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.

B1LK77

- DUT_ECOSM

UniProt

B1LK77 - DUT_ECOSM

(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
Deoxyuridine 5'-triphosphate nucleotidohydrolase
Gene
dut, EcSMS35_3975
Organism
Escherichia coli (strain SMS-3-5 / SECEC)
Status
Reviewed - 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 By similarity.UniRule annotation

Catalytic activityi

dUTP + H2O = dUMP + diphosphate.UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841Substrate By similarity
Binding sitei98 – 981Substrate; via amide nitrogen and carbonyl oxygen By similarity

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 nucleotidohydrolase (EC:3.6.1.23)
Short name:
dUTPase
Alternative name(s):
dUTP pyrophosphatase
Gene namesi
Name:dut
Ordered Locus Names:EcSMS35_3975
OrganismiEscherichia coli (strain SMS-3-5 / SECEC)
Taxonomic identifieri439855 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000007011: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152Deoxyuridine 5'-triphosphate nucleotidohydrolaseUniRule annotation
PRO_1000117568Add
BLAST

Interactioni

Subunit structurei

Homotrimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi439855.EcSMS35_3975.

Structurei

3D structure databases

ProteinModelPortaliB1LK77.
SMRiB1LK77. Positions 1-139.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni71 – 733Substrate binding By similarity
Regioni88 – 903Substrate binding By similarity

Sequence similaritiesi

Belongs to the dUTPase family.

Phylogenomic databases

eggNOGiCOG0756.
HOGENOMiHOG000028968.
KOiK01520.
OMAiSIYIGDP.
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

MMKKIDVKIL DPRVGKEFPL PTYATSGSAG LDLRACLDDA VELAPGDTTL    50
VPTGLAIHIA DPSLAAMMLP RSGLGHKHGI VLGNLVGLID SDYQGQLMIS 100
VWNRGQDSFT IQPGERIAQM IFVPVVQAEF NLVEDFDATD RGEGGFGHSG 150
RQ 152
Length:152
Mass (Da):16,288
Last modified:April 29, 2008 - v1
Checksum:i6F271ECB6AE246AE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000970 Genomic DNA. Translation: ACB18936.1.
RefSeqiYP_001745940.1. NC_010498.1.

Genome annotation databases

EnsemblBacteriaiACB18936; ACB18936; EcSMS35_3975.
GeneIDi6146695.
KEGGiecm:EcSMS35_3975.
PATRICi18436859. VBIEscCol6161_4112.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000970 Genomic DNA. Translation: ACB18936.1 .
RefSeqi YP_001745940.1. NC_010498.1.

3D structure databases

ProteinModelPortali B1LK77.
SMRi B1LK77. Positions 1-139.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 439855.EcSMS35_3975.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACB18936 ; ACB18936 ; EcSMS35_3975 .
GeneIDi 6146695.
KEGGi ecm:EcSMS35_3975.
PATRICi 18436859. VBIEscCol6161_4112.

Phylogenomic databases

eggNOGi COG0756.
HOGENOMi HOG000028968.
KOi K01520.
OMAi SIYIGDP.
OrthoDBi EOG689HXK.

Enzyme and pathway databases

UniPathwayi UPA00610 ; UER00666 .
BioCyci ECOL439855:GHHB-3971-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. "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: June 11, 2014
This is version 48 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