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B1IUT5

- SURE_ECOLC

UniProt

B1IUT5 - SURE_ECOLC

Protein

5'/3'-nucleotidase SurE

Gene

surE

Organism
Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 40 (01 Oct 2014)
      Sequence version 1 (29 Apr 2008)
      Previous versions | rss
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    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

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciECOL481805:GI3G-989-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:EcolC_0968
    OrganismiEscherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)
    Taxonomic identifieri481805 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000317: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2532535'/3'-nucleotidase SurEPRO_1000075027Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi481805.EcolC_0968.

    Structurei

    3D structure databases

    ProteinModelPortaliB1IUT5.
    SMRiB1IUT5. 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.

    B1IUT5-1 [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:April 29, 2008 - v1
    Checksum:i33A7CD0AEE13C3DB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000946 Genomic DNA. Translation: ACA76637.1.
    RefSeqiYP_001723964.1. NC_010468.1.

    Genome annotation databases

    EnsemblBacteriaiACA76637; ACA76637; EcolC_0968.
    GeneIDi6068171.
    KEGGiecl:EcolC_0968.
    PATRICi18224557. VBIEscCol82905_1030.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000946 Genomic DNA. Translation: ACA76637.1 .
    RefSeqi YP_001723964.1. NC_010468.1.

    3D structure databases

    ProteinModelPortali B1IUT5.
    SMRi B1IUT5. Positions 1-253.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 481805.EcolC_0968.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACA76637 ; ACA76637 ; EcolC_0968 .
    GeneIDi 6068171.
    KEGGi ecl:EcolC_0968.
    PATRICi 18224557. VBIEscCol82905_1030.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci ECOL481805:GI3G-989-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. "Complete sequence of Escherichia coli C str. ATCC 8739."
      Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.
      , Kyrpides N., Mikhailova N., Ingram L., Richardson P.
      Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 8739 / DSM 1576 / Crooks.

    Entry informationi

    Entry nameiSURE_ECOLC
    AccessioniPrimary (citable) accession number: B1IUT5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: April 29, 2008
    Last modified: October 1, 2014
    This is version 40 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