ID   SURE_RHIEC              Reviewed;         257 AA.
AC   Q2K966;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=5'-nucleotidase SurE {ECO:0000255|HAMAP-Rule:MF_00060};
DE            EC=3.1.3.5 {ECO:0000255|HAMAP-Rule:MF_00060};
DE   AltName: Full=Nucleoside 5'-monophosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00060};
GN   Name=surE {ECO:0000255|HAMAP-Rule:MF_00060}; OrderedLocusNames=RHE_CH01827;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
CC   -!- FUNCTION: Nucleotidase that shows phosphatase activity on nucleoside
CC       5'-monophosphates. {ECO:0000255|HAMAP-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   -!- 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; CP000133; ABC90620.1; -; Genomic_DNA.
DR   RefSeq; WP_011425117.1; NC_007761.1.
DR   AlphaFoldDB; Q2K966; -.
DR   SMR; Q2K966; -.
DR   STRING; 347834.RHE_CH01827; -.
DR   EnsemblBacteria; ABC90620; ABC90620; RHE_CH01827.
DR   KEGG; ret:RHE_CH01827; -.
DR   eggNOG; COG0496; Bacteria.
DR   HOGENOM; CLU_045192_1_2_5; -.
DR   OMA; DCVHIAL; -.
DR   Proteomes; UP000001936; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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;
KW   Reference proteome.
FT   CHAIN           1..257
FT                   /note="5'-nucleotidase SurE"
FT                   /id="PRO_1000007777"
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         40
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   257 AA;  27961 MW;  1C789A26A2535E72 CRC64;
     MRILLTNDDG VHAGGLAALE RIARTLSDDV WIVAPETDQS GLAHSLSLSE PLRLRKISDK
     HFALRGTPTD CVIMGIRQVM DIKPDLVLSG VNSGSNVADD VTYSGTIAGA IEGTMQGVRS
     FALSQAYLYE DGARIVPWEV CETHAPALLE KLMVLDLPDG TFLNLNFPNC RPDEVDGAEV
     TMQGKLAFNL QVDARSDGRG FPYYWLKFGE RAGAFIEGTD IHALKHNKIS VTPLKLDLTD
     YSVTDRVARA LGYGAQV