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Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene

dut

Organism
Acinetobacter baumannii (strain AB0057)
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

Pathwayi: dUMP 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. dCTP 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)DescriptionActionsGraphical viewLength
Binding sitei82SubstrateUniRule annotation1
Binding sitei96Substrate; via amide nitrogen and carbonyl oxygenUniRule annotation1

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

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:AB57_0934
OrganismiAcinetobacter baumannii (strain AB0057)
Taxonomic identifieri480119 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001175621 – 150Deoxyuridine 5'-triphosphate nucleotidohydrolaseAdd BLAST150

Structurei

3D structure databases

ProteinModelPortaliB7I7U2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni69 – 71Substrate bindingUniRule annotation3
Regioni86 – 88Substrate bindingUniRule annotation3

Sequence similaritiesi

Belongs to the dUTPase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000028968.
KOiK01520.
OMAiICERIFL.

Family and domain databases

CDDicd07557. trimeric_dUTPase. 1 hit.
Gene3Di2.70.40.10. 1 hit.
HAMAPiMF_00116. dUTPase_bact. 1 hit.
InterProiIPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR008181. dUTPase_1.
IPR033704. dUTPase_trimeric.
[Graphical view]
PfamiPF00692. dUTPase. 1 hit.
[Graphical view]
SUPFAMiSSF51283. SSF51283. 1 hit.
TIGRFAMsiTIGR00576. dut. 1 hit.

Sequencei

Sequence statusi: Complete.

B7I7U2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVQVKLLDP RLGKEWPLPS YATAGSAGLD LRACLDEAIE IEPGQTVLVK
60 70 80 90 100
TGMAIYIHDV NFAGLILPRS GLGHKHGIVL GNLVGLIDSD YQGELMVSVW
110 120 130 140 150
NRGQTTFRLE PGERLAQYVL VPVVQAEFEQ VEEFEETLRG AGGFGHTGKQ
Length:150
Mass (Da):16,371
Last modified:February 10, 2009 - v1
Checksum:iF3EBE361AA5BE853
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001182 Genomic DNA. Translation: ACJ40726.1.
RefSeqiWP_000868152.1. NC_011586.1.

Genome annotation databases

EnsemblBacteriaiACJ40726; ACJ40726; AB57_0934.
KEGGiabn:AB57_0934.
PATRICi20695687. VBIAciBau111166_0912.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001182 Genomic DNA. Translation: ACJ40726.1.
RefSeqiWP_000868152.1. NC_011586.1.

3D structure databases

ProteinModelPortaliB7I7U2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACJ40726; ACJ40726; AB57_0934.
KEGGiabn:AB57_0934.
PATRICi20695687. VBIAciBau111166_0912.

Phylogenomic databases

HOGENOMiHOG000028968.
KOiK01520.
OMAiICERIFL.

Enzyme and pathway databases

UniPathwayiUPA00610; UER00666.

Family and domain databases

CDDicd07557. trimeric_dUTPase. 1 hit.
Gene3Di2.70.40.10. 1 hit.
HAMAPiMF_00116. dUTPase_bact. 1 hit.
InterProiIPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR008181. dUTPase_1.
IPR033704. dUTPase_trimeric.
[Graphical view]
PfamiPF00692. dUTPase. 1 hit.
[Graphical view]
SUPFAMiSSF51283. SSF51283. 1 hit.
TIGRFAMsiTIGR00576. dut. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDUT_ACIB5
AccessioniPrimary (citable) accession number: B7I7U2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: November 2, 2016
This is version 53 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

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 one 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.