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Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene

dut

Organism
Corynebacterium glutamicum (strain R)
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

BioCyciCGLU340322:GJBE-1814-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:cgR_1734
OrganismiCorynebacterium glutamicum (strain R)
Taxonomic identifieri340322 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000006698: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 149149Deoxyuridine 5'-triphosphate nucleotidohydrolasePRO_1000015463Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi340322.cgR_1734.

Structurei

3D structure databases

ProteinModelPortaliA4QER2.
SMRiA4QER2. Positions 7-141.
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.

A4QER2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDLAPIKIV RLDKELPLPK RAHRGDAGVD LHATTDAVIA PGHREIVGTG
60 70 80 90 100
IAIALPLGTV GLVHPRSGLA AREGLSIVNA PGTIDADYRG EIKVCLINLD
110 120 130 140
PEKPIMITRG DRIAQLVIQK VELVDFEEVE ELDDTVRGDQ GYGSTGKTA
Length:149
Mass (Da):15,889
Last modified:May 15, 2007 - v1
Checksum:i487B754324712844
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009044 Genomic DNA. Translation: BAF54728.1.
RefSeqiYP_001138630.1. NC_009342.1.

Genome annotation databases

EnsemblBacteriaiBAF54728; BAF54728; cgR_1734.
GeneIDi4993152.
KEGGicgt:cgR_1734.
PATRICi21508076. VBICorGlu58097_1785.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009044 Genomic DNA. Translation: BAF54728.1.
RefSeqiYP_001138630.1. NC_009342.1.

3D structure databases

ProteinModelPortaliA4QER2.
SMRiA4QER2. Positions 7-141.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi340322.cgR_1734.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAF54728; BAF54728; cgR_1734.
GeneIDi4993152.
KEGGicgt:cgR_1734.
PATRICi21508076. VBICorGlu58097_1785.

Phylogenomic databases

eggNOGiCOG0756.
HOGENOMiHOG000028966.
KOiK01520.
OMAiILPRSGM.
OrthoDBiEOG689HXK.

Enzyme and pathway databases

UniPathwayiUPA00610; UER00666.
BioCyciCGLU340322:GJBE-1814-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. "Comparative analysis of the Corynebacterium glutamicum group and complete genome sequence of strain R."
    Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M., Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.
    Microbiology 153:1042-1058(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: R.

Entry informationi

Entry nameiDUT_CORGB
AccessioniPrimary (citable) accession number: A4QER2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 15, 2007
Last modified: January 7, 2015
This is version 51 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.