| IED ID | IndEnz0002007954 |
| Enzyme Type ID | protease007954 |
| Protein Name |
Endopolyphosphatase EC 3.6.1.10 Deoxyadenosine triphosphate phosphohydrolase dATP phosphohydrolase EC 3.6.1.- Exopolyphosphatase EC 3.6.1.11 Phosphate metabolism protein 5 |
| Gene Name | PPN1 PHM5 YDR452W D9461.37 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MVVVGKSEVRNVSMSRPKKKSLIAILSTCVLFFLVFIIGAKFQYVSVFSKFLDDRGDNESLQLLNDIEFTRLGLTPREPVIIKDVKTGKERKLHGRFLHITDIHPDPYYVEGSSIDAVCHTGKPSKKKDVAPKFGKAMSGCDSPVILMEETLRWIKENLRDKIDFVIWTGDNIRHDNDRKHPRTEAQIFDMNNIVADKMTELFSAGNEEDPRDFDVSVIPSLGNNDVFPHNMFALGPTLQTREYYRIWKNFVPQQQQRTFDRSASFLTEVIPGKLAVLSINTLYLFKANPLVDNCNSKKEPGYQLLLWFGYVLEELRSRGMKVWLSGHVPPIAKNFDQSCYDKFTLWTHEYRDIIIGGLYGHMNIDHFIPTDGKKARKSLLKAMEQSTRVQQGEDSNEEDEETELNRILDHAMAAKEVFLMGAKPSNKEAYMNTVRDTYYRKVWNKLERVDEKNVENEKKKKEKKDKKKKKPITRKELIERYSIVNIGGSVIPTFNPSFRIWEYNITDIVNDSNFAVSEYKPWDEFFESLNKIMEDSLLEDEMDSSNIEVGINREKMGEKKNKKKKKNDKTMPIEMPDKYELGPAYVPQLFTPTRFVQFYADLEKINQELHNSFVESKDIFRYEIEYTSDEKPYSMDSLTVGSYLDLAGRLYENKPAWEKYVEWSFASSGYKDD |
| Enzyme Length | 674 |
| Uniprot Accession Number | Q04119 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by heparin and EDTA. {ECO:0000269|PubMed:15170373}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=[phosphate](n+1) + n H2O = n H(+) + (n+1) phosphate; Xref=Rhea:RHEA:22452, Rhea:RHEA-COMP:14280, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838, ChEBI:CHEBI:43474; EC=3.6.1.10; Evidence={ECO:0000269|PubMed:15792812}; CATALYTIC ACTIVITY: Reaction=[phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate; Xref=Rhea:RHEA:21528, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14279, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838, ChEBI:CHEBI:43474; EC=3.6.1.11; Evidence={ECO:0000269|PubMed:15170373}; CATALYTIC ACTIVITY: Reaction=dATP + H2O = dADP + H(+) + phosphate; Xref=Rhea:RHEA:51908, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57667, ChEBI:CHEBI:61404; Evidence={ECO:0000269|Ref.16}; |
| DNA Binding | |
| EC Number | 3.6.1.10; 3.6.1.-; 3.6.1.11 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of inorganic polyphosphate (polyP) chains of many hundreds of phosphate residues into shorter lengths both by cleaving phosphate from the chain end and by fragmenting long-chain polymers into shorter ones. The limited digestion products are 1 and 3 P(i) residues (PubMed:11102525, PubMed:11447286, PubMed:15170373, PubMed:15342119, PubMed:15792812, PubMed:8900207, Ref.16). Also releases phosphate from dATP. dATP phosphohydrolase activity is about 7-fold lower than the exopolyphosphatase activity (Ref.16). {ECO:0000269|PubMed:11102525, ECO:0000269|PubMed:11447286, ECO:0000269|PubMed:15170373, ECO:0000269|PubMed:15342119, ECO:0000269|PubMed:15792812, ECO:0000269|PubMed:8900207, ECO:0000269|Ref.16}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 7.5. {ECO:0000269|PubMed:8900207}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Cross-link (1); Glycosylation (3); Mutagenesis (4); Propeptide (2); Region (1); Topological domain (2); Transmembrane (1) |
| Keywords | Cytoplasm;Direct protein sequencing;Glycoprotein;Hydrolase;Isopeptide bond;Membrane;Metal-binding;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Ubl conjugation;Vacuole;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:11566881, ECO:0000269|PubMed:11788821, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15086787, ECO:0000269|PubMed:8900207}; Single-pass type II membrane protein {ECO:0000269|PubMed:11566881, ECO:0000269|PubMed:11788821, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15086787, ECO:0000269|PubMed:8900207}. Cytoplasm {ECO:0000269|PubMed:17009950}. Note=The cytoplasmic form appears in the cytosol during the transition of cells from stationary growth phase to new budding on glucose addition and phosphate excess. {ECO:0000269|PubMed:17009950}. |
| Modified Residue | |
| Post Translational Modification | PTM: Processing by proteases in the vacuole is required for activation. {ECO:0000305|PubMed:11447286}.; PTM: Ubiquitinated. Ubiquitination mediates sorting into internal vesicles in late endosomes. TUL1 and RSP5 are required for ubiquitination. Other cytoplasmic Lys residues than Lys-6 may also be ubiquitinated. {ECO:0000269|PubMed:11566881}.; PTM: N-glycosylated (Probable). N-glycosylation is essential for the protease-mediated maturation. {ECO:0000269|PubMed:15792812, ECO:0000305}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10739469; 10900456; 11283351; 12062051; 14988731; 15925310; 16429126; 16554755; 16700065; 16779667; 16862600; 16871795; 17140377; 18294131; 18793138; 18976214; 19344251; 19536198; 19580157; 19817683; 20489023; 20673205; 21179020; 21314609; 21734642; 22357655; 22842922; 23663411; 24228884; 24450634; 24845516; 24954599; 25034634; 25584613; 26837754; 26862210; |
| Motif | |
| Gene Encoded By | |
| Mass | 78,344 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=185 nM for polyP(750) {ECO:0000269|PubMed:8900207}; KM=3.5 uM for polyP(208) {ECO:0000269|PubMed:15170373}; KM=75 uM for polyP(15) {ECO:0000269|PubMed:15170373}; KM=1100 uM for polyP(3) {ECO:0000269|PubMed:15170373}; KM=0.88 mM for dATP {ECO:0000269|Ref.16}; |
| Metal Binding | |
| Rhea ID | RHEA:22452; RHEA:21528; RHEA:51908 |
| Cross Reference Brenda | 3.6.1.10;3.6.1.11; |