Detail Information for IndEnz0018000998
IED ID IndEnz0018000998
Enzyme Type ID peroxidase000998
Protein Name L-ascorbate peroxidase, cytosolic
AP
EC 1.11.1.11
PsAPx01
Gene Name APX1 APPX1
Organism Pisum sativum (Garden pea)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Fabales Fabaceae Papilionoideae 50 kb inversion clade NPAAA clade Hologalegina IRL clade Fabeae Pisum Pisum sativum (Garden pea)
Enzyme Sequence MGKSYPTVSPDYQKAIEKAKRKLRGFIAEKKCAPLILRLAWHSAGTFDSKTKTGGPFGTIKHQAELAHGANNGLDIAVRLLEPIKEQFPIVSYADFYQLAGVVAVEITGGPEVPFHPGREDKPEPPPEGRLPDATKGSDHLRDVFGKAMGLSDQDIVALSGGHTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLTGEKDGLLQLPSDKALLTDSVFRPLVEKYAADEDVFFADYAEAHLKLSELGFAEA
Enzyme Length 250
Uniprot Accession Number P48534
Absorption
Active Site ACT_SITE 42; /note=Proton acceptor
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=H2O2 + L-ascorbate = 2 H2O + L-dehydroascorbate; Xref=Rhea:RHEA:22996, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:38290, ChEBI:CHEBI:58539; EC=1.11.1.11;
DNA Binding
EC Number 1.11.1.11
Enzyme Function FUNCTION: Plays a key role in hydrogen peroxide removal.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Beta strand (2); Chain (1); Compositional bias (1); Helix (14); Initiator methionine (1); Metal binding (6); Region (1); Site (1); Turn (5)
Keywords 3D-structure;Calcium;Cytoplasm;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Potassium;Stress response
Interact With
Induction INDUCTION: By stress. {ECO:0000269|PubMed:1400489}.
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 1APX;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 27,193
Kinetics
Metal Binding METAL 163; /note="Iron (heme b axial ligand)"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:7703247"; METAL 164; /note="Potassium"; /evidence="ECO:0000269|PubMed:7703247, ECO:0007744|PDB:1APX"; METAL 180; /note="Potassium"; /evidence="ECO:0000269|PubMed:7703247, ECO:0007744|PDB:1APX"; METAL 182; /note="Potassium"; /evidence="ECO:0000269|PubMed:7703247, ECO:0007744|PDB:1APX"; METAL 185; /note="Potassium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:7703247, ECO:0007744|PDB:1APX"; METAL 187; /note="Potassium"; /evidence="ECO:0000269|PubMed:7703247, ECO:0007744|PDB:1APX"
Rhea ID RHEA:22996
Cross Reference Brenda