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Reviewed, UniProtKB/Swiss-Prot Q9SZB9 (PER47_ARATH)

Last modified June 16, 2009. Version 65. 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

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Names and origin

Protein namesRecommended name:
    Peroxidase 47
      Short name=Atperox P47
    EC=1.11.1.7
Alternative name(s):
    ATP32
Gene names
Name: PER47
Synonyms: P47
Ordered Locus Names: At4g33420
ORF Names: F17M5.180
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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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.

Developmental stage

Up-regulated during leaf development. Ref.3

Miscellaneous

There are 73 peroxidase genes in A.thaliana.

Sequence similarities

Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

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Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Heme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

response to oxidative stress

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

electron carrier activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 314289Peroxidase 47
PRO_0000023713

Sites

Active site661Proton acceptor By similarity
Metal binding671Calcium 1 By similarity
Metal binding721Calcium 1; via carbonyl oxygen By similarity
Metal binding741Calcium 1 By similarity
Metal binding761Calcium 1 By similarity
Metal binding1911Iron (heme axial ligand) By similarity
Metal binding1921Calcium 2 By similarity
Metal binding2351Calcium 2 By similarity
Metal binding2371Calcium 2 By similarity
Metal binding2421Calcium 2 By similarity
Binding site1611Substrate; via carbonyl oxygen By similarity
Site621Transition state stabilizer By similarity

Amino acid modifications

Glycosylation1661N-linked (GlcNAc...) Potential
Disulfide bond35 ↔ 114 By similarity
Disulfide bond68 ↔ 73 By similarity
Disulfide bond120 ↔ 310 By similarity
Disulfide bond198 ↔ 224 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9SZB9-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: EF500FACD2FDA692

FASTA31434,585
        10         20         30         40         50         60 
MVRANIVSMV LLMHAIVGFP FHARGLSMTY YMMSCPFAEQ IVKNSVNNAL QADPTLAAGL 

        70         80         90        100        110        120 
IRMLFHDCFI EGCDASILLD STKDNTAEKD SPANLSLRGY EIIDDAKEKI ENRCPGVVSC 

       130        140        150        160        170        180 
ADIVAMAARD AVFWAGGPYY DIPKGRFDGK RSKIEDTRNL PSPFLNASQL IQTFGQRGFT 

       190        200        210        220        230        240 
PQDVVALSGA HTLGVARCSS FKARLTVPDS SLDSTFANTL SKTCSAGDNA EQPFDATRND 

       250        260        270        280        290        300 
FDNAYFNALQ MKSGVLFSDQ TLFNTPRTRN LVNGYALNQA KFFFDFQQAM RKMSNLDVKL 

       310 
GSQGEVRQNC RSIN

« Hide

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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.
[2]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed: 10617198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"Toward elucidating the global gene expression patterns of developing Arabidopsis: parallel analysis of 8300 genes by a high-density oligonucleotide probe array."
Zhu T., Budworth P., Han B., Brown D., Chang H.-S., Zou G., Wang X.
Plant Physiol. Biochem. 39:221-242(2001)
Cited for: DEVELOPMENTAL STAGE.
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: 12034502] [Abstract]
Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE.
Strain: cv. Columbia.

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Cross-references

Sequence databases

AF451951 mRNA. Translation: AAL40837.1.
AL035678 Genomic DNA. Translation: CAB38800.1.
AL161583 Genomic DNA. Translation: CAB80059.1.
IPIIPI00539387.
PIRT05993.

3D structure databases

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

Protein family/group databases

PeroxiBase213. AtPrx47.

Proteomic databases

PRIDEQ9SZB9.

Genome annotation databases

GenomeReviewsGene locus AT4G33420 in contig CT486007_GR.
NMPDRfig|3702.1.peg.21384.

Organism-specific databases

GeneFarm1879. 61.
TAIRAt4g33420.

Enzyme and pathway databases

BRENDA1.11.1.7. 302.

Gene expression databases

GermOnlineAT4G33420. 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...

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Entry information

Entry namePER47_ARATH
AccessionPrimary (citable) accession number: Q9SZB9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: May 1, 2000
Last modified: June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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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