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 24-JAN-2024, entry version 120. 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) (Lathyrus oleraceus). 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}. 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 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 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 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:SF35; L-ASCORBATE PEROXIDASE 2, CYTOSOLIC; 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 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 //