ID   APX1_ORYSI              Reviewed;         250 AA.
AC   A2XFC7; P93404; Q84QS3; Q8GZZ2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   02-SEP-2026, entry version 81.
DE   RecName: Full=L-ascorbate peroxidase 1, cytosolic;
DE            Short=APXa;
DE            EC=1.11.1.11;
DE   AltName: Full=OsAPx01;
GN   Name=APX1; ORFNames=OsI_010770;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Khao Dawk Mali 105;
RA   Duriyapong F., Peyachoknagul S., Apisitwanich S.;
RT   "Cloning of ascorbate peroxidase gene from indica rice, Khao Dawk Mali
RT   105.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
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., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., 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   [3]
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 peroxidase
RT   gene family: inferences from the rice genome.";
RL   J. Mol. Evol. 59:761-770(2004).
RN   [4]
RP   INDUCTION.
RX   PubMed=15832681; DOI=10.1016/j.jplph.2004.06.004;
RA   Tsai Y.-C., Hong C.-Y., Liu L.-F., Kao C.H.;
RT   "Expression of ascorbate peroxidase and glutathione reductase in roots of
RT   rice seedlings in response to NaCl and H2O2.";
RL   J. Plant Physiol. 162:291-299(2005).
CC   -!- FUNCTION: Plays a key role in hydrogen peroxide removal. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-ascorbate + H2O2 = L-dehydroascorbate + 2 H2O;
CC         Xref=Rhea:RHEA:22996, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:38290, ChEBI:CHEBI:58539; EC=1.11.1.11;
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: By salt stress and hydrogen peroxide.
CC       {ECO:0000269|PubMed:15832681}.
CC   -!- MISCELLANEOUS: Binds one cation per subunit; probably K(+), but might
CC       also be Ca(2+). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY254495; AAP13093.1; -; mRNA.
DR   EMBL; CM000128; EAY89537.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2XFC7; -.
DR   SMR; A2XFC7; -.
DR   STRING; 39946.A2XFC7; -.
DR   EnsemblPlants; BGIOSGA012372-TA; BGIOSGA012372-PA; BGIOSGA012372.
DR   Gramene; BGIOSGA012372-TA; BGIOSGA012372-PA; BGIOSGA012372.
DR   HOGENOM; CLU_036959_3_0_1; -.
DR   OMA; MAKNYPV; -.
DR   Proteomes; UP000007015; Chromosome 3.
DR   GO; GO:0009507; C:chloroplast; IEA:TreeGrafter.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0016688; F:L-ascorbate peroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:TreeGrafter.
DR   GO; GO:0000302; P:response to reactive oxygen species; IEA:TreeGrafter.
DR   CDD; cd00691; ascorbate_peroxidase; 1.
DR   FunFam; 1.10.520.10:FF:000003; Cytosolic ascorbate peroxidase; 1.
DR   FunFam; 1.10.420.10:FF:000003; L-ascorbate peroxidase, cytosolic; 1.
DR   Gene3D; 1.10.520.10; -; 1.
DR   Gene3D; 1.10.420.10; Peroxidase, domain 2; 1.
DR   InterPro; IPR044831; Ccp1-like.
DR   InterPro; IPR002016; Haem_peroxidase.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR002207; Peroxidase_I.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   PANTHER; PTHR31356:SF57; L-ASCORBATE PEROXIDASE 1, CYTOSOLIC; 1.
DR   PANTHER; PTHR31356; THYLAKOID LUMENAL 29 KDA PROTEIN, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00459; ASPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
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; Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Peroxidase; Potassium; Reference proteome; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..250
FT                   /note="L-ascorbate peroxidase 1, cytosolic"
FT                   /id="PRO_0000300257"
FT   REGION          113..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        42
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT                   ECO:0000255|PROSITE-ProRule:PRU10012"
FT   BINDING         163
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         164
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   SITE            38
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   CONFLICT        218
FT                   /note="C -> R (in Ref. 1; AAP13093)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   250 AA;  27103 MW;  7867C10191CC92E9 CRC64;
     MAKNYPVVSA EYQEAVEKAR QKLRALIAEK SCAPLMLRLA WHSAGTFDVS SKTGGPFGTM
     KTPAELSHAA NAGLDIAVRM LEPIKEEIPT ISYADFYQLA GVVAVEVSGG PAVPFHPGRE
     DKPAPPPEGR LPDATKGSDH LRQVFGAQMG LSDQDIVALS GGHTLGRCHK ERSGFEGPWT
     RNPLQFDNSY FTELLSGDKE GLLQLPSDKA LLSDPAFCPL VEKYAADEKA FFEDYKEAHL
     KLSELGFADA
//