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Protein

Peroxidase 9

Gene

PER9

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
Sitei81 – 811Transition state stabilizerPROSITE-ProRule annotation
Active sitei85 – 851Proton acceptorPROSITE-ProRule annotation
Metal bindingi86 – 861Calcium 1PROSITE-ProRule annotation
Metal bindingi89 – 891Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi91 – 911Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi93 – 931Calcium 1PROSITE-ProRule annotation
Metal bindingi95 – 951Calcium 1PROSITE-ProRule annotation
Binding sitei182 – 1821Substrate; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi212 – 2121Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi213 – 2131Calcium 2PROSITE-ProRule annotation
Metal bindingi264 – 2641Calcium 2PROSITE-ProRule annotation
Metal bindingi267 – 2671Calcium 2PROSITE-ProRule annotation
Metal bindingi272 – 2721Calcium 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:AT1G44970-MONOMER.

Protein family/group databases

PeroxiBasei85. AtPrx09.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidase 9 (EC:1.11.1.7)
Short name:
Atperox P9
Alternative name(s):
ATP18a
Gene namesi
Name:PER9
Synonyms:P9
Ordered Locus Names:At1g44970
ORF Names:F27F5.6, T22C22.24
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G44970.

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 – 2323Sequence analysisAdd
BLAST
Chaini24 – 346323Peroxidase 9PRO_0000023675Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 134PROSITE-ProRule annotation
Disulfide bondi87 ↔ 92PROSITE-ProRule annotation
Disulfide bondi140 ↔ 342PROSITE-ProRule annotation
Glycosylationi185 – 1851N-linked (GlcNAc...)Sequence analysis
Disulfide bondi219 ↔ 251PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ96512.
PRIDEiQ96512.

Expressioni

Gene expression databases

ExpressionAtlasiQ96512. baseline and differential.
GenevisibleiQ96512. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT1G44970.1.

Structurei

3D structure databases

ProteinModelPortaliQ96512.
SMRiQ96512. Positions 45-346.
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

eggNOGiENOG410IIDC. Eukaryota.
ENOG410YFB5. LUCA.
HOGENOMiHOG000237557.
InParanoidiQ96512.
KOiK00430.
OMAiRFDNTYF.
PhylomeDBiQ96512.

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.

Q96512-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAISKLIPTL VLFVLFSFDV SVAHPGLGFG WGSNSPIGGS FYSNLYPQFY
60 70 80 90 100
QFSCPQADEI VMTVLEKAIA KEPRMAASLL RLHFHDCFVQ GCDASILLDD
110 120 130 140 150
SATIRSEKNA GPNKNSVRGF QVIDEIKAKL EQACPQTVSC ADILALAARG
160 170 180 190 200
STILSGGPSW ELPLGRRDSR TASLNGANTN IPAPNSTIQN LLTMFQRKGL
210 220 230 240 250
NEEDLVSLSG GHTIGVARCT TFKQRLYNQN GNNQPDETLE RSYYYGLRSI
260 270 280 290 300
CPPTGGDNNI SPLDLASPAR FDNTYFKLLL WGKGLLTSDE VLLTGNVGKT
310 320 330 340
GALVKAYAED ERLFFQQFAK SMVNMGNIQP LTGFNGEIRK SCHVIN
Length:346
Mass (Da):37,741
Last modified:February 1, 1997 - v1
Checksum:i47EFD6297469A065
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti269 – 2691A → S in AAM63684 (Ref. 5) Curated
Sequence conflicti290 – 2901E → Q in AAM63684 (Ref. 5) Curated
Sequence conflicti302 – 3021A → S in AAM63684 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98804 mRNA. Translation: CAA67336.1.
AC007915 Genomic DNA. Translation: AAF69153.1.
AC020576 Genomic DNA. Translation: AAF78280.1.
CP002684 Genomic DNA. Translation: AEE32069.1.
BT008612 mRNA. Translation: AAP40436.1.
AY086626 mRNA. Translation: AAM63684.1.
RefSeqiNP_175117.1. NM_103577.3.
UniGeneiAt.140.
At.74270.

Genome annotation databases

EnsemblPlantsiAT1G44970.1; AT1G44970.1; AT1G44970.
GeneIDi841062.
GrameneiAT1G44970.1; AT1G44970.1; AT1G44970.
KEGGiath:AT1G44970.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98804 mRNA. Translation: CAA67336.1.
AC007915 Genomic DNA. Translation: AAF69153.1.
AC020576 Genomic DNA. Translation: AAF78280.1.
CP002684 Genomic DNA. Translation: AEE32069.1.
BT008612 mRNA. Translation: AAP40436.1.
AY086626 mRNA. Translation: AAM63684.1.
RefSeqiNP_175117.1. NM_103577.3.
UniGeneiAt.140.
At.74270.

3D structure databases

ProteinModelPortaliQ96512.
SMRiQ96512. Positions 45-346.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G44970.1.

Protein family/group databases

PeroxiBasei85. AtPrx09.

Proteomic databases

PaxDbiQ96512.
PRIDEiQ96512.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G44970.1; AT1G44970.1; AT1G44970.
GeneIDi841062.
GrameneiAT1G44970.1; AT1G44970.1; AT1G44970.
KEGGiath:AT1G44970.

Organism-specific databases

TAIRiAT1G44970.

Phylogenomic databases

eggNOGiENOG410IIDC. Eukaryota.
ENOG410YFB5. LUCA.
HOGENOMiHOG000237557.
InParanoidiQ96512.
KOiK00430.
OMAiRFDNTYF.
PhylomeDBiQ96512.

Enzyme and pathway databases

BioCyciARA:AT1G44970-MONOMER.

Miscellaneous databases

PROiQ96512.

Gene expression databases

ExpressionAtlasiQ96512. baseline and differential.
GenevisibleiQ96512. 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., Hansen L.N., Rasmussen S.K.
    Submitted (JUN-1996) 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. "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.
  5. "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].
  6. "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.
  7. "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 nameiPER9_ARATH
AccessioniPrimary (citable) accession number: Q96512
Secondary accession number(s): Q9LPD4
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.