ID   SURE_SHIF8              Reviewed;         253 AA.
AC   Q0T1H5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Multifunctional protein surE;
DE   Includes:
DE     RecName: Full=5'/3'-nucleotidase;
DE              EC=3.1.3.5;
DE              EC=3.1.3.6;
DE     AltName: Full=Nucleoside monophosphate phosphohydrolase;
DE   Includes:
DE     RecName: Full=Exopolyphosphatase;
DE              EC=3.6.1.11;
GN   Name=surE; OrderedLocusNames=SFV_2754;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z.,
RA   Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y.,
RA   Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
CC   -!- FUNCTION: Nucleotidase with a broad substrate specificity as it
CC       can dephosphorylate various ribo- and deoxyribonucleoside 5'-
CC       monophosphates and ribonucleoside 3'-monophosphates with highest
CC       affinity to 3'-AMP. Also hydrolyzes polyphosphate
CC       (exopolyphosphatase activity) with the preference for short-chain-
CC       length substrates (P20-25). Might be involved in the regulation of
CC       dNTP and NTP pools, and in the turnover of 3'-mononucleotides
CC       produced by numerous intracellular RNases (T1, T2, and F) during
CC       the degradation of various RNAs (By similarity).
CC   -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside
CC       + phosphate.
CC   -!- CATALYTIC ACTIVITY: A 3'-ribonucleotide + H(2)O = a ribonucleoside
CC       + phosphate.
CC   -!- CATALYTIC ACTIVITY: (Polyphosphate)(n) + H(2)O =
CC       (polyphosphate)(n-1) + 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.
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DR   EMBL; CP000266; ABF04840.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_690145.1; -.
DR   GeneID; 4210404; -.
DR   GenomeReviews; CP000266_GR; SFV_2754.
DR   KEGG; sfv:SFV_2754; -.
DR   HOGENOM; Q0T1H5; -.
DR   BioCyc; SFLE373384:SFV_2754-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008254; F:3'-nucleotidase activity; IEA:EC.
DR   GO; GO:0008253; F:5'-nucleotidase activity; IEA:HAMAP.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IEA:EC.
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   Multifunctional enzyme; Nucleotide-binding.
FT   CHAIN         1    253       Multifunctional protein surE.
FT                                /FTId=PRO_0000335283.
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        92     92       Divalent metal cation (By similarity).
SQ   SEQUENCE   253 AA;  26931 MW;  291667BAEF02C2CB CRC64;
     MRILLSNDDG VHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS LRTFTFENGD
     IAVQMGTPTD CVYLGVNALM RPRPDIVVSG INAGPNLGDD VIYSGTVAAA MEGRHLGFPA
     LAVSLDGHKH YDTAAAVTCS ILRALCKEPL RTGRILNINV QDLPLDQIKG IRVTRCGTRH
     PADQVIPQQD PRGNTLYWIG PPGGKCDAGP GTDFAAVDEG YVSITPLHVD LTAHSAQDVV
     SDWLNSVGVG TQW
//