SURE_ECOSE
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 03-AUG-2022, entry version 70.
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}; OrderedLocusNames=ECSE_2996;
OS Escherichia coli (strain SE11).
OC Bacteria; Proteobacteria; 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 EnsemblBacteria; BAG78520; BAG78520; ECSE_2996.
DR GeneID; 67413964; -.
DR KEGG; ecy:ECSE_2996; -.
DR HOGENOM; CLU_045192_1_2_6; -.
DR OMA; DCVHIAL; -.
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; -; 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 PANTHER; PTHR30457; PTHR30457; 1.
DR Pfam; PF01975; SurE; 1.
DR SUPFAM; SSF64167; SSF64167; 1.
DR TIGRFAMs; TIGR00087; surE; 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
