Detail Information for IndEnz0019000053
IED ID IndEnz0019000053
Enzyme Type ID polyphenol oxidase000053
Protein Name Purine nucleoside phosphorylase MW1070
EC 2.4.2.1
Adenosine deaminase MW1070
EC 3.5.4.4
S-methyl-5'-thioadenosine phosphorylase MW1070
EC 2.4.2.28
Gene Name MW1070
Organism Staphylococcus aureus (strain MW2)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus aureus Staphylococcus aureus (strain MW2)
Enzyme Sequence MNDNFKKQPHHLIYEELLQQGITLGITTRGDGLSDYPKNAFNMARYIDDRPYNITQHQLQLAEEIAFDRKNWVFPIQTHENKVACITKDDIGTNIDTLTDALHGIDAMYTYDSNVLLTMCYADCVPVYFYSTKHHFIALAHAGWRGTYTEIVKEVLKHVNFDLKDLHVVIGPSTSSSYEINDDIKNKFETLPIDSANYIETRGRDRHGIDLKKANAALLNYYGVPKENIYTTAYATSEHLELFFSYRLEKGQTGRMLAFIGQQ
Enzyme Length 263
Uniprot Accession Number Q8NX32
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;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 30,199
Kinetics
Metal Binding METAL 79; /note=Zn(2+); catalytic; /evidence=ECO:0000250|UniProtKB:P84138; METAL 124; /note=Zn(2+); catalytic; /evidence=ECO:0000250|UniProtKB:P84138; METAL 141; /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