Reviewed, UniProtKB/Swiss-Prot Q5PAE6 (DUT_ANAMM)

Names and origin

Protein names

Recommended name:
    Deoxyuridine 5'-triphosphate nucleotidohydrolase
      Short name=dUTPase
    EC=3.6.1.23
Alternative name(s):
    dUTP pyrophosphatase

Gene names

Name:	dut
Ordered Locus Names:	AM805

Organism

Anaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]

Taxonomic identifier

234826 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	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.
Catalytic activity	dUTP + H2O = dUMP + diphosphate. HAMAP MF_00116
Cofactor	Magnesium By similarity.
Pathway	Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. HAMAP MF_00116
Sequence similarities	Belongs to the dUTPase family.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	dUTP metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	dUTP diphosphatase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 147	147	Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP MF_00116		PRO_0000231396
Regions
	Region	67 – 69	3	Substrate binding By similarity
	Region	84 – 86	3	Substrate binding By similarity
Sites
	Binding site	80	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5PAE6-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 661713874DE1CC9E	FASTA	147	15,464
	10 20 30 40 50 60 MLKVKILRLA SGYGLPLPSY ATPKSAGLDL YAAVDSKLVV HPGGRCAVKT GVALELPDGY 70 80 90 100 110 120 EAQIRSRSGL AANFGICVLN APGTIDSDYR GEITVVLSNF GSEDYVISRG DRVAQMVIAP 130 140 VERVEWEEVN SITATSRGEG GFGSTGT

References

[1]

"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins." Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr. Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000030 Genomic DNA. Translation: AAV86734.1.
RefSeq	YP_153989.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5PAE6.
Genome annotation databases
GeneID	3171654.
GenomeReviews	Gene locus AM805 in contig CP000030_GR.
KEGG	ama:AM805.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5PAE6.
OMA	GTIDEGY.
Enzyme and pathway databases
BioCyc	AMAR234826:AM805-MON.
Family and domain databases
HAMAP	MF_00116. [Tree]
InterPro	IPR008180. DeoxyUTP_pyroPase_dom. IPR008181. dUTP_pyrophosphatase_subfam_1. [Graphical view]
Pfam	PF00692. dUTPase. 1 hit. [Graphical view]
ProDom	PD004900. dCTP_deaminase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00576. dut. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DUT_ANAMM

Accession

Primary (citable) accession number: Q5PAE6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	January 4, 2005
Last modified:	November 3, 2009
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)