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A8A3M3

- SURE_ECOHS

UniProt

A8A3M3 - SURE_ECOHS

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Protein

5'/3'-nucleotidase SurE

Gene

surE

Organism
Escherichia coli O9:H4 (strain HS)
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.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

BioCyciECOL331112:GHHI-2867-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:EcHS_A2882
OrganismiEscherichia coli O9:H4 (strain HS)
Taxonomic identifieri331112 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001123: 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_1000057411Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi331112.EcHS_A2882.

Structurei

3D structure databases

ProteinModelPortaliA8A3M3.
SMRiA8A3M3. Positions 1-253.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SurE nucleotidase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0496.
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.

A8A3M3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRILLSNDDG 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 PDLPLDQIKG IRVTRCGTRH PADQVIPQQD PRGNTLYWIG
210 220 230 240 250
PPGGKCDAGP GTDFAAVDEG YVSITPLHVD LTAHSAQDVV SDWLNSVGVG

TQW
Length:253
Mass (Da):26,900
Last modified:October 23, 2007 - v1
Checksum:i33A7CD0AEE13C3DB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000802 Genomic DNA. Translation: ABV07127.1.
RefSeqiYP_001459510.1. NC_009800.1.

Genome annotation databases

EnsemblBacteriaiABV07127; ABV07127; EcHS_A2882.
GeneIDi5591782.
KEGGiecx:EcHS_A2882.
PATRICi18315739. VBIEscCol77814_2814.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000802 Genomic DNA. Translation: ABV07127.1 .
RefSeqi YP_001459510.1. NC_009800.1.

3D structure databases

ProteinModelPortali A8A3M3.
SMRi A8A3M3. Positions 1-253.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 331112.EcHS_A2882.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABV07127 ; ABV07127 ; EcHS_A2882 .
GeneIDi 5591782.
KEGGi ecx:EcHS_A2882.
PATRICi 18315739. VBIEscCol77814_2814.

Phylogenomic databases

eggNOGi COG0496.
HOGENOMi HOG000122500.
KOi K03787.
OMAi QGKLEFG.
OrthoDBi EOG68WR45.

Enzyme and pathway databases

BioCyci ECOL331112:GHHI-2867-MONOMER.

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. "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
    Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
    J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HS.

Entry informationi

Entry nameiSURE_ECOHS
AccessioniPrimary (citable) accession number: A8A3M3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: October 29, 2014
This is version 46 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