Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A9R116 (SURE_YERPG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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:YpAngola_A0961
OrganismYersinia pestis bv. Antiqua (strain Angola) [Complete proteome] [HAMAP]
Taxonomic identifier349746 [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_1000092052

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
A9R116 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 99C139F3E5D4E4F6

FASTA25427,231
        10         20         30         40         50         60 
MIRILLSNDD GISAPGIQTL ASALRGFAQV 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 VPDLPLAEIK GIRVTRCGSR 

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

       250 
VESWLANTEV DGEW 

« Hide

References

[1]"Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Angola.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000901 Genomic DNA. Translation: ABX85503.1.
RefSeqYP_001605525.1. NC_010159.1.

3D structure databases

ProteinModelPortalA9R116.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349746.YpAngola_A0961.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX85503; ABX85503; YpAngola_A0961.
GeneID5799424.
KEGGypg:YpAngola_A0961.
PATRIC18570956. VBIYerPes97331_1273.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0496.
HOGENOMHOG000122500.
KOK03787.
OMAIPSMALS.
OrthoDBEOG68WR45.

Enzyme and pathway databases

BioCycYPES349746:GHPB-961-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_YERPG
AccessionPrimary (citable) accession number: A9R116
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: May 14, 2014
This is version 46 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