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Q9SD46 (PER36_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 36
Short name=Atperox P36
EC=1.11.1.7
Gene names
Name:PER36
Synonyms:P36
Ordered Locus Names:At3g50990
ORF Names:F24M12.30
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 length344 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.

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 CAB62621.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Heme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 2828 Potential
Chain29 – 344316Peroxidase 36
PRO_0000023702

Sites

Active site811Proton acceptor By similarity
Metal binding821Calcium 1 By similarity
Metal binding851Calcium 1; via carbonyl oxygen By similarity
Metal binding871Calcium 1; via carbonyl oxygen By similarity
Metal binding891Calcium 1 By similarity
Metal binding911Calcium 1 By similarity
Metal binding2081Iron (heme axial ligand) By similarity
Metal binding2091Calcium 2 By similarity
Metal binding2601Calcium 2 By similarity
Metal binding2631Calcium 2 By similarity
Metal binding2681Calcium 2 By similarity
Binding site1781Substrate; via carbonyl oxygen By similarity
Site771Transition state stabilizer By similarity

Amino acid modifications

Glycosylation2241N-linked (GlcNAc...) Potential
Disulfide bond50 ↔ 130 By similarity
Disulfide bond83 ↔ 88 By similarity
Disulfide bond136 ↔ 337 By similarity
Disulfide bond215 ↔ 247 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9SD46 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: 0D86D9CE285EAB13

FASTA34438,237
        10         20         30         40         50         60 
MNTKTVKSMA GIVLSQISLV ALFPLCICYQ THQSTSSVAS LSPQFYENSC PNAQAIVQSY 

        70         80         90        100        110        120 
VANAYFNDPR MAASILRLHF HDCFVNGCDA SVLLDSSGTM ESEKRSNANR DSARGFEVID 

       130        140        150        160        170        180 
EIKSALENEC PETVSCADLL ALVARDSIVI CGGPSWEVYL GRRDAREASL IGSMENIPSP 

       190        200        210        220        230        240 
ESTLQTILTM FNFQGLDLTD LVALLGSHTI GNSRCIGFRQ RLYNHTGNND PDQTLNQDYA 

       250        260        270        280        290        300 
SMLQQGCPIS GNDQNLFNLD YVTPTKFDNY YYKNLVNFRG LLSSDEILFT QSIETMEMVK 

       310        320        330        340 
YYAENEGAFF EQFAKSMVKM GNISPLTGTD GEIRRICRRV NHDV

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed: 11130713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"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] OF 9-344.
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL132980 Genomic DNA. Translation: CAB62621.1. Different initiation.
CP002686 Genomic DNA. Translation: AEE78735.1.
AK229843 mRNA. Translation: BAF01672.1.
AK229896 mRNA. Translation: BAF01724.1.
AK229990 mRNA. Translation: BAF01814.1.
AK230084 mRNA. Translation: BAF01904.1.
BT010535 mRNA. Translation: AAQ65158.1.
IPIIPI00519412.
PIRT45730.
RefSeqNP_190668.2. NM_114959.3.
UniGeneAt.35434.

3D structure databases

ProteinModelPortalQ9SD46.
SMRQ9SD46. Positions 40-343.
ModBaseSearch...

Protein family/group databases

PeroxiBase202. AtPrx36.

Proteomic databases

PRIDEQ9SD46.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G50990.1; AT3G50990.1; AT3G50990.
GeneID824263.
GenomeReviewsGene locus AT3G50990 in contig BA000014_GR.
KEGGath:AT3G50990.
NMPDRfig|3702.1.peg.16350.

Organism-specific databases

GeneFarm1863. 61.
TAIRAt3g50990.

Phylogenomic databases

GeneTreeEPGT00070000027987.
HOGENOMHBG597790.
InParanoidQ9SD46.
OMASALENEC.
PhylomeDBQ9SD46.
ProtClustDBCLSN2918824.

Gene expression databases

ArrayExpressQ9SD46.
GenevestigatorQ9SD46.
GermOnlineAT3G50990. 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]
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 namePER36_ARATH
AccessionPrimary (citable) accession number: Q9SD46
Secondary accession number(s): Q0WLV3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: June 26, 2007
Last modified: December 14, 2011
This is version 86 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