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Q43729 (PER57_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peroxidase 57

Short name=Atperox P57
EC=1.11.1.7
Alternative name(s):
ATP13a
PRXR10
Gene names
Name:PER57
Synonyms:P57
Ordered Locus Names:At5g17820
ORF Names:MVA3.18, MVA3.170
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length313 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.

Catalytic activity

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

Cofactor

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

Binds 2 calcium ions per subunit By similarity.

Subcellular location

Secreted By similarity.

Tissue specificity

Mainly expressed in roots. Ref.8

Induction

Positively light-regulated during the firt stage of development. Up-regulated transiently by a cold treatment. Induced in shoots of plants subjected to a long Fe deficiency stress. Down-regulated by salicylic acid, a plant defense-related signaling molecule. Ref.9 Ref.10 Ref.11 Ref.12

Miscellaneous

There are 73 peroxidase genes in A.thaliana.

Sequence similarities

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

Sequence caution

The sequence AAM65434.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Heme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   PTMDisulfide bond
Pyrrolidone carboxylic acid
   Technical termComplete 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

membrane

Inferred from direct assay. Source: TAIR

plant-type cell wall

Inferred from direct assay. Source: TAIR

plasmodesma

Inferred from direct assay. Source: TAIR

   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 – 2222 Potential
Chain23 – 313291Peroxidase 57
PRO_0000023722

Sites

Active site641Proton acceptor By similarity
Metal binding651Calcium 1 By similarity
Metal binding681Calcium 1; via carbonyl oxygen By similarity
Metal binding701Calcium 1; via carbonyl oxygen By similarity
Metal binding721Calcium 1 By similarity
Metal binding741Calcium 1 By similarity
Metal binding1851Iron (heme axial ligand) By similarity
Metal binding1861Calcium 2 By similarity
Metal binding2331Calcium 2 By similarity
Metal binding2361Calcium 2 By similarity
Metal binding2411Calcium 2 By similarity
Binding site1551Substrate; via carbonyl oxygen By similarity
Site601Transition state stabilizer By similarity

Amino acid modifications

Modified residue231Pyrrolidone carboxylic acid By similarity
Disulfide bond33 ↔ 109 By similarity
Disulfide bond66 ↔ 71 By similarity
Disulfide bond115 ↔ 309 By similarity
Disulfide bond192 ↔ 224 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q43729 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: BFD2855EC45DFF26

FASTA31334,098
        10         20         30         40         50         60 
MMKGAKFSSL LVLFFIFPIA FAQLRVGFYS QSCPQAETIV RNLVRQRFGV TPTVTAALLR 

        70         80         90        100        110        120 
MHFHDCFVKG CDASLLIDST NSEKTAGPNG SVREFDLIDR IKAQLEAACP STVSCADIVT 

       130        140        150        160        170        180 
LATRDSVALA GGPSYSIPTG RRDGRVSNNL DVTLPGPTIS VSGAVSLFTN KGMNTFDAVA 

       190        200        210        220        230        240 
LLGAHTVGQG NCGLFSDRIT SFQGTGRPDP SMDPALVTSL RNTCRNSATA ALDQSSPLRF 

       250        260        270        280        290        300 
DNQFFKQIRK RRGVLQVDQR LASDPQTRGI VARYANNNAF FKRQFVRAMV KMGAVDVLTG 

       310 
RNGEIRRNCR RFN 

« Hide

References

« Hide 'large scale' references
[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 (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[3]"Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence features of the regions of 1,044,062 bp covered by thirteen physically assigned P1 clones."
Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N., Tabata S.
DNA Res. 4:291-300(1997) [PubMed: 9405937] [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. 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.
[6]"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].
[7]"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.
[8]"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.
[9]"Differential gene expression in Arabidopsis monitored using cDNA arrays."
Desprez T., Amselem J., Caboche M., Hoefte H.
Plant J. 14:643-652(1998) [PubMed: 9675907] [Abstract]
Cited for: INDUCTION.
Strain: cv. Columbia.
[10]"Coordinated plant defense responses in Arabidopsis revealed by microarray analysis."
Schenk P.M., Kazan K., Wilson I., Anderson J.P., Richmond T., Somerville S.C., Manners J.M.
Proc. Natl. Acad. Sci. U.S.A. 97:11655-11660(2000) [PubMed: 11027363] [Abstract]
Cited for: INDUCTION.
Strain: cv. Columbia.
[11]"Response of Arabidopsis to iron deficiency stress as revealed by microarray analysis."
Thimm O., Essigmann B., Kloska S., Altmann T., Buckhout T.J.
Plant Physiol. 127:1030-1043(2001) [PubMed: 11706184] [Abstract]
Cited for: INDUCTION.
Strain: cv. Columbia.
[12]"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: 12172015] [Abstract]
Cited for: INDUCTION.
Strain: cv. Columbia.
[13]"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
X98322 mRNA. Translation: CAA66966.1.
X98776 mRNA. Translation: CAA67312.1.
AB006706 Genomic DNA. Translation: BAB09581.1.
CP002688 Genomic DNA. Translation: AED92474.1.
BT002958 mRNA. Translation: AAO22769.2.
AY087882 mRNA. Translation: AAM65434.1. Different initiation.
IPIIPI00544734.
RefSeqNP_197284.1. NM_121788.3.
UniGeneAt.25535.

3D structure databases

ProteinModelPortalQ43729.
SMRQ43729. Positions 23-313.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ43729.

Protein family/group databases

PeroxiBase223. AtPrx57.

Proteomic databases

PRIDEQ43729.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G17820.1; AT5G17820.1; AT5G17820.
GeneID831650.
GenomeReviewsGene locus AT5G17820 in contig BA000015_GR.
KEGGath:AT5G17820.

Organism-specific databases

GeneFarm1912. 61.
TAIRAt5g17820.

Phylogenomic databases

HOGENOMHBG597790.
InParanoidQ43729.
OMAARYANNN.
PhylomeDBQ43729.
ProtClustDBCLSN2913407.

Gene expression databases

ArrayExpressQ43729.
GenevestigatorQ43729.
GermOnlineAT5G17820. 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 namePER57_ARATH
AccessionPrimary (citable) accession number: Q43729
Secondary accession number(s): Q84WN8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: November 1, 1996
Last modified: December 14, 2011
This is version 99 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

SIMILARITY comments

Index of protein domains and families