Reviewed, UniProtKB/Swiss-Prot Q9FLC0 (PER52_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxidase 52
      Short name=Atperox P52
    EC=1.11.1.7
Alternative name(s):
    ATP49

Gene names

Name:	PER52
Synonyms:	P52
Ordered Locus Names:	At5g05340
ORF Names:	K18I23.14

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	324 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	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.
Miscellaneous	There are 73 peroxidase genes in A.thaliana.
Sequence similarities	Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	apoplast Inferred from direct assay. Source: TAIR cell wall Inferred from direct assay. Source: TAIR
Molecular function	calcium 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 324	304	Peroxidase 52		PRO_0000023717
Sites
	Active site	70	1	Proton acceptor By similarity
	Metal binding	71	1	Calcium 1 By similarity
	Metal binding	74	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	76	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	78	1	Calcium 1 By similarity
	Metal binding	80	1	Calcium 1 By similarity
	Metal binding	197	1	Iron (heme axial ligand) By similarity
	Metal binding	198	1	Calcium 2 By similarity
	Metal binding	244	1	Calcium 2 By similarity
	Metal binding	247	1	Calcium 2 By similarity
	Metal binding	252	1	Calcium 2 By similarity
	Binding site	167	1	Substrate; via carbonyl oxygen By similarity
	Site	66	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	213	1	N-linked (GlcNAc...) Potential
	Disulfide bond	39 ↔ 119		By similarity
	Disulfide bond	72 ↔ 77		By similarity
	Disulfide bond	125 ↔ 320		By similarity
	Disulfide bond	204 ↔ 229		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9FLC0-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: F891CD4EEEEC5AD4	FASTA	324	34,215
	10 20 30 40 50 60 MASNKLISIL VLVVTLLLQG DNNYVVEAQL TTNFYSTSCP NLLSTVQTAV KSAVNSEARM 70 80 90 100 110 120 GASILRLFFH DCFVNGCDGS ILLDDTSSFT GEQNAAPNRN SARGFNVIDN IKSAVEKACP 130 140 150 160 170 180 GVVSCADILA IAARDSVVAL GGPNWNVKVG RRDARTASQA AANSNIPAPT SSLSQLISSF 190 200 210 220 230 240 SAVGLSTRDM VALSGAHTIG QSRCTNFRAR IYNETNINAA FATTRQRTCP RASGSGDGNL 250 260 270 280 290 300 APLDVTTAAS FDNNYFKNLM TQRGLLHSDQ VLFNGGSTDS IVRGYSNNPS SFNSDFTAAM 310 320 IKMGDISPLT GSSGEIRKVC GRTN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones." Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N., Tabata S. DNA Res. 5:131-145(1998) [PubMed: 9679202] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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. , 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.
[3]	"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
EMBLGenBankDDBJ	AB010692 Genomic DNA. Translation: BAB09977.1. AY065270 mRNA. Translation: AAL38746.1.
IPI	IPI00527468.
RefSeq	NP_196153.1.
UniGene	At.28537
3D structure databases
HSSP	HSSP built from PDB template 1SCH based on UniProtKB P22195.
ModBase	Search...
Protein family/group databases
PeroxiBase	218. AtPrx52.
Proteomic databases
PRIDE	Q9FLC0.
Genome annotation databases
GeneID	830416.
GenomeReviews	Gene locus AT5G05340 in contig BA000015_GR.
KEGG	ath:AT5G05340.
NMPDR	fig|3702.1.peg.22639.
Organism-specific databases
GeneFarm	1905. 61.
TAIR	At5g05340.
Phylogenomic databases
OMA	Q9FLC0. TNFRARI.
Enzyme and pathway databases
BRENDA	1.11.1.7. 302.
Gene expression databases
ArrayExpress	Q9FLC0.
GermOnline	AT5G05340. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002016. Haem_peroxidase_pln/fun/bac. IPR000823. Peroxidase_pln. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00458. PEROXIDASE. PR00461. PLPEROXIDASE.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PER52_ARATH

Accession

Primary (citable) accession number: Q9FLC0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	March 1, 2001
Last modified:	June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)