ID   APX_PSEMZ               Reviewed;          10 AA.
AC   P85940;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=L-ascorbate peroxidase, cytosolic {ECO:0000250|UniProtKB:P48534};
DE            EC=1.11.1.11;
DE   Flags: Fragment;
OS   Pseudotsuga menziesii (Douglas-fir) (Abies menziesii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae;
OC   Pseudotsuga.
OX   NCBI_TaxID=3357;
RN   [1]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18602030; DOI=10.1016/j.jprot.2008.06.004;
RA   Islam M.A., Sturrock R.N., Ekramoddoullah A.K.M.;
RT   "A proteomics approach to identify proteins differentially expressed in
RT   Douglas-fir seedlings infected by Phellinus sulphurascens.";
RL   J. Proteomics 71:425-438(2008).
CC   -!- FUNCTION: Plays a key role in hydrogen peroxide removal.
CC       {ECO:0000250|UniProtKB:P48534}.
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   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:P48534};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group.
CC       {ECO:0000250|UniProtKB:P48534};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48534}.
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:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calcium; Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Peroxidase; Potassium.
FT   CHAIN           <1..10
FT                   /note="L-ascorbate peroxidase, cytosolic"
FT                   /id="PRO_0000347322"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:18602030"
FT   NON_TER         10
FT                   /evidence="ECO:0000303|PubMed:18602030"
SQ   SEQUENCE   10 AA;  1099 MW;  58F4A4A76736D727 CRC64;
     EGLLQLPSDK