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; |