[1]	NUCLEOTIDE SEQUENCE [MRNA], ENZYME REGULATION, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. STRAIN=cv. Nipponbare; DOI=10.1007/s10529-004-6587-0; PubMed=15685422 [NCBI, ExPASy, EBI, Israel, Japan] Lu Z., Takano T., Liu S.; "Purification and characterization of two ascorbate peroxidases of rice (Oryza sativa L.) expressed in Escherichia coli."; Biotechnol. Lett. 27:63-67(2005).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Nipponbare; Morita S., Kaminaka H., Masumura T., Tanaka K.; "The expression of two cytosolic ascorbate peroxidase genes in rice."; Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Nipponbare; The international rice genome sequencing project (IRGSP) consortium; "Oryza sativa nipponbare chromosome 7 genomic DNA sequence."; Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[4]	PROTEIN SEQUENCE OF 26-35. STRAIN=cv. Nipponbare; TISSUE=Anther, Panicle, and Stem; DOI=10.1093/nar/gkh020; PubMed=14681440 [NCBI, ExPASy, EBI, Israel, Japan] Komatsu S., Kojima K., Suzuki K., Ozaki K., Higo K.; "Rice proteome database based on two-dimensional polyacrylamide gel electrophoresis: its status in 2003."; Nucleic Acids Res. 32:D388-D392(2004).
[5]	NUCLEOTIDE SEQUENCE [MRNA] OF 202-251. TISSUE=Callus; Uchimiya H.; Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
[6]	TISSUE SPECIFICITY, AND INDUCTION. DOI=10.1016/j.gene.2003.08.017; PubMed=14644501 [NCBI, ExPASy, EBI, Israel, Japan] Agrawal G.K., Jwa N.-S., Iwahashi H., Rakwal R.; "Importance of ascorbate peroxidases OsAPX1 and OsAPX2 in the rice pathogen response pathways and growth and reproduction revealed by their transcriptional profiling."; Gene 322:93-103(2003).
[7]	NOMENCLATURE. DOI=10.1007/s00239-004-2666-z; PubMed=15599508 [NCBI, ExPASy, EBI, Israel, Japan] Teixeira F.K., Menezes-Benavente L., Margis R., Margis-Pinheiro M.; "Analysis of the molecular evolutionary history of the ascorbate peroxidase gene family: inferences from the rice genome."; J. Mol. Evol. 59:761-770(2004).

Comments

FUNCTION: Plays a key role in hydrogen peroxide removal.
CATALYTIC ACTIVITY: L-ascorbate + H₂O₂ = dehydroascorbate + 2 H₂O.
COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group (By similarity).
COFACTOR: Binds 1 potassium or calcium ion per subunit (By similarity).
ENZYME REGULATION: Inhibited by p-chloromercuriphenylsulfonic acid (CMPSA).

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=1 mM for ascorbate;
	K_M=0.7 mM for H₂O₂;
	V_max=20 mM/min/mg enzyme with ascorbate as substrate;
	V_max=3 mM/min/mg enzyme with H₂O₂ as substrate;
pH dependence:	Optimum pH is 6-7;

SUBCELLULAR LOCATION: Cytoplasm (Probable).
TISSUE SPECIFICITY: Expressed in aerial vegetative parts and reproductive organs.
INDUCTION: By stress and hormones. By infection with rice blast fungus (M.grisea). Circadian-regulation. Expression is higher during the light phase than during the dark phase.
SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB053297; BAB20889.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB050724; BAB17666.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP005199; BAC84063.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D25238; BAA04962.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

T04114; T04114.

NP_001060741.1; -.

3D structure databases

HSSP

Q43758; 1OAF. [HSSP ENTRY / PDB]

SMR

Q9FE01; 4-250.

ModBase

Q9FE01.

Protein family/group databases

PeroxiBase

1866; OsAPx02.

2D gel databases

ANU-2DPAGE

Q9FE01; -.

Organism-specific databases

Gramene

Q9FE01; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016688;	Molecular function: L-ascorbate peroxidase activity (inferred from electronic annotation from EC).
GO:0030955;	Molecular function: potassium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0042744;	Biological process: hydrogen peroxide catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002207; Asc_perxdse.
IPR002016; Haem_peroxidase_pln/fun/bac.
Graphical view of domain structure.

Pfam

PF00141; peroxidase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00459; ASPEROXIDASE.
PR00458; PEROXIDASE.

PROSITE

PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q9FE01.

Genome annotation databases

GeneID

4344397; -.

KEGG

osa:4344397; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calcium; Cytoplasm; Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Potassium; Stress response.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 251`	`251`	`L-ascorbate peroxidase 2, cytosolic.`	`PRO_0000055594`
`ACT_SITE`	`43 43`		`Proton acceptor (By similarity).`
`METAL`	`164 164`		`Iron (heme axial ligand) (By similarity).`
`METAL`	`165 165`		`Potassium or calcium (By similarity).`
`METAL`	`181 181`		`Potassium or calcium (By similarity).`
`METAL`	`183 183`		`Potassium or calcium (By similarity).`
`METAL`	`186 186`		`Potassium or calcium; via carbonyl oxygen (By similarity).`
`METAL`	`188 188`		`Potassium or calcium (By similarity).`
`SITE`	`39 39`	`1`	`Transition state stabilizer (By similarity).`
`CONFLICT`	`202 215`		`GLLQLPSDKALMAD -> PSSSCQVTKPSWLT (in Ref. 5).`

Sequence information

Length: 251 AA [This is the length of the unprocessed precursor]

Molecular weight: 27118 Da [This is the MW of the unprocessed precursor]

CRC64: D6497B224285DF93 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGSKSYPTVS DEYLAAVGKA KRKLRGLIAE KNCAPLMLRL AWHSAGTFDV SSRTGGPFGT 

        70         80         90        100        110        120 
MKNPGEQSHA ANAGLDIAVR LLDPIKDQLP ILSYADFYQL AGVVAVEVTG GPEVPFHPGR 

       130        140        150        160        170        180 
QDKPEPPPEG RLPDATQGSD HLRQVFSAQM GLSDKDIVAL SGGHTLGRCH KERSGFEGAW 

       190        200        210        220        230        240 
TSNPLIFDNS YFTELVSGEK EGLLQLPSDK ALMADPAFRP LVEKYAADED AFFADYAEAH 

       250 
LKLSELGFAE E

Q9FE01 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools