APX1_ORYSI
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 03-AUG-2022, entry version 73.
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=H2O2 + L-ascorbate = 2 H2O + L-dehydroascorbate;
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 PRIDE; 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:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016688; F:L-ascorbate peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
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; PTHR31356; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00459; ASPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 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 COMPBIAS 121..137
FT /note="Basic and acidic residues"
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
