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Q8FPH9

- DUT_COREF

UniProt

Q8FPH9 - DUT_COREF

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Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene

dut

Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
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 sitei109 – 1091SubstrateUniRule annotation
Binding sitei123 – 1231Substrate; 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:CE1799
OrganismiCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Taxonomic identifieri196164 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000001409: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 181181Deoxyuridine 5'-triphosphate nucleotidohydrolasePRO_0000182854Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi196164.CE1799.

Structurei

3D structure databases

ProteinModelPortaliQ8FPH9.
SMRiQ8FPH9. Positions 36-171.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni96 – 983Substrate bindingUniRule annotation
Regioni113 – 1153Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the dUTPase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000028966.
KOiK01520.
OMAiIVANPYS.
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.

Q8FPH9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MILSHRWQCT IVPVDSGRQR RAYPEGVTEN LNTIDSIRLL RLDPGLPMPR
60 70 80 90 100
RAHRGDAGVD LHSTTDVVIA PGHRELVGTG VAIALPLGTV GLIHPRSGLA
110 120 130 140 150
AREGLSIVNA PGTVDADYRG EIKVCLINLD PSTPITITRG DRIAQLIIQR
160 170 180
VELVDFVEVD ELDETTRGDQ GHGSTGRGST A
Length:181
Mass (Da):19,462
Last modified:March 1, 2003 - v1
Checksum:i184F50AE22C6E56B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC18609.1.
RefSeqiNP_738409.1. NC_004369.1.

Genome annotation databases

EnsemblBacteriaiBAC18609; BAC18609; BAC18609.
GeneIDi1034420.
KEGGicef:CE1799.
PATRICi21489751. VBICorEff9312_1789.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC18609.1 .
RefSeqi NP_738409.1. NC_004369.1.

3D structure databases

ProteinModelPortali Q8FPH9.
SMRi Q8FPH9. Positions 36-171.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 196164.CE1799.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC18609 ; BAC18609 ; BAC18609 .
GeneIDi 1034420.
KEGGi cef:CE1799.
PATRICi 21489751. VBICorEff9312_1789.

Phylogenomic databases

HOGENOMi HOG000028966.
KOi K01520.
OMAi IVANPYS.
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. "Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
    Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
    Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Entry informationi

Entry nameiDUT_COREF
AccessioniPrimary (citable) accession number: Q8FPH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 66 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