APX6_ORYSJ
ID APX6_ORYSJ Reviewed; 309 AA.
AC P0C0L1; A0A0N7KTN6; Q2QWY2;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Probable L-ascorbate peroxidase 6, chloroplastic/mitochondrial {ECO:0000305};
DE EC=1.11.1.11 {ECO:0000305};
DE AltName: Full=OsAPx6 {ECO:0000303|PubMed:15599508};
DE Flags: Precursor;
GN Name=APX6 {ECO:0000303|PubMed:15599508};
GN OrderedLocusNames=Os12g0178100 {ECO:0000312|EMBL:BAT16122.1},
GN LOC_Os12g07820 {ECO:0000312|EMBL:ABA96617.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
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=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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
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 [7]
RP SUBCELLULAR LOCATION, AND 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).
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 Evidence={ECO:0000305};
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: Plastid, chloroplast stroma {ECO:0000305}.
CC Mitochondrion {ECO:0000269|PubMed:16397796}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and flowers.
CC {ECO:0000269|PubMed:16397796}.
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; DP000011; ABA96617.1; -; Genomic_DNA.
DR EMBL; AP008218; BAF29324.1; -; Genomic_DNA.
DR EMBL; AP014968; BAT16122.1; -; Genomic_DNA.
DR EMBL; AK061107; BAG87732.1; -; mRNA.
DR EMBL; AK099201; BAG93994.1; -; mRNA.
DR RefSeq; XP_015618175.1; XM_015762689.1.
DR AlphaFoldDB; P0C0L1; -.
DR SMR; P0C0L1; -.
DR STRING; 4530.OS12T0178100-01; -.
DR PeroxiBase; 1870; OsAPx06.
DR PaxDb; P0C0L1; -.
DR PRIDE; P0C0L1; -.
DR EnsemblPlants; Os12t0178100-01; Os12t0178100-01; Os12g0178100.
DR GeneID; 4351663; -.
DR Gramene; Os12t0178100-01; Os12t0178100-01; Os12g0178100.
DR KEGG; osa:4351663; -.
DR eggNOG; ENOG502QS7Q; Eukaryota.
DR HOGENOM; CLU_036959_2_1_1; -.
DR InParanoid; P0C0L1; -.
DR OMA; QEIGRRP; -.
DR OrthoDB; 1228462at2759; -.
DR BRENDA; 1.11.1.11; 4460.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR Genevisible; P0C0L1; OS.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; 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: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; 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; PS50873; PEROXIDASE_4; 1.
PE 2: Evidence at transcript level;
KW Calcium; Chloroplast; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW Mitochondrion; Oxidoreductase; Peroxidase; Plastid; Potassium;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..32
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 33..309
FT /note="Probable L-ascorbate peroxidase 6,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000042656"
FT REGION 197..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 198
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 199
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT SITE 65
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ SEQUENCE 309 AA; 33502 MW; DB5600BC16FC0984 CRC64;
MAVVHRLLRR GLSAASPLPS LQELGRRPAS SSAAAAGDAA AELRGAREDV KQLLKSTSCH
PILVRLGWHD AGTYDKNITE WPKCGGANGS LRFEIELKHA ANAGLVNALK LIQPIKDKHA
GVTYADLFQL ASATAIEEAG GPKIPMIYGR VDVAAPEQCP PEGRLPAAGP PSPAEHLREV
FYRMGLSDKE IVALSGAHTL GRSRPERSGW GKPETKYTKN GPGAPGGQSW TSQWLKFDNS
YFKDIKERRD EDLLVLPTDA VLFEDSSFKI YAEKYAADQD AFFEDYAEAH AKLSNLGAKF
DPPKGISLE
