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UniProtKB/Swiss-Prot entry P66881


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SURE_SALTY
Primary accession number P66881
Secondary accession number Q8XFG4
Integrated into Swiss-Prot on October 11, 2004
Sequence was last modified on October 11, 2004 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 25)
Name and origin of the protein
Protein name Multifunctional protein surE
Synonyms None
Includes 5'/3'-nucleotidase
     (EC 3.1.3.5)
     (EC 3.1.3.6)
     (Nucleoside monophosphate phosphohydrolase)
Exopolyphosphatase
     (EC 3.6.1.11)
Gene name
Name: surE
OrderedLocusNames: STM2927
From
Salmonella typhimurium [TaxID: 602] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Salmonella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LT2 / SGSC1412 / ATCC 700720;
DOI=10.1038/35101614; PubMed=11677609 [NCBI, ExPASy, EBI, Israel, Japan]
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.;
"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
Nature 413:852-856(2001).
Comments
  • FUNCTION: Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs (By similarity).
  • CATALYTIC ACTIVITY: A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
  • CATALYTIC ACTIVITY: A 3'-ribonucleotide + H2O = a ribonucleoside + phosphate.
  • CATALYTIC ACTIVITY: (Polyphosphate)(n) + H2O = (polyphosphate)(n-1) + phosphate.
  • COFACTOR: Binds 1 divalent metal cation per subunit (By similarity).
  • SUBCELLULAR LOCATION: Cytoplasm (Potential).
  • SIMILARITY: Belongs to the surE nucleotidase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE008833; AAL21807.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_461848.1; -.
3D structure databases
HSSP P96112; 1J9L. [HSSP ENTRY / PDB]
ModBase P66881.
Enzyme and pathway databases
BioCyc STYP99287:STM2927-MON; -.
Organism-specific databases
StyGene SG?????; surE.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0008254; Molecular function: 3'-nucleotidase activity (inferred from electronic annotation from EC).
GO:0008253; Molecular function: 5'-nucleotidase activity (inferred from electronic annotation from HAMAP).
GO:0004309; Molecular function: exopolyphosphatase activity (inferred from electronic annotation from EC).
GO:0046872; Molecular function: metal ion binding (inferred from electronic annotation from HAMAP).
GO:0000166; Molecular function: nucleotide binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_00060; -; 1.
PBIL [Tree]
InterPro IPR002828; SurE-like_Pase/nucleotidase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.1210.10; SurE-like_Pase/nucleotidase; 1.
Pfam PF01975; SurE; 1.
Pfam graphical view of domain structure.
ProDom PD005378; SurE; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00087; surE; 1.
Proteomics databases
PRIDE P66881; -.
Genome annotation databases
GeneID 1254450; -.
GenomeReviews AE006468_GR; STM2927.
KEGG stm:STM2927; -.
Phylogenomic databases
HOGENOM P66881; -.
Genome annotation databases
CMR P66881; STM2927.
Other
ProtoNet P66881.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Multifunctional enzyme; Nucleotide-binding.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   1   253  253     Multifunctional protein surE. PRO_0000111839
METAL   8     8        Divalent metal cation (By similarity). 
METAL   9     9        Divalent metal cation (By similarity). 
METAL   39    39        Divalent metal cation (By similarity). 
METAL   92    92        Divalent metal cation (By similarity). 
Sequence information
Length: 253 AA [This is the length of the unprocessed precursor] Molecular weight: 26980 Da [This is the MW of the unprocessed precursor] CRC64: A8C4DD6EE42372F8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRILLSNDDG VHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS LRTFTFDNGD 

        70         80         90        100        110        120 
IAVQMGTPTD CVYLGVNALM RPRPDIVVSG INAGPNLGDD VIYSGTVAAA MEGRHLGFPA 

       130        140        150        160        170        180 
LAVSLNGYQH YDTAAAVTCA LLRGLSREPL RTGRILNVNV PDLPLAQVKG IRVTRCGSRH 

       190        200        210        220        230        240 
PADKVIPQED PRGNTLYWIG PPGDKYDAGP DTDFAAVDEG YVSVTPLHVD LTAHSAHDVV 

       250 
SDWLDSVGVG TQW 

P66881 in FASTA format

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