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Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene

dut

Organism
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
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

Pathway:idUMP biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes dUMP from dCTP (dUTP route).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Deoxycytidine triphosphate deaminase (dcd)
  2. Deoxyuridine 5'-triphosphate nucleotidohydrolase (dut)
This subpathway is part of the pathway dUMP biosynthesis, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes dUMP from dCTP (dUTP route), the pathway dUMP biosynthesis and in Pyrimidine metabolism.

Sites

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMAVI262316:GCQR-2854-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:MAP_2814c
OrganismiMycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Taxonomic identifieri262316 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)
ProteomesiUP000000580 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 154154Deoxyuridine 5'-triphosphate nucleotidohydrolasePRO_0000182883Add
BLAST

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Protein-protein interaction databases

STRINGi262316.MAP2814c.

Structurei

3D structure databases

ProteinModelPortaliP61910.
SMRiP61910. 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.
KOiK01520.
OMAiINHDPRT.
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.

P61910-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTSLAIVRL DPGLPLPSRA HEGDAGVDLY SAEDVRLEPG RRALVRTGVA
60 70 80 90 100
VAIPFGMVGL VHPRSGLAAR VGLSIVNSPG TIDAGYRGEI KVALINLDPA
110 120 130 140 150
EPIVVHRGDR IAQLLVQRVE LVELVEVSSF DEAGLAGTSR GDGGHGSSGG

HASL
Length:154
Mass (Da):15,900
Last modified:June 7, 2004 - v1
Checksum:iDCF46895A079E33B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016958 Genomic DNA. Translation: AAS05131.1.
RefSeqiWP_003875248.1. NC_002944.2.

Genome annotation databases

EnsemblBacteriaiAAS05131; AAS05131; MAP_2814c.
GeneIDi2721774.
KEGGimpa:MAP2814c.
PATRICi17998340. VBIMycAvi108102_2980.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016958 Genomic DNA. Translation: AAS05131.1.
RefSeqiWP_003875248.1. NC_002944.2.

3D structure databases

ProteinModelPortaliP61910.
SMRiP61910. Positions 1-144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262316.MAP2814c.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS05131; AAS05131; MAP_2814c.
GeneIDi2721774.
KEGGimpa:MAP2814c.
PATRICi17998340. VBIMycAvi108102_2980.

Phylogenomic databases

eggNOGiCOG0756.
KOiK01520.
OMAiINHDPRT.
OrthoDBiEOG689HXK.

Enzyme and pathway databases

UniPathwayiUPA00610; UER00666.
BioCyciMAVI262316:GCQR-2854-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. "The complete genome sequence of Mycobacterium avium subspecies paratuberculosis."
    Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V.
    Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-968 / K-10.

Entry informationi

Entry nameiDUT_MYCPA
AccessioniPrimary (citable) accession number: P61910
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: July 22, 2015
This is version 74 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

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.