IED ID | IndEnz0019000055 |
Enzyme Type ID | polyphenol oxidase000055 |
Protein Name |
Purine nucleoside phosphorylase XF_0940 EC 2.4.2.1 Adenosine deaminase XF_0940 EC 3.5.4.4 S-methyl-5'-thioadenosine phosphorylase XF_0940 EC 2.4.2.28 |
Gene Name | XF_0940 |
Organism | Xylella fastidiosa (strain 9a5c) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Xylella Xylella fastidiosa Xylella fastidiosa (strain 9a5c) |
Enzyme Sequence | MGRFPSWVLVADWPAPPGVMVLSTLRGGPGVSVAPFDRLNLGNCSGVAGDAPVCVERNRSRLVEMLGLPSVPHWLRQVHGVEVLRVDALLQSIARVVEPTADAAVTSVVGAVLAILTADCLPVVLAAVDGSEIGVVHAGWRGLADDVLGRTVAALRTSPEYLQAWLGPAAGPQAYEVGVDVYAAFVERDSGAACAFSVTRPGHWYVDLYALARQRLMRAGLSAVSIYGGGLCTISDPQRFFSHRRDRRSGRFATLAWIGC |
Enzyme Length | 260 |
Uniprot Accession Number | Q9PET8 |
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 | 27,613 |
Kinetics | |
Metal Binding | METAL 79; /note=Zn(2+); catalytic; /evidence=ECO:0000250|UniProtKB:P84138; METAL 120; /note=Zn(2+); catalytic; /evidence=ECO:0000250|UniProtKB:P84138; METAL 137; /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 |