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

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › 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 MF_00116
Catalytic activity	dUTP + H2O = dUMP + diphosphate. HAMAP MF_00116
Cofactor	Magnesium.
Pathway	Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. HAMAP 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 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	dUTP metabolic process Inferred from direct assay Ref.4. Source: MTBBASE growth Inferred from mutant phenotype. 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 MF_00116

PRO_0000182884

Regions

Region

64 – 66

3

Substrate binding HAMAP MF_00116

Region

81 – 83

3

Substrate binding HAMAP 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

4 – 11

8

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 – 83

6

Beta strand

91 – 96

6

Beta strand

103 – 105

3

Beta strand

110 – 118

9

Beta strand

123 – 126

4

Helix

130 – 133

4

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: 9634230] [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: 12218036] [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: 15276840] [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

BX842580 Genomic DNA. Translation: CAB09487.1.
AE000516 Genomic DNA. Translation: AAK47086.1.

PIR

D70530.

RefSeq

NP_217213.1. NC_000962.2.
NP_337272.1. NC_002755.2.

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 1-144.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000002676; EBMYCP00000002676; EBMYCG00000002674.
EBMYCT00000071629; EBMYCP00000069688; EBMYCG00000071624.

GeneID

887290.
925523.

GenomeReviews

Gene locus MT2771 in contig AE000516_GR.
Gene locus Rv2697c in contig AL123456_GR.

KEGG

mtc:MT2771.
mtu:Rv2697c.

PATRIC

18127836. VBIMycTub22151_3017.

TIGR

MT2771.

Organism-specific databases

TubercuList

Rv2697c.

Phylogenomic databases

GeneTree

EBGT00050000017683.

HOGENOM

HBG436079.

OMA

KIAQMVI.

PhylomeDB

P0A552.

ProtClustDB

PRK00601.

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_MYCTU

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program