Reviewed, UniProtKB/Swiss-Prot A2YPX3 (PER2_ORYSI)

Names and origin

Protein names

Recommended name:
    Peroxidase 2
    EC=1.11.1.7

Gene names

Name:	PRX112
Synonyms:	POXGX9
ORF Names:	OsI_026366

Organism

Oryza sativa subsp. indica (Rice)

Taxonomic identifier

39946 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza

Protein attributes

Sequence length	314 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Removal of H(2)O(2), 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 + H(2)O(2) = oxidized donor + 2 H(2)O.
Cofactor	Binds 2 calcium ions per subunit. Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
Subcellular location	SecretedBy similarity.
Sequence similarities	Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.
Sequence caution	The sequence EAZ05134.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Glycoprotein Pyrrolidone carboxylic acid
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-KW
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 iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW peroxidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 314	291	Peroxidase 2		PRO_0000300259
Sites
	Active site	65	1	Proton acceptor By similarity
	Metal binding	66	1	Calcium 1 By similarity
	Metal binding	69	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	71	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	73	1	Calcium 1 By similarity
	Metal binding	75	1	Calcium 1 By similarity
	Metal binding	187	1	Iron (heme axial ligand) By similarity
	Metal binding	188	1	Calcium 2 By similarity
	Metal binding	234	1	Calcium 2 By similarity
	Metal binding	237	1	Calcium 2 By similarity
	Metal binding	242	1	Calcium 2 By similarity
	Binding site	157	1	Substrate; via carbonyl oxygen By similarity
	Site	61	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	24	1	Pyrrolidone carboxylic acid Potential
	Glycosylation	148	1	N-linked (GlcNAc...) Potential
	Glycosylation	169	1	N-linked (GlcNAc...) Potential
	Glycosylation	203	1	N-linked (GlcNAc...) Potential
	Glycosylation	274	1	N-linked (GlcNAc...) Potential
	Glycosylation	309	1	N-linked (GlcNAc...) Potential
	Disulfide bond	34 ↔ 109		By similarity
	Disulfide bond	67 ↔ 72		By similarity
	Disulfide bond	115 ↔ 310		By similarity
	Disulfide bond	194 ↔ 219		By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2YPX3-1 [UniParc]. Last modified September 11, 2007. Version 2. Checksum: 232C913657D6C7FB	FASTA	314	32,634
	10 20 30 40 50 60 MASASSVSLM LLVAAAMASA ASAQLSATFY DTSCPNALST IKSAVTAAVN SEPRMGASLV 70 80 90 100 110 120 RLHFHDCFVQ GCDASVLLSG QEQNAGPNAG SLRGFNVVDN IKTQVEAICS QTVSCADILA 130 140 150 160 170 180 VAARDSVVAL GGPSWTVLLG RRDSTTANES QANTDLPAPS SSLAELIGNF SRKGLDVTDM 190 200 210 220 230 240 VALSGAHTIG QAQCQNFRDR LYNETNIDSS FATALKANCP RPTGSGDSNL APLDTTTPNA 250 260 270 280 290 300 FDSAYYTNLL SNKGLLHSDQ VLFNGGSTDN TVRNFSSNTA AFNSAFTVAM VKMGNISPLT 310 GTQGQIRLNC SKVN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Differential induction of a peroxidase gene family during infection of rice by Xanthomonas oryzae pv. oryzae." Chittoor J.M., Leach J.E., White F.F. Mol. Plant Microbe Interact. 10:861-871(1997) [PubMed: 9304860] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. IRBB10.
[2]	"The genomes of Oryza sativa: a history of duplications." Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H. PLoS Biol. 3:266-281(2005) [PubMed: 15685292] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. 93-11.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF014470 Genomic DNA. Translation: AAC49821.1. CM000132 Genomic DNA. Translation: EAZ05134.1. Sequence problems.
3D structure databases
HSSP	HSSP built from PDB template 1SCH based on UniProtKB P22195.
ModBase	Search...
Organism-specific databases
Gramene	P37835.
Family and domain databases
InterPro	IPR002016. Haem_peroxidase_pln/fun/bac. IPR000823. Peroxidase_pln. [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

PER2_ORYSI

Accession

Primary (citable) accession number: A2YPX3
Secondary accession number(s): O22441, P37835, Q7F1U3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	September 11, 2007
Last modified:	November 25, 2008
This is version 14 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)