Q92SM6 (DUT_RHIME) 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
Synonyms:	dnaS
Ordered Locus Names:	R00345
ORF Names:	SMc00461

Organism

Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

266834 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

Protein attributes

Sequence length	160 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
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: 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 – 160	160	Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP MF_00116		PRO_0000182900
Regions
	Region	79 – 81	3	Substrate binding By similarity
	Region	96 – 98	3	Substrate binding By similarity
Sites
	Binding site	92	1	Substrate By similarity
	Binding site	106	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q92SM6 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: F430D6A6938CCC0A	FASTA	160	16,724
	10 20 30 40 50 60 MHTPENRPAL TPGLTLVRLP HGEGLDLPAY ETAGAAGMDL RAALPADEPM TIRPGERALV 70 80 90 100 110 120 PTGFIFEIPA GHEGQIRPRS GLAFKHGITC LNTPGTVDSD YRGEVKVLLV NLGAEDFAVE 130 140 150 160 RGMRIAQMVI APVTRLAIRE AGGATTTARG AGGFGSTGTK

References

[1]	"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021." Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F. Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed: 11481430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.
[2]	"The composite genome of the legume symbiont Sinorhizobium meliloti." Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J. Science 293:668-672(2001) [PubMed: 11474104] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591688 Genomic DNA. Translation: CAC41782.1.
RefSeq	NP_384451.1. NC_003047.1.
3D structure databases
ProteinModelPortal	Q92SM6.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1231979.
GenomeReviews	Gene locus R00345 in contig AL591688_GR.
KEGG	sme:SMc00461.
NMPDR	fig|266834.1.peg.1639.
PATRIC	23629893. VBISinMel96828_1716.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG436079.
OMA	LDLRACI.
ProtClustDB	PRK00601.
Enzyme and pathway databases
BioCyc	SMEL266834:SMC00461-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_RHIME

Accession

Primary (citable) accession number: Q92SM6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2002
Last sequence update:	December 1, 2001
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program