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UniProt functional annotation for P50389 | ||
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| UniProt code: P50389. |
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| Organism: | |
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus). |
| Taxonomy: | |
Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; Saccharolobus. |
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| Function: | |
Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules. Cleaves inosine, guanosine, and adenosine with a better efficiency than MTA. {ECO:0000269|PubMed:15819883, ECO:0000269|PubMed:7929153}. |
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| 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:15819883, ECO:0000269|PubMed:7929153}; |
| Catalytic activity: | |
Reaction=a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, ChEBI:CHEBI:26386, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, ChEBI:CHEBI:142355; EC=2.4.2.1; Evidence={ECO:0000269|PubMed:15819883, ECO:0000269|PubMed:7929153}; |
| Catalytic activity: | |
Reaction=a purine 2'-deoxy-D-ribonucleoside + phosphate = 2-deoxy- alpha-D-ribose 1-phosphate + a purine nucleobase; Xref=Rhea:RHEA:36431, ChEBI:CHEBI:26386, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259, ChEBI:CHEBI:142361; EC=2.4.2.1; Evidence={ECO:0000269|PubMed:15819883}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=154 uM for S-methyl-5'-thioadenosine {ECO:0000269|PubMed:15819883}; KM=25.4 uM for adenosine {ECO:0000269|PubMed:15819883}; KM=84 uM for inosine {ECO:0000269|PubMed:15819883}; KM=113.6 uM for guanosine {ECO:0000269|PubMed:15819883}; Temperature dependence: Optimum temperature is 120 degrees Celsius. Highly thermostable. {ECO:0000269|PubMed:15819883}; |
| Pathway: | |
Purine metabolism; purine nucleoside salvage. |
| Subunit: | |
Homohexamer; disulfide-linked. Trimer of homodimers, with three symmetric intersubunit disulfide bonds linking the dimers to one another. {ECO:0000269|PubMed:11489901, ECO:0000269|PubMed:7929153}. |
| Similarity: | |
Belongs to the PNP/UDP phosphorylase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.