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UniProt functional annotation for P33644 | ||
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| UniProt code: P33644. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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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). May also act as a polyphenol oxidase: able to oxidize syringaldazine and 2,2'-azino-bis(3-ethylbenzthiazoline-6- sulfonic acid) (ABTS) in vitro (PubMed:16740638). {ECO:0000269|PubMed:16740638, 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=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:16740638}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P84138}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=23 uM for 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid (at pH 4.5 and 40 degrees Celsius) {ECO:0000269|PubMed:16740638}; KM=1.10 uM for syringaldazine (at pH 4.5 and 40 degrees Celsius) {ECO:0000269|PubMed:16740638}; Note=kcat is 1450 min(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline- 6-sulfonic acid as substrate. kcat is 21720 min(-1) with syringaldazine as substrate (at pH 4.5 and 40 degrees Celsius). {ECO:0000269|PubMed:16740638}; pH dependence: Optimum pH is 5.5-8.4. Maintains 80% activity at pH 5.0-9.0. {ECO:0000269|PubMed:16740638}; Temperature dependence: Optimum temperature is 44 degrees Celsius. Maintains more than 80% activity at 50 degrees Celsius. {ECO:0000269|PubMed:16740638}; |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:16740638}. |
| Disruption phenotype: | |
Cells lacking this gene are more sensitive to ampicillin, cephradine and cefoxitin than wild-type. {ECO:0000269|PubMed:20065048}. |
| Similarity: | |
Belongs to the purine nucleoside phosphorylase YfiH/LACC1 family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.