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Reviewed, UniProtKB/Swiss-Prot P59120 (PER58_ARATH)

Last modified June 16, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Peroxidase 58
      Short name=Atperox P58
    EC=1.11.1.7
Alternative name(s):
    ATP42
Gene names
Name: PER58
Synonyms: P58
Ordered Locus Names: At5g19880
ORF Names: F28I16.30
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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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

Donor + H2O2 = oxidized 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.

Miscellaneous

There are 73 peroxidase genes in A.thaliana.

Sequence similarities

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

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Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

electron carrier activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 329306Peroxidase 58
PRO_0000023723

Sites

Active site651Proton acceptor By similarity
Metal binding661Calcium 1 By similarity
Metal binding691Calcium 1; via carbonyl oxygen By similarity
Metal binding711Calcium 1; via carbonyl oxygen By similarity
Metal binding731Calcium 1 By similarity
Metal binding751Calcium 1 By similarity
Metal binding1941Iron (heme axial ligand) By similarity
Metal binding1951Calcium 2 By similarity
Metal binding2471Calcium 2 By similarity
Metal binding2501Calcium 2 By similarity
Metal binding2551Calcium 2 By similarity
Binding site1641Substrate; via carbonyl oxygen By similarity
Site611Transition state stabilizer By similarity

Amino acid modifications

Modified residue241Pyrrolidone carboxylic acid By similarity
Glycosylation361N-linked (GlcNAc...) Potential
Glycosylation2101N-linked (GlcNAc...) Potential
Disulfide bond34 ↔ 116 By similarity
Disulfide bond67 ↔ 72 By similarity
Disulfide bond122 ↔ 325 By similarity
Disulfide bond201 ↔ 234 By similarity

Experimental info

Sequence conflict1421L → W in AAM60837. Ref.3
Sequence conflict3251C → Y in BAC42706. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P59120-1 [UniParc].

Last modified December 6, 2002. Version 1.
Checksum: 77B7B10F9A63942B

FASTA32935,429
        10         20         30         40         50         60 
MGLSKTIPLV LLPILMFGVL SNAQLTSDFY STTCPNVTAI ARGLIERASR NDVRLTAKVM 

        70         80         90        100        110        120 
RLHFHDCFVN GCDGSVLLDA APADGVEGEK EAFQNAGSLD GFEVIDDIKT ALENVCPGVV 

       130        140        150        160        170        180 
SCADILAIAA EISVALAGGP SLDVLLGRRD GRTAIRADAV AALPLGPDSL EILTSKFSVH 

       190        200        210        220        230        240 
NLDTTDLVAL SGAHTFGRVQ CGVINNRLHN FSGNSGQSDP SIEPEFLQTL RRQCPQGGDL 

       250        260        270        280        290        300 
TARANLDPTS PDSFDNDYFK NLQNNRGVIE SDQILFSSTG APTVSLVNRF AENQNEFFTN 

       310        320 
FARSMIKMGN VRILTGREGE IRRDCRRVN

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References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed: 11130714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed: 11910074] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[3]"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].
[4]"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.

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Cross-references

Sequence databases

AF296836 Genomic DNA. No translation available.
AK118075 mRNA. Translation: BAC42706.1.
AY084241 mRNA. Translation: AAM60837.1.
IPIIPI00520745.
RefSeqNP_197488.1.
UniGeneAt.31241

3D structure databases

HSSPHSSP built from PDB template 1PA2 based on UniProtKB Q42578.
ModBaseSearch...

Protein family/group databases

PeroxiBase224. AtPrx58.

Proteomic databases

PRIDEP59120.

Genome annotation databases

GeneID832110.
KEGGath:AT5G19880.

Organism-specific databases

GeneFarm1913. 61.
TAIRAt5g19880.

Phylogenomic databases

OMAP59120. NLQNNRG.

Enzyme and pathway databases

BRENDA1.11.1.7. 302.

Gene expression databases

ArrayExpressP59120.

Family and domain databases

InterProIPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSPR00458. PEROXIDASE.
PR00461. PLPEROXIDASE.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePER58_ARATH
AccessionPrimary (citable) accession number: P59120
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: December 6, 2002
Last modified: June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents