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.

Q83PN3

- DUT_SHIFL

UniProt

Q83PN3 - DUT_SHIFL

(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, SF3679, S4089
Organism
Shigella flexneri
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
Complete GO annotation...

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 nucleotidohydrolase (EC:3.6.1.23)
Short name:
dUTPase
Alternative name(s):
dUTP pyrophosphatase
Gene namesi
Name:dut
Ordered Locus Names:SF3679, S4089
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000001006: Chromosome, UP000002673: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152Deoxyuridine 5'-triphosphate nucleotidohydrolaseUniRule annotation
PRO_0000182908Add
BLAST

Proteomic databases

PaxDbiQ83PN3.

Interactioni

Protein-protein interaction databases

STRINGi198214.SF3679.

Structurei

3D structure databases

ProteinModelPortaliQ83PN3.
SMRiQ83PN3. 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.

Q83PN3-1 [UniParc]FASTAAdd to Basket

« Hide

MMKKIDVKIL DPRVRKEFPL PTYATSGSAG LDLRACLDDA VELAPGDTTL    50
VPTGLAIHIA DPSLAAMMLP RSGLGHKHGI VLGNLVGLID SDYQGQLMIS 100
VWNRGQDSFT IQPGERIAQM IFVPVVQAEF NLVEDFDATD RGEGGFGHSG 150
RQ 152
Length:152
Mass (Da):16,387
Last modified:June 1, 2003 - v1
Checksum:i6E9C1E6B6BE246BE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005674 Genomic DNA. Translation: AAN45126.1.
AE014073 Genomic DNA. Translation: AAP19066.1.
RefSeqiNP_709419.1. NC_004337.2.
NP_839255.1. NC_004741.1.

Genome annotation databases

EnsemblBacteriaiAAN45126; AAN45126; SF3679.
AAP19066; AAP19066; S4089.
GeneIDi1026233.
1080296.
KEGGisfl:SF3679.
sfx:S4089.
PATRICi18710090. VBIShiFle31049_4452.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005674 Genomic DNA. Translation: AAN45126.1 .
AE014073 Genomic DNA. Translation: AAP19066.1 .
RefSeqi NP_709419.1. NC_004337.2.
NP_839255.1. NC_004741.1.

3D structure databases

ProteinModelPortali Q83PN3.
SMRi Q83PN3. Positions 1-139.
ModBasei Search...

Protein-protein interaction databases

STRINGi 198214.SF3679.

Proteomic databases

PaxDbi Q83PN3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN45126 ; AAN45126 ; SF3679 .
AAP19066 ; AAP19066 ; S4089 .
GeneIDi 1026233.
1080296.
KEGGi sfl:SF3679.
sfx:S4089.
PATRICi 18710090. VBIShiFle31049_4452.

Phylogenomic databases

eggNOGi COG0756.
HOGENOMi HOG000028968.
KOi K01520.
OMAi SIYIGDP.
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. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiDUT_SHIFL
AccessioniPrimary (citable) accession number: Q83PN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2003
Last modified: June 11, 2014
This is version 71 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