Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9SY33 (PER7_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxidase 7
Short name=Atperox P7
EC=1.11.1.7
Alternative name(s):
ATP30
Gene names
Name:PER7
Synonyms:P7
Ordered Locus Names:At1g30870
ORF Names:F17F8.26, T17H7.19
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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

2 phenolic donor + H2O2 = 2 phenoxyl radical of the 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.

Sequence caution

The sequence BT002890 differs from that shown. Reason: Frameshift at position 53.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionheme binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 349327Peroxidase 7
PRO_0000023673

Sites

Active site911Proton acceptor By similarity
Metal binding921Calcium 1 By similarity
Metal binding951Calcium 1; via carbonyl oxygen By similarity
Metal binding971Calcium 1; via carbonyl oxygen By similarity
Metal binding991Calcium 1 By similarity
Metal binding1011Calcium 1 By similarity
Metal binding2131Iron (heme axial ligand) By similarity
Metal binding2141Calcium 2 By similarity
Metal binding2621Calcium 2 By similarity
Metal binding2651Calcium 2 By similarity
Metal binding2701Calcium 2 By similarity
Binding site1831Substrate; via carbonyl oxygen By similarity
Site871Transition state stabilizer By similarity

Amino acid modifications

Glycosylation2311N-linked (GlcNAc...) Potential
Disulfide bond60 ↔ 136 By similarity
Disulfide bond93 ↔ 98 By similarity
Disulfide bond142 ↔ 341 By similarity
Disulfide bond220 ↔ 252 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9SY33 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 840F66EFCB43CE8A

FASTA34938,339
        10         20         30         40         50         60 
MKLAVVSVVV ILGVLVAWPV SAGRKDLPGA GGYGGDDDDD TKSLFPLDNL LSLNYYDRIC 

        70         80         90        100        110        120 
PDFEKIVVTK VREWTKSDSS LGPALLRLIF HDCGVTGCDA SVLLDYEGTE RRSPASKTLR 

       130        140        150        160        170        180 
GFELIDDIKS EMEKSCPGKV SCADILTSAS RAATVQLGGP YWPNVYGRRD SKHSYARDVE 

       190        200        210        220        230        240 
KVPSGRRDVT ALLETFQSYG LNVLDLVVLS GAHTIGKASC GTIQSRLYNY NATSGSDPSI 

       250        260        270        280        290        300 
DAKYADYLQR RCRWASETVD LDPVTPAVFD NQYYINLQKH MGVLSTDQEL VKDPRTAPLV 

       310        320        330        340 
KTFAEQSPQI FRQQFAVSMA KLVNVGVLTG EDRVGEIRKV CSKSNSRAY

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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. expand/collapse author list , 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.
[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] [Europe PMC] [Abstract]
Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC000107 Genomic DNA. Translation: AAF98194.1.
AC004135 Genomic DNA. Translation: AAD32944.1.
CP002684 Genomic DNA. Translation: AEE31287.1.
BT002890 mRNA. No translation available.
IPIIPI00547900.
RefSeqNP_174372.1. NM_102824.2.
UniGeneAt.27629.

3D structure databases

ProteinModelPortalQ9SY33.
SMRQ9SY33. Positions 51-345.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT1G30870.1-P.

Protein family/group databases

PeroxiBase83. AtPrx07.

Proteomic databases

PaxDbQ9SY33.
PRIDEQ9SY33.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G30870.1; AT1G30870.1; AT1G30870.
GeneID839971.
KEGGath:AT1G30870.

Organism-specific databases

GeneFarm1501. 61.
TAIRAt1g30870.

Phylogenomic databases

eggNOGCOG0376.
HOGENOMHOG000237557.
InParanoidQ9SY33.
KOK00430.
OMAHTIGRAT.
PhylomeDBQ9SY33.
ProtClustDBCLSN2914154.

Gene expression databases

GenevestigatorQ9SY33.
GermOnlineAT1G30870. Arabidopsis thaliana.

Family and domain databases

InterProIPR010255. Haem_peroxidase.
IPR002016. 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.
SUPFAMSSF48113. Peroxidase_super. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePER7_ARATH
AccessionPrimary (citable) accession number: Q9SY33
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: May 1, 2000
Last modified: May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents