Reviewed, UniProtKB/Swiss-Prot P0C0L0 (APX5_ORYSJ)

Names and origin

Protein names

Recommended name:
    Probable L-ascorbate peroxidase 5, chloroplastic
    EC=1.11.1.11
Alternative name(s):
    OsAPx05

Gene names

Name:	APX5
Ordered Locus Names:	Os12g0178200, LOC_Os12g07830

Organism

Oryza sativa subsp. japonica (Rice)

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	320 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	Plays a key role in hydrogen peroxide removal By similarity.
Catalytic activity	L-ascorbate + H(2)O(2) = dehydroascorbate + 2 H(2)O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group By similarity. Binds 1 potassium or calcium ion per subunit By similarity.
Subcellular location	Plastid › chloroplast stromaProbable.
Sequence similarities	Belongs to the peroxidase family. Ascorbate peroxidase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Calcium Heme Iron Metal-binding Potassium
Molecular function	Oxidoreductase Peroxidase
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	chloroplast Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-ascorbate peroxidase activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW potassium ion binding 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
	Transit peptide	1 – 42	42	Chloroplast Potential
	Chain	43 – 320	278	Probable L-ascorbate peroxidase 5, chloroplastic		PRO_0000042655
Sites
	Active site	80	1	Proton acceptor By similarity
	Metal binding	209	1	Iron (heme axial ligand) By similarity
	Metal binding	210	1	Potassium or calcium By similarity
	Metal binding	242	1	Potassium or calcium By similarity
	Metal binding	249	1	Potassium or calcium By similarity
	Site	76	1	Transition state stabilizer By similarity
Experimental info
	Sequence conflict	181	1	P → Q Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P0C0L0-1 [UniParc]. Last modified October 25, 2005. Version 1. Checksum: FE8CD65D291ACB2A	FASTA	320	34,759
	10 20 30 40 50 60 MAVVHRILRR GLSAASPLPS LRGLLLVSPQ ELGRRPASSS SSAAAAAGDV EAELRAARED 70 80 90 100 110 120 VRQLLKSNPC HPILVRLGWH DAGTYDKNIT EWPKCGGANG SLRFGVELVH AANKGLLKAL 130 140 150 160 170 180 FLVIPIKSKY AGVTYADIFQ LASATAIEEA GGPKIPMIYG RADVADGEEC PPEGRLPAAD 190 200 210 220 230 240 PPSPAEHLRE VFYRMGLSDK EIVALSGAHT LGRARPERSG WGKPETKYTE NGPGAPGGQS 250 260 270 280 290 300 WTSEWLKFDN SYFKEIKERR DEDLLVLPTD AVLFEDSSFK IHAEKYAEDQ DAFFEDYAEA 310 320 HAKLSNLGAK FDPPKGISLE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence of rice chromosomes 11 and 12, rich in disease resistance genes and recent gene duplications." The rice chromosomes 11 and 12 sequencing consortia BMC Biol. 3:20-20(2005) [PubMed: 16188032] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[2]	"Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice." The rice full-length cDNA consortium Science 301:376-379(2003) [PubMed: 12869764] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Nipponbare.
[3]	"Analysis of the molecular evolutionary history of the ascorbate peroxidase gene family: inferences from the rice genome." Teixeira F.K., Menezes-Benavente L., Margis R., Margis-Pinheiro M. J. Mol. Evol. 59:761-770(2004) [PubMed: 15599508] [Abstract] Cited for: NOMENCLATURE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL732376 Genomic DNA. No translation available. AK073910 mRNA. No translation available.
RefSeq	NP_001066306.1.
UniGene	Os.18504
3D structure databases
SMR	P0C0L0. Positions 47-320.
ModBase	Search...
Genome annotation databases
GeneID	4351664.
KEGG	osa:4351664.
Organism-specific databases
Gramene	P0C0L0.
Family and domain databases
InterPro	IPR002207. Asc_perxdse. IPR002016. Haem_peroxidase_pln/fun/bac. [Graphical view]
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00459. ASPEROXIDASE. PR00458. PEROXIDASE.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. False negative. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APX5_ORYSJ

Accession

Primary (citable) accession number: P0C0L0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	October 25, 2005
Last modified:	November 25, 2008
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)