ID A0A498HU70_MALDO Unreviewed; 579 AA.
AC A0A498HU70;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=L-ascorbate peroxidase {ECO:0000256|ARBA:ARBA00012940};
DE EC=1.11.1.11 {ECO:0000256|ARBA:ARBA00012940};
GN ORFNames=DVH24_029717 {ECO:0000313|EMBL:RXH74996.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH74996.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH74996.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH74996.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000939};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC subfamily. {ECO:0000256|ARBA:ARBA00006873}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXH74996.1}.
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DR EMBL; RDQH01000341; RXH74996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498HU70; -.
DR STRING; 3750.A0A498HU70; -.
DR EnsemblPlants; mRNA:MD15G0213100; mRNA:MD15G0213100; MD15G0213100.
DR EnsemblPlants; mRNA:MD15G0213200; mRNA:MD15G0213200; MD15G0213200.
DR Gramene; mRNA:MD15G0213100; mRNA:MD15G0213100; MD15G0213100.
DR Gramene; mRNA:MD15G0213200; mRNA:MD15G0213200; MD15G0213200.
DR Proteomes; UP000290289; Chromosome 15.
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 CDD; cd00691; ascorbate_peroxidase; 2.
DR Gene3D; 1.10.520.10; -; 2.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 2.
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:SF36; L-ASCORBATE PEROXIDASE 3; 1.
DR PANTHER; PTHR31356; THYLAKOID LUMENAL 29 KDA PROTEIN, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00459; ASPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 2.
DR PROSITE; PS00435; PEROXIDASE_1; 2.
DR PROSITE; PS00436; PEROXIDASE_2; 2.
DR PROSITE; PS50873; PEROXIDASE_4; 2.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000290289}.
FT DOMAIN 32..291
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT DOMAIN 325..572
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 410..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 63860 MW; 9EE721FBC28CA59E CRC64;
MAGGVVVDAQ YLKEVEKARR DLRALIAYRN CAPIMLRLAW HDAGTYNAET KTGGANGSIR
NEHELGHGAN SGLKIAVNFC EEVKAKYSKI TYADLYQLAG VVAVEVTGGP TIEFVPGRKD
SLESPEEGRL PDAKKGASHL KDIFYRMGLS DKDIVALSGA HTLGRAHPER SGFEGPWTSE
PLKFDNSYFT ELLKGESEGL LKLPTDKALL DDPEFRRYVE LYAKDEDAFF KDYAASHKKL
SELGFTPSSC VKEAAKTSTI LAQSAVGVAV TAAVVILSYL YEVRKNANLR FHALMAAPVV
NEEYLKEIEK ARRDLRALIY SKNCAPIMLR IAWHDAATYD ARLKTRIPGG PNGSIRNKEE
LSHSGNKGLE TAVELCEQVK AKHPKITYAD LYQLAGVVAV EITGGPSIDF VPGRKDSNQS
PPEGRLPDAK LGASHLREVF YRMGLSDKDI VVLSGGHTLG KEHKRSGFQG PWTKEPSKFD
NSYFVDLLKG ETEGLLQLPT DKALVEDPVF RRYVELYARD NDAFFRDYAV SHKKLSELGF
NPPSQRPKVV LTLTIAAAVV AALVYDKCES FIKNMTSLI
//
