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Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene

dut

Organism
Escherichia coli (strain SMS-3-5 / SECEC)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

Mg2+UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841SubstrateUniRule annotation
Binding sitei98 – 981Substrate; 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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciECOL439855:GHHB-3971-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:EcSMS35_3975
OrganismiEscherichia coli (strain SMS-3-5 / SECEC)
Taxonomic identifieri439855 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000007011 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152Deoxyuridine 5'-triphosphate nucleotidohydrolasePRO_1000117568Add
BLAST

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Protein-protein interaction databases

STRINGi439855.EcSMS35_3975.

Structurei

3D structure databases

ProteinModelPortaliB1LK77.
SMRiB1LK77. Positions 1-139.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni71 – 733Substrate bindingUniRule annotation
Regioni88 – 903Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the dUTPase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0756.
HOGENOMiHOG000028968.
KOiK01520.
OMAiILPRSGM.
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.

B1LK77-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMKKIDVKIL DPRVGKEFPL PTYATSGSAG LDLRACLDDA VELAPGDTTL
60 70 80 90 100
VPTGLAIHIA DPSLAAMMLP RSGLGHKHGI VLGNLVGLID SDYQGQLMIS
110 120 130 140 150
VWNRGQDSFT IQPGERIAQM IFVPVVQAEF NLVEDFDATD RGEGGFGHSG

RQ
Length:152
Mass (Da):16,288
Last modified:April 29, 2008 - v1
Checksum:i6F271ECB6AE246AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000970 Genomic DNA. Translation: ACB18936.1.
RefSeqiYP_001745940.1. NC_010498.1.

Genome annotation databases

EnsemblBacteriaiACB18936; ACB18936; EcSMS35_3975.
KEGGiecm:EcSMS35_3975.
PATRICi18436859. VBIEscCol6161_4112.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000970 Genomic DNA. Translation: ACB18936.1.
RefSeqiYP_001745940.1. NC_010498.1.

3D structure databases

ProteinModelPortaliB1LK77.
SMRiB1LK77. Positions 1-139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi439855.EcSMS35_3975.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACB18936; ACB18936; EcSMS35_3975.
KEGGiecm:EcSMS35_3975.
PATRICi18436859. VBIEscCol6161_4112.

Phylogenomic databases

eggNOGiCOG0756.
HOGENOMiHOG000028968.
KOiK01520.
OMAiILPRSGM.
OrthoDBiEOG689HXK.

Enzyme and pathway databases

UniPathwayiUPA00610; UER00666.
BioCyciECOL439855:GHHB-3971-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

  1. "Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5."
    Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.
    J. Bacteriol. 190:6779-6794(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SMS-3-5 / SECEC.

Entry informationi

Entry nameiDUT_ECOSM
AccessioniPrimary (citable) accession number: B1LK77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: April 1, 2015
This is version 52 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.