ID   SURE_SERP5              Reviewed;         253 AA.
AC   A8G9Z5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 85.
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=Spro_0829;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000826; ABV39935.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8G9Z5; -.
DR   SMR; A8G9Z5; -.
DR   STRING; 399741.Spro_0829; -.
DR   KEGG; spe:Spro_0829; -.
DR   eggNOG; COG0496; Bacteria.
DR   HOGENOM; CLU_045192_1_2_6; -.
DR   OrthoDB; 9780815at2; -.
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_0000335269"
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;  26842 MW;  CC6B502A1B030085 CRC64;
     MRILLSNDDG VTAPGIQVLA AALREFAEVQ VVAPDRNRSG SSNALTLESP LRTLTMPNGD
     IAVQQGTPTD CVYLGVNALM QPAPDIVVSG INAGPNLGDD VIYSGTVAAA MEGRHLGLPA
     LAVSLNGHQH YATAAAITCR VLRALQREPL RTGKILNINV PDLPLDQIKG IRVTRCGSRH
     PADKVFCQQD PRGQNLYWIG PPGDKFDAGP DTDFAAVEQG YVAITPLQVD LTAYAAQDVV
     KTWLTKAGVG GEW
//