Detail Information for IndEnz0018000860
IED ID IndEnz0018000860
Enzyme Type ID peroxidase000860
Protein Name Bifunctional purple acid phosphatase 26
Includes: Acid phosphatase
EC 3.1.3.2
; Peroxidase
EC 1.11.1.7
Gene Name PAP26 At5g34850 T5E15.10
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 MNHLVIISVFLSSVLLLYRGESGITSSFIRSEWPAVDIPLDHHVFKVPKGYNAPQQVHITQGDYDGKAVIISWVTPDEPGSSQVHYGAVQGKYEFVAQGTYHNYTFYKYKSGFIHHCLVSDLEHDTKYYYKIESGESSREFWFVTPPHVHPDASYKFGIIGDMGQTFNSLSTLEHYMESGAQAVLFLGDLSYADRYQYNDVGVRWDSWGRFVERSTAYQPWLWSAGNHEVDYMPYMGEVTPFRNYLQRYTTPYLASKSSSPLWYAVRRASAHIIVLSSYSPFVKYTPQWHWLSEELTRVDREKTPWLIVLMHVPIYNSNEAHFMEGESMRAAFEEWFVQHKVDVIFAGHVHAYERSYRISNVRYNVSSGDRYPVPDKSAPVYITVGDGGNQEGLAGRFTEPQPDYSAFREASYGHSTLDIKNRTHAIYHWNRNDDGKKVATDEFVLHNQYWGKNIRRRKLKKHYIRSVVGGWIAT
Enzyme Length 475
Uniprot Accession Number Q949Y3
Absorption BIOPHYSICOCHEMICAL PROPERTIES: Absorption: Abs(max)=520 nm {ECO:0000269|PubMed:16963519};
Active Site ACT_SITE 322; /note=Proton donor; /evidence=ECO:0000250
Activity Regulation ACTIVITY REGULATION: Activated by Mg(2+), Co(2+), Mn(2+) and Ba(2+). Inhibited by Fe(2+), Cu(2+), Zn(2+), NaF, molybdate, arsenate, vanadate and inorganic phosphate. No effect of tartrate, Asp, Gln, glutathione, Asn, ascorbic acid and phosphite.
Binding Site BINDING 227; /note=Substrate; /evidence=ECO:0000250
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2; CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
DNA Binding
EC Number 3.1.3.2; 1.11.1.7
Enzyme Function FUNCTION: Metallo-phosphoesterase involved in phosphate metabolism. Acid phosphatase activity with phosphoenolpyruvate, inorganic pyrophosphate, phenyl-phosphate and p-nitrophenyl-phosphate as the most effective substrates. No activity with phytic acid, phosphocholine or bis-p-nitrophenyl-phosphate. Has a peroxidase activity at alkaline pH. {ECO:0000269|PubMed:16963519}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.6 for the phosphatase activity and 8.8 for the peroxidase activity. {ECO:0000269|PubMed:16963519};
Pathway
nucleotide Binding
Features Active site (1); Binding site (1); Chain (1); Glycosylation (3); Metal binding (8); Region (1); Sequence conflict (3); Signal peptide (1)
Keywords Direct protein sequencing;Glycoprotein;Hydrogen peroxide;Hydrolase;Iron;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome;Signal;Vacuole;Zinc
Interact With
Induction INDUCTION: Not induced at the transcription level by phosphate starvation, but accumulation of the protein in starved shoots. {ECO:0000269|PubMed:16963519}.
Subcellular Location SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:16963519}.
Modified Residue
Post Translational Modification PTM: Glycosylated. {ECO:0000269|PubMed:16963519}.
Signal Peptide SIGNAL 1..30; /evidence=ECO:0000269|PubMed:16963519
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12609038; 12609039; 14617064; 15122033; 15208337; 15215502; 15539469; 16242667; 16461884; 17526915; 18775970; 18796151; 20348213; 20545876; 23072540; 23125358; 24528675; 25170100; 25270985; 26251878; 28627464; 30156702; 30341950; 30555844; 33101335;
Motif
Gene Encoded By
Mass 55,010
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.8 mM for phosphoenolpyruvate (for the phosphatase activity) {ECO:0000269|PubMed:16963519};
Metal Binding METAL 162; /note=Iron; /evidence=ECO:0000250; METAL 189; /note=Iron; /evidence=ECO:0000250; METAL 189; /note=Zinc; /evidence=ECO:0000250; METAL 192; /note=Iron; /evidence=ECO:0000250; METAL 227; /note=Zinc; /evidence=ECO:0000250; METAL 312; /note=Zinc; /evidence=ECO:0000250; METAL 349; /note=Zinc; /evidence=ECO:0000250; METAL 351; /note=Iron; /evidence=ECO:0000250
Rhea ID RHEA:15017; RHEA:56136
Cross Reference Brenda 3.1.3.2;