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Reviewed, UniProtKB/Swiss-Prot O80912 (PER23_ARATH)

Last modified November 25, 2008. Version 72. 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 23
      Short name=Atperox P23
    EC=1.11.1.7
Alternative name(s):
    ATP34
Gene names
Name: PER23
Synonyms: P23
Ordered Locus Names: At2g38390
ORF Names: T19C21.12
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

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 H(2)O(2), 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 + H(2)O(2) = oxidized donor + 2 H(2)O.

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity.

Binds 2 calcium ions per subunit By similarity.

Subcellular location

SecretedProbable. VacuoleProbable. Note= Carboxy-terminal extension appears to target the protein to vacuoles.

Induction

By methyl jasmonate, a plant defense-related signaling molecule.

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 – 2929 Potential
Chain30 – 349320Peroxidase 23
PRO_0000023689

Sites

Active site711Proton acceptor By similarity
Metal binding721Calcium 1 By similarity
Metal binding751Calcium 1; via carbonyl oxygen By similarity
Metal binding771Calcium 1; via carbonyl oxygen By similarity
Metal binding791Calcium 1 By similarity
Metal binding811Calcium 1 By similarity
Metal binding1991Iron (heme axial ligand) By similarity
Metal binding2001Calcium 2 By similarity
Metal binding2511Calcium 2 By similarity
Metal binding2541Calcium 2 By similarity
Metal binding2591Calcium 2 By similarity
Binding site1681Substrate; via carbonyl oxygen By similarity
Site671Transition state stabilizer By similarity

Amino acid modifications

Modified residue301Pyrrolidone carboxylic acid By similarity
Glycosylation861N-linked (GlcNAc...) Potential
Glycosylation2171N-linked (GlcNAc...) Potential
Glycosylation2431N-linked (GlcNAc...) Potential
Disulfide bond40 ↔ 120 By similarity
Disulfide bond73 ↔ 78 By similarity
Disulfide bond126 ↔ 329 By similarity
Disulfide bond206 ↔ 238 By similarity

Sequences

Sequence LengthMass (Da)Tools
O80912-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 74A1C6F71A415169

FASTA34938,100
        10         20         30         40         50         60 
MGFSSSLSCS AMGALIVGCL LLQASNSNAQ LRPDFYFRTC PPIFNIIGDT IVNELRTDPR 

        70         80         90        100        110        120 
IAASLLRLHF HDCFVRGCDA SILLDNSTSF RTEKDAAPNK NSVRGFDVID RMKAAIERAC 

       130        140        150        160        170        180 
PRTVSCADII TIASQISVLL SGGPWWPVPL GRRDSVEAFF ALANTALPSP FSTLTQLKTA 

       190        200        210        220        230        240 
FADVGLNRPS DLVALSGGHT FGKAQCQFVT PRLYNFNGTN RPDPSLNPTY LVELRRLCPQ 

       250        260        270        280        290        300 
NGNGTVLVNF DSVTPTTFDR QYYTNLLNGK GLIQSDQVLF STPGADTIPL VNQYSSNTFV 

       310        320        330        340 
FFGAFVDAMI RMGNLKPLTG TQGEIRQNCR VVNPRIRVVE NDDGVVSSI 

« Hide

References

« Hide 'large scale' references
[1]"Structural diversity and transcription of class III peroxidases from Arabidopsis thaliana."
Welinder K.G., Justesen A.F., Kjaersgaard I.V.H., Jensen R.B., Rasmussen S.K., Jespersen H.M., Duroux L.
Eur. J. Biochem. 269:6063-6081(2002) [PubMed: 12473102] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
Tissue: Root.
[2]"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.
[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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Coordinated plant defense responses in Arabidopsis revealed by microarray analysis."
Schenk P.M., Kazan K., Wilson I., Anderson J.P., Richmond T., Somerville S.C., Manners J.M.
Proc. Natl. Acad. Sci. U.S.A. 97:11655-11660(2000) [PubMed: 11027363] [Abstract]
Cited for: INDUCTION.
Strain: cv. Columbia.
[5]"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

AF452385 mRNA. Translation: AAL40849.1.
AC004683 Genomic DNA. Translation: AAC28765.1.
AY099555 mRNA. Translation: AAM20407.1.
BT001238 mRNA. Translation: AAN65125.1.
PIRT02506.
RefSeqNP_181373.1.
UniGeneAt.28466

3D structure databases

HSSPHSSP built from PDB template 1GWU based on UniProtKB P00433.
ModBaseSearch...

Protein family/group databases

PeroxiBase116. AtPrx23.

Genome annotation databases

GeneID818420.
GenomeReviewsGene locus AT2G38390 in contig CT485783_GR.
KEGGath:AT2G38390.
NMPDRfig|3702.1.peg.10952.

Organism-specific databases

GeneFarm1847. 61.
TAIRAt2g38390.

Gene expression databases

ArrayExpressO80912.
GermOnlineAT2G38390. Arabidopsis thaliana.

Family and domain databases

InterProIPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
[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 namePER23_ARATH
AccessionPrimary (citable) accession number: O80912
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: November 1, 1998
Last modified: November 25, 2008
This is version 72 of the entry and version 1 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