ID   APX3_ORYSJ              Reviewed;         291 AA.
AC   Q0JEQ2; Q6TY83; Q7XWZ7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   05-MAY-2009, entry version 25.
DE   RecName: Full=Probable L-ascorbate peroxidase 3;
DE            EC=1.11.1.11;
DE   AltName: Full=OsAPx03;
GN   Name=APX3; OrderedLocusNames=Os04g0223300, LOC_Os04g14680;
GN   ORFNames=OSJNBb0072N21.2, OsJ_013310;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Ehrhartoideae; Oryzeae; Oryza.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   MEDLINE=22337377; PubMed=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J.,
RA   Liu Y., Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y.,
RA   Weng Q., Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D.,
RA   Liu X., Lu T., Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J.,
RA   Wu M., Zhang R., Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H.,
RA   Cai Z., Ren S., Lv G., Gu W., Zhu G., Tu Y., Jia J., Zhang Y.,
RA   Chen J., Kang H., Chen X., Shao C., Sun Y., Hu Q., Zhang X., Zhang W.,
RA   Wang L., Ding C., Sheng H., Gu J., Chen S., Ni L., Zhu F., Chen W.,
RA   Lan L., Lai Y., Cheng Z., Gu M., Jiang J., Li J., Hong G., Xue Y.,
RA   Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=17210932; DOI=10.1101/gr.5509507;
RG   The rice annotation project (RAP);
RT   "Curated genome annotation of Oryza sativa ssp. japonica and
RT   comparative genome analysis with Arabidopsis thaliana.";
RL   Genome Res. 17:175-183(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H.,
RA   Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
RA   Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
RA   Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
RA   Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
RA   Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
RA   Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
RA   Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
RA   Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
RA   Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA   Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA   Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA   Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
RA   Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   NOMENCLATURE.
RX   PubMed=15599508; DOI=10.1007/s00239-004-2666-z;
RA   Teixeira F.K., Menezes-Benavente L., Margis R., Margis-Pinheiro M.;
RT   "Analysis of the molecular evolutionary history of the ascorbate
RT   peroxidase gene family: inferences from the rice genome.";
RL   J. Mol. Evol. 59:761-770(2004).
CC   -!- FUNCTION: Plays a key role in hydrogen peroxide removal (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: L-ascorbate + H(2)O(2) = dehydroascorbate + 2
CC       H(2)O.
CC   -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group (By
CC       similarity).
CC   -!- COFACTOR: Binds 1 potassium or calcium ion per subunit (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC       subfamily.
CC   -!- CAUTION: According to PubMed:15599508, it may be peroxisomal.
CC       There is however no experimental evidence to prove this.
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DR   EMBL; AL606634; CAD39836.2; -; Genomic_DNA.
DR   EMBL; AP008210; BAF14185.1; -; Genomic_DNA.
DR   EMBL; CM000141; EAZ29827.1; -; Genomic_DNA.
DR   RefSeq; NP_001052271.1; -.
DR   UniGene; Os.4987; -.
DR   HSSP; P48534; 1APX.
DR   PeroxiBase; 1867; OsAPx03.
DR   GeneID; 4335202; -.
DR   KEGG; osa:4335202; -.
DR   Gramene; Q6TY83; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0016688; F:L-ascorbate peroxidase activity; IEA:EC.
DR   GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002207; Asc_perxdse.
DR   InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00459; ASPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Heme; Hydrogen peroxide; Iron; Membrane; Metal-binding;
KW   Oxidoreductase; Peroxidase; Potassium; Transmembrane.
FT   CHAIN         1    291       Probable L-ascorbate peroxidase 3.
FT                                /FTId=PRO_0000055595.
FT   TRANSMEM    263    283       Potential.
FT   ACT_SITE     41     41       Proton acceptor (By similarity).
FT   METAL       161    161       Iron (heme axial ligand) (By similarity).
FT   METAL       162    162       Potassium or calcium (By similarity).
FT   METAL       178    178       Potassium or calcium (By similarity).
FT   METAL       185    185       Potassium or calcium (By similarity).
FT   SITE         37     37       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   291 AA;  32048 MW;  53CCEA0D39781236 CRC64;
     MSAAPVVDAE YMAEVERARR DLRALIASKS CAPIMLRLAW HDAGTYDKAT KTGGPNGSIR
     FPQEYSHAAN AGIKIAIDLL EPMKQKHPKI TYADLYQLAG VVAVEVTGGP TIDYVPGRRD
     SSDSPEEGRL PDAKKGAAHL REVFYRMGLS DKDIVALSGG HTLGKARPER SGFDGAWTKD
     PLKFDNSYFI ELLKENSEGL LKLPTDKALV EDPTFRRYVE LYAKDEDAFF RDYAESHKKL
     SELGFTPPRS AFIYKSCQKP KSLLMQTAAG VAVAAAVVAW AYLCESNKRL G
//