SURE_AQUAE
ID SURE_AQUAE Reviewed; 251 AA.
AC O67004;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=aq_832;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC06967.1; -; Genomic_DNA.
DR PIR; A70372; A70372.
DR RefSeq; NP_213565.1; NC_000918.1.
DR RefSeq; WP_010880503.1; NC_000918.1.
DR PDB; 2WQK; X-ray; 1.50 A; A/B=1-251.
DR PDBsum; 2WQK; -.
DR AlphaFoldDB; O67004; -.
DR SMR; O67004; -.
DR STRING; 224324.aq_832; -.
DR EnsemblBacteria; AAC06967; AAC06967; aq_832.
DR KEGG; aae:aq_832; -.
DR PATRIC; fig|224324.8.peg.650; -.
DR eggNOG; COG0496; Bacteria.
DR HOGENOM; CLU_045192_1_2_0; -.
DR InParanoid; O67004; -.
DR OMA; DCVHIAL; -.
DR OrthoDB; 1909278at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008254; F:3'-nucleotidase activity; IBA:GO_Central.
DR GO; GO:0008253; F:5'-nucleotidase activity; IBA:GO_Central.
DR GO; GO:0004309; F:exopolyphosphatase activity; IBA:GO_Central.
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 GO; GO:0046050; P:UMP catabolic process; IBA:GO_Central.
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 Reference proteome.
FT CHAIN 1..251
FT /note="5'-nucleotidase SurE"
FT /id="PRO_0000111788"
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 94
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:2WQK"
FT HELIX 15..24
FT /evidence="ECO:0007829|PDB:2WQK"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:2WQK"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:2WQK"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:2WQK"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:2WQK"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:2WQK"
FT TURN 79..83
FT /evidence="ECO:0007829|PDB:2WQK"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:2WQK"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:2WQK"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:2WQK"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:2WQK"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:2WQK"
FT HELIX 135..152
FT /evidence="ECO:0007829|PDB:2WQK"
FT STRAND 158..167
FT /evidence="ECO:0007829|PDB:2WQK"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:2WQK"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:2WQK"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:2WQK"
FT STRAND 199..207
FT /evidence="ECO:0007829|PDB:2WQK"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:2WQK"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:2WQK"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:2WQK"
FT HELIX 238..248
FT /evidence="ECO:0007829|PDB:2WQK"
SQ SEQUENCE 251 AA; 28165 MW; 7D36DDD8BEB1C55B CRC64;
MPTFLLVNDD GYFSPGINAL REALKSLGRV VVVAPDRNLS GVGHSLTFTE PLKMRKIDTD
FYTVIDGTPA DCVHLGYRVI LEEKKPDLVL SGINEGPNLG EDITYSGTVS GAMEGRILGI
PSIAFSAFGR ENIMFEEIAK VCVDIVKKVL NEGIPEDTYL NVNIPNLRYE EIKGIKVTRQ
GKRAYKERVF KYIDPYGKPF YWIAAEEFGW HAEEGTDYWA VLNGYVSVTP LHLDLTNYKV
MKSIKYLEDS P
