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Protein

Peroxidase 46

Gene

PER46

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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
Sitei65 – 651Transition state stabilizerPROSITE-ProRule annotation
Active sitei69 – 691Proton acceptorPROSITE-ProRule annotation
Metal bindingi70 – 701Calcium 1PROSITE-ProRule annotation
Metal bindingi73 – 731Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi75 – 751Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi77 – 771Calcium 1PROSITE-ProRule annotation
Metal bindingi79 – 791Calcium 1PROSITE-ProRule annotation
Metal bindingi192 – 1921Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi193 – 1931Calcium 2PROSITE-ProRule annotation
Metal bindingi246 – 2461Calcium 2PROSITE-ProRule annotation
Metal bindingi249 – 2491Calcium 2PROSITE-ProRule annotation
Metal bindingi254 – 2541Calcium 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:AT4G31760-MONOMER.

Protein family/group databases

PeroxiBasei212. AtPrx46.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase 46 (EC:1.11.1.7)
Short name:
Atperox P46
Alternative name(s):
ATP48
Gene namesi
Name:PER46
Synonyms:P46
Ordered Locus Names:At4g31760
ORF Names:F28M20.50
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G31760.

Subcellular locationi

  • Secreted PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence analysisAdd
BLAST
Chaini28 – 326299Peroxidase 46PRO_0000023712Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi28 – 281N-linked (GlcNAc...)Sequence analysis
Disulfide bondi38 ↔ 114PROSITE-ProRule annotation
Disulfide bondi71 ↔ 76PROSITE-ProRule annotation
Glycosylationi85 – 851N-linked (GlcNAc...)Sequence analysis
Disulfide bondi120 ↔ 322PROSITE-ProRule annotation
Disulfide bondi199 ↔ 233PROSITE-ProRule annotation
Glycosylationi278 – 2781N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO81772.
PRIDEiO81772.

Expressioni

Gene expression databases

GenevisibleiO81772. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G31760.1.

Structurei

3D structure databases

ProteinModelPortaliO81772.
SMRiO81772. Positions 28-326.
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

eggNOGiENOG410IE9G. Eukaryota.
ENOG410Y94T. LUCA.
HOGENOMiHOG000237556.
InParanoidiO81772.
KOiK00430.
PhylomeDBiO81772.

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
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.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O81772-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSYRINCS TLLHLLMFLS SLLTSSANLS FNFYASSCSV AEFLVRNTVR
60 70 80 90 100
SATSSDPTIP GKLLRLFFHD CFVQGCDASV LIQGNSTEKS DPGNASLGGF
110 120 130 140 150
SVIDTAKNAI ENLCPATVSC ADIVALAARD AVEAAGGPVV EIPTGRRDGK
160 170 180 190 200
ESMAANVRPN IIDTDFTLDQ MIDAFSSKGL SIQDLVVLSG AHTIGASHCN
210 220 230 240 250
AFNGRFQRDS KGNFEVIDAS LDNSYAETLM NKCSSSESSS LTVSNDPETS
260 270 280 290 300
AVFDNQYYRN LETHKGLFQT DSALMEDNRT RTMVEELASD EESFFQRWSE
310 320
SFVKLSMVGV RVGEDGEIRR SCSSVN
Length:326
Mass (Da):35,244
Last modified:November 1, 1998 - v1
Checksum:i1FC9CA566895967B
GO

Sequence cautioni

The sequence AEE85954.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL031004 Genomic DNA. Translation: CAA19747.1.
AL161579 Genomic DNA. Translation: CAB79894.1.
CP002687 Genomic DNA. Translation: AEE85954.1. Sequence problems.
PIRiT05094.
RefSeqiNP_194904.2. NM_119325.2.
UniGeneiAt.54570.

Genome annotation databases

EnsemblPlantsiAT4G31760.1; AT4G31760.1; AT4G31760.
GeneIDi829304.
GrameneiAT4G31760.1; AT4G31760.1; AT4G31760.
KEGGiath:AT4G31760.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL031004 Genomic DNA. Translation: CAA19747.1.
AL161579 Genomic DNA. Translation: CAB79894.1.
CP002687 Genomic DNA. Translation: AEE85954.1. Sequence problems.
PIRiT05094.
RefSeqiNP_194904.2. NM_119325.2.
UniGeneiAt.54570.

3D structure databases

ProteinModelPortaliO81772.
SMRiO81772. Positions 28-326.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G31760.1.

Protein family/group databases

PeroxiBasei212. AtPrx46.

Proteomic databases

PaxDbiO81772.
PRIDEiO81772.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G31760.1; AT4G31760.1; AT4G31760.
GeneIDi829304.
GrameneiAT4G31760.1; AT4G31760.1; AT4G31760.
KEGGiath:AT4G31760.

Organism-specific databases

TAIRiAT4G31760.

Phylogenomic databases

eggNOGiENOG410IE9G. Eukaryota.
ENOG410Y94T. LUCA.
HOGENOMiHOG000237556.
InParanoidiO81772.
KOiK00430.
PhylomeDBiO81772.

Enzyme and pathway databases

BioCyciARA:AT4G31760-MONOMER.

Miscellaneous databases

PROiO81772.

Gene expression databases

GenevisibleiO81772. AT.

Family and domain databases

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
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.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "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 nameiPER46_ARATH
AccessioniPrimary (citable) accession number: O81772
Secondary accession number(s): F4JSS1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: November 1, 1998
Last modified: July 6, 2016
This is version 123 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.