ID   SURE_ECOSE              Reviewed;         253 AA.
AC   B6I6D4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 78.
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=ECSE_2996;
OS   Escherichia coli (strain SE11).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=409438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE11;
RX   PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA   Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA   Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the wild-type
RT   commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL   DNA Res. 15:375-386(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}.
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DR   EMBL; AP009240; BAG78520.1; -; Genomic_DNA.
DR   RefSeq; WP_001295182.1; NC_011415.1.
DR   AlphaFoldDB; B6I6D4; -.
DR   SMR; B6I6D4; -.
DR   GeneID; 75205607; -.
DR   KEGG; ecy:ECSE_2996; -.
DR   HOGENOM; CLU_045192_1_2_6; -.
DR   Proteomes; UP000008199; 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..253
FT                   /note="5'/3'-nucleotidase SurE"
FT                   /id="PRO_1000092003"
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
//