| UniProt functional annotation for P66881 | |||
| UniProt code: P66881. |
| Organism: | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). | |
| Taxonomy: | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Salmonella. | |
| Function: | Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. {ECO:0000255|HAMAP- Rule:MF_00060}. | |
| Catalytic activity: | Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00060}; | |
| Catalytic activity: | Reaction=a ribonucleoside 3'-phosphate + H2O = a ribonucleoside + phosphate; Xref=Rhea:RHEA:10144, ChEBI:CHEBI:13197, ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474; EC=3.1.3.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00060}; | |
| Catalytic activity: | Reaction=[phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate; Xref=Rhea:RHEA:21528, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14279, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838, ChEBI:CHEBI:43474; EC=3.6.1.11; Evidence={ECO:0000255|HAMAP- Rule:MF_00060}; | |
| Cofactor: | Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|HAMAP-Rule:MF_00060}; Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP- Rule:MF_00060}; | |
| Subcellular location: | Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00060}. | |
| Similarity: | Belongs to the SurE nucleotidase family. {ECO:0000255|HAMAP-Rule:MF_00060}. | |
Annotations taken from UniProtKB at the EBI.