ID SURE_ECODH Reviewed; 253 AA. AC B1XCS0; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 1. DT 27-MAR-2024, entry version 80. 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=ECDH10B_2912; OS Escherichia coli (strain K12 / DH10B). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=316385; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / DH10B; RX PubMed=18245285; DOI=10.1128/jb.01695-07; RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B., RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., RA Posfai G., Weinstock G.M., Blattner F.R.; RT "The complete genome sequence of Escherichia coli DH10B: insights into the RT biology of a laboratory workhorse."; RL J. Bacteriol. 190:2597-2606(2008). 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; CP000948; ACB03861.1; -; Genomic_DNA. DR RefSeq; WP_001295182.1; NC_010473.1. DR AlphaFoldDB; B1XCS0; -. DR SMR; B1XCS0; -. DR GeneID; 75205607; -. DR KEGG; ecd:ECDH10B_2912; -. DR HOGENOM; CLU_045192_1_2_6; -. DR BRENDA; 3.6.1.22; 2026. DR BRENDA; 3.6.1.45; 2026. 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..253 FT /note="5'/3'-nucleotidase SurE" FT /id="PRO_1000092002" 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; 26900 MW; 33A7CD0AEE13C3DB CRC64; MRILLSNDDG VHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS LRTFTFENGD IAVQMGTPTD CVYLGVNALM RPRPDIVVSG INAGPNLGDD VIYSGTVAAA MEGRHLGFPA LAVSLDGHKH YDTAAAVTCS ILRALCKEPL RTGRILNINV PDLPLDQIKG IRVTRCGTRH PADQVIPQQD PRGNTLYWIG PPGGKCDAGP GTDFAAVDEG YVSITPLHVD LTAHSAQDVV SDWLNSVGVG TQW //