bindingi241 – 2411Calcium 2PROSITE-ProRule annotation
Metal bindingi243 – 2431Calcium 2PROSITE-ProRule annotation
Metal bindingi248 – 2481Calcium 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:AT5G42180-MONOMER.

Protein family/group databases

PeroxiBasei230. AtPrx64.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase 64 (EC:1.11.1.7)
Short name:
Atperox P64
Alternative name(s):
ATP17a
PRXR4
Gene namesi
Name:PER64
Synonyms:P64
Ordered Locus Names:At5g42180
ORF Names:MJC20.29
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G42180.

Subcellular locationi

  • Secreted PROSITE-ProRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 317295Peroxidase 64PRO_0000023729Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 ↔ 111PROSITE-ProRule annotation
Disulfide bondi65 ↔ 70PROSITE-ProRule annotation
Disulfide bondi117 ↔ 313PROSITE-ProRule annotation
Glycosylationi163 – 1631N-linked (GlcNAc...)Sequence analysis
Disulfide bondi195 ↔ 227PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ43872.
PRIDEiQ43872.

PTM databases

iPTMnetiQ43872.

Expressioni

Tissue specificityi

Expressed in the whole plant, but preferentially in roots.

Inductioni

Pathogen and elicitor-induced. Up-regulated transiently by a cold treatment.2 Publications

Gene expression databases

GenevisibleiQ43872. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT5G42180.1.

Structurei

3D structure databases

ProteinModelPortaliQ43872.
SMRiQ43872. Positions 23-316.
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

eggNOGiENOG410IHQ5. Eukaryota.
ENOG410YE7F. LUCA.
HOGENOMiHOG000237556.
InParanoidiQ43872.
KOiK00430.
OMAiDEVRANC.
PhylomeDBiQ43872.

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
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.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q43872-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAHMLNLLV IVIFVVSFDV QALSPHYYDH TCPQADHIVT NAVKKAMSND
60 70 80 90 100
QTVPAALLRM HFHDCFVRGC DGSVLLDSKG KNKAEKDGPP NISLHAFYVI
110 120 130 140 150
DNAKKALEEQ CPGIVSCADI LSLAARDAVA LSGGPTWAVP KGRKDGRISK
160 170 180 190 200
AIETRQLPAP TFNISQLRQN FGQRGLSMHD LVALSGGHTL GFAHCSSFQN
210 220 230 240 250
RLHKFNTQKE VDPTLNPSFA ARLEGVCPAH NTVKNAGSNM DGTVTSFDNI
260 270 280 290 300
YYKMLIQGKS LFSSDESLLA VPSTKKLVAK YANSNEEFER AFVKSMIKMS
310
SISGNGNEVR LNCRRVR
Length:317
Mass (Da):34,706
Last modified:November 1, 1996 - v1
Checksum:i79536112BA918690
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98316 mRNA. Translation: CAA66960.1.
X99096 mRNA. Translation: CAA67550.1.
AB017067 Genomic DNA. Translation: BAB08451.1.
CP002688 Genomic DNA. Translation: AED94776.1.
AY063962 mRNA. Translation: AAL36318.1.
AY096403 mRNA. Translation: AAM20043.1.
RefSeqiNP_199033.1. NM_123583.3.
UniGeneiAt.23304.

Genome annotation databases

EnsemblPlantsiAT5G42180.1; AT5G42180.1; AT5G42180.
GeneIDi834223.
GrameneiAT5G42180.1; AT5G42180.1; AT5G42180.
KEGGiath:AT5G42180.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98316 mRNA. Translation: CAA66960.1.
X99096 mRNA. Translation: CAA67550.1.
AB017067 Genomic DNA. Translation: BAB08451.1.
CP002688 Genomic DNA. Translation: AED94776.1.
AY063962 mRNA. Translation: AAL36318.1.
AY096403 mRNA. Translation: AAM20043.1.
RefSeqiNP_199033.1. NM_123583.3.
UniGeneiAt.23304.

3D structure databases

ProteinModelPortaliQ43872.
SMRiQ43872. Positions 23-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT5G42180.1.

Protein family/group databases

PeroxiBasei230. AtPrx64.

PTM databases

iPTMnetiQ43872.

Proteomic databases

PaxDbiQ43872.
PRIDEiQ43872.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G42180.1; AT5G42180.1; AT5G42180.
GeneIDi834223.
GrameneiAT5G42180.1; AT5G42180.1; AT5G42180.
KEGGiath:AT5G42180.

Organism-specific databases

TAIRiAT5G42180.

Phylogenomic databases

eggNOGiENOG410IHQ5. Eukaryota.
ENOG410YE7F. LUCA.
HOGENOMiHOG000237556.
InParanoidiQ43872.
KOiK00430.
OMAiDEVRANC.
PhylomeDBiQ43872.

Enzyme and pathway databases

BioCyciARA:AT5G42180-MONOMER.

Miscellaneous databases

PROiQ43872.

Gene expression databases

GenevisibleiQ43872. AT.

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
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.
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 (JUL-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  3. "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence features of the regions of 1,011,550 bp covered by seventeen P1 and TAC clones."
    Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H., Miyajima N., Tabata S.
    DNA Res. 6:183-195(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "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.
  6. "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.
  7. "Isolation of putative defense-related genes from Arabidopsis thaliana and expression in fungal elicitor-treated cells."
    Trezzini G.F., Horrichs A., Somssich I.E.
    Plant Mol. Biol. 21:385-389(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: cv. Columbia.
  8. "Arabidopsis transcriptome profiling indicates that multiple regulatory pathways are activated during cold acclimation in addition to the CBF cold response pathway."
    Fowler S., Thomashow M.F.
    Plant Cell 14:1675-1690(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: cv. Columbia.
  9. "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 nameiPER64_ARATH
AccessioniPrimary (citable) accession number: Q43872
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: November 1, 1996
Last modified: February 17, 2016
This is version 130 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.