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L-ascorbate peroxidase, cytosolic (AP) (EC 1.11.1.11) (PsAPx01)

 APX1_PEA                Reviewed;         250 AA.
P48534;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 103.
RecName: Full=L-ascorbate peroxidase, cytosolic;
Short=AP;
EC=1.11.1.11;
AltName: Full=PsAPx01;
Name=APX1; Synonyms=APPX1;
Pisum sativum (Garden pea).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Fabeae; Pisum.
NCBI_TaxID=3888;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Little Marvel; TISSUE=Leaf;
PubMed=1915856; DOI=10.1016/0014-5793(91)81083-K;
Mittler R., Zilinskas B.A.;
"Molecular cloning and nucleotide sequence analysis of a cDNA encoding
pea cytosolic ascorbate peroxidase.";
FEBS Lett. 289:257-259(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
STRAIN=cv. Little Marvel;
PubMed=1400489;
Mittler R., Zilinskas B.A.;
"Molecular cloning and characterization of a gene encoding pea
cytosolic ascorbate peroxidase.";
J. Biol. Chem. 267:21802-21807(1992).
[3]
ERRATUM.
Mittler R., Zilinskas B.A.;
J. Biol. Chem. 268:4568-4568(1993).
[4]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH HEME AND
POTASSIUM IONS.
PubMed=7703247; DOI=10.1021/bi00013a023;
Patterson W.R., Poulos T.L.;
"Crystal structure of recombinant pea cytosolic ascorbate
peroxidase.";
Biochemistry 34:4331-4341(1995).
-!- FUNCTION: Plays a key role in hydrogen peroxide removal.
-!- CATALYTIC ACTIVITY: 2 L-ascorbate + H(2)O(2) + 2 H(+) = L-
ascorbate + L-dehydroascorbate + 2 H(2)O.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
subunit.;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- INDUCTION: By stress. {ECO:0000269|PubMed:1400489}.
-!- MISCELLANEOUS: Binds one cation per subunit; probably K(+), but
might also be Ca(2+).
-!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
subfamily. {ECO:0000305}.
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EMBL; M93051; AAA33645.1; -; Genomic_DNA.
EMBL; X62077; CAA43992.1; -; mRNA.
PIR; A45116; A45116.
PDB; 1APX; X-ray; 2.20 A; A/B/C/D=2-250.
PDBsum; 1APX; -.
ProteinModelPortal; P48534; -.
SMR; P48534; -.
PeroxiBase; 2462; PsAPx01.
PRIDE; P48534; -.
SABIO-RK; P48534; -.
EvolutionaryTrace; P48534; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0016688; F:L-ascorbate peroxidase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
InterPro; IPR002207; Peroxidase_I.
InterPro; IPR019794; Peroxidases_AS.
InterPro; IPR019793; Peroxidases_heam-ligand_BS.
Pfam; PF00141; peroxidase; 1.
PRINTS; PR00459; ASPEROXIDASE.
PRINTS; PR00458; PEROXIDASE.
SUPFAM; SSF48113; SSF48113; 1.
PROSITE; PS00435; PEROXIDASE_1; 1.
PROSITE; PS00436; PEROXIDASE_2; 1.
PROSITE; PS50873; PEROXIDASE_4; 1.
1: Evidence at protein level;
3D-structure; Calcium; Cytoplasm; Heme; Hydrogen peroxide; Iron;
Metal-binding; Oxidoreductase; Peroxidase; Potassium; Stress response.
INIT_MET 1 1 Removed.
CHAIN 2 250 L-ascorbate peroxidase, cytosolic.
/FTId=PRO_0000055597.
ACT_SITE 42 42 Proton acceptor.
METAL 163 163 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00297,
ECO:0000269|PubMed:7703247}.
METAL 164 164 Potassium or calcium.
METAL 180 180 Potassium or calcium.
METAL 182 182 Potassium or calcium.
METAL 185 185 Potassium or calcium; via carbonyl
oxygen.
METAL 187 187 Potassium or calcium.
SITE 38 38 Transition state stabilizer.
HELIX 10 30 {ECO:0000244|PDB:1APX}.
HELIX 33 44 {ECO:0000244|PDB:1APX}.
TURN 49 52 {ECO:0000244|PDB:1APX}.
STRAND 55 58 {ECO:0000244|PDB:1APX}.
HELIX 59 61 {ECO:0000244|PDB:1APX}.
HELIX 63 66 {ECO:0000244|PDB:1APX}.
HELIX 69 71 {ECO:0000244|PDB:1APX}.
HELIX 74 86 {ECO:0000244|PDB:1APX}.
HELIX 93 107 {ECO:0000244|PDB:1APX}.
HELIX 138 145 {ECO:0000244|PDB:1APX}.
TURN 146 148 {ECO:0000244|PDB:1APX}.
HELIX 153 160 {ECO:0000244|PDB:1APX}.
HELIX 161 164 {ECO:0000244|PDB:1APX}.
TURN 170 172 {ECO:0000244|PDB:1APX}.
STRAND 177 181 {ECO:0000244|PDB:1APX}.
HELIX 189 195 {ECO:0000244|PDB:1APX}.
HELIX 206 209 {ECO:0000244|PDB:1APX}.
TURN 210 212 {ECO:0000244|PDB:1APX}.
HELIX 217 226 {ECO:0000244|PDB:1APX}.
HELIX 228 243 {ECO:0000244|PDB:1APX}.
TURN 244 246 {ECO:0000244|PDB:1APX}.
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


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