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B7N6X4 (SURE_ECOLU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:ECUMN_3068
OrganismEscherichia coli O17:K52:H18 (strain UMN026 / ExPEC) [Complete proteome] [HAMAP]
Taxonomic identifier585056 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length253 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 – 2532535'/3'-nucleotidase SurE HAMAP-Rule MF_00060
PRO_1000196599

Sites

Metal binding81Divalent metal cation By similarity
Metal binding91Divalent metal cation By similarity
Metal binding391Divalent metal cation By similarity
Metal binding921Divalent metal cation By similarity

Sequences

Sequence LengthMass (Da)Tools
B7N6X4 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 2F493F0AEE06363B

FASTA25326,900
        10         20         30         40         50         60 
MRILLSNDDG VHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS LRTFTFENGD 

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

       130        140        150        160        170        180 
LAVSLDGHKH YDTAAAVTCS ILRALCKEPL RTGRILNINV PDLPLDQIKG IRVTRCGTRH 

       190        200        210        220        230        240 
PADKVIPQQD PRGNTLYWIG PPGGKCDAGP GTDFAAVDEG YVSITPLHVD LTAHSAQDVV 

       250 
SDWLNSVGVG TQW 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU928163 Genomic DNA. Translation: CAR14235.1.
RefSeqYP_002413757.1. NC_011751.1.

3D structure databases

ProteinModelPortalB7N6X4.
SMRB7N6X4. Positions 1-253.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING585056.ECUMN_3068.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR14235; CAR14235; ECUMN_3068.
GeneID7157397.
KEGGeum:ECUMN_3068.
PATRIC18445418. VBIEscCol32010_3244.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0496.
HOGENOMHOG000122500.
KOK03787.
OMADCVHIAL.
OrthoDBEOG68WR45.
ProtClustDBPRK00346.

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_ECOLU
AccessionPrimary (citable) accession number: B7N6X4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: April 16, 2014
This is version 35 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