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Reviewed, UniProtKB/Swiss-Prot Q9SUT2 (PER39_ARATH)

Last modified June 16, 2009. Version 70. 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 39
      Short name=Atperox P39
    EC=1.11.1.7
Alternative name(s):
    ATP19a
Gene names
Name: PER39
Synonyms: P39
Ordered Locus Names: At4g11290
ORF Names: F8L21.80
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 length326 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Tissue specificity

Slightly expressed in roots.

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

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 2323 Potential
Chain24 – 326303Peroxidase 39
PRO_0000023705

Sites

Active site651Proton acceptor By similarity
Metal binding661Calcium 1 By similarity
Metal binding691Calcium 1; via carbonyl oxygen By similarity
Metal binding711Calcium 1; via carbonyl oxygen By similarity
Metal binding731Calcium 1 By similarity
Metal binding751Calcium 1 By similarity
Metal binding1921Iron (heme axial ligand) By similarity
Metal binding1931Calcium 2 By similarity
Metal binding2451Calcium 2 By similarity
Metal binding2481Calcium 2 By similarity
Metal binding2531Calcium 2 By similarity
Binding site1621Substrate; via carbonyl oxygen By similarity
Site611Transition state stabilizer By similarity

Amino acid modifications

Modified residue241Pyrrolidone carboxylic acid By similarity
Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation1671N-linked (GlcNAc...) Potential
Glycosylation2081N-linked (GlcNAc...) Potential
Glycosylation2381N-linked (GlcNAc...) Potential
Disulfide bond34 ↔ 114 By similarity
Disulfide bond67 ↔ 72 By similarity
Disulfide bond120 ↔ 322 By similarity
Disulfide bond199 ↔ 232 By similarity

Experimental info

Sequence conflict171L → F Ref.1
Sequence conflict191T → I Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q9SUT2-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 523BC879A4A52BFF

FASTA32635,601
        10         20         30         40         50         60 
MTRFGLALLM ILVIQGLVTF SEAQLKMGFY DQTCPYAEKI VQDVVNQHIN NAPSLAAGLI 

        70         80         90        100        110        120 
RMHFHDCFVR GCDGSILINA TSSNQQVEKL APPNLTVRGF DFIDKVKSAL ESKCPGIVSC 

       130        140        150        160        170        180 
ADIITLATRD SIVAIGGPTW NVPTGRRDGR ISNFAEAMNN IPPPFGNFTT LITLFGNQGL 

       190        200        210        220        230        240 
DVKDLVLLSG AHTIGVSHCS SFSNRLFNFT GVGDQDPSLD SEYADNLKSR RCLSIADNTT 

       250        260        270        280        290        300 
KVEMDPGSRN TFDLSYYRLV LKRRGLFESD AALTMNPAAL AQVKRFAGGS EQEFFAEFSN 

       310        320 
SMEKMGRIGV KTGSDGEIRR TCAFVN

« Hide

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References

« Hide 'large scale' references
[1]"From expressed sequence tags to structure, function, evolution and expression of 28 ER-targeted Arabidopsis peroxidases."
Welinder K.G., Jespersen H.M., Kjaersgaard I.V.H., Justesen A.F., Oestergaard L., Abelskov A.K., Hansen L.N., Rasmussen S.K.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
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]"Computational analyses and annotations of the Arabidopsis peroxidase gene family."
Oestergaard L., Pedersen A.G., Jespersen H.M., Brunak S., Welinder K.G.
FEBS Lett. 433:98-102(1998) [PubMed: 9738941] [Abstract]
Cited for: CHARACTERIZATION.
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

X98805 mRNA. Translation: CAA67337.1.
AL096882 Genomic DNA. Translation: CAB51413.1.
AL161531 Genomic DNA. Translation: CAB81230.1.
IPIIPI00531288.
PIRT13020.
RefSeqNP_192868.1.
UniGeneAt.22642

3D structure databases

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

Protein family/group databases

PeroxiBase205. AtPrx39.

Proteomic databases

PRIDEQ9SUT2.

Genome annotation databases

GeneID826731.
GenomeReviewsGene locus AT4G11290 in contig CT486007_GR.
KEGGath:AT4G11290.
NMPDRfig|3702.1.peg.18797.

Organism-specific databases

GeneFarm1868. 61.
TAIRAt4g11290.

Phylogenomic databases

OMAQ9SUT2. QLKMGFY.

Enzyme and pathway databases

BRENDA1.11.1.7. 302.

Gene expression databases

ArrayExpressQ9SUT2.
GermOnlineAT4G11290. 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 namePER39_ARATH
AccessionPrimary (citable) accession number: Q9SUT2
Secondary accession number(s): Q96508
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: May 1, 2000
Last modified: June 16, 2009
This is version 70 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