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Q42578 (PER53_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxidase 53
Short name=Atperox P53
EC=1.11.1.7
Alternative name(s):
ATPA2
Gene names
Name:PER53
Synonyms:P53
Ordered Locus Names:At5g06720
ORF Names:MPH15.8
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Binds 2 calcium ions per subunit.

Binds 1 heme B (iron-protoporphyrin IX) group per subunit.

Subcellular location

Secreted By similarity.

Tissue specificity

Mainly expressed in roots.

Miscellaneous

There are 73 peroxidase genes in A.thaliana.

Sequence similarities

Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Heme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   PTMDisulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionheme binding

Inferred from electronic annotation. Source: InterPro

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 335305Peroxidase 53
PRO_0000023718

Sites

Active site721Proton acceptor
Metal binding731Calcium 1
Metal binding761Calcium 1; via carbonyl oxygen
Metal binding781Calcium 1; via carbonyl oxygen
Metal binding801Calcium 1
Metal binding821Calcium 1
Metal binding1991Iron (heme axial ligand) By similarity
Metal binding2001Calcium 2
Metal binding2511Calcium 2
Metal binding2541Calcium 2
Metal binding2591Calcium 2
Binding site1691Substrate; via carbonyl oxygen
Site681Transition state stabilizer

Amino acid modifications

Modified residue311Pyrrolidone carboxylic acid
Glycosylation331N-linked (GlcNAc...) Potential
Glycosylation431N-linked (GlcNAc...) Potential
Glycosylation1651N-linked (GlcNAc...) Potential
Glycosylation1771N-linked (GlcNAc...) Potential
Glycosylation2151N-linked (GlcNAc...) Potential
Glycosylation2271N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Disulfide bond41 ↔ 121 By similarity
Disulfide bond74 ↔ 79 By similarity
Disulfide bond127 ↔ 329 By similarity
Disulfide bond206 ↔ 238 By similarity

Experimental info

Sequence conflict211V → L in AAM65211. Ref.5
Sequence conflict1721I → V in AAM65211. Ref.5
Sequence conflict1801F → S in AAM65211. Ref.5
Sequence conflict2701D → N in AAM65211. Ref.5

Secondary structure

1 .................................................. 335
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q42578 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 57E375B212F1BC6B

FASTA33534,989
        10         20         30         40         50         60 
MAVTNLPTCD GLFIISLIVI VSSIFGTSSA QLNATFYSGT CPNASAIVRS TIQQALQSDT 

        70         80         90        100        110        120 
RIGASLIRLH FHDCFVNGCD ASILLDDTGS IQSEKNAGPN VNSARGFNVV DNIKTALENA 

       130        140        150        160        170        180 
CPGVVSCSDV LALASEASVS LAGGPSWTVL LGRRDSLTAN LAGANSSIPS PIESLSNITF 

       190        200        210        220        230        240 
KFSAVGLNTN DLVALSGAHT FGRARCGVFN NRLFNFSGTG NPDPTLNSTL LSTLQQLCPQ 

       250        260        270        280        290        300 
NGSASTITNL DLSTPDAFDN NYFANLQSND GLLQSDQELF STTGSSTIAI VTSFASNQTL 

       310        320        330 
FFQAFAQSMI NMGNISPLTG SNGEIRLDCK KVNGS

« Hide

References

« Hide 'large scale' references
[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: 8977116] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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. expand/collapse author list , 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: 14593172] [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: 9738941] [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: 11117266] [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: 11551197] [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: 12034502] [Abstract]
Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00531924.
RefSeqNP_196290.1. NM_120755.2.
UniGeneAt.93.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PA2X-ray1.45A31-335[»]
1QO4X-ray3.00A31-335[»]
ProteinModelPortalQ42578.
SMRQ42578. Positions 31-335.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ42578.

Protein family/group databases

PeroxiBase219. AtPrx53.

Proteomic databases

PRIDEQ42578.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G06720.1; AT5G06720.1; AT5G06720.
GeneID830561.
GenomeReviewsGene locus AT5G06720 in contig BA000015_GR.
KEGGath:AT5G06720.
NMPDRfig|3702.1.peg.22803.

Organism-specific databases

GeneFarm1907. 61.
TAIRAt5g06720.

Phylogenomic databases

HOGENOMHBG597790.
InParanoidQ42578.
OMAKFSAVGL.
PhylomeDBQ42578.
ProtClustDBCLSN2686891.

Gene expression databases

ArrayExpressQ42578.
GenevestigatorQ42578.
GermOnlineAT5G06720. Arabidopsis thaliana.

Family and domain databases

InterProIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
KOK00430.
PfamPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSPR00458. PEROXIDASE.
PR00461. PLPEROXIDASE.
SUPFAMSSF48113. Peroxidase_super. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePER53_ARATH
AccessionPrimary (citable) accession number: Q42578
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: November 1, 1996
Last modified: December 14, 2011
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents