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Protein

Peroxidase 53

Gene

PER53

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.
Closely linked to lignin formation by showing monolignol substrate specificity.

Catalytic activityi

2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 2 calcium ions per subunit.
  • heme bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei68 – 681Transition state stabilizer
Active sitei72 – 721Proton acceptor
Metal bindingi73 – 731Calcium 1
Metal bindingi76 – 761Calcium 1; via carbonyl oxygen
Metal bindingi78 – 781Calcium 1; via carbonyl oxygen
Metal bindingi80 – 801Calcium 1
Metal bindingi82 – 821Calcium 1
Binding sitei169 – 1691Substrate; via carbonyl oxygen
Metal bindingi199 – 1991Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi200 – 2001Calcium 2
Metal bindingi251 – 2511Calcium 2
Metal bindingi254 – 2541Calcium 2
Metal bindingi259 – 2591Calcium 2

GO - Molecular functioni

GO - Biological processi

  • defense response to nematode Source: TAIR
  • flower development Source: TAIR
  • hydrogen peroxide catabolic process Source: UniProtKB-KW
  • response to oxidative stress Source: InterPro
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:AT5G06720-MONOMER.

Protein family/group databases

PeroxiBasei219. AtPrx53.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase 53 (EC:1.11.1.7)
Short name:
Atperox P53
Alternative name(s):
ATPA2
Gene namesi
Name:PER53
Synonyms:P53
Ordered Locus Names:At5g06720
ORF Names:MPH15.8
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G06720.

Subcellular locationi

  • Secreted PROSITE-ProRule annotation

GO - Cellular componenti

  • extracellular region Source: UniProtKB-SubCell
  • Golgi apparatus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence analysisAdd
BLAST
Chaini31 – 335305Peroxidase 53PRO_0000023718Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311Pyrrolidone carboxylic acidPROSITE-ProRule annotation1 Publication
Glycosylationi33 – 331N-linked (GlcNAc...)Sequence analysis
Disulfide bondi41 ↔ 121PROSITE-ProRule annotation
Glycosylationi43 – 431N-linked (GlcNAc...)Sequence analysis
Disulfide bondi74 ↔ 79PROSITE-ProRule annotation
Disulfide bondi127 ↔ 329PROSITE-ProRule annotation
Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence analysis
Glycosylationi177 – 1771N-linked (GlcNAc...)Sequence analysis
Disulfide bondi206 ↔ 238PROSITE-ProRule annotation
Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence analysis
Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence analysis
Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence analysis
Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiQ42578.
PRIDEiQ42578.

Expressioni

Tissue specificityi

Mainly expressed in roots.

Gene expression databases

GenevisibleiQ42578. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT5G06720.1.

Structurei

Secondary structure

1
335
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni34 – 407Combined sources
Helixi44 – 5613Combined sources
Helixi62 – 7413Combined sources
Turni75 – 773Combined sources
Beta strandi78 – 814Combined sources
Helixi82 – 843Combined sources
Helixi94 – 963Combined sources
Turni98 – 1036Combined sources
Helixi107 – 12014Combined sources
Turni122 – 1243Combined sources
Helixi127 – 14115Combined sources
Helixi161 – 1677Combined sources
Helixi175 – 18410Combined sources
Helixi189 – 1968Combined sources
Helixi197 – 2004Combined sources
Beta strandi201 – 2055Combined sources
Helixi206 – 2083Combined sources
Helixi210 – 2123Combined sources
Helixi216 – 2183Combined sources
Beta strandi219 – 2213Combined sources
Helixi228 – 23710Combined sources
Beta strandi247 – 2504Combined sources
Beta strandi252 – 2576Combined sources
Helixi261 – 2677Combined sources
Helixi274 – 2818Combined sources
Helixi287 – 29610Combined sources
Helixi298 – 31316Combined sources
Beta strandi322 – 3243Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PA2X-ray1.45A31-335[»]
1QO4X-ray3.00A31-335[»]
ProteinModelPortaliQ42578.
SMRiQ42578. Positions 31-335.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ42578.

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IK8B. Eukaryota.
ENOG410YBAI. LUCA.
HOGENOMiHOG000237557.
InParanoidiQ42578.
KOiK00430.
OMAiQICPQNG.
PhylomeDBiQ42578.

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.

Q42578-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVTNLPTCD GLFIISLIVI VSSIFGTSSA QLNATFYSGT CPNASAIVRS
60 70 80 90 100
TIQQALQSDT RIGASLIRLH FHDCFVNGCD ASILLDDTGS IQSEKNAGPN
110 120 130 140 150
VNSARGFNVV DNIKTALENA CPGVVSCSDV LALASEASVS LAGGPSWTVL
160 170 180 190 200
LGRRDSLTAN LAGANSSIPS PIESLSNITF KFSAVGLNTN DLVALSGAHT
210 220 230 240 250
FGRARCGVFN NRLFNFSGTG NPDPTLNSTL LSTLQQLCPQ NGSASTITNL
260 270 280 290 300
DLSTPDAFDN NYFANLQSND GLLQSDQELF STTGSSTIAI VTSFASNQTL
310 320 330
FFQAFAQSMI NMGNISPLTG SNGEIRLDCK KVNGS
Length:335
Mass (Da):34,989
Last modified:November 1, 1996 - v1
Checksum:i57E375B212F1BC6B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211V → L in AAM65211 (Ref. 5) Curated
Sequence conflicti172 – 1721I → V in AAM65211 (Ref. 5) Curated
Sequence conflicti180 – 1801F → S in AAM65211 (Ref. 5) Curated
Sequence conflicti270 – 2701D → N in AAM65211 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99952 mRNA. Translation: CAA68212.1.
AP002032 Genomic DNA. Translation: BAB09806.1.
CP002688 Genomic DNA. Translation: AED91055.1.
AY056186 mRNA. Translation: AAL07035.1.
AY096713 mRNA. Translation: AAM20347.1.
AY087674 mRNA. Translation: AAM65211.1.
RefSeqiNP_196290.1. NM_120755.2.
UniGeneiAt.93.

Genome annotation databases

EnsemblPlantsiAT5G06720.1; AT5G06720.1; AT5G06720.
GeneIDi830561.
GrameneiAT5G06720.1; AT5G06720.1; AT5G06720.
KEGGiath:AT5G06720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99952 mRNA. Translation: CAA68212.1.
AP002032 Genomic DNA. Translation: BAB09806.1.
CP002688 Genomic DNA. Translation: AED91055.1.
AY056186 mRNA. Translation: AAL07035.1.
AY096713 mRNA. Translation: AAM20347.1.
AY087674 mRNA. Translation: AAM65211.1.
RefSeqiNP_196290.1. NM_120755.2.
UniGeneiAt.93.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PA2X-ray1.45A31-335[»]
1QO4X-ray3.00A31-335[»]
ProteinModelPortaliQ42578.
SMRiQ42578. Positions 31-335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT5G06720.1.

Protein family/group databases

PeroxiBasei219. AtPrx53.

Proteomic databases

PaxDbiQ42578.
PRIDEiQ42578.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G06720.1; AT5G06720.1; AT5G06720.
GeneIDi830561.
GrameneiAT5G06720.1; AT5G06720.1; AT5G06720.
KEGGiath:AT5G06720.

Organism-specific databases

TAIRiAT5G06720.

Phylogenomic databases

eggNOGiENOG410IK8B. Eukaryota.
ENOG410YBAI. LUCA.
HOGENOMiHOG000237557.
InParanoidiQ42578.
KOiK00430.
OMAiQICPQNG.
PhylomeDBiQ42578.

Enzyme and pathway databases

BioCyciARA:AT5G06720-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ42578.
PROiQ42578.

Gene expression databases

GenevisibleiQ42578. 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. "Structure and organ specificity of an anionic peroxidase from Arabidopsis thaliana cell suspension culture."
    Oestergaard L., Abelskov A.K., Mattsson O., Welinder K.G.
    FEBS Lett. 398:243-247(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PYROGLUTAMATE FORMATION AT GLN-31.
    Strain: cv. Columbia.
  2. "Structural analysis of Arabidopsis thaliana chromosome 5. XI."
    Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    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. "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].
  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. "Arabidopsis ATP A2 peroxidase. Expression and high-resolution structure of a plant peroxidase with implications for lignification."
    Oestergaard L., Teilum K., Mirza O., Mattsson O., Petersen M., Welinder K.G., Mundy J., Gajhede M., Henriksen A.
    Plant Mol. Biol. 44:231-243(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
    Strain: cv. Columbia.
  8. "Differential activity and structure of highly similar peroxidases. Spectroscopic, crystallographic, and enzymatic analyses of lignifying Arabidopsis thaliana peroxidase A2 and horseradish peroxidase A2."
    Nielsen K.L., Indiani C., Henriksen A., Feis A., Becucci M., Gajhede M., Smulevich G., Welinder K.G.
    Biochemistry 40:11013-11021(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
    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 nameiPER53_ARATH
AccessioniPrimary (citable) accession number: Q42578
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: November 1, 1996
Last modified: February 17, 2016
This is version 139 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.