Reviewed, UniProtKB/Swiss-Prot O22959 (PER19_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxidase 19
      Short name=Atperox P19
    EC=1.11.1.7
Alternative name(s):
    ATP51

Gene names

Name:	PER19
Synonyms:	P19
Ordered Locus Names:	At2g34060
ORF Names:	T14G11.18

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	346 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 – 31	31	Potential
	Chain	32 – 346	315	Peroxidase 19		PRO_0000023685
Sites
	Active site	82	1	Proton acceptor By similarity
	Metal binding	83	1	Calcium 1 By similarity
	Metal binding	86	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	88	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	90	1	Calcium 1 By similarity
	Metal binding	92	1	Calcium 1 By similarity
	Metal binding	212	1	Iron (heme axial ligand) By similarity
	Metal binding	213	1	Calcium 2 By similarity
	Metal binding	265	1	Calcium 2 By similarity
	Metal binding	268	1	Calcium 2 By similarity
	Metal binding	273	1	Calcium 2 By similarity
	Binding site	182	1	Substrate; via carbonyl oxygen By similarity
	Site	78	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	185	1	N-linked (GlcNAc...) Potential
	Disulfide bond	51 ↔ 134		By similarity
	Disulfide bond	84 ↔ 89		By similarity
	Disulfide bond	140 ↔ 342		By similarity
	Disulfide bond	219 ↔ 251		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O22959-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 85D43E7B4C17A814	FASTA	346	38,228
	10 20 30 40 50 60 MHVISLSLSS IFFFLFLTST ILISPVQPTT SKPPAPRPHR ELSADYYSKK CPQLETLVGS 70 80 90 100 110 120 VTSQRFKEVP ISAPATIRLF FHDCFVEGCD GSILIETKKG SKKLAEREAY ENKELREEGF 130 140 150 160 170 180 DSIIKAKALV ESHCPSLVSC SDILAIAARD FIHLAGGPYY QVKKGRWDGK RSTAKNVPPN 190 200 210 220 230 240 IPRSNSTVDQ LIKLFASKGL TVEELVVLSG SHTIGFAHCK NFLGRLYDYK GTKRPDPSLD 250 260 270 280 290 300 QRLLKELRMS CPFSGGSSGV VLPLDATTPF VFDNGYFTGL GTNMGLLGSD QALFLDPRTK 310 320 330 340 PIALEMARDK QKFLKAFGDA MDKMGSIGVK RGKRHGEIRT DCRVFL

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	AC002341 Genomic DNA. Translation: AAB67624.1. AY080602 mRNA. Translation: AAL86286.1. BT002341 mRNA. Translation: AAN86174.1.
IPI	IPI00536410.
PIR	H84751.
RefSeq	NP_180953.1.
UniGene	At.37862
3D structure databases
HSSP	HSSP built from PDB template 1QGJ based on UniProtKB Q39034.
ModBase	Search...
Protein family/group databases
PeroxiBase	100. AtPrx19.
Proteomic databases
PRIDE	O22959.
Genome annotation databases
GeneID	817967.
GenomeReviews	Gene locus AT2G34060 in contig CT485783_GR.
KEGG	ath:AT2G34060.
NMPDR	fig|3702.1.peg.10493.
Organism-specific databases
GeneFarm	1843. 61.
TAIR	At2g34060.
Phylogenomic databases
OMA	O22959. KGRWDGK.
Enzyme and pathway databases
BRENDA	1.11.1.7. 302.
Gene expression databases
ArrayExpress	O22959.
GermOnline	AT2G34060. 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

PER19_ARATH

Accession

Primary (citable) accession number: O22959
Secondary accession number(s): Q8RXZ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)