APX1_PEA
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 03-AUG-2022, entry version 116.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Little Marvel; TISSUE=Leaf;
RX 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 pea
RT cytosolic ascorbate peroxidase.";
RL FEBS Lett. 289:257-259(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=cv. Little Marvel;
RX PubMed=1400489; DOI=10.1016/s0021-9258(19)36683-9;
RA Mittler R., Zilinskas B.A.;
RT "Molecular cloning and characterization of a gene encoding pea cytosolic
RT ascorbate peroxidase.";
RL J. Biol. Chem. 267:21802-21807(1992).
RN [3]
RP ERRATUM OF PUBMED:1400489.
RA Mittler R., Zilinskas B.A.;
RL J. Biol. Chem. 268:4568-4568(1993).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH HEME AND POTASSIUM
RP IONS.
RX PubMed=7703247; DOI=10.1021/bi00013a023;
RA Patterson W.R., Poulos T.L.;
RT "Crystal structure of recombinant pea cytosolic ascorbate peroxidase.";
RL Biochemistry 34:4331-4341(1995).
CC -!- FUNCTION: Plays a key role in hydrogen peroxide removal.
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 Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By stress. {ECO:0000269|PubMed:1400489}.
CC -!- MISCELLANEOUS: Binds one cation per subunit; probably K(+), but might
CC also be Ca(2+).
CC -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC subfamily. {ECO:0000305}.
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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 AlphaFoldDB; P48534; -.
DR SMR; P48534; -.
DR PeroxiBase; 2462; PsAPx01.
DR PRIDE; P48534; -.
DR EnsemblPlants; Psat7g223000.1; Psat7g223000.1.cds; Psat7g223000.
DR Gramene; Psat7g223000.1; Psat7g223000.1.cds; Psat7g223000.
DR SABIO-RK; P48534; -.
DR EvolutionaryTrace; P48534; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
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; PTHR31356; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00459; ASPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
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
FT /note="Removed"
FT CHAIN 2..250
FT /note="L-ascorbate peroxidase, cytosolic"
FT /id="PRO_0000055597"
FT REGION 113..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 42
FT /note="Proton acceptor"
FT BINDING 163
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:7703247"
FT BINDING 164
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:7703247,
FT ECO:0007744|PDB:1APX"
FT BINDING 180
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:7703247,
FT ECO:0007744|PDB:1APX"
FT BINDING 182
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:7703247,
FT ECO:0007744|PDB:1APX"
FT BINDING 185
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:7703247,
FT ECO:0007744|PDB:1APX"
FT BINDING 187
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:7703247,
FT ECO:0007744|PDB:1APX"
FT SITE 38
FT /note="Transition state stabilizer"
FT HELIX 10..30
FT /evidence="ECO:0007829|PDB:1APX"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:1APX"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:1APX"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1APX"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1APX"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:1APX"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1APX"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:1APX"
FT HELIX 93..107
FT /evidence="ECO:0007829|PDB:1APX"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:1APX"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1APX"
FT HELIX 153..160
FT /evidence="ECO:0007829|PDB:1APX"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:1APX"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1APX"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:1APX"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:1APX"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:1APX"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:1APX"
FT HELIX 217..226
FT /evidence="ECO:0007829|PDB:1APX"
FT HELIX 228..243
FT /evidence="ECO:0007829|PDB:1APX"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:1APX"
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
