SubmitCancel

Skip Header

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

P0A841

- SURE_ECOL6

UniProt

P0A841 - SURE_ECOL6

(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, c3311
Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Status
Reviewed - 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 By similarity.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 By similarity.

Sites

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

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

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:surE
Ordered Locus Names:c3311
OrganismiEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Taxonomic identifieri199310 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001410: Chromosome

Subcellular locationi

Cytoplasm Reviewed prediction UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2532535'/3'-nucleotidase SurEUniRule annotation
PRO_0000111811Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi199310.c3311.

Structurei

3D structure databases

ProteinModelPortaliP0A841.
SMRiP0A841. Positions 1-253.

Family & Domainsi

Sequence similaritiesi

Belongs to the SurE nucleotidase family.

Phylogenomic databases

HOGENOMiHOG000122500.
KOiK03787.
OMAiQGKLEFG.
OrthoDBiEOG68WR45.

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.

P0A841-1 [UniParc]FASTAAdd to Basket

« Hide

MRILLSNDDG VHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS    50
LRTFTFENGD IAVQMGTPTD CVYLGVNALM RPRPDIVVSG INAGPNLGDD 100
VIYSGTVAAA MEGRHLGFPA LAVSLDGHKH YDTAAAVTCS ILRALCKEPL 150
RTGRILNINV PDLPLDQIKG IRVTRCGTRH PADQVIPQQD PRGNTLYWIG 200
PPGGKCDAGP GTDFAAVDEG YVSITPLHVD LTAHSAQDVV SDWLNSVGVG 250
TQW 253
Length:253
Mass (Da):26,900
Last modified:June 7, 2005 - v1
Checksum:i33A7CD0AEE13C3DB
GO

Sequence cautioni

The sequence AAN81760.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014075 Genomic DNA. Translation: AAN81760.1. Different initiation.
RefSeqiNP_755190.1. NC_004431.1.

Genome annotation databases

EnsemblBacteriaiAAN81760; AAN81760; c3311.
GeneIDi1039131.
KEGGiecc:c3311.
PATRICi18284457. VBIEscCol75197_3118.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014075 Genomic DNA. Translation: AAN81760.1 . Different initiation.
RefSeqi NP_755190.1. NC_004431.1.

3D structure databases

ProteinModelPortali P0A841.
SMRi P0A841. Positions 1-253.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 199310.c3311.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN81760 ; AAN81760 ; c3311 .
GeneIDi 1039131.
KEGGi ecc:c3311.
PATRICi 18284457. VBIEscCol75197_3118.

Phylogenomic databases

HOGENOMi HOG000122500.
KOi K03787.
OMAi QGKLEFG.
OrthoDBi EOG68WR45.

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: CFT073 / ATCC 700928 / UPEC.

Entry informationi

Entry nameiSURE_ECOL6
AccessioniPrimary (citable) accession number: P0A841
Secondary accession number(s): P36664
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: May 14, 2014
This is version 60 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi