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A8G9Z5 (SURE_SERP5) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 44. 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:Spro_0829
OrganismSerratia proteamaculans (strain 568) [Complete proteome] [HAMAP]
Taxonomic identifier399741 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

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_0000335269

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
A8G9Z5 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: CC6B502A1B030085

FASTA25326,842
        10         20         30         40         50         60 
MRILLSNDDG VTAPGIQVLA AALREFAEVQ VVAPDRNRSG SSNALTLESP LRTLTMPNGD 

        70         80         90        100        110        120 
IAVQQGTPTD CVYLGVNALM QPAPDIVVSG INAGPNLGDD VIYSGTVAAA MEGRHLGLPA 

       130        140        150        160        170        180 
LAVSLNGHQH YATAAAITCR VLRALQREPL RTGKILNINV PDLPLDQIKG IRVTRCGSRH 

       190        200        210        220        230        240 
PADKVFCQQD PRGQNLYWIG PPGDKFDAGP DTDFAAVEQG YVAITPLQVD LTAYAAQDVV 

       250 
KTWLTKAGVG GEW 

« Hide

References

[1]"Complete sequence of chromosome of Serratia proteamaculans 568."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Taghavi S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 568.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000826 Genomic DNA. Translation: ABV39935.1.
RefSeqYP_001477063.1. NC_009832.1.

3D structure databases

ProteinModelPortalA8G9Z5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING399741.Spro_0829.

Proteomic databases

PRIDEA8G9Z5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV39935; ABV39935; Spro_0829.
GeneID5603034.
KEGGspe:Spro_0829.
PATRIC32414302. VBISerPro44537_0858.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSPRO399741:GI55-857-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_SERP5
AccessionPrimary (citable) accession number: A8G9Z5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 13, 2007
Last modified: April 16, 2014
This is version 44 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