ID   SURE_VIBCH              Reviewed;         250 AA.
AC   Q9KUI9;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 2.
DT   03-AUG-2022, entry version 112.
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=VC_0531;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF93699.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE003852; AAF93699.1; ALT_INIT; Genomic_DNA.
DR   PIR; F82311; F82311.
DR   RefSeq; NP_230182.1; NC_002505.1.
DR   RefSeq; WP_000698379.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KUI9; -.
DR   SMR; Q9KUI9; -.
DR   STRING; 243277.VC_0531; -.
DR   DNASU; 2615200; -.
DR   EnsemblBacteria; AAF93699; AAF93699; VC_0531.
DR   GeneID; 57739249; -.
DR   KEGG; vch:VC_0531; -.
DR   PATRIC; fig|243277.26.peg.507; -.
DR   eggNOG; COG0496; Bacteria.
DR   HOGENOM; CLU_045192_1_2_6; -.
DR   OMA; DCVHIAL; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008254; F:3'-nucleotidase activity; IBA:GO_Central.
DR   GO; GO:0008253; F:5'-nucleotidase activity; IBA:GO_Central.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IBA:GO_Central.
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   GO; GO:0046050; P:UMP catabolic process; IBA:GO_Central.
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..250
FT                   /note="5'-nucleotidase SurE"
FT                   /id="PRO_0000111849"
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   250 AA;  27213 MW;  CBD6442B3D4D25F4 CRC64;
     MKILLSNDDG VYAQGIHALA DALRDLAEIV IVAPDRNRSG ASNSLTLEHP LRVSQIAENT
     YSVQGTPTDC VHFALNELMK DALPDLVLSG INHGANLGDD VLYSGTVAAA MEGHFLGVQS
     IAFSLAGTTH FASAAHFVRQ LVEQHLANPI PTNRLLNVNI PDRPLELIQG IEVTRLGARH
     HAESMIKQKD PRGHDIYWLG PPGKEQDAGP GTDFHAIERG WVSLTPLQVD LTAHESLRSM
     DHWLKEKVNG