ID D7L8B0_ARALL Unreviewed; 251 AA.
AC D7L8B0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 22-FEB-2023, entry version 58.
DE RecName: Full=L-ascorbate peroxidase {ECO:0000256|ARBA:ARBA00012940};
DE EC=1.11.1.11 {ECO:0000256|ARBA:ARBA00012940};
GN ORFNames=ARALYDRAFT_478284 {ECO:0000313|EMBL:EFH58890.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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 EMBL; GL348715; EFH58890.1; -; Genomic_DNA.
DR RefSeq; XP_002882631.1; XM_002882585.1.
DR AlphaFoldDB; D7L8B0; -.
DR STRING; 81972.D7L8B0; -.
DR EnsemblPlants; fgenesh2_kg.3__985__AT3G09640.2; fgenesh2_kg.3__985__AT3G09640.2; fgenesh2_kg.3__985__AT3G09640.2.
DR Gramene; fgenesh2_kg.3__985__AT3G09640.2; fgenesh2_kg.3__985__AT3G09640.2; fgenesh2_kg.3__985__AT3G09640.2.
DR eggNOG; ENOG502QR1E; Eukaryota.
DR HOGENOM; CLU_036959_3_0_1; -.
DR OrthoDB; 168803at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblPlants.
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; 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; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR31356:SF35; L-ASCORBATE PEROXIDASE 2, CYTOSOLIC; 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; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
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:UP000008694}.
FT DOMAIN 75..251
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
SQ SEQUENCE 251 AA; 28179 MW; 3FFE2CCE049A20B6 CRC64;
MVNKSYPEVK EEYKKAVQRC KRKLRGLIAE KHCAPIVLRL AWHSAGTFDV KTKTGGPFGT
IRHPQELAHE ANNGLDIAIR LLEPIKELFP ILSYADFYQL AGVVAVEITG GPEIPFHPGR
LDKVEPPPEG RLPQATKGVD HLRDVFSRMG LNDKDIVALS GGHTLGRCHK ERSGFEGAWT
QNPLIFDNSY FKEILSGEKE GLLQLPSDKA LLDDPLFRPF VERYAADEDA FFEDYKEAHL
KLSELGFADK E
//
