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A0QW08

- DUT_MYCS2

UniProt

A0QW08 - DUT_MYCS2

Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene

dut

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (09 Jan 2007)
      Previous versions | rss
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    Functioni

    This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.UniRule annotation

    Catalytic activityi

    dUTP + H2O = dUMP + diphosphate.UniRule annotation

    Cofactori

    Magnesium.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei77 – 771SubstrateUniRule annotation
    Binding sitei91 – 911Substrate; via amide nitrogen and carbonyl oxygenUniRule annotation

    GO - Molecular functioni

    1. dUTP diphosphatase activity Source: UniProtKB-HAMAP
    2. magnesium ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. dUMP biosynthetic process Source: UniProtKB-UniPathway
    2. dUTP metabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMSME246196:GJ4Y-2765-MONOMER.
    UniPathwayiUPA00610; UER00666.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deoxyuridine 5'-triphosphate nucleotidohydrolaseUniRule annotation (EC:3.6.1.23UniRule annotation)
    Short name:
    dUTPaseUniRule annotation
    Alternative name(s):
    dUTP pyrophosphataseUniRule annotation
    Gene namesi
    Name:dutUniRule annotation
    Ordered Locus Names:MSMEG_2765, MSMEI_2696
    OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
    Taxonomic identifieri246196 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000000757: Chromosome, UP000006158: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 154153Deoxyuridine 5'-triphosphate nucleotidohydrolasePRO_1000015485Add
    BLAST

    Interactioni

    Subunit structurei

    Homotrimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi246196.MSMEG_2765.

    Structurei

    3D structure databases

    ProteinModelPortaliA0QW08.
    SMRiA0QW08. Positions 1-144.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni64 – 663Substrate bindingUniRule annotation
    Regioni81 – 833Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the dUTPase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0756.
    HOGENOMiHOG000028966.
    KOiK01520.
    OMAiFERFDRI.
    OrthoDBiEOG689HXK.

    Family and domain databases

    Gene3Di2.70.40.10. 1 hit.
    HAMAPiMF_00116. dUTPase_bact.
    InterProiIPR029054. dUTPase-like.
    IPR008180. dUTPase/dCTP_deaminase.
    IPR008181. dUTPase_1.
    [Graphical view]
    PfamiPF00692. dUTPase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51283. SSF51283. 1 hit.
    TIGRFAMsiTIGR00576. dut. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    A0QW08-1 [UniParc]FASTAAdd to Basket

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    MSTSLAVVRL DRELPMPTRA HDGDAGVDLY SAENVELAPG QRALVSTGIA    50
    VAIPHGMVGL VHPRSGLAAR VGLSIVNSPG TIDAGYRGEI KVSLINLDPQ 100
    TPVVISRGDR IAQLLVQRVE LPELVEVTSF DEAGLADTTR GDGGHGSSGG 150
    HASL 154
    Length:154
    Mass (Da):15,935
    Last modified:January 9, 2007 - v1
    Checksum:i174F07E308AEA944
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000480 Genomic DNA. Translation: ABK69761.1.
    CP001663 Genomic DNA. Translation: AFP39164.1.
    RefSeqiYP_006567459.1. NC_018289.1.
    YP_887096.1. NC_008596.1.

    Genome annotation databases

    EnsemblBacteriaiABK69761; ABK69761; MSMEG_2765.
    AFP39164; AFP39164; MSMEI_2696.
    GeneIDi4532868.
    KEGGimsg:MSMEI_2696.
    msm:MSMEG_2765.
    PATRICi18077962. VBIMycSme59918_2733.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000480 Genomic DNA. Translation: ABK69761.1 .
    CP001663 Genomic DNA. Translation: AFP39164.1 .
    RefSeqi YP_006567459.1. NC_018289.1.
    YP_887096.1. NC_008596.1.

    3D structure databases

    ProteinModelPortali A0QW08.
    SMRi A0QW08. Positions 1-144.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 246196.MSMEG_2765.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABK69761 ; ABK69761 ; MSMEG_2765 .
    AFP39164 ; AFP39164 ; MSMEI_2696 .
    GeneIDi 4532868.
    KEGGi msg:MSMEI_2696.
    msm:MSMEG_2765.
    PATRICi 18077962. VBIMycSme59918_2733.

    Phylogenomic databases

    eggNOGi COG0756.
    HOGENOMi HOG000028966.
    KOi K01520.
    OMAi FERFDRI.
    OrthoDBi EOG689HXK.

    Enzyme and pathway databases

    UniPathwayi UPA00610 ; UER00666 .
    BioCyci MSME246196:GJ4Y-2765-MONOMER.

    Family and domain databases

    Gene3Di 2.70.40.10. 1 hit.
    HAMAPi MF_00116. dUTPase_bact.
    InterProi IPR029054. dUTPase-like.
    IPR008180. dUTPase/dCTP_deaminase.
    IPR008181. dUTPase_1.
    [Graphical view ]
    Pfami PF00692. dUTPase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51283. SSF51283. 1 hit.
    TIGRFAMsi TIGR00576. dut. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
      Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155.
    2. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
      Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
      Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155.
    3. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
      Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
      Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE.
      Strain: ATCC 700084 / mc(2)155.

    Entry informationi

    Entry nameiDUT_MYCS2
    AccessioniPrimary (citable) accession number: A0QW08
    Secondary accession number(s): I7G9E1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: January 9, 2007
    Last modified: October 1, 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

    Miscellaneous

    Each trimer binds three substrate molecules. The ligands are bound between subunits, and for each substrate molecule, residues from adjacent subunits contribute to the binding interactions By similarity.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3