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UniProt functional annotation for P84138 | ||
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| UniProt code: P84138. |
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| Organism: | |
Geobacillus stearothermophilus (strain DSM 13240 / CIP 106956 / 10). |
| Taxonomy: | |
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. |
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| 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 (PubMed:31978345). Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate (PubMed:31978345). Also has adenosine deaminase activity (PubMed:31978345). {ECO:0000269|PubMed:31978345}. |
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| 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:0000269|PubMed:31978345}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27643; Evidence={ECO:0000269|PubMed:31978345}; |
| 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:0000269|PubMed:31978345}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11853; Evidence={ECO:0000269|PubMed:31978345}; |
| 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:0000269|PubMed:31978345}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27647; Evidence={ECO:0000269|PubMed:31978345}; |
| 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:0000269|PubMed:31978345}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409; Evidence={ECO:0000269|PubMed:31978345}; |
| Cofactor: | |
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:31978345}; Note=Binds 2 zinc ions (PubMed:31978345). One zinc is catalytic and mediates binding to the substrate, while the second is probably structural (PubMed:31978345). {ECO:0000269|PubMed:31978345}; |
| Similarity: | |
Belongs to the purine nucleoside phosphorylase YfiH/LACC1 family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.