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A0PT52

- DUT_MYCUA

UniProt

A0PT52 - DUT_MYCUA

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Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene

dut

Organism
Mycobacterium ulcerans (strain Agy99)
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.UniRule annotation

Catalytic activityi

dUTP + H2O = dUMP + diphosphate.UniRule annotation

Cofactori

Mg2+UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei77 – 771SubstrateUniRule annotation
Binding sitei91 – 911Substrate; 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

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:MUL_3335
OrganismiMycobacterium ulcerans (strain Agy99)
Taxonomic identifieri362242 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000000765: Chromosome

Organism-specific databases

GenoListiMUL_3335.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 154154Deoxyuridine 5'-triphosphate nucleotidohydrolasePRO_1000015489Add
BLAST

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Protein-protein interaction databases

STRINGi362242.MUL_3335.

Structurei

3D structure databases

ProteinModelPortaliA0PT52.
SMRiA0PT52. 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.
HOGENOMiHOG000028966.
KOiK01520.
OMAiFERFDRI.
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.

A0PT52-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSNSLAVVRL DPGLPLPSRA HDGDAGVDLY SAEDVVLPPG QRALVRTGVA
60 70 80 90 100
VAIPFGMVGL VHPRSGLASR VGLSIVNSPG TIDAGYRGEL KVVLINLDPA
110 120 130 140 150
TPIVVNRGDR IAQLLVQRVE LLELVEVSSF DEAGLAATSR GDGGHGSSGG

HASL
Length:154
Mass (Da):15,789
Last modified:January 9, 2007 - v1
Checksum:i9E77BD37BA1D89A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000325 Genomic DNA. Translation: ABL05521.1.
RefSeqiWP_011741129.1. NC_008611.1.
YP_906992.1. NC_008611.1.

Genome annotation databases

EnsemblBacteriaiABL05521; ABL05521; MUL_3335.
GeneIDi4554460.
KEGGimul:MUL_3335.
PATRICi18174105. VBIMycUlc37413_3879.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000325 Genomic DNA. Translation: ABL05521.1 .
RefSeqi WP_011741129.1. NC_008611.1.
YP_906992.1. NC_008611.1.

3D structure databases

ProteinModelPortali A0PT52.
SMRi A0PT52. Positions 1-144.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 362242.MUL_3335.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABL05521 ; ABL05521 ; MUL_3335 .
GeneIDi 4554460.
KEGGi mul:MUL_3335.
PATRICi 18174105. VBIMycUlc37413_3879.

Organism-specific databases

GenoListi MUL_3335.

Phylogenomic databases

eggNOGi COG0756.
HOGENOMi HOG000028966.
KOi K01520.
OMAi FERFDRI.
OrthoDBi EOG689HXK.

Enzyme and pathway databases

UniPathwayi UPA00610 ; UER00666 .

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. "Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
    Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.
    , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
    Genome Res. 17:192-200(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Agy99.

Entry informationi

Entry nameiDUT_MYCUA
AccessioniPrimary (citable) accession number: A0PT52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: November 26, 2014
This is version 56 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3