ID SURE_SHIFL Reviewed; 253 AA. AC Q83JY2; Q7UBT1; DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 2. DT 27-MAR-2024, entry version 126. 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=SF2767, S2960; OS Shigella flexneri. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 / Serotype 2a; RX PubMed=12384590; DOI=10.1093/nar/gkf566; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella flexneri RT serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). 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 -!- CAUTION: Tyr-8 is present instead of the conserved Asp which is CC expected to be a metal-binding site residue. {ECO:0000305}. 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; AE005674; AAN44256.2; -; Genomic_DNA. DR EMBL; AE014073; AAP18082.1; -; Genomic_DNA. DR RefSeq; NP_708549.2; NC_004337.2. DR RefSeq; WP_011069490.1; NZ_WPGW01000039.1. DR AlphaFoldDB; Q83JY2; -. DR SMR; Q83JY2; -. DR STRING; 198214.SF2767; -. DR PaxDb; 198214-SF2767; -. DR GeneID; 1025770; -. DR KEGG; sfl:SF2767; -. DR KEGG; sfx:S2960; -. DR PATRIC; fig|198214.7.peg.3294; -. DR HOGENOM; CLU_045192_1_2_6; -. DR Proteomes; UP000001006; Chromosome. DR Proteomes; UP000002673; 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_0000111842" 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; 26980 MW; 191A97BAEF07A082 CRC64; MRILLSNYDG VHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS LRTFTFENGD IAVQMGTPTD CVYLGVNALM RPRPDIVVSG INAGPNLGDD VIYSGTVAAA MEGRHLGFPA LAVSLDGHKH YDTAAAVTCS ILRALCKEPL RTGRILNINV QDLPLDQIKG IRVTRCGTRH PADQVIPQQD PRGNTLYWIG PPGGKCDAGP GTDFAAVDEG YVSITPLHVD LTAHSAQDVV SDWLNSVGVG TQW //