O31801 (YNCF_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable deoxyuridine 5'-triphosphate nucleotidohydrolase YncF
Short name=dUTPase
EC=3.6.1.23

Alternative name(s):
dUTP pyrophosphatase

Gene names

Name:	yncF
Ordered Locus Names:	BSU17660

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	144 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.
Catalytic activity	dUTP + H2O = dUMP + diphosphate.
Cofactor	Magnesium By similarity.
Pathway	Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Subunit structure	Homotrimer By similarity.
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 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 – 144

144

Probable deoxyuridine 5'-triphosphate nucleotidohydrolase YncF

PRO_0000389001

Regions

Region

63 – 65

3

Substrate binding By similarity

Region

80 – 82

3

Substrate binding By similarity

Sites

Binding site

76

1

Substrate By similarity

Secondary structure

1

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144

Helix Strand Turn

Details...

Beta strand

3 – 11

9

Beta strand

22 – 24

3

Beta strand

26 – 29

4

Beta strand

34 – 36

3

Beta strand

41 – 51

11

Beta strand

56 – 62

7

Helix

66 – 70

5

Beta strand

72 – 74

3

Beta strand

77 – 82

6

Beta strand

91 – 100

10

Beta strand

102 – 104

3

Beta strand

109 – 117

9

Beta strand

122 – 126

5

Sequences

	Sequence		Length	Mass (Da)
	O31801 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 2E15AE84170ED23B	FASTA	144	16,410
	10 20 30 40 50 60 MTMQIKIKYL DETQTRISKI EQGDWIDLRA AEDVTIKKDE FKLVPLGVAM ELPEGYEAHV 70 80 90 100 110 120 VPRSSTYKNF GVIQTNSMGV IDESYKGDND FWFFPAYALR DTEIKKGDRI CQFRIMKKMP 130 140 AVELVEVEHL GNEDRGGLGS TGTK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[2]	"Crystallization and preliminary X-ray analysis of three dUTPases from Gram-positive bacteria." Li G.-L., Wang J., Li L.-F., Su X.-D. Acta Crystallogr. F 65:339-342(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY CRYSTALLIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL009126 Genomic DNA. Translation: CAB13650.1.

PIR

H69888.

RefSeq

NP_389649.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2XCD	X-ray	1.84	A/B/C/D/E/F	1-144	[»]
2XCE	X-ray	1.85	A/B/C/D/E/F	1-144	[»]

ProteinModelPortal

O31801.

SMR

O31801. Positions 2-130.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU17660.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB13650; CAB13650; BSU17660.

GeneID

939541.

KEGG

bsu:BSU17660.

PATRIC

18975351. VBIBacSub10457_1867.

Organism-specific databases

GenoList

BSU17660.

Phylogenomic databases

HOGENOM

HOG000028966.

KO

K01520.

OMA

PRSSTFK.

ProtClustDB

CLSK887343.

Enzyme and pathway databases

BioCyc

BSUB:BSU17660-MONOMER.

UniPathway

UPA00610; UER00666.

Family and domain databases

InterPro

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

PANTHER

PTHR11241. PTHR11241. 1 hit.

Pfam

PF00692. dUTPase. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O31801.

Entry information

Entry name

YNCF_BACSU

Accession

Primary (citable) accession number: O31801

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 24, 2009
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program