Skip Header

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

P66881

- SURE_SALTY

UniProt

P66881 - SURE_SALTY

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

5'/3'-nucleotidase SurE

Gene

surE

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

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

Binds 1 divalent metal cation per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi8 – 81Divalent metal cationUniRule annotation
Metal bindingi9 – 91Divalent metal cationUniRule annotation
Metal bindingi39 – 391Divalent metal cationUniRule annotation
Metal bindingi92 – 921Divalent metal cationUniRule annotation

GO - Molecular functioni

  1. 3'-nucleotidase activity Source: UniProtKB-HAMAP
  2. 5'-nucleotidase activity Source: UniProtKB-HAMAP
  3. exopolyphosphatase activity Source: UniProtKB-HAMAP
  4. metal ion binding Source: UniProtKB-HAMAP
  5. nucleotide binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciSENT99287:GCTI-2943-MONOMER.

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:STM2927
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2532535'/3'-nucleotidase SurEPRO_0000111839Add
BLAST

Proteomic databases

PRIDEiP66881.

Interactioni

Protein-protein interaction databases

STRINGi99287.STM2927.

Structurei

Secondary structure

1
253
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi14 – 2310Combined sources
Turni24 – 263Combined sources
Beta strandi27 – 3610Combined sources
Beta strandi52 – 554Combined sources
Beta strandi61 – 644Combined sources
Helixi68 – 7710Combined sources
Beta strandi80 – 823Combined sources
Beta strandi85 – 9410Combined sources
Helixi98 – 1036Combined sources
Helixi105 – 1117Combined sources
Turni112 – 1154Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi120 – 12910Combined sources
Helixi131 – 14717Combined sources
Beta strandi154 – 1607Combined sources
Helixi165 – 1673Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi178 – 1803Combined sources
Beta strandi185 – 1895Combined sources
Beta strandi195 – 1995Combined sources
Beta strandi205 – 2073Combined sources
Helixi213 – 2186Combined sources
Beta strandi222 – 2276Combined sources
Helixi234 – 2363Combined sources
Helixi237 – 24711Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V4NX-ray1.70A1-253[»]
2V4OX-ray2.71A/B/C/D1-253[»]
4G9OX-ray2.12A/B1-253[»]
4GADX-ray2.35A/B1-253[»]
ProteinModelPortaliP66881.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP66881.

Family & Domainsi

Sequence similaritiesi

Belongs to the SurE nucleotidase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000122500.
KOiK03787.
OMAiVCDLIPK.
OrthoDBiEOG68WR45.
PhylomeDBiP66881.

Family and domain databases

Gene3Di3.40.1210.10. 1 hit.
HAMAPiMF_00060. SurE.
InterProiIPR002828. SurE-like_Pase/nucleotidase.
[Graphical view]
PfamiPF01975. SurE. 1 hit.
[Graphical view]
SUPFAMiSSF64167. SSF64167. 1 hit.
TIGRFAMsiTIGR00087. surE. 1 hit.

Sequencei

Sequence statusi: Complete.

P66881-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRILLSNDDG VHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS
60 70 80 90 100
LRTFTFDNGD IAVQMGTPTD CVYLGVNALM RPRPDIVVSG INAGPNLGDD
110 120 130 140 150
VIYSGTVAAA MEGRHLGFPA LAVSLNGYQH YDTAAAVTCA LLRGLSREPL
160 170 180 190 200
RTGRILNVNV PDLPLAQVKG IRVTRCGSRH PADKVIPQED PRGNTLYWIG
210 220 230 240 250
PPGDKYDAGP DTDFAAVDEG YVSVTPLHVD LTAHSAHDVV SDWLDSVGVG

TQW
Length:253
Mass (Da):26,980
Last modified:October 11, 2004 - v1
Checksum:iA8C4DD6EE42372F8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006468 Genomic DNA. Translation: AAL21807.1.
RefSeqiNP_461848.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL21807; AAL21807; STM2927.
GeneIDi1254450.
KEGGistm:STM2927.
PATRICi32384539. VBISalEnt20916_3081.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006468 Genomic DNA. Translation: AAL21807.1 .
RefSeqi NP_461848.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2V4N X-ray 1.70 A 1-253 [» ]
2V4O X-ray 2.71 A/B/C/D 1-253 [» ]
4G9O X-ray 2.12 A/B 1-253 [» ]
4GAD X-ray 2.35 A/B 1-253 [» ]
ProteinModelPortali P66881.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 99287.STM2927.

Proteomic databases

PRIDEi P66881.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL21807 ; AAL21807 ; STM2927 .
GeneIDi 1254450.
KEGGi stm:STM2927.
PATRICi 32384539. VBISalEnt20916_3081.

Phylogenomic databases

HOGENOMi HOG000122500.
KOi K03787.
OMAi VCDLIPK.
OrthoDBi EOG68WR45.
PhylomeDBi P66881.

Enzyme and pathway databases

BioCyci SENT99287:GCTI-2943-MONOMER.

Miscellaneous databases

EvolutionaryTracei P66881.

Family and domain databases

Gene3Di 3.40.1210.10. 1 hit.
HAMAPi MF_00060. SurE.
InterProi IPR002828. SurE-like_Pase/nucleotidase.
[Graphical view ]
Pfami PF01975. SurE. 1 hit.
[Graphical view ]
SUPFAMi SSF64167. SSF64167. 1 hit.
TIGRFAMsi TIGR00087. surE. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.

Entry informationi

Entry nameiSURE_SALTY
AccessioniPrimary (citable) accession number: P66881
Secondary accession number(s): Q8XFG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: October 29, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3