Detail Information for IndEnz0019000045
IED ID IndEnz0019000045
Enzyme Type ID polyphenol oxidase000045
Protein Name Purine nucleoside phosphorylase Cj1217c
EC 2.4.2.1
Adenosine deaminase Cj1217c
EC 3.5.4.4
S-methyl-5'-thioadenosine phosphorylase Cj1217c
EC 2.4.2.28
Gene Name Cj1217c
Organism Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria delta/epsilon subdivisions Epsilonproteobacteria Campylobacterales Campylobacteraceae Campylobacter Campylobacter jejuni Campylobacter jejuni subsp. jejuni Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Enzyme Sequence MGRSRKNFLSLLENDKVGIFCAFDKDYNVFRAKIHNENLFSHLGFKDIEKCVFMDQIHSHKVIIYDENLKNLSCDGLISKEKNIALCVLSADCLPLILYHESGIIAALHSGRKGSFENILKECVDQITMQNSHLDKNKFHLFILPGICAKNYEIDGEILEFAKKEFKEFVQDDKLDLKALVKFQAQNLGIENIKDCGICSFDDESFFSYRRDKTTKRFVSVVYLKD
Enzyme Length 226
Uniprot Accession Number Q9PN78
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 17615063;
Motif
Gene Encoded By
Mass 26,064
Kinetics
Metal Binding METAL 58; /note=Zn(2+); catalytic; /evidence=ECO:0000250|UniProtKB:P84138; METAL 93; /note=Zn(2+); catalytic; /evidence=ECO:0000250|UniProtKB:P84138; METAL 109; /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