ID A0A1S3U8Q6_VIGRR Unreviewed; 388 AA.
AC A0A1S3U8Q6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=L-ascorbate peroxidase {ECO:0000256|ARBA:ARBA00012940};
DE EC=1.11.1.11 {ECO:0000256|ARBA:ARBA00012940};
GN Name=LOC106762832 {ECO:0000313|RefSeq:XP_014502401.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014502401.1};
RN [1] {ECO:0000313|RefSeq:XP_014502401.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014502401.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR RefSeq; XP_014502401.1; XM_014646915.2.
DR AlphaFoldDB; A0A1S3U8Q6; -.
DR GeneID; 106762832; -.
DR OrthoDB; 168803at2759; -.
DR Proteomes; UP000087766; Chromosome 5.
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 CDD; cd00691; ascorbate_peroxidase; 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; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR31356:SF67; L-ASCORBATE PEROXIDASE S, CHLOROPLASTIC_MITOCHONDRIAL; 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; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|RefSeq:XP_014502401.1};
KW Peroxidase {ECO:0000313|RefSeq:XP_014502401.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087766}.
FT DOMAIN 181..388
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 259..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 388 AA; 42441 MW; 65F495E0C3540F18 CRC64;
MAERVFLTAS SRPLPSQQHT STAMALFSGA ASARIIPSVS LSSSTRSFFS LSSSSSSLQC
LRSSPRISHL FLNQRRAEVR FSSGGYGTVS APKSFASDPD QLKSAREDIK ELLRSKFCHP
ILIRLGWHDA GTYNKNIEEW PQRGGANGSL RFEIELKHGA NAGLVNALKL LQPIKDKYSG
VTYADLFQLA GATAVEEAGG PKLPMKYGRV DVSGPEQCPE EGRLPDAGPP SPADHLRQVF
YRMGLNDKEI VVLSGAHTLG RSRPDRSGWG KPETKYTKDG PGAPGGQSWT VQWLKFDNSY
FKDIKEKKDE DLLVLPTDAA LFEDPSFKVY AEKYAEDQEA FFKDYAEAHA KLSNLGAKFD
PPEGIVIDES PNAGAEKFVA AKYSTGKE
//
