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Reviewed, UniProtKB/Swiss-Prot O22862 (PER26_ARATH)

Last modified June 16, 2009. Version 75. 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:
    Probable peroxidase 26
      Short name=Atperox P26
    EC=1.11.1.7
Alternative name(s):
    ATP50
Gene names
Name: PER26
Synonyms: P26
Ordered Locus Names: At2g43480
ORF Names: T1O24.22
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length335 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 Probable. The enzyme activity has to be proved.

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.

Caution

Lacks the distal histidine (here Ser-77), present in the active site, which is one of the conserved features of the classical plant (class III) peroxidase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 335317Probable peroxidase 26
PRO_0000023692

Sites

Active site731 By similarity
Metal binding781Calcium 1 By similarity
Metal binding811Calcium 1; via carbonyl oxygen By similarity
Metal binding831Calcium 1; via carbonyl oxygen By similarity
Metal binding851Calcium 1 By similarity
Metal binding871Calcium 1 By similarity
Metal binding1981Iron (heme axial ligand) By similarity
Metal binding1991Calcium 2 By similarity
Metal binding2551Calcium 2 By similarity
Metal binding2581Calcium 2 By similarity
Binding site1681Substrate; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation2161N-linked (GlcNAc...) Potential
Glycosylation2591N-linked (GlcNAc...) Potential
Glycosylation2731N-linked (GlcNAc...) Potential
Disulfide bond46 ↔ 122 By similarity
Disulfide bond79 ↔ 84 By similarity
Disulfide bond128 ↔ 331 By similarity
Disulfide bond205 ↔ 237 By similarity

Experimental info

Sequence conflict1401V → I in AAL84934. Ref.2
Sequence conflict1891L → R in AAL84934. Ref.2
Sequence conflict2081V → A in AAL84934. Ref.2
Sequence conflict2861N → D in AAL84934. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O22862-1 [UniParc].

Last modified November 25, 2002. Version 2.
Checksum: CAF4B893D9C3CC24

FASTA33537,568
        10         20         30         40         50         60 
MVMIHIFLTV MVVGGVSLFP ETAEAIVMGP SMQKLTWHYY KVYNTCENAE NFVRHQVEIF 

        70         80         90        100        110        120 
YKNDKSIAPK LLRLLYSDCF VSGCDASVLL EGPNSEKMAP QNRGLGGFVL IDKIKIVLEQ 

       130        140        150        160        170        180 
RCPGVVSCAD ILNLATRDAV HLAGAPSYPV FTGRRDGLTS DKQTVDLPSP SISWDQAMSY 

       190        200        210        220        230        240 
FKSRGLNVLD MATLLGSHSM GRTHCSYVVD RLYNYNKTGK PSPTMNKYFL SEMAKQCPPR 

       250        260        270        280        290        300 
TRKGQTDPLV YLNPDSGSNH SFTSSFYSRI LSNKSVLEVD QQLLYNDDTK QISKEFSEGF 

       310        320        330 
EDFRKSFALS MSKMGAINVL TKTEGEIRKD CRHIN 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed: 10617197] [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]"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

AC002335 Genomic DNA. Translation: AAB64327.1. Different initiation.
AY078928 mRNA. Translation: AAL84934.1.
IPIIPI00520349.
RefSeqNP_181876.2.
UniGeneAt.36889

3D structure databases

HSSPHSSP built from PDB template 1PA2 based on UniProtKB Q42578.
ModBaseSearch...

Protein family/group databases

PeroxiBase119. AtPrx26.

Genome annotation databases

GeneID818949.
GenomeReviewsGene locus AT2G43480 in contig CT485783_GR.
KEGGath:AT2G43480.
NMPDRfig|3702.1.peg.11504.

Organism-specific databases

GeneFarm1853. 61.
TAIRAt2g43480.

Phylogenomic databases

OMAO22862. LLYSDCF.

Enzyme and pathway databases

BRENDA1.11.1.7. 302.

Gene expression databases

ArrayExpressO22862.
GermOnlineAT2G43480. 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. False negative.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePER26_ARATH
AccessionPrimary (citable) accession number: O22862
Secondary accession number(s): Q8RY36
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: November 25, 2002
Last modified: June 16, 2009
This is version 75 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