ID SURE_SHIDS Reviewed; 253 AA. AC Q32CI6; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, 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=SDY_2943; OS Shigella dysenteriae serotype 1 (strain Sd197). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=300267; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sd197; RX PubMed=16275786; DOI=10.1093/nar/gki954; RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., RA Jin Q.; RT "Genome dynamics and diversity of Shigella species, the etiologic agents of RT bacillary dysentery."; RL Nucleic Acids Res. 33:6445-6458(2005). 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; CP000034; ABB62969.1; -; Genomic_DNA. DR RefSeq; WP_005019613.1; NC_007606.1. DR RefSeq; YP_404460.1; NC_007606.1. DR AlphaFoldDB; Q32CI6; -. DR SMR; Q32CI6; -. DR STRING; 300267.SDY_2943; -. DR EnsemblBacteria; ABB62969; ABB62969; SDY_2943. DR KEGG; sdy:SDY_2943; -. DR PATRIC; fig|300267.13.peg.3535; -. DR HOGENOM; CLU_045192_1_2_6; -. DR Proteomes; UP000002716; 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; KW Reference proteome. FT CHAIN 1..253 FT /note="5'/3'-nucleotidase SurE" FT /id="PRO_0000235650" FT BINDING 8 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060" 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 39 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060" FT BINDING 92 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060" SQ SEQUENCE 253 AA; 26940 MW; 847309C8950E7008 CRC64; MRILLSNDDG VHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS LRTFTFENGD IAVQMGTPTD CVYLGVNALM RPRPDIVVSG INAGPNLGDD VIYSGTVAAA MEGRHFGFPA LAVSLDGHNH YDTAAAVTCS ILRALCEEPL RTGRILNINV PDLPLDQIKG IRVTRCGTRH PADQVIPQQD PRGNTLYWIG PPGGKCDAGP GTDFAAVDEG YVSITPLRVD LTAHSAQDVV SDWLNSVGVG TQW //