Q45920 (DUT_COXBU) 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:	CBU_0293

Organism

Coxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]

Taxonomic identifier

227377 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella › Coxiella burnetii

Protein attributes

Sequence length	152 AA.
Sequence status	Complete.
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 By similarity. HAMAP-Rule MF_00116
Catalytic activity	dUTP + H2O = dUMP + diphosphate. HAMAP-Rule MF_00116
Cofactor	Magnesium By similarity.
Pathway	Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. HAMAP-Rule MF_00116
Sequence similarities	Belongs to the dUTPase family.
Sequence caution	The sequence AAO89850.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome 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 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 – 152

152

Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP-Rule MF_00116

PRO_0000182856

Regions

Region

71 – 73

3

Substrate binding By similarity

Region

88 – 90

3

Substrate binding By similarity

Sites

Binding site

84

1

Substrate By similarity

Binding site

98

1

Substrate; via amide nitrogen and carbonyl oxygen By similarity

Secondary structure

1

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152

Helix Strand Turn

Details...

Beta strand

6 – 9

4

Turn

15 – 17

3

Beta strand

29 – 34

6

Beta strand

41 – 43

3

Beta strand

48 – 58

11

Beta strand

64 – 69

6

Helix

72 – 78

7

Beta strand

80 – 82

3

Beta strand

85 – 89

5

Beta strand

95 – 103

9

Beta strand

105 – 107

3

Beta strand

109 – 111

3

Beta strand

116 – 124

9

Sequences

	Sequence		Length	Mass (Da)
	Q45920 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 00041727C1882C57	FASTA	152	16,214
	10 20 30 40 50 60 MTHSVQLKIL DKRLGSEFPL PAYATTGSAG LDLRACLDEP LKIEPDETCL ISTGLAIYLG 70 80 90 100 110 120 HSNVAATILP RSGLGHKHGI VLGNLVGLID SDYQGPLMVS CWNRGKEPYT INPGDRIAQL 130 140 150 VVLPILKAQF AVVEEFELTE RGAGGFGSSG QN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Thiele D., Willems H., Oswald W., Krauss H. Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Nine Mile phase I.
[2]	"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii." Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. , Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F. Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RSA 493 / Nine Mile phase I.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X79075 Genomic DNA. Translation: CAA55678.1.
AE016828 Genomic DNA. Translation: AAO89850.2. Different initiation.

PIR

S44300.

RefSeq

NP_819336.2. NC_002971.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3TQZ	X-ray	1.75	A	1-152	[»]

ProteinModelPortal

Q45920.

SMR

Q45920. Positions 1-139.

ModBase

Search...

Protein-protein interaction databases

STRING

227377.CBU_0293.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAO89850; AAO89850; CBU_0293.

GeneID

1208175.

KEGG

cbu:CBU_0293.

PATRIC

17929281. VBICoxBur82552_0288.

Phylogenomic databases

eggNOG

COG0756.

HOGENOM

HOG000028968.

KO

K01520.

OMA

ILPRSGM.

ProtClustDB

PRK00601.

Enzyme and pathway databases

BioCyc

CBUR227377:GJ7S-300-MONOMER.

UniPathway

UPA00610; UER00666.

Family and domain databases

HAMAP

MF_00116. dUTPase_bact.

InterPro

IPR008180. dUTP_pyroPase.
IPR008181. dUTP_pyroPase_sf.
[Graphical view]

PANTHER

PTHR11241. PTHR11241. 1 hit.

Pfam

PF00692. dUTPase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00576. dut. 1 hit.

ProtoNet

Search...

Entry information

Entry name

DUT_COXBU

Accession

Primary (citable) accession number: Q45920

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program