Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

5'/3'-nucleotidase SurE

Gene

surE

Organism
Shigella flexneri
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.UniRule annotation
A 3'-ribonucleotide + H2O = a ribonucleoside + phosphate.UniRule annotation
(Polyphosphate)(n) + H2O = (polyphosphate)(n-1) + phosphate.UniRule annotation

Cofactori

a divalent metal cationUniRule annotationNote: Binds 1 divalent metal cation per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi9 – 91Divalent metal cationUniRule annotation
Metal bindingi39 – 391Divalent metal cationUniRule annotation
Metal bindingi92 – 921Divalent metal cationUniRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
5'/3'-nucleotidase SurEUniRule annotation (EC:3.1.3.5UniRule annotation, EC:3.1.3.6UniRule annotation)
Alternative name(s):
ExopolyphosphataseUniRule annotation (EC:3.6.1.11UniRule annotation)
Nucleoside monophosphate phosphohydrolaseUniRule annotation
Gene namesi
Name:surEUniRule annotation
Ordered Locus Names:SF2767, S2960
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000002673 Componenti: Chromosome UP000001006 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2532535'/3'-nucleotidase SurEPRO_0000111842Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi198214.SF2767.

Structurei

3D structure databases

ProteinModelPortaliQ83JY2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SurE nucleotidase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0496.
HOGENOMiHOG000122500.
KOiK03787.
OMAiANGFYYV.
OrthoDBiEOG68WR45.

Family and domain databases

Gene3Di3.40.1210.10. 1 hit.
HAMAPiMF_00060. SurE.
InterProiIPR030048. SurE.
IPR002828. SurE-like_Pase/nucleotidase.
[Graphical view]
PfamiPF01975. SurE. 1 hit.
[Graphical view]
SUPFAMiSSF64167. SSF64167. 1 hit.
TIGRFAMsiTIGR00087. surE. 1 hit.

Sequencei

Sequence statusi: Complete.

Q83JY2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRILLSNYDG VHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS
60 70 80 90 100
LRTFTFENGD IAVQMGTPTD CVYLGVNALM RPRPDIVVSG INAGPNLGDD
110 120 130 140 150
VIYSGTVAAA MEGRHLGFPA LAVSLDGHKH YDTAAAVTCS ILRALCKEPL
160 170 180 190 200
RTGRILNINV QDLPLDQIKG IRVTRCGTRH PADQVIPQQD PRGNTLYWIG
210 220 230 240 250
PPGGKCDAGP GTDFAAVDEG YVSITPLHVD LTAHSAQDVV SDWLNSVGVG

TQW
Length:253
Mass (Da):26,980
Last modified:December 15, 2003 - v2
Checksum:i191A97BAEF07A082
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN44256.2.
AE014073 Genomic DNA. Translation: AAP18082.1.
RefSeqiNP_708549.2. NC_004337.2.
WP_011069490.1. NZ_LM651928.1.

Genome annotation databases

EnsemblBacteriaiAAN44256; AAN44256; SF2767.
AAP18082; AAP18082; S2960.
GeneIDi1025770.
KEGGisfl:SF2767.
PATRICi18707590. VBIShiFle31049_3250.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN44256.2.
AE014073 Genomic DNA. Translation: AAP18082.1.
RefSeqiNP_708549.2. NC_004337.2.
WP_011069490.1. NZ_LM651928.1.

3D structure databases

ProteinModelPortaliQ83JY2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198214.SF2767.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN44256; AAN44256; SF2767.
AAP18082; AAP18082; S2960.
GeneIDi1025770.
KEGGisfl:SF2767.
PATRICi18707590. VBIShiFle31049_3250.

Phylogenomic databases

eggNOGiCOG0496.
HOGENOMiHOG000122500.
KOiK03787.
OMAiANGFYYV.
OrthoDBiEOG68WR45.

Family and domain databases

Gene3Di3.40.1210.10. 1 hit.
HAMAPiMF_00060. SurE.
InterProiIPR030048. SurE.
IPR002828. SurE-like_Pase/nucleotidase.
[Graphical view]
PfamiPF01975. SurE. 1 hit.
[Graphical view]
SUPFAMiSSF64167. SSF64167. 1 hit.
TIGRFAMsiTIGR00087. surE. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiSURE_SHIFL
AccessioniPrimary (citable) accession number: Q83JY2
Secondary accession number(s): Q7UBT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: July 22, 2015
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Tyr-8 is present instead of the conserved Asp which is expected to be a metal-binding site residue.Curated

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.