ID SURE_RHOP5 Reviewed; 255 AA. AC Q07N44; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 1. DT 15-MAR-2017, entry version 66. 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=RPE_2703; OS Rhodopseudomonas palustris (strain BisA53). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316055; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BisA53; 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., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N., Kim E., RA Harwood C.S., Oda Y., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris BisA53."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Nucleotidase that shows phosphatase activity on CC nucleoside 5'-monophosphates. {ECO:0000255|HAMAP-Rule:MF_00060}. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. {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. CC {ECO:0000255|HAMAP-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000463; ABJ06640.1; -; Genomic_DNA. DR RefSeq; WP_011664118.1; NC_008435.1. DR ProteinModelPortal; Q07N44; -. DR SMR; Q07N44; -. DR STRING; 316055.RPE_2703; -. DR EnsemblBacteria; ABJ06640; ABJ06640; RPE_2703. DR KEGG; rpe:RPE_2703; -. DR PATRIC; 23259966; VBIRhoPal93214_2727. DR eggNOG; ENOG4105CV2; Bacteria. DR eggNOG; COG0496; LUCA. DR HOGENOM; HOG000122501; -. DR KO; K03787; -. DR OMA; MGARHIL; -. DR OrthoDB; POG091H01CP; -. DR Proteomes; UP000000654; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. 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 Pfam; PF01975; SurE; 1. DR SUPFAM; SSF64167; SSF64167; 1. DR TIGRFAMs; TIGR00087; surE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Metal-binding; KW Nucleotide-binding. FT CHAIN 1 255 5'-nucleotidase SurE. FT /FTId=PRO_1000007781. FT METAL 8 8 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00060}. FT METAL 9 9 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00060}. FT METAL 40 40 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00060}. FT METAL 93 93 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00060}. SQ SEQUENCE 255 AA; 27466 MW; 56B27AB251A8E899 CRC64; MRILCTNDDG VHAPGLKIVE EIARALSDDV WVVAPELDQS GVSHSLSLND PLRLREIGPR HFAVRGTPTD CVIMGARHIL GDKGPDLVLS GVNKGRNVAE DVVYSGTIAG ALEGTILGIP SFALSQEYSH DSRSAPLWET ALAHGPKILR KALDAGVPKN TVINVNFPAC APEEVAGVLV TRQGKRNQGF LRVDERRDGR GNPYFWIGFE RVVVVDTPAE GTDLAALAAR YISVTPLKLD RTDEGFSEAL RSTLA //