Q58502 (DUT_METJA) 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):
MjDUT
dUTP pyrophosphatase

Gene names

Name:	dut
Ordered Locus Names:	MJ1102

Organism

Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]

Taxonomic identifier

243232 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus › Methanocaldococcus jannaschii

Protein attributes

Sequence length	156 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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. HAMAP-Rule MF_00635
Catalytic activity	dUTP + H2O = dUMP + diphosphate. HAMAP-Rule MF_00635
Pathway	Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. HAMAP-Rule MF_00635
Subunit structure	Homotrimer Probable.
Sequence similarities	Belongs to the dCTP deaminase family. Archaeal dUTPase subfamily.
Sequence caution	The sequence AAB99105.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Molecular function	Hydrolase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	dUMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway dUTP metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	dUTP diphosphatase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 156	155	Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP-Rule MF_00635		PRO_0000153638

Sequences

	Sequence		Length	Mass (Da)
	Q58502 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: AF6E28A4CF91FF3D	FASTA	156	18,070
	10 20 30 40 50 60 MIIGANTSKN FFDNLEEEQI QQCGIDLRVW KIFKIEGEGV IDFSNEKRKL PNYIEIFNSE 70 80 90 100 110 120 KDEHIKLDRG VYIVKVADYI KIPENVAGFA YPRSSLLRMG ATLYSAVHDP GYEGRPEYLM 130 140 150 QVFNPITIYK YARIAQIVFV ECRDVKGVYE GIYKGR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]	"A bifunctional dCTP deaminase-dUTP nucleotidohydrolase from the hyperthermophilic archaeon Methanocaldococcus jannaschii." Bjoernberg O., Neuhard J., Nyman P.O. J. Biol. Chem. 278:20667-20672(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-10, CHARACTERIZATION.
[3]	"The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase." Li H., Xu H., Graham D.E., White R.H. J. Biol. Chem. 278:11100-11106(2003) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L77117 Genomic DNA. Translation: AAB99105.1. Different initiation.
PIR	E64437.
RefSeq	NP_248095.1. NC_000909.1.
3D structure databases
ProteinModelPortal	Q58502.
ModBase	Search...
Protein-protein interaction databases
STRING	243232.MJ1102.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAB99105; AAB99105; MJ_1102.
GeneID	1451999.
KEGG	mja:MJ_1102.
Phylogenomic databases
eggNOG	COG0717.
KO	K01520.
OMA	QCGIDLR.
ProtClustDB	CLSK876451.
Enzyme and pathway databases
SABIO-RK	Q58502.
UniPathway	UPA00610; UER00666.
Family and domain databases
HAMAP	MF_00635. dUTPase_arch.
InterPro	IPR008180. dUTP_pyroPase. IPR023537. dUTP_pyroPase_arch. [Graphical view]
Pfam	PF00692. dUTPase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DUT_METJA

Accession

Primary (citable) accession number: Q58502

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 79 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program