AC   MF_00060;
DC   Protein; auto
TR   HAMAP; MF_00060; -; 1; level=0
XX
Names: SurE
XX
ID   SURE
case <OC:Enterobacterales>
DE   RecName: Full=5'/3'-nucleotidase SurE;
DE            EC=3.1.3.5;
DE            EC=3.1.3.6;
DE   AltName: Full=Exopolyphosphatase;
DE            EC=3.6.1.11;
DE   AltName: Full=Nucleoside monophosphate phosphohydrolase;
end case
case not <OC:Enterobacterales>
DE   RecName: Full=5'-nucleotidase SurE;
DE            EC=3.1.3.5;
DE   AltName: Full=Nucleoside 5'-monophosphate phosphohydrolase;
end case
GN   Name=surE;
XX
case <OC:Enterobacterales>
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.
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   -!- 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   -!- 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;
end case
case not <OC:Enterobacterales>
CC   -!- FUNCTION: Nucleotidase that shows phosphatase activity on nucleoside
CC       5'-monophosphates.
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;
end case
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC       Note=Binds 1 divalent metal cation per subunit.;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the SurE nucleotidase family.
XX
DR   Pfam; PF01975; SurE; 1; trigger=no
DR   NCBIfam; TIGR00087; SurE; 1; trigger=no
XX
KW   Cytoplasm
KW   Hydrolase
KW   Metal-binding
KW   Nucleotide-binding
XX
GO   GO:0008253; F:5'-nucleotidase activity
case <OC:Enterobacterales>
GO   GO:0004309; F:exopolyphosphatase activity
GO   GO:0008254; F:3'-nucleotidase activity
end case
GO   GO:0046872; F:metal ion binding
GO   GO:0005737; C:cytoplasm
XX
FT   From: SURE_THEMA (P96112)
FT   BINDING         8
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   Condition: D
FT   BINDING         9
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   Condition: D
FT   BINDING         39
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   Condition: S
FT   BINDING         95
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   Condition: N
XX
Size: 244-283;
Related: None;
Template: P96112; P0A840; Q8ZU79;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in BURL3, CHLCV, PYRAE, THET2
Plasmid: in THET2, THET8
Comments: In some organisms, surE was originally annotated as an acid
 phosphatase (EC 3.1.3.2).
 Weird C-terminal sequence in TREPA; no obvious frameshift; not shown in
 alignment and not used in size range.
 There are divergent second copies of surE in NOSS1 (alr3139) and SYNY3
 (sll1459).
XX
# Revision 1.41 2023/06/01
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