Detail Information for IndEnz0018001595
IED ID IndEnz0018001595
Enzyme Type ID peroxidase001595
Protein Name Probable peroxygenase 3
AtPXG3
EC 1.11.2.3
Caleosin-3
Protein RESPONSIVE TO DESICCATION 20
Gene Name PXG3 CLO3 RD20 At2g33380 F4P9.15
Organism Arabidopsis thaliana (Mouse-ear cress)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress)
Enzyme Sequence MAGEAEALATTAPLAPVTSQRKVRNDLEETLPKPYMARALAAPDTEHPNGTEGHDSKGMSVMQQHVAFFDQNDDGIVYPWETYKGFRDLGFNPISSIFWTLLINLAFSYVTLPSWVPSPLLPVYIDNIHKAKHGSDSSTYDTEGRYVPVNLENIFSKYALTVKDKLSFKEVWNVTEGNRMAIDPFGWLSNKVEWILLYILAKDEDGFLSKEAVRGCFDGSLFEQIAKERANSRKQD
Enzyme Length 236
Uniprot Accession Number O22788
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=RH + ROOH = ROH + ROH.; EC=1.11.2.3;
DNA Binding
EC Number 1.11.2.3
Enzyme Function FUNCTION: Probable calcium-binding peroxygenase. May be involved in the degradation of storage lipid in oil bodies, in abiotic stress-related signaling pathway and in drought tolerance through stomatal control under water deficit conditions. {ECO:0000269|PubMed:19467604, ECO:0000269|PubMed:20952421}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Chain (1); Domain (1); Initiator methionine (1); Metal binding (5); Modified residue (2); Motif (1)
Keywords Acetylation;Alternative splicing;Calcium;Chloroplast;Endoplasmic reticulum;Heme;Iron;Lipid droplet;Membrane;Metal-binding;Microsome;Oxidoreductase;Phosphoprotein;Plastid;Reference proteome
Interact With
Induction INDUCTION: Up-regulated by drought, abscisic acid, osmotic stress, salicylic acid, wounding and pathogens, but very low induction by jasmonic acid. {ECO:0000269|PubMed:10965948, ECO:0000269|PubMed:11197322, ECO:0000269|PubMed:19467604, ECO:0000269|PubMed:20952421, ECO:0000269|PubMed:21673513}.
Subcellular Location SUBCELLULAR LOCATION: Microsome membrane. Plastid, chloroplast membrane. Lipid droplet.
Modified Residue MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0007744|PubMed:22223895; MOD_RES 220; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O81270
Post Translational Modification PTM: Phosphorylated. Increased phosphorylation upon stress. {ECO:0000269|PubMed:19467604}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11230576; 12102506; 12372144; 12432076; 12481097; 12509522; 12509532; 12535340; 14973164; 15047901; 15086800; 15247402; 15319476; 15341629; 15539469; 15546358; 15734912; 16258012; 16284313; 16317577; 16463051; 16463099; 16553894; 16673935; 16830180; 16901781; 17337630; 17582382; 17660356; 17662035; 17905899; 18441212; 18671872; 18779215; 18783601; 19825648; 21798944; 22505693; 23505340; 23898029; 24214535; 24556609; 25056921; 25234727; 25657344; 25764319; 25830533; 25933420; 27770200; 29247649; 29490615; 31712757; 32219438; 34599731;
Motif MOTIF 113..122; /note=Proline-knot
Gene Encoded By
Mass 26,600
Kinetics
Metal Binding METAL 65; /note=Iron (heme axial ligand); /evidence=ECO:0000250; METAL 70; /note=Calcium; /evidence=ECO:0000255; METAL 72; /note=Calcium; /evidence=ECO:0000255; METAL 74; /note=Calcium; /evidence=ECO:0000255; METAL 81; /note=Calcium; /evidence=ECO:0000255
Rhea ID
Cross Reference Brenda 1.11.2.3;