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Protein

Peroxidase 57

Gene

PER57

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
Sitei60 – 601Transition state stabilizerPROSITE-ProRule annotation
Active sitei64 – 641Proton acceptorPROSITE-ProRule annotation
Metal bindingi65 – 651Calcium 1PROSITE-ProRule annotation
Metal bindingi68 – 681Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi70 – 701Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi72 – 721Calcium 1PROSITE-ProRule annotation
Metal bindingi74 – 741Calcium 1PROSITE-ProRule annotation
Binding sitei155 – 1551Substrate; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi185 – 1851Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi186 – 1861Calcium 2PROSITE-ProRule annotation
Metal bindingi233 – 2331Calcium 2PROSITE-ProRule annotation
Metal bindingi236 – 2361Calcium 2PROSITE-ProRule annotation
Metal bindingi241 – 2411Calcium 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:AT5G17820-MONOMER.

Protein family/group databases

PeroxiBasei223. AtPrx57.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase 57 (EC:1.11.1.7)
Short name:
Atperox P57
Alternative name(s):
ATP13a
PRXR10
Gene namesi
Name:PER57
Synonyms:P57
Ordered Locus Names:At5g17820
ORF Names:MVA3.170, MVA3.18
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G17820.

Subcellular locationi

  • Secreted PROSITE-ProRule annotation

GO - Cellular componenti

  • cell wall Source: TAIR
  • extracellular region Source: UniProtKB-SubCell
  • membrane Source: TAIR
  • plant-type cell wall Source: TAIR
  • plasmodesma 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 – 313291Peroxidase 57PRO_0000023722Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 ↔ 109PROSITE-ProRule annotation
Disulfide bondi66 ↔ 71PROSITE-ProRule annotation
Disulfide bondi115 ↔ 309PROSITE-ProRule annotation
Disulfide bondi192 ↔ 224PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ43729.
PRIDEiQ43729.

PTM databases

iPTMnetiQ43729.

Expressioni

Tissue specificityi

Mainly expressed in roots.1 Publication

Inductioni

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.4 Publications

Gene expression databases

ExpressionAtlasiQ43729. baseline and differential.
GenevisibleiQ43729. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT5G17820.1.

Structurei

3D structure databases

ProteinModelPortaliQ43729.
SMRiQ43729. Positions 23-313.
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

eggNOGiENOG410IEWY. Eukaryota.
ENOG4110UVG. LUCA.
HOGENOMiHOG000237556.
InParanoidiQ43729.
KOiK00430.
OMAiNTCRNSA.
PhylomeDBiQ43729.

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.

Q43729-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMKGAKFSSL LVLFFIFPIA FAQLRVGFYS QSCPQAETIV RNLVRQRFGV
60 70 80 90 100
TPTVTAALLR MHFHDCFVKG CDASLLIDST NSEKTAGPNG SVREFDLIDR
110 120 130 140 150
IKAQLEAACP STVSCADIVT LATRDSVALA GGPSYSIPTG RRDGRVSNNL
160 170 180 190 200
DVTLPGPTIS VSGAVSLFTN KGMNTFDAVA LLGAHTVGQG NCGLFSDRIT
210 220 230 240 250
SFQGTGRPDP SMDPALVTSL RNTCRNSATA ALDQSSPLRF DNQFFKQIRK
260 270 280 290 300
RRGVLQVDQR LASDPQTRGI VARYANNNAF FKRQFVRAMV KMGAVDVLTG
310
RNGEIRRNCR RFN
Length:313
Mass (Da):34,098
Last modified:November 1, 1996 - v1
Checksum:iBFD2855EC45DFF26
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_197284.1. NM_121788.3.
UniGeneiAt.25535.

Genome annotation databases

EnsemblPlantsiAT5G17820.1; AT5G17820.1; AT5G17820.
GeneIDi831650.
GrameneiAT5G17820.1; AT5G17820.1; AT5G17820.
KEGGiath:AT5G17820.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_197284.1. NM_121788.3.
UniGeneiAt.25535.

3D structure databases

ProteinModelPortaliQ43729.
SMRiQ43729. Positions 23-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT5G17820.1.

Protein family/group databases

PeroxiBasei223. AtPrx57.

PTM databases

iPTMnetiQ43729.

Proteomic databases

PaxDbiQ43729.
PRIDEiQ43729.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G17820.1; AT5G17820.1; AT5G17820.
GeneIDi831650.
GrameneiAT5G17820.1; AT5G17820.1; AT5G17820.
KEGGiath:AT5G17820.

Organism-specific databases

TAIRiAT5G17820.

Phylogenomic databases

eggNOGiENOG410IEWY. Eukaryota.
ENOG4110UVG. LUCA.
HOGENOMiHOG000237556.
InParanoidiQ43729.
KOiK00430.
OMAiNTCRNSA.
PhylomeDBiQ43729.

Enzyme and pathway databases

BioCyciARA:AT5G17820-MONOMER.

Miscellaneous databases

PROiQ43729.

Gene expression databases

ExpressionAtlasiQ43729. baseline and differential.
GenevisibleiQ43729. 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. "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] [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. "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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE.
    Strain: cv. Columbia.

Entry informationi

Entry nameiPER57_ARATH
AccessioniPrimary (citable) accession number: Q43729
Secondary accession number(s): Q84WN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 131 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.