| IED ID | IndEnz0019000038 |
| Enzyme Type ID | polyphenol oxidase000038 |
| Protein Name |
Purine nucleoside phosphorylase YfiH EC 2.4.2.1 Adenosine deaminase YfiH EC 3.5.4.4 S-methyl-5'-thioadenosine phosphorylase YfiH EC 2.4.2.28 |
| Gene Name | yfiH SF2654 |
| Organism | Shigella flexneri |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Shigella Shigella flexneri |
| Enzyme Sequence | MSKLIVPQWPLPKGVAACSSTRIGGVSLPPYDSLNLGAHCGDNPDHVEENRKRLFAAGNLPSKPVWLEQVHGKDVLKLTGEPYASKRADASYSNTPGTVCAVMTADCLPVLFCNRAGTEVAAVHAGWRGLCAGVLEETVSCFADKPENILAWLGPAIGPRAFEVGAEVREAFMAVDAKASAAFIQHGDKYLADIYQLARQRLANVGVEQIFGGDRCTYTENETFFSYRRDKTTGRMASFIWLI |
| Enzyme Length | 243 |
| Uniprot Accession Number | A0A384KG77 |
| 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 | Beta strand (12); Chain (1); Helix (8); Metal binding (3); Turn (4) |
| Keywords | 3D-structure;Copper;Hydrolase;Metal-binding;Oxidoreductase;Reference proteome;Transferase;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1U05; 1XAF; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 26,380 |
| Kinetics | |
| Metal Binding | METAL 71; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:16498617, ECO:0000269|Ref.2, ECO:0007744|PDB:1U05, ECO:0007744|PDB:1XAF"; METAL 107; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:16498617, ECO:0000269|Ref.2, ECO:0007744|PDB:1U05, ECO:0007744|PDB:1XAF"; METAL 124; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:16498617, ECO:0000269|Ref.2, ECO:0007744|PDB:1U05, ECO:0007744|PDB:1XAF" |
| Rhea ID | RHEA:27642; RHEA:27643; RHEA:11852; RHEA:11853; RHEA:27646; RHEA:27647; RHEA:24408; RHEA:24409 |
| Cross Reference Brenda |