SURE_THET8
ID SURE_THET8 Reviewed; 244 AA.
AC Q53W92;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=TTHB070;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OG Plasmid pTT27.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AP008227; BAD71866.1; -; Genomic_DNA.
DR RefSeq; WP_011229220.1; NC_006462.1.
DR RefSeq; YP_145309.1; NC_006462.1.
DR PDB; 2E69; X-ray; 2.20 A; A/B/C/D=1-244.
DR PDB; 2E6B; X-ray; 2.50 A; A/B/C/D=1-244.
DR PDB; 2E6C; X-ray; 2.05 A; A/B/C/D=1-244.
DR PDB; 2E6E; X-ray; 2.50 A; A/B/C/D=1-244.
DR PDB; 2E6G; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L=1-244.
DR PDB; 2E6H; X-ray; 2.10 A; A/B/C/D=1-244.
DR PDBsum; 2E69; -.
DR PDBsum; 2E6B; -.
DR PDBsum; 2E6C; -.
DR PDBsum; 2E6E; -.
DR PDBsum; 2E6G; -.
DR PDBsum; 2E6H; -.
DR AlphaFoldDB; Q53W92; -.
DR SMR; Q53W92; -.
DR EnsemblBacteria; BAD71866; BAD71866; BAD71866.
DR GeneID; 3169602; -.
DR KEGG; ttj:TTHB070; -.
DR PATRIC; fig|300852.9.peg.2014; -.
DR HOGENOM; CLU_045192_1_3_0; -.
DR OMA; MHVEERI; -.
DR PhylomeDB; Q53W92; -.
DR EvolutionaryTrace; Q53W92; -.
DR Proteomes; UP000000532; Plasmid pTT27.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Metal-binding; Nucleotide-binding;
KW Plasmid; Reference proteome.
FT CHAIN 1..244
FT /note="5'-nucleotidase SurE"
FT /id="PRO_0000235662"
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 96
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2E6C"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:2E6C"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:2E6C"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:2E6C"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:2E6C"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:2E6C"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:2E6C"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:2E6C"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:2E6C"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:2E6C"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:2E6C"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:2E6C"
FT HELIX 138..152
FT /evidence="ECO:0007829|PDB:2E6C"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:2E6C"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:2E6C"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:2E6C"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2E6G"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:2E6C"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:2E6C"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:2E6C"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:2E6C"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:2E6G"
SQ SEQUENCE 244 AA; 26597 MW; 9D45179793B5F5BC CRC64;
MRILVTNDDG IYSPGLWALA EAASQFGEVF VAAPDTEQSA AGHAITIAHP VRAYPHPSPL
HAPHFPAYRV RGTPADCVAL GLHLFGPVDL VLSGVNLGSN LGHEIWHSGT VAAAKQGYLF
GLSAAAFSVP LNGEVPDFAG LRPWLLRTLE TLLRLERPFL VNVNLPLRPK GFLWTRQSVR
AYEGVVIPGE DPMGRPFYWF APRPLKEAEE GTDRWAVAQG FVSATPLRLD LTDETRLQPT
LAHD
