P0A552 (DUT_MYCTU) 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:	Rv2697c, MT2771
ORF Names:	MTCY05A6.18c

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	154 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. HAMAP-Rule MF_00116
Catalytic activity	dUTP + H2O = dUMP + diphosphate. HAMAP-Rule MF_00116
Cofactor	Magnesium.
Pathway	Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. HAMAP-Rule MF_00116
Subunit structure	Homotrimer. Ref.4
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. HAMAP-Rule MF_00116
Sequence similarities	Belongs to the dUTPase family.

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 direct assay Ref.4. Source: MTBBASE growth Inferred from mutant phenotype PubMed 12657046. Source: MTBBASE
Molecular_function	dUTP diphosphatase activity Inferred from direct assay Ref.4. Source: MTBBASE magnesium ion binding Inferred from direct assay Ref.4. Source: MTBBASE
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-Rule MF_00116

PRO_0000182884

Regions

Region

64 – 66

3

Substrate binding HAMAP-Rule MF_00116

Region

81 – 83

3

Substrate binding HAMAP-Rule MF_00116

Sites

Binding site

77

1

Substrate

Binding site

91

1

Substrate; via amide nitrogen and carbonyl oxygen

Secondary structure

1

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154

Helix Strand Turn

Details...

Beta strand

6 – 11

6

Beta strand

27 – 30

4

Beta strand

35 – 37

3

Beta strand

42 – 46

5

Beta strand

48 – 52

5

Beta strand

57 – 62

6

Helix

65 – 71

7

Beta strand

73 – 75

3

Beta strand

78 – 82

5

Beta strand

91 – 96

6

Beta strand

103 – 105

3

Beta strand

110 – 118

9

Beta strand

123 – 126

4

Turn

130 – 134

5

Beta strand

139 – 142

4

Turn

145 – 148

4

Sequences

	Sequence		Length	Mass (Da)
	P0A552 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 836D5E6420EF455B	FASTA	154	15,803
	10 20 30 40 50 60 MSTTLAIVRL DPGLPLPSRA HDGDAGVDLY SAEDVELAPG RRALVRTGVA VAVPFGMVGL 70 80 90 100 110 120 VHPRSGLATR VGLSIVNSPG TIDAGYRGEI KVALINLDPA APIVVHRGDR IAQLLVQRVE 130 140 150 LVELVEVSSF DEAGLASTSR GDGGHGSSGG HASL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Crystal structure of dUTPase from Mycobacterium tuberculosis." Sawaya M.R., Chan S., Segelke B.W., Lekin T., Heike K., Cho U.S., Naranjo C., Perry L.J., Yeates T.O., Eisenberg D. Submitted (SEP-2002) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
[4]	"Crystal structure of the Mycobacterium tuberculosis dUTPase: insights into the catalytic mechanism." Chan S., Segelke B., Lekin T., Krupka H., Cho U.S., Kim M.-Y., So M., Kim C.-Y., Naranjo C.M., Rogers Y.C., Park M.S., Waldo G.S., Pashkov I., Cascio D., Perry J.L., Sawaya M.R. J. Mol. Biol. 341:503-517(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH MAGNESIUM ION AND SUBSTRATE ANALOG, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000516 Genomic DNA. Translation: AAK47086.1.
AL123456 Genomic DNA. Translation: CCP45495.1.

PIR

D70530.

RefSeq

NP_217213.1. NC_000962.3.
NP_337272.1. NC_002755.2.
YP_006516141.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MQ7	X-ray	1.95	A	1-154	[»]
1SIX	X-ray	1.30	A	1-154	[»]
1SJN	X-ray	1.80	A/B/C	1-154	[»]
1SLH	X-ray	3.00	A/B/C	1-154	[»]
1SM8	X-ray	2.90	A/B/C	1-154	[»]
1SMC	X-ray	2.10	A/B/C	1-154	[»]
1SNF	X-ray	1.85	A/B/C	1-154	[»]
2PY4	X-ray	1.49	A	1-154	[»]
3H6D	X-ray	1.80	A	1-154	[»]
3HZA	X-ray	1.20	A	1-154	[»]
3I93	X-ray	1.80	A	1-138	[»]
3LOJ	X-ray	1.25	A	1-154	[»]

ProteinModelPortal

P0A552.

SMR

P0A552. Positions 1-138.

ModBase

Search...

Protein-protein interaction databases

STRING

83332.Rv2697c.

Proteomic databases

PRIDE

P0A552.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAK47086; AAK47086; MT2771.

GeneID

13319424.
887290.
925523.

KEGG

mtc:MT2771.
mtu:Rv2697c.

PATRIC

18127836. VBIMycTub22151_3017.

Organism-specific databases

TubercuList

Rv2697c.

Phylogenomic databases

eggNOG

COG0756.

HOGENOM

HOG000028966.

KO

K01520.

OMA

KVCLINH.

ProtClustDB

PRK00601.

Enzyme and pathway databases

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...

Other

EvolutionaryTrace

P0A552.

Entry information

Entry name

DUT_MYCTU

Accession

Primary (citable) accession number: P0A552
Secondary accession number(s): L0TAD4, O07199

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	May 29, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program