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Protein

Peroxidase 11

Gene

PER11

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 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
Sitei66 – 661Transition state stabilizerPROSITE-ProRule annotation
Active sitei70 – 701Proton acceptorPROSITE-ProRule annotation
Metal bindingi71 – 711Calcium 1PROSITE-ProRule annotation
Metal bindingi74 – 741Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi76 – 761Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi78 – 781Calcium 1PROSITE-ProRule annotation
Metal bindingi80 – 801Calcium 1PROSITE-ProRule annotation
Binding sitei167 – 1671Substrate; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi197 – 1971Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi198 – 1981Calcium 2PROSITE-ProRule annotation
Metal bindingi251 – 2511Calcium 2PROSITE-ProRule annotation
Metal bindingi254 – 2541Calcium 2PROSITE-ProRule annotation
Metal bindingi259 – 2591Calcium 2PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Biological rhythms, Hydrogen peroxide

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT1G68850-MONOMER.

Protein family/group databases

PeroxiBasei92. AtPrx11.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase 11 (EC:1.11.1.7)
Short name:
Atperox P11
Alternative name(s):
ATP23a/ATP23b
Gene namesi
Name:PER11
Synonyms:P11
Ordered Locus Names:At1g68850
ORF Names:F14K14.4, T6L1.4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G68850.

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 – 2020Sequence analysisAdd
BLAST
Chaini21 – 336316Peroxidase 11PRO_0000023677Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi39 ↔ 119PROSITE-ProRule annotation
Disulfide bondi72 ↔ 77PROSITE-ProRule annotation
Disulfide bondi125 ↔ 331PROSITE-ProRule annotation
Disulfide bondi204 ↔ 236PROSITE-ProRule annotation
Glycosylationi246 – 2461N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ96519.
PRIDEiQ96519.

Expressioni

Tissue specificityi

Expressed in roots and stems.

Inductioni

Expressed under a diurnal rhythm.1 Publication

Gene expression databases

GenevisibleiQ96519. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT1G68850.1.

Structurei

3D structure databases

ProteinModelPortaliQ96519.
SMRiQ96519. Positions 30-335.
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

eggNOGiENOG410IHG7. Eukaryota.
ENOG410YA9R. LUCA.
HOGENOMiHOG000237557.
InParanoidiQ96519.
KOiK00430.
OMAiEMYSSLF.
PhylomeDBiQ96519.

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.

Q96519-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMRLLFVFFM VHTIFIPCFS FDTPGKDLPL TLDYYKSTCP TVFDVIKKEM
60 70 80 90 100
ECIVKEDPRN AAIIIRLHFH DCFVQGCDGS VLLDETETLQ GEKKASPNIN
110 120 130 140 150
SLKGYKIVDR IKNIIESECP GVVSCADLLT IGARDATILV GGPYWDVPVG
160 170 180 190 200
RKDSKTASYE LATTNLPTPE EGLISIIAKF YSQGLSVEDM VALIGAHTIG
210 220 230 240 250
KAQCRNFRSR IYGDFQVTSA LNPVSETYLA SLREICPASS GEGDSNVTAI
260 270 280 290 300
DNVTPNLFDN SIYHTLLRGE GLLNSDQEMY TSLFGIQTRR IVSKYAEDPV
310 320 330
AFFEQFSKSM VKMGNILNSE SLADGEVRRN CRFVNT
Length:336
Mass (Da):37,313
Last modified:February 1, 1997 - v1
Checksum:i846D69A84530900B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti192 – 1943ALI → YLL in CAA72485 (Ref. 1) Curated
Sequence conflicti218 – 2181T → M in CAA72485 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08782 mRNA. Translation: CAA70035.1.
Y11789 mRNA. Translation: CAA72485.1.
AC011665 Genomic DNA. Translation: AAG51588.1.
AC011914 Genomic DNA. Translation: AAG52033.1.
CP002684 Genomic DNA. Translation: AEE34850.1.
PIRiC96713.
RefSeqiNP_564948.1. NM_105559.3.
UniGeneiAt.87.

Genome annotation databases

EnsemblPlantsiAT1G68850.1; AT1G68850.1; AT1G68850.
GeneIDi843218.
GrameneiAT1G68850.1; AT1G68850.1; AT1G68850.
KEGGiath:AT1G68850.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08782 mRNA. Translation: CAA70035.1.
Y11789 mRNA. Translation: CAA72485.1.
AC011665 Genomic DNA. Translation: AAG51588.1.
AC011914 Genomic DNA. Translation: AAG52033.1.
CP002684 Genomic DNA. Translation: AEE34850.1.
PIRiC96713.
RefSeqiNP_564948.1. NM_105559.3.
UniGeneiAt.87.

3D structure databases

ProteinModelPortaliQ96519.
SMRiQ96519. Positions 30-335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G68850.1.

Protein family/group databases

PeroxiBasei92. AtPrx11.

Proteomic databases

PaxDbiQ96519.
PRIDEiQ96519.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G68850.1; AT1G68850.1; AT1G68850.
GeneIDi843218.
GrameneiAT1G68850.1; AT1G68850.1; AT1G68850.
KEGGiath:AT1G68850.

Organism-specific databases

TAIRiAT1G68850.

Phylogenomic databases

eggNOGiENOG410IHG7. Eukaryota.
ENOG410YA9R. LUCA.
HOGENOMiHOG000237557.
InParanoidiQ96519.
KOiK00430.
OMAiEMYSSLF.
PhylomeDBiQ96519.

Enzyme and pathway databases

BioCyciARA:AT1G68850-MONOMER.

Miscellaneous databases

PROiQ96519.

Gene expression databases

GenevisibleiQ96519. 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. "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 (MAR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    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. "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.
  5. "Microarray analysis of diurnal and circadian-regulated genes in Arabidopsis."
    Schaffer R., Landgraf J., Accerbi M., Simon V., Larson M., Wisman E.
    Plant Cell 13:113-123(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: cv. Columbia.
  6. "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 nameiPER11_ARATH
AccessioniPrimary (citable) accession number: Q96519
Secondary accession number(s): P93723
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: February 1, 1997
Last modified: February 17, 2016
This is version 124 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.