Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene

dut

Organism
Rhodococcus erythropolis (strain PR4 / NBRC 100887)
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 sitei79 – 791SubstrateUniRule annotation
Binding sitei93 – 931Substrate; 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

BioCyciRERY234621:GHDE-2850-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:RER_28220
OrganismiRhodococcus erythropolis (strain PR4 / NBRC 100887)
Taxonomic identifieri234621 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus
ProteomesiUP000002204: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 164164Deoxyuridine 5'-triphosphate nucleotidohydrolasePRO_1000202988Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi234621.RER_28220.

Structurei

3D structure databases

ProteinModelPortaliC0ZYU5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni66 – 683Substrate bindingUniRule annotation
Regioni83 – 853Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the dUTPase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0756.
HOGENOMiHOG000028966.
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.

C0ZYU5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDHLSIALK RLDPDLPVPQ RAHPGDAGVD LCSTSDVTIE PGHRTLVGTG
60 70 80 90 100
IAIALPVGTV GLIHPRSGLA AKSGLSIVNA PGTVDAGYRG ELKVCLINLD
110 120 130 140 150
PATAIDIRRG DRIAQLVVQR VELPVFEEVE SLDDTTRGTG GYGSSGGHAI
160
LDTDAPGAVV GEGV
Length:164
Mass (Da):16,815
Last modified:May 26, 2009 - v1
Checksum:i38DF54CE450ECF2C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008957 Genomic DNA. Translation: BAH33530.1.
RefSeqiYP_002766269.1. NC_012490.1.

Genome annotation databases

EnsemblBacteriaiBAH33530; BAH33530; RER_28220.
GeneIDi7711369.
KEGGirer:RER_28220.
PATRICi23192050. VBIRhoEry66701_3316.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008957 Genomic DNA. Translation: BAH33530.1.
RefSeqiYP_002766269.1. NC_012490.1.

3D structure databases

ProteinModelPortaliC0ZYU5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi234621.RER_28220.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAH33530; BAH33530; RER_28220.
GeneIDi7711369.
KEGGirer:RER_28220.
PATRICi23192050. VBIRhoEry66701_3316.

Phylogenomic databases

eggNOGiCOG0756.
HOGENOMiHOG000028966.
KOiK01520.
OMAiILPRSGM.
OrthoDBiEOG689HXK.

Enzyme and pathway databases

UniPathwayiUPA00610; UER00666.
BioCyciRERY234621:GHDE-2850-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. "Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
    Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PR4 / NBRC 100887.

Entry informationi

Entry nameiDUT_RHOE4
AccessioniPrimary (citable) accession number: C0ZYU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: January 7, 2015
This is version 42 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, 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

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.