ID SURE_YERPS Reviewed; 254 AA. AC Q66EC0; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 97. DE RecName: Full=5'/3'-nucleotidase SurE {ECO:0000255|HAMAP-Rule:MF_00060}; DE EC=3.1.3.5 {ECO:0000255|HAMAP-Rule:MF_00060}; DE EC=3.1.3.6 {ECO:0000255|HAMAP-Rule:MF_00060}; DE AltName: Full=Exopolyphosphatase {ECO:0000255|HAMAP-Rule:MF_00060}; DE EC=3.6.1.11 {ECO:0000255|HAMAP-Rule:MF_00060}; DE AltName: Full=Nucleoside monophosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00060}; GN Name=surE {ECO:0000255|HAMAP-Rule:MF_00060}; GN OrderedLocusNames=YPTB0773; OS Yersinia pseudotuberculosis serotype I (strain IP32953). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=273123; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IP32953; RX PubMed=15358858; DOI=10.1073/pnas.0404012101; RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M., RA Derbise A., Hauser L.J., Garcia E.; RT "Insights into the evolution of Yersinia pestis through whole-genome RT comparison with Yersinia pseudotuberculosis."; RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004). CC -!- FUNCTION: Nucleotidase with a broad substrate specificity as it can CC dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates CC and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. CC Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the CC preference for short-chain-length substrates (P20-25). Might be CC involved in the regulation of dNTP and NTP pools, and in the turnover CC of 3'-mononucleotides produced by numerous intracellular RNases (T1, CC T2, and F) during the degradation of various RNAs. {ECO:0000255|HAMAP- CC Rule:MF_00060}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + CC phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00060}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 3'-phosphate + H2O = a ribonucleoside + CC phosphate; Xref=Rhea:RHEA:10144, ChEBI:CHEBI:13197, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474; EC=3.1.3.6; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00060}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate; CC Xref=Rhea:RHEA:21528, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14279, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838, CC ChEBI:CHEBI:43474; EC=3.6.1.11; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00060}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00060}; CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00060}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00060}. CC -!- SIMILARITY: Belongs to the SurE nucleotidase family. CC {ECO:0000255|HAMAP-Rule:MF_00060}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX936398; CAH20013.1; -; Genomic_DNA. DR RefSeq; WP_011191778.1; NZ_CP009712.1. DR AlphaFoldDB; Q66EC0; -. DR SMR; Q66EC0; -. DR GeneID; 66842806; -. DR KEGG; ypo:BZ17_1783; -. DR KEGG; yps:YPTB0773; -. DR PATRIC; fig|273123.14.peg.1888; -. DR Proteomes; UP000001011; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008254; F:3'-nucleotidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004309; F:exopolyphosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.1210.10; Survival protein SurE-like phosphatase/nucleotidase; 1. DR HAMAP; MF_00060; SurE; 1. DR InterPro; IPR030048; SurE. DR InterPro; IPR002828; SurE-like_Pase/nucleotidase. DR InterPro; IPR036523; SurE-like_sf. DR NCBIfam; TIGR00087; surE; 1. DR PANTHER; PTHR30457; 5'-NUCLEOTIDASE SURE; 1. DR PANTHER; PTHR30457:SF12; 5'_3'-NUCLEOTIDASE SURE; 1. DR Pfam; PF01975; SurE; 1. DR SUPFAM; SSF64167; SurE-like; 1. PE 3: Inferred from homology; KW Cytoplasm; Hydrolase; Metal-binding; Nucleotide-binding. FT CHAIN 1..254 FT /note="5'/3'-nucleotidase SurE" FT /id="PRO_0000235673" FT BINDING 9 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060" FT BINDING 10 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060" FT BINDING 40 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060" FT BINDING 93 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060" SQ SEQUENCE 254 AA; 27289 MW; C1BBACEC6F9B2661 CRC64; MIRILLSNDD GISAPGIQTL ASALREFAQV QIVAPDRNRS GASNALTLDS ALRITTLSNG DIAVQQGTPT DCVYLGVNAL MRPRPDIVVS GINAGPNLGD DVIYSGTVAA AMEGRHLGYP ALAVSLNGHQ HYDTAAAVTC RLLRALQRKP LRTGKILNIN VPDLPLSEIK GIRVTRCGSR HPAEQVFCQQ DPRGQDLYWI GPPGEKYDAG PDTDFAAVEQ GYVSITPLQV DLTAYTAQEV VESWLANTEV DGEW //