Reviewed, UniProtKB/Swiss-Prot O80822 (PER25_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxidase 25
      Short name=Atperox P25
    EC=1.11.1.7

Gene names

Name:	PER25
Synonyms:	P25
Ordered Locus Names:	At2g41480
ORF Names:	T26J13.7

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	328 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	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 26	26	Potential
	Chain	27 – 328	302	Peroxidase 25		PRO_0000023691
Sites
	Active site	69	1	Proton acceptor
	Metal binding	70	1	Calcium 1 By similarity
	Metal binding	73	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	75	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	77	1	Calcium 1 By similarity
	Metal binding	79	1	Calcium 1 By similarity
	Metal binding	191	1	Iron (heme axial ligand) By similarity
	Metal binding	192	1	Calcium 2 By similarity
	Metal binding	243	1	Calcium 2 By similarity
	Metal binding	246	1	Calcium 2 By similarity
	Metal binding	251	1	Calcium 2 By similarity
	Binding site	161	1	Substrate; via carbonyl oxygen By similarity
	Site	65	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	207	1	N-linked (GlcNAc...) Potential
	Disulfide bond	38 ↔ 114		By similarity
	Disulfide bond	71 ↔ 76		By similarity
	Disulfide bond	120 ↔ 324		By similarity
	Disulfide bond	198 ↔ 230		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O80822-1 [UniParc]. Last modified November 25, 2002. Version 2. Checksum: 9CBE84061EBAFE3A	FASTA	328	35,886
	10 20 30 40 50 60 MGVYLGKYCY IMIIMLVLVL GKEVRSQLLK NGYYSTSCPK AESIVRSTVE SHFDSDPTIS 70 80 90 100 110 120 PGLLRLHFHD CFVQGCDGSV LIKGKSAEQA ALPNLGLRGL EVIDDAKARL EAVCPGVVSC 130 140 150 160 170 180 ADILALAARD SVDLSDGPSW RVPTGRKDGR ISLATEASNL PSPLDSVAVQ KQKFQDKGLD 190 200 210 220 230 240 THDLVTLLGA HTIGQTDCLF FRYRLYNFTV TGNSDPTISP SFLTQLKTLC PPNGDGSKRV 250 260 270 280 290 300 ALDIGSPSKF DESFFKNLRD GNAILESDQR LWSDAETNAV VKKYASRLRG LLGFRFDYEF 310 320 GKAMIKMSSI DVKTDVDGEV RKVCSKVN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [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	AC004625 Genomic DNA. Translation: AAC23733.1. Different initiation. AY139994 mRNA. Translation: AAM98136.1. BT008727 mRNA. Translation: AAP42740.1.
IPI	IPI00538575.
PIR	T02443.
3D structure databases
HSSP	HSSP built from PDB template 1QGJ based on UniProtKB Q39034.
ModBase	Search...
Protein family/group databases
PeroxiBase	118. AtPrx25.
Proteomic databases
PRIDE	O80822.
Genome annotation databases
GenomeReviews	Gene locus AT2G41480 in contig CT485783_GR.
NMPDR	fig|3702.1.peg.11286.
Organism-specific databases
GeneFarm	1851. 61.
TAIR	At2g41480.
Phylogenomic databases
OMA	O80822. GNSDPTI.
Enzyme and pathway databases
BRENDA	1.11.1.7. 302.
Gene expression databases
ArrayExpress	O80822.
GermOnline	AT2G41480. 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

PER25_ARATH

Accession

Primary (citable) accession number: O80822
Secondary accession number(s): Q8L728

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	November 25, 2002
Last modified:	June 16, 2009
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)