| IED ID | IndEnz0019000039 |
| Enzyme Type ID | polyphenol oxidase000039 |
| Protein Name |
Purine nucleoside phosphorylase aq_167 EC 2.4.2.1 Adenosine deaminase aq_167 EC 3.5.4.4 S-methyl-5'-thioadenosine phosphorylase aq_167 EC 2.4.2.28 |
| Gene Name | aq_167 |
| Organism | Aquifex aeolicus (strain VF5) |
| Taxonomic Lineage | cellular organisms Bacteria Aquificae Aquificae Aquificales Aquificaceae Aquifex Aquifex aeolicus Aquifex aeolicus (strain VF5) |
| Enzyme Sequence | MYKQDFPEGKEALNLEIRLGNKLVRFRKFTGKEKIYLPIQRHTDKVIKLIDKDSPPLEGDAVITNLKNVEIGVRTADCVPIILLGKEWVGAVHAGWRGLKKGIIAKTLKALKEEGEDDITALVFPSAKGCCYEVGKEFKEFFRRNLKERNGKLFFDPQREAVEQLRENGIKSILVWEKCTICSPELPSYRRDKTKERMLTSVVILF |
| Enzyme Length | 206 |
| Uniprot Accession Number | O66554 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:27642, ChEBI:CHEBI:16335, ChEBI:CHEBI:16708, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; Evidence={ECO:0000250|UniProtKB:P84138};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27643; Evidence={ECO:0000250|UniProtKB:P84138}; CATALYTIC ACTIVITY: Reaction=phosphate + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:11852, ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:43474, ChEBI:CHEBI:58533; EC=2.4.2.28; Evidence={ECO:0000250|UniProtKB:P84138};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11853; Evidence={ECO:0000250|UniProtKB:P84138}; CATALYTIC ACTIVITY: Reaction=inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthine; Xref=Rhea:RHEA:27646, ChEBI:CHEBI:17368, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; Evidence={ECO:0000250|UniProtKB:P84138};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27647; Evidence={ECO:0000250|UniProtKB:P84138}; CATALYTIC ACTIVITY: Reaction=adenosine + H(+) + H2O = inosine + NH4(+); Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; Evidence={ECO:0000250|UniProtKB:P84138};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409; Evidence={ECO:0000250|UniProtKB:P84138}; |
| DNA Binding | |
| EC Number | 2.4.2.1; 3.5.4.4; 2.4.2.28 |
| Enzyme Function | FUNCTION: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity. {ECO:0000250|UniProtKB:P84138}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Metal binding (3) |
| Keywords | Copper;Hydrolase;Metal-binding;Oxidoreductase;Reference proteome;Transferase;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 23,637 |
| Kinetics | |
| Metal Binding | METAL 42; /note=Zn(2+); catalytic; /evidence=ECO:0000250|UniProtKB:P84138; METAL 78; /note=Zn(2+); catalytic; /evidence=ECO:0000250|UniProtKB:P84138; METAL 93; /note=Zn(2+); catalytic; /evidence=ECO:0000250|UniProtKB:P84138 |
| Rhea ID | RHEA:27642; RHEA:27643; RHEA:11852; RHEA:11853; RHEA:27646; RHEA:27647; RHEA:24408; RHEA:24409 |
| Cross Reference Brenda |