SURE_BRUA1
ID SURE_BRUA1 Reviewed; 255 AA.
AC B2S5B9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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};
GN OrderedLocusNames=BAbS19_I08450;
OS Brucella abortus (strain S19).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=430066;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S19;
RX PubMed=18478107; DOI=10.1371/journal.pone.0002193;
RA Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S.,
RA Bricker B., Yu G., Du L., Sobral B.W.;
RT "Genome sequence of Brucella abortus vaccine strain S19 compared to
RT virulent strains yields candidate virulence genes.";
RL PLoS ONE 3:E2193-E2193(2008).
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; CP000887; ACD72366.1; -; Genomic_DNA.
DR RefSeq; WP_002966786.1; NC_010742.1.
DR PDB; 4ZG5; X-ray; 1.90 A; A/C/D/G=1-255.
DR PDBsum; 4ZG5; -.
DR AlphaFoldDB; B2S5B9; -.
DR SMR; B2S5B9; -.
DR EnsemblBacteria; ACD72366; ACD72366; BAbS19_I08450.
DR GeneID; 3788979; -.
DR KEGG; bmc:BAbS19_I08450; -.
DR HOGENOM; CLU_045192_1_2_5; -.
DR OMA; DCVHIAL; -.
DR Proteomes; UP000002565; Chromosome 1.
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.
FT CHAIN 1..255
FT /note="5'-nucleotidase SurE"
FT /id="PRO_1000091987"
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 40
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT BINDING 92
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:4ZG5"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:4ZG5"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:4ZG5"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:4ZG5"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:4ZG5"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:4ZG5"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:4ZG5"
FT STRAND 85..94
FT /evidence="ECO:0007829|PDB:4ZG5"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:4ZG5"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:4ZG5"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:4ZG5"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:4ZG5"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:4ZG5"
FT HELIX 138..155
FT /evidence="ECO:0007829|PDB:4ZG5"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:4ZG5"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:4ZG5"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:4ZG5"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:4ZG5"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:4ZG5"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:4ZG5"
FT STRAND 228..236
FT /evidence="ECO:0007829|PDB:4ZG5"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:4ZG5"
SQ SEQUENCE 255 AA; 27509 MW; 1494C219789E17F4 CRC64;
MRILLTNDDG IHAEGLAVLE RIARKLSDDV WVVAPETDQS GLAHSLTLLE PLRLRQIDAR
HFALRGTPTD CVIMGVRHVL PGAPDLVLSG VNSGANMADD VTYSGTVAGA MEGTLLGVRA
IALSQEYEYA GDRRIVPWET AEAHAPELIG RLMEAGWPEG VLLNLNFPNC APEEVKGVRV
TAQGKLSHDA RLDERRDGRG FPYFWLHFGR GKAPVADDSD IAAIRSGCIS MTPLHLDLTA
HKVRAELGAA LGVEA
