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Q9SZB9 (PER47_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 85. 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 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)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length325 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.

Developmental stage

Up-regulated during leaf development. Ref.5

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 AAL40837.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAB38800.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAB80059.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Heme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processresponse to oxidative stress

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionheme binding

Inferred from electronic annotation. Source: InterPro

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 – 3636 Potential
Chain37 – 325289Peroxidase 47
PRO_0000023713

Sites

Active site771Proton acceptor By similarity
Metal binding781Calcium 1 By similarity
Metal binding831Calcium 1; via carbonyl oxygen By similarity
Metal binding851Calcium 1 By similarity
Metal binding871Calcium 1 By similarity
Metal binding2021Iron (heme axial ligand) By similarity
Metal binding2031Calcium 2 By similarity
Metal binding2461Calcium 2 By similarity
Metal binding2481Calcium 2 By similarity
Metal binding2531Calcium 2 By similarity
Binding site1721Substrate; via carbonyl oxygen By similarity
Site731Transition state stabilizer By similarity

Amino acid modifications

Glycosylation1771N-linked (GlcNAc...) Potential
Disulfide bond46 ↔ 125 By similarity
Disulfide bond79 ↔ 84 By similarity
Disulfide bond131 ↔ 321 By similarity
Disulfide bond209 ↔ 235 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9SZB9 [UniParc].

Last modified May 31, 2011. Version 2.
Checksum: 786CFEE1E476A6AD

FASTA32535,975
        10         20         30         40         50         60 
MLTRFKKQNN KMVRANIVSM VLLMHAIVGF PFHARGLSMT YYMMSCPFAE QIVKNSVNNA 

        70         80         90        100        110        120 
LQADPTLAAG LIRMLFHDCF IEGCDASILL DSTKDNTAEK DSPANLSLRG YEIIDDAKEK 

       130        140        150        160        170        180 
IENRCPGVVS CADIVAMAAR DAVFWAGGPY YDIPKGRFDG KRSKIEDTRN LPSPFLNASQ 

       190        200        210        220        230        240 
LIQTFGQRGF TPQDVVALSG AHTLGVARCS SFKARLTVPD SSLDSTFANT LSKTCSAGDN 

       250        260        270        280        290        300 
AEQPFDATRN DFDNAYFNAL QMKSGVLFSD QTLFNTPRTR NLVNGYALNQ AKFFFDFQQA 

       310        320 
MRKMSNLDVK LGSQGEVRQN CRSIN

« 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.
[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]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Arabidopsis ORF clones."
De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"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.
[6]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF451951 mRNA. Translation: AAL40837.1. Different initiation.
AL035678 Genomic DNA. Translation: CAB38800.1. Different initiation.
AL161583 Genomic DNA. Translation: CAB80059.1. Different initiation.
CP002687 Genomic DNA. Translation: AEE86222.1.
BT044614 mRNA. Translation: ACI31314.1.
IPIIPI00539387.
PIRT05993.
RefSeqNP_567919.1. NM_119496.3.
UniGeneAt.28650.

3D structure databases

ProteinModelPortalQ9SZB9.
SMRQ9SZB9. Positions 43-315.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9SZB9.

Protein family/group databases

PeroxiBase213. AtPrx47.

Proteomic databases

PRIDEQ9SZB9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G33420.1; AT4G33420.1; AT4G33420.
GeneID829479.
GenomeReviewsGene locus AT4G33420 in contig CT486007_GR.
KEGGath:AT4G33420.
NMPDRfig|3702.1.peg.21384.

Organism-specific databases

GeneFarm1879. 61.
TAIRAt4g33420.

Phylogenomic databases

GeneTreeEPGT00050000003124.
HOGENOMHBG597790.
InParanoidQ9SZB9.

Gene expression databases

GenevestigatorQ9SZB9.
GermOnlineAT4G33420. 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]
KOK00430.
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 namePER47_ARATH
AccessionPrimary (citable) accession number: Q9SZB9
Secondary accession number(s): B5X0P5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: May 31, 2011
Last modified: December 14, 2011
This is version 85 of the entry and version 2 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