APX1_ORYSJ
ID APX1_ORYSJ Reviewed; 250 AA.
AC Q10N21; B7E6Z4; P93404; Q84QS3; Q8GZZ2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=L-ascorbate peroxidase 1, cytosolic {ECO:0000305};
DE Short=APXa {ECO:0000303|Ref.1};
DE EC=1.11.1.11 {ECO:0000269|PubMed:15685422};
DE AltName: Full=OsAPx1 {ECO:0000303|PubMed:15599508};
GN Name=APX1 {ECO:0000303|PubMed:15599508};
GN OrderedLocusNames=Os03g0285700 {ECO:0000312|EMBL:BAS83623.1},
GN LOC_Os03g17690 {ECO:0000312|EMBL:ABF95353.1};
GN ORFNames=OsJ_009999 {ECO:0000312|EMBL:EAZ26516.1},
GN OSJNBa0013D02.10 {ECO:0000312|EMBL:AAO17000.1};
OS Oryza sativa subsp. japonica (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=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Nipponbare; TISSUE=Seedling;
RA Morita S., Kaminaka H., Yokoi H., Masumura T., Tanaka K.;
RT "Cloning and characterization of cytosolic ascorbate peroxidase cDNA from
RT rice.";
RL (er) Plant Gene Register PGR97-012(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ilpoombyeo; TISSUE=Seed;
RA Yoon U.H., Kim Y.H.;
RT "Structural and expression analysis of germinating seed genes in Oryza
RT sativa L.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [4]
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 [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [7]
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., 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 [8]
RP PROTEIN SEQUENCE OF 2-11, AND INDUCTION.
RC STRAIN=cv. Nipponbare; TISSUE=Leaf;
RX PubMed=12203890;
RX DOI=10.1002/1615-9861(200208)2:8<947::aid-prot947>3.0.co;2-j;
RA Agrawal G.K., Rakwal R., Yonekura M., Kubo A., Saji H.;
RT "Proteome analysis of differentially displayed proteins as a tool for
RT investigating ozone stress in rice (Oryza sativa L.) seedlings.";
RL Proteomics 2:947-959(2002).
RN [9]
RP PROTEIN SEQUENCE OF 2-11; 25-34 AND 107-116, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Nipponbare;
RC TISSUE=Anther, Callus, Panicle, Root, Sheath, and Stem;
RX PubMed=14681440; DOI=10.1093/nar/gkh020;
RA Komatsu S., Kojima K., Suzuki K., Ozaki K., Higo K.;
RT "Rice proteome database based on two-dimensional polyacrylamide gel
RT electrophoresis: its status in 2003.";
RL Nucleic Acids Res. 32:D388-D392(2004).
RN [10]
RP INDUCTION.
RX PubMed=11181723; DOI=10.1093/jxb/52.354.145;
RA Sato Y., Murakami T., Funatsuki H., Matsuba S., Saruyama H., Tanida M.;
RT "Heat shock-mediated APX gene expression and protection against chilling
RT injury in rice seedlings.";
RL J. Exp. Bot. 52:145-151(2001).
RN [11]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14644501; DOI=10.1016/j.gene.2003.08.017;
RA Agrawal G.K., Jwa N.-S., Iwahashi H., Rakwal R.;
RT "Importance of ascorbate peroxidases OsAPX1 and OsAPX2 in the rice pathogen
RT response pathways and growth and reproduction revealed by their
RT transcriptional profiling.";
RL Gene 322:93-103(2003).
RN [12]
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 [13]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=15685422; DOI=10.1007/s10529-004-6587-0;
RA Lu Z., Takano T., Liu S.;
RT "Purification and characterization of two ascorbate peroxidases of rice
RT (Oryza sativa L.) expressed in Escherichia coli.";
RL Biotechnol. Lett. 27:63-67(2005).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=16397796; DOI=10.1007/s00425-005-0214-8;
RA Teixeira F.K., Menezes-Benavente L., Galvao V.C., Margis R.,
RA Margis-Pinheiro M.;
RT "Rice ascorbate peroxidase gene family encodes functionally diverse
RT isoforms localized in different subcellular compartments.";
RL Planta 224:300-314(2006).
RN [15]
RP INDUCTION BY HYDROGEN PEROXIDE.
RX PubMed=25546583; DOI=10.1016/j.jplph.2014.09.020;
RA Li Z., Su D., Lei B., Wang F., Geng W., Pan G., Cheng F.;
RT "Transcriptional profile of genes involved in ascorbate glutathione cycle
RT in senescing leaves for an early senescence leaf (esl) rice mutant.";
RL J. Plant Physiol. 176:1-15(2015).
CC -!- FUNCTION: Plays a key role in hydrogen peroxide removal.
CC {ECO:0000269|PubMed:15685422}.
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 Evidence={ECO:0000269|PubMed:15685422};
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 -!- ACTIVITY REGULATION: Inhibited by p-chloromercuriphenylsulfonic acid
CC (CMPSA). {ECO:0000269|PubMed:15685422}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4 mM for ascorbate {ECO:0000269|PubMed:15685422};
CC KM=0.3 mM for H(2)O(2) {ECO:0000269|PubMed:15685422};
CC Vmax=15 mM/min/mg enzyme with ascorbate as substrate
CC {ECO:0000269|PubMed:15685422};
CC Vmax=1 mM/min/mg enzyme with H(2)O(2) as substrate
CC {ECO:0000269|PubMed:15685422};
CC pH dependence:
CC Optimum pH is 6-7. {ECO:0000269|PubMed:15685422};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14681440}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, aerial vegetative parts and
CC reproductive organs (PubMed:14644501, Ref.1). Expressed in roots,
CC leaves, stems and flowers (PubMed:16397796).
CC {ECO:0000269|PubMed:14644501, ECO:0000269|PubMed:16397796,
CC ECO:0000269|Ref.1}.
CC -!- INDUCTION: By stress and hormones. By infection with rice blast fungus
CC (M.grisea). Circadian-regulation. Expression is higher during the light
CC phase than during the dark phase. Induced by hydrogen peroxide in
CC leaves (PubMed:25546583). {ECO:0000269|PubMed:11181723,
CC ECO:0000269|PubMed:12203890, ECO:0000269|PubMed:14644501,
CC ECO:0000269|PubMed:25546583}.
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; D45423; BAA08264.1; -; mRNA.
DR EMBL; GQ848050; ADM86863.1; -; mRNA.
DR EMBL; AC134232; AAO17000.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF95353.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11683.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS83623.1; -; Genomic_DNA.
DR EMBL; CM000140; EAZ26516.1; -; Genomic_DNA.
DR EMBL; AK061841; BAG88141.1; -; mRNA.
DR PIR; T03595; T03595.
DR RefSeq; XP_015630498.1; XM_015775012.1.
DR AlphaFoldDB; Q10N21; -.
DR SMR; Q10N21; -.
DR STRING; 4530.OS03T0285700-01; -.
DR PeroxiBase; 1865; OsAPx01.
DR PaxDb; Q10N21; -.
DR PRIDE; Q10N21; -.
DR EnsemblPlants; Os03t0285700-01; Os03t0285700-01; Os03g0285700.
DR GeneID; 4332474; -.
DR Gramene; Os03t0285700-01; Os03t0285700-01; Os03g0285700.
DR KEGG; osa:4332474; -.
DR eggNOG; ENOG502QR1E; Eukaryota.
DR HOGENOM; CLU_036959_3_0_1; -.
DR InParanoid; Q10N21; -.
DR OMA; MAKNYPV; -.
DR OrthoDB; 1228462at2759; -.
DR BRENDA; 1.11.1.11; 4460.
DR SABIO-RK; Q10N21; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q10N21; OS.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
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:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0000302; P:response to reactive oxygen species; IBA:GO_Central.
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 1: Evidence at protein level;
KW Calcium; Cytoplasm; Direct protein sequencing; Heme; Hydrogen peroxide;
KW Iron; Metal-binding; Oxidoreductase; Peroxidase; Potassium;
KW Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12203890,
FT ECO:0000269|PubMed:14681440"
FT CHAIN 2..250
FT /note="L-ascorbate peroxidase 1, cytosolic"
FT /id="PRO_0000055593"
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"
SQ SEQUENCE 250 AA; 27156 MW; 637D70B191CC92E9 CRC64;
MAKNYPVVSA EYQEAVEKAR QKLRALIAEK SCAPLMLRLA WHSAGTFDVS SKTGGPFGTM
KTPAELSHAA NAGLDIAVRM LEPIKEEIPT ISYADFYQLA GVVAVEVSGG PAVPFHPGRE
DKPAPPPEGR LPDATKGSDH LRQVFGAQMG LSDQDIVALS GGHTLGRCHK ERSGFEGPWT
RNPLQFDNSY FTELLSGDKE GLLQLPSDKA LLSDPAFRPL VEKYAADEKA FFEDYKEAHL
KLSELGFADA
