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Q66EC0 (SURE_YERPS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
5'/3'-nucleotidase SurE

EC=3.1.3.5
EC=3.1.3.6
Alternative name(s):
Exopolyphosphatase
EC=3.6.1.11
Nucleoside monophosphate phosphohydrolase
Gene names
Name:surE
Ordered Locus Names:YPTB0773
OrganismYersinia pseudotuberculosis serotype I (strain IP32953) [Complete proteome] [HAMAP]
Taxonomic identifier273123 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (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. HAMAP-Rule MF_00060

Catalytic activity

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate. HAMAP-Rule MF_00060

A 3'-ribonucleotide + H2O = a ribonucleoside + phosphate. HAMAP-Rule MF_00060

(Polyphosphate)(n) + H2O = (polyphosphate)(n-1) + phosphate. HAMAP-Rule MF_00060

Cofactor

Binds 1 divalent metal cation per subunit By similarity.

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00060.

Sequence similarities

Belongs to the SurE nucleotidase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3'-nucleotidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

5'-nucleotidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

exopolyphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2542545'/3'-nucleotidase SurE HAMAP-Rule MF_00060
PRO_0000235673

Sites

Metal binding91Divalent metal cation By similarity
Metal binding101Divalent metal cation By similarity
Metal binding401Divalent metal cation By similarity
Metal binding931Divalent metal cation By similarity

Sequences

Sequence LengthMass (Da)Tools
Q66EC0 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: C1BBACEC6F9B2661

FASTA25427,289
        10         20         30         40         50         60 
MIRILLSNDD GISAPGIQTL ASALREFAQV QIVAPDRNRS GASNALTLDS ALRITTLSNG 

        70         80         90        100        110        120 
DIAVQQGTPT DCVYLGVNAL MRPRPDIVVS GINAGPNLGD DVIYSGTVAA AMEGRHLGYP 

       130        140        150        160        170        180 
ALAVSLNGHQ HYDTAAAVTC RLLRALQRKP LRTGKILNIN VPDLPLSEIK GIRVTRCGSR 

       190        200        210        220        230        240 
HPAEQVFCQQ DPRGQDLYWI GPPGEKYDAG PDTDFAAVEQ GYVSITPLQV DLTAYTAQEV 

       250 
VESWLANTEV DGEW 

« Hide

References

[1]"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis."
Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B. expand/collapse author list , Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E.
Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IP32953.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX936398 Genomic DNA. Translation: CAH20013.1.
RefSeqYP_069314.1. NC_006155.1.

3D structure databases

ProteinModelPortalQ66EC0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273123.YPTB0773.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH20013; CAH20013; YPTB0773.
GeneID2956654.
KEGGyps:YPTB0773.
PATRIC18639846. VBIYerPse22266_1016.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0496.
HOGENOMHOG000122500.
KOK03787.
OMAIPSMALS.
OrthoDBEOG68WR45.

Enzyme and pathway databases

BioCycYPSE273123:GI1M-814-MONOMER.

Family and domain databases

Gene3D3.40.1210.10. 1 hit.
HAMAPMF_00060. SurE.
InterProIPR002828. SurE-like_Pase/nucleotidase.
[Graphical view]
PfamPF01975. SurE. 1 hit.
[Graphical view]
SUPFAMSSF64167. SSF64167. 1 hit.
TIGRFAMsTIGR00087. surE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSURE_YERPS
AccessionPrimary (citable) accession number: Q66EC0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: October 11, 2004
Last modified: May 14, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families