Q49992 (DUT_MYCLE) Reviewed, UniProtKB/Swiss-Prot

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:	ML1028

Organism

Mycobacterium leprae [Complete proteome] [HAMAP]

Taxonomic identifier

1769 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	154 AA.
Sequence status	Complete.
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. HAMAP MF_00116
Catalytic activity	dUTP + H2O = dUMP + diphosphate. HAMAP MF_00116
Cofactor	Magnesium By similarity. HAMAP MF_00116
Pathway	Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. HAMAP MF_00116
Subunit structure	Homotrimer By similarity. HAMAP MF_00116
Miscellaneous	Each trimer binds three substrate molecules. The ligands are bound between subunits, and for each substrate molecule, residues from adjacent subunits contribute to the binding interactions By similarity. HAMAP MF_00116
Sequence similarities	Belongs to the dUTPase family.
Sequence caution	The sequence AAA62960.1 differs from that shown. Reason: Erroneous initiation.

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: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 154	154	Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP MF_00116		PRO_0000182882
Regions
	Region	64 – 66	3	Substrate binding By similarity
	Region	81 – 83	3	Substrate binding By similarity
Sites
	Binding site	77	1	Substrate By similarity
	Binding site	91	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q49992 [UniParc]. Last modified April 27, 2001. Version 3. Checksum: 27756BFC21340F82	FASTA	154	15,928
	10 20 30 40 50 60 MSTSLAVVRL DPGLPLPSRA HDGDAGVDLY SVEDVKLAPG QRALVRTGLA VAIPFGMVGL 70 80 90 100 110 120 IHPRSGLAVR VGLSIVNSPG TVDAGYRGEI KVALINLDPV EPLVVHRGDR IAQLLVQRVE 130 140 150 LVELVEVSSF DEAGLAETSR GDGGHGSSGG HASL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Smith D.R., Robison K. Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. , Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., Barrell B.G. Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U15181 Genomic DNA. Translation: AAA62960.1. Different initiation. AL583920 Genomic DNA. Translation: CAC31409.1.
PIR	F87037.
RefSeq	NP_301761.1. NC_002677.1.
3D structure databases
ProteinModelPortal	Q49992.
SMR	Q49992. Positions 1-144.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000028551; EBMYCP00000028157; EBMYCG00000028546.
GeneID	910096.
GenomeReviews	Gene locus ML1028 in contig AL450380_GR.
KEGG	mle:ML1028.
NMPDR	fig|272631.1.peg.633.
PATRIC	18053824. VBIMycLep78757_1857.
Organism-specific databases
Leproma	ML1028.
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000017683.
HOGENOM	HBG436079.
OMA	KIAQMVI.
ProtClustDB	PRK00601.
Enzyme and pathway databases
BioCyc	MLEP272631:ML1028-MONOMER.
Family and domain databases
HAMAP	MF_00116. dUTPase_bact. [Tree]
InterPro	IPR008180. dUTP_pyroPase. IPR008181. dUTP_pyroPase_sf. [Graphical view]
KO	K01520.
PANTHER	PTHR11241. PTHR11241. 1 hit.
Pfam	PF00692. dUTPase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00576. Dut. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DUT_MYCLE

Accession

Primary (citable) accession number: Q49992

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	April 27, 2001
Last modified:	January 25, 2012
This is version 78 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program