SURE_YERPP
ID SURE_YERPP Reviewed; 254 AA.
AC A4TQ00;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=YPDSF_3002;
OS Yersinia pestis (strain Pestoides F).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=386656;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pestoides F;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Worsham P., Chu M., Bearden S., Garcia E.,
RA Richardson P.;
RT "Complete sequence of chromosome of Yersinia pestis Pestoides F.";
RL Submitted (FEB-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; CP000668; ABP41362.1; -; Genomic_DNA.
DR RefSeq; WP_002209394.1; NZ_CP009715.1.
DR AlphaFoldDB; A4TQ00; -.
DR SMR; A4TQ00; -.
DR GeneID; 57975351; -.
DR KEGG; ypp:YPDSF_3002; -.
DR PATRIC; fig|386656.14.peg.1361; -.
DR OMA; DCVHIAL; -.
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.
FT CHAIN 1..254
FT /note="5'/3'-nucleotidase SurE"
FT /id="PRO_1000007805"
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; 27231 MW; 99C139F3E5D4E4F6 CRC64;
MIRILLSNDD GISAPGIQTL ASALRGFAQV QIVAPDRNRS GASNALTLDS ALRITTLSNG
DIAVQQGTPT DCVYLGVNAL MRPRPDIVVS GINAGPNLGD DVIYSGTVAA AMEGRHLGYP
ALAVSLNGHQ HYDTAAAVTC RLLRALQRKP LRTGKILNIN VPDLPLAEIK GIRVTRCGSR
HPAEQVFCQQ DPRGQDLYWI GPPGEKYDAG PDTDFAAVEQ GYVSITPLQV DLTAYMAQEV
VESWLANTEV DGEW
