ID   APX1_PEA                Reviewed;         250 AA.
AC   P48534;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 73.
DE   RecName: Full=L-ascorbate peroxidase, cytosolic;
DE            Short=AP;
DE            EC=1.11.1.11;
DE   AltName: Full=PsAPx01;
GN   Name=APX1; Synonyms=APPX1;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Little Marvel; TISSUE=Leaf;
RX   MEDLINE=92008636; PubMed=1915856; DOI=10.1016/0014-5793(91)81083-K;
RA   Mittler R., Zilinskas B.A.;
RT   "Molecular cloning and nucleotide sequence analysis of a cDNA encoding
RT   pea cytosolic ascorbate peroxidase.";
RL   FEBS Lett. 289:257-259(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Little Marvel;
RX   MEDLINE=93016138; PubMed=1400489;
RA   Mittler R., Zilinskas B.A.;
RT   "Molecular cloning and characterization of a gene encoding pea
RT   cytosolic ascorbate peroxidase.";
RL   J. Biol. Chem. 267:21802-21807(1992).
RN   [3]
RP   ERRATUM.
RA   Mittler R., Zilinskas B.A.;
RL   J. Biol. Chem. 268:4568-4568(1993).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   MEDLINE=95217899; PubMed=7703247; DOI=10.1021/bi00013a023;
RA   Patterson W.R., Poulos T.L.;
RT   "Crystal structure of recombinant pea cytosolic ascorbate
RT   peroxidase.";
RL   Biochemistry 34:4331-4341(1995).
CC   -!- FUNCTION: Plays a key role in hydrogen peroxide removal.
CC   -!- CATALYTIC ACTIVITY: L-ascorbate + H(2)O(2) = dehydroascorbate + 2
CC       H(2)O.
CC   -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per
CC       subunit.
CC   -!- COFACTOR: Binds 1 potassium or calcium ion per subunit.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: By stress.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC       subfamily.
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DR   EMBL; M93051; AAA33645.1; -; Genomic_DNA.
DR   EMBL; X62077; CAA43992.1; -; mRNA.
DR   PIR; A45116; A45116.
DR   PDB; 1APX; X-ray; 2.20 A; A/B/C/D=2-250.
DR   PDBsum; 1APX; -.
DR   PeroxiBase; 2462; PsAPx01.
DR   BRENDA; 1.11.1.11; 287.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0016688; F:L-ascorbate peroxidase activity; IEA:EC.
DR   GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002207; Asc_perxdse.
DR   InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00459; ASPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cytoplasm; Heme; Hydrogen peroxide; Iron;
KW   Metal-binding; Oxidoreductase; Peroxidase; Potassium; Stress response.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    250       L-ascorbate peroxidase, cytosolic.
FT                                /FTId=PRO_0000055597.
FT   ACT_SITE     42     42       Proton acceptor.
FT   METAL       163    163       Iron (heme axial ligand).
FT   METAL       164    164       Potassium or calcium.
FT   METAL       180    180       Potassium or calcium.
FT   METAL       182    182       Potassium or calcium.
FT   METAL       185    185       Potassium or calcium; via carbonyl
FT                                oxygen.
FT   METAL       187    187       Potassium or calcium.
FT   SITE         38     38       Transition state stabilizer.
FT   HELIX        10     30
FT   HELIX        33     44
FT   TURN         49     52
FT   STRAND       55     58
FT   HELIX        59     61
FT   HELIX        63     66
FT   HELIX        69     71
FT   HELIX        74     86
FT   HELIX        93    107
FT   HELIX       138    145
FT   TURN        146    148
FT   HELIX       153    160
FT   HELIX       161    164
FT   TURN        170    172
FT   STRAND      177    181
FT   HELIX       189    195
FT   HELIX       206    209
FT   TURN        210    212
FT   HELIX       217    226
FT   HELIX       228    243
FT   TURN        244    246
SQ   SEQUENCE   250 AA;  27193 MW;  6F51006D0A13B42C CRC64;
     MGKSYPTVSP DYQKAIEKAK RKLRGFIAEK KCAPLILRLA WHSAGTFDSK TKTGGPFGTI
     KHQAELAHGA NNGLDIAVRL LEPIKEQFPI VSYADFYQLA GVVAVEITGG PEVPFHPGRE
     DKPEPPPEGR LPDATKGSDH LRDVFGKAMG LSDQDIVALS GGHTIGAAHK ERSGFEGPWT
     SNPLIFDNSY FTELLTGEKD GLLQLPSDKA LLTDSVFRPL VEKYAADEDV FFADYAEAHL
     KLSELGFAEA
//