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Reviewed, UniProtKB/Swiss-Prot Q9FJR1 (PER65_ARATH)

Last modified June 16, 2009. Version 70. 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

Names and origin

Protein namesRecommended name:
    Peroxidase 65
      Short name=Atperox P65
    EC=1.11.1.7
Alternative name(s):
    ATP43
Gene names
Name: PER65
Synonyms: P65
Ordered Locus Names: At5g47000
ORF Names: MQD22.14
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length334 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

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 334306Peroxidase 65
PRO_0000023730

Sites

Active site731Proton acceptor By similarity
Metal binding741Calcium 1 By similarity
Metal binding791Calcium 1; via carbonyl oxygen By similarity
Metal binding811Calcium 1 By similarity
Metal binding831Calcium 1 By similarity
Metal binding2011Iron (heme axial ligand) By similarity
Metal binding2021Calcium 2 By similarity
Metal binding2501Calcium 2 By similarity
Metal binding2531Calcium 2 By similarity
Metal binding2581Calcium 2 By similarity
Binding site1711Substrate; via carbonyl oxygen By similarity
Site691Transition state stabilizer By similarity

Amino acid modifications

Glycosylation1741N-linked (GlcNAc...) Potential
Glycosylation2381N-linked (GlcNAc...) Potential
Glycosylation2821N-linked (GlcNAc...) Potential
Glycosylation2941N-linked (GlcNAc...) Potential
Disulfide bond42 ↔ 123 By similarity
Disulfide bond75 ↔ 80 By similarity
Disulfide bond129 ↔ 326 By similarity
Disulfide bond208 ↔ 236 By similarity

Experimental info

Sequence conflict161L → F in AAM65654. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9FJR1-1 [UniParc].

Last modified December 6, 2002. Version 2.
Checksum: DC07C78864450E44

FASTA33437,014
        10         20         30         40         50         60 
MSNMQFSRGF NPFVILFCLA VVAPIISADV AILRTDYYQK TCPDFHKIVR EAVTTKQVQQ 

        70         80         90        100        110        120 
PTTAAGTLRL FFHDCFLEGC DASVLIATNS FNKAERDDDL NDSLPGDAFD IVTRIKTALE 

       130        140        150        160        170        180 
LSCPGVVSCA DILAQATRDL VTMVGGPYFD VKLGRKDGFE SKAHKVRGNV PMANQTVPDI 

       190        200        210        220        230        240 
HGIFKKNGFS LREMVALSGA HTIGFSHCKE FSDRLYGSRA DKEINPRFAA ALKDLCKNHT 

       250        260        270        280        290        300 
VDDTIAAFND VMTPGKFDNM YFKNLKRGLG LLASDHILIK DNSTKPFVDL YATNETAFFE 

       310        320        330 
DFARAMEKLG TVGVKGDKDG EVRRRCDHFN NLNV 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones."
Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S.
DNA Res. 5:203-216(1998) [PubMed: 9734815] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"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: 14593172] [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.

Cross-references

Sequence databases

AB013394 Genomic DNA. Translation: BAB10239.1. Different initiation.
AY093131 mRNA. Translation: AAM13130.1.
BT008821 mRNA. Translation: AAP68260.1.
AY088108 mRNA. Translation: AAM65654.1.
IPIIPI00544962.
RefSeqNP_568674.1.
UniGeneAt.29916

3D structure databases

HSSPHSSP built from PDB template 1QGJ based on UniProtKB Q39034.
ModBaseSearch...

Protein family/group databases

PeroxiBase231. AtPrx65.

Proteomic databases

PRIDEQ9FJR1.

Genome annotation databases

GeneID834746.
GenomeReviewsGene locus AT5G47000 in contig BA000015_GR.
KEGGath:AT5G47000.
NMPDRfig|3702.1.peg.26498.

Organism-specific databases

GeneFarm1924. 61.
TAIRAt5g47000.

Phylogenomic databases

OMAQ9FJR1. EKPPGQP.

Enzyme and pathway databases

BRENDA1.11.1.7. 302.

Gene expression databases

ArrayExpressQ9FJR1.
GermOnlineAT5G47000. Arabidopsis thaliana.

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...

Entry information

Entry namePER65_ARATH
AccessionPrimary (citable) accession number: Q9FJR1
Secondary accession number(s): Q8RWF3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: December 6, 2002
Last modified: June 16, 2009
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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