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SURE_PHOLL
ID   SURE_PHOLL              Reviewed;         254 AA.
AC   Q7N8K4;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=plu0716;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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; BX571861; CAE13011.1; -; Genomic_DNA.
DR   RefSeq; WP_011145092.1; NC_005126.1.
DR   AlphaFoldDB; Q7N8K4; -.
DR   SMR; Q7N8K4; -.
DR   STRING; 243265.plu0716; -.
DR   EnsemblBacteria; CAE13011; CAE13011; plu0716.
DR   GeneID; 24167929; -.
DR   KEGG; plu:plu0716; -.
DR   eggNOG; COG0496; Bacteria.
DR   HOGENOM; CLU_045192_1_2_6; -.
DR   OMA; DCVHIAL; -.
DR   OrthoDB; 1909278at2; -.
DR   BioCyc; PLUM243265:PLU_RS03575-MON; -.
DR   Proteomes; UP000002514; 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;
KW   Reference proteome.
FT   CHAIN           1..254
FT                   /note="5'/3'-nucleotidase SurE"
FT                   /id="PRO_0000111826"
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         10
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         93
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
SQ   SEQUENCE   254 AA;  27288 MW;  56DAFE9896594CE4 CRC64;
     MLRILLSNDD GVTAPGIQVL AAALRENYHV QVVAPDRNRS GASNALTLDR SLSVNTLENG
     DISVLGGTPT DCVYLGVNRL VLPRPEIVVS GINRGPNLGD DVIYSGTVAA AMEGRHLGLP
     ALAISLNGEL HYQTAAEITC RLLQMLQTTP LRAGNILNVN VPDLPLEHIK GFRVTRCGSR
     HAAEEVYSMQ DPKGNMLYWL GPPGDKHDAG PETDFAAVEQ GYVSITPLQV DLTAYKAQAL
     VRDWLAKAEV DGEC
 
 
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