ID SURE_BORA1 Reviewed; 252 AA. AC Q2L006; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 21. DE RecName: Full=5'-nucleotidase surE; DE EC=3.1.3.5; DE AltName: Full=Nucleoside 5'-monophosphate phosphohydrolase; GN Name=surE; OrderedLocusNames=BAV1981; OS Bordetella avium (strain 197N). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=360910; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16885469; DOI=10.1128/JB.01927-05; RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., RA King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., RA Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., RA Squares S., Woodward J., Parkhill J., Temple L.M.; RT "Comparison of the genome sequence of the poultry pathogen Bordetella RT avium with those of B. bronchiseptica, B. pertussis, and B. RT parapertussis reveals extensive diversity in surface structures RT associated with host interaction."; RL J. Bacteriol. 188:6002-6015(2006). CC -!- FUNCTION: Nucleotidase that shows phosphatase activity on CC nucleoside 5'-monophosphates (By similarity). CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: Binds 1 divalent metal cation per subunit (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- SIMILARITY: Belongs to the surE nucleotidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM167904; CAJ49590.1; -; Genomic_DNA. DR RefSeq; YP_786497.1; -. DR GeneID; 6267490; -. DR GenomeReviews; AM167904_GR; BAV1981. DR KEGG; bav:BAV1981; -. DR NMPDR; fig|521.1.peg.1517; -. DR HOGENOM; Q2L006; -. DR OMA; Q2L006; NLNIPPC. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:HAMAP. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR HAMAP; MF_00060; -; 1. DR InterPro; IPR002828; SurE-like_Pase/nucleotidase. DR Gene3D; G3DSA:3.40.1210.10; SurE-like_Pase/nucleotidase; 1. DR Pfam; PF01975; SurE; 1. DR ProDom; PD005378; SurE; 1. DR TIGRFAMs; TIGR00087; surE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Metal-binding; KW Nucleotide-binding. FT CHAIN 1 252 5'-nucleotidase surE. FT /FTId=PRO_0000235594. FT METAL 8 8 Divalent metal cation (By similarity). FT METAL 9 9 Divalent metal cation (By similarity). FT METAL 39 39 Divalent metal cation (By similarity). FT METAL 91 91 Divalent metal cation (By similarity). SQ SEQUENCE 252 AA; 26751 MW; 6A759E8BD4C93B3E CRC64; MRILVSNDDG YNAPGLEALV EALSDLGELT VVAPETNHSG ASNSLTLNRP LSVRQAANGF LYVNGTPTDC VHVALTGLMD TRPDLVVSGI NNGANLGDDT LYSGTVAAAS EAHLFGIPAI AFSLVDKGWE HLESAARAAR RIVERQIAAP LGVPALLNVN IPNRRYEDLR GVRVTRLGKR HPAEPVVRTT TPYGDTVYWI GPVGLAADAT PGTDFHAIAD GAVSLTPLRL DLTQYAQLEQ LGQWADPLCA NL //