SURE_COXBU
ID SURE_COXBU Reviewed; 258 AA.
AC Q9KI21;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=CBU_1671;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Nine Mile phase I;
RX PubMed=11447163; DOI=10.1128/iai.69.8.4874-4883.2001;
RA Seshadri R., Samuel J.E.;
RT "Characterization of a stress-induced alternate sigma factor, RpoS, of
RT Coxiella burnetii and its expression during the development cycle.";
RL Infect. Immun. 69:4874-4883(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AF244357; AAF73516.1; -; Genomic_DNA.
DR EMBL; AE016828; AAO91167.2; -; Genomic_DNA.
DR RefSeq; NP_820653.2; NC_002971.3.
DR RefSeq; WP_005770587.1; NZ_CCYB01000011.1.
DR PDB; 3TY2; X-ray; 1.88 A; A/B=1-258.
DR PDBsum; 3TY2; -.
DR AlphaFoldDB; Q9KI21; -.
DR SMR; Q9KI21; -.
DR STRING; 227377.CBU_1671; -.
DR EnsemblBacteria; AAO91167; AAO91167; CBU_1671.
DR GeneID; 1209582; -.
DR KEGG; cbu:CBU_1671; -.
DR PATRIC; fig|227377.7.peg.1661; -.
DR eggNOG; COG0496; Bacteria.
DR HOGENOM; CLU_045192_1_2_6; -.
DR OMA; DCVHIAL; -.
DR Proteomes; UP000002671; 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..258
FT /note="5'-nucleotidase SurE"
FT /id="PRO_0000111807"
FT BINDING 16
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT BINDING 17
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT BINDING 47
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT BINDING 99
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:3TY2"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:3TY2"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:3TY2"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:3TY2"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:3TY2"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:3TY2"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:3TY2"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:3TY2"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:3TY2"
FT STRAND 92..101
FT /evidence="ECO:0007829|PDB:3TY2"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:3TY2"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:3TY2"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:3TY2"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:3TY2"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:3TY2"
FT HELIX 140..156
FT /evidence="ECO:0007829|PDB:3TY2"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:3TY2"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:3TY2"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:3TY2"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:3TY2"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:3TY2"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:3TY2"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:3TY2"
FT STRAND 230..236
FT /evidence="ECO:0007829|PDB:3TY2"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:3TY2"
FT HELIX 246..256
FT /evidence="ECO:0007829|PDB:3TY2"
SQ SEQUENCE 258 AA; 28066 MW; C620B037CBF471ED CRC64;
MKKTATPKLR LLLSNDDGVY AKGLAILAKT LADLGEVDVV APDRNRSGAS NSLTLNAPLH
IKNLENGMIS VEGTPTDCVH LAITGVLPEM PDMVVAGINA GPNLGDDVWY SGTVAAAMEG
RFLGLPALAV SLGGELFRYY ETAAKVVYQL IQRIEKDPLP PSTILNINVP DLPYEELKGF
EVTRLGTRHR AEPTIRQIDP RGHPIYWVGA AGPEQDSGPG TDFFAMNHHC VSITPLRVDL
THYEAFDQLA SWVKRLEM
