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O30931

- DUT_PEPDI

UniProt

O30931 - DUT_PEPDI

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Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene

dut

Organism
Peptoclostridium difficile (Clostridium difficile)
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

Magnesium.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei76 – 761SubstrateUniRule annotation
Binding sitei90 – 901Substrate; 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
Synonyms:dutA
OrganismiPeptoclostridium difficile (Clostridium difficile)
Taxonomic identifieri1496 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptostreptococcaceaePeptoclostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 143143Deoxyuridine 5'-triphosphate nucleotidohydrolasePRO_0000182851Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliO30931.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni63 – 653Substrate bindingUniRule annotation
Regioni80 – 823Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the dUTPase family.UniRule annotation

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.

O30931-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYNLKVKKLN DDAIIPNFAH KGDAGMDLYS IEEVVIPPGE TKLIKTGICI
60 70 80 90 100
ELPTMTEAQV RPRSGLALKH SVTVLNTPGT IDEGYRGELK IILINHGKND
110 120 130 140
FKVEKHMKIA QMIVKPIYDI NIEEVKELSD SERGKGGFGS TGF
Length:143
Mass (Da):15,823
Last modified:January 1, 1998 - v1
Checksum:i69CA36D446937C27
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF022240 Genomic DNA. Translation: AAB84097.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF022240 Genomic DNA. Translation: AAB84097.1 .

3D structure databases

ProteinModelPortali O30931.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "Nucleotide sequence and expression of a gene encoding the Clostridium difficile dUTP pyrophosphatase (dUTPase)."
    Ivey D.M., Winters D.K.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiDUT_PEPDI
AccessioniPrimary (citable) accession number: O30931
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: October 1, 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

Documents

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

External Data

Dasty 3