ID A0A4U5Q6S0_POPAL Unreviewed; 286 AA.
AC A0A4U5Q6S0;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE RecName: Full=L-ascorbate peroxidase {ECO:0000256|ARBA:ARBA00012940};
DE EC=1.11.1.11 {ECO:0000256|ARBA:ARBA00012940};
GN ORFNames=D5086_0000135960 {ECO:0000313|EMBL:TKS05499.1};
OS Populus alba (White poplar).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=43335 {ECO:0000313|EMBL:TKS05499.1, ECO:0000313|Proteomes:UP000309997};
RN [1] {ECO:0000313|Proteomes:UP000309997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PAL-ZL1 {ECO:0000313|Proteomes:UP000309997};
RX PubMed=30661181; DOI=10.1007/s11427-018-9455-2;
RA Liu Y.-J., Wang X.-R., Zeng Q.-Y.;
RT "De novo assembly of white poplar genome and genetic diversity of white
RT poplar population in Irtysh River basin in China.";
RL Sci. China Life Sci. 62:609-618(2019).
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:TKS05499.1}.
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DR EMBL; RCHU01000435; TKS05499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U5Q6S0; -.
DR STRING; 43335.A0A4U5Q6S0; -.
DR OrthoDB; 168803at2759; -.
DR Proteomes; UP000309997; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF36; L-ASCORBATE PEROXIDASE 3; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:TKS05499.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000309997};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 258..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..286
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
SQ SEQUENCE 286 AA; 31554 MW; 7290369CA8B8BBD4 CRC64;
MALPVVDTEY LKEIDKARRD LRALIAYKNC APIMLRLAWH DAGTYDKNSK TGGANGSIRN
EEEYSHGSNS GLKIAIDFCE GVKAKHPKIT YADLYQLAGV VAVEVTGGPT IDFVPGRRDS
NICPKEGRLP NAKLGSPHLR DIFYRMGLSD KDIVALSGGH TLGRAHPDRS GFEGPWTQEP
LKFDNSYFVE LLKGETDGLL KLPTDTALLD DPAFRPYVEL YAKDEEAFFR DYAASHKKLS
ELGFTQESSG FKVKDTTVLA QSVAGVAVAA AVVILSYFYE VRKKMK
//
