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O31801 (YNCF_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length144 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processNucleotide metabolism
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdUMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

dUTP metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functiondUTP diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 144144Probable deoxyuridine 5'-triphosphate nucleotidohydrolase YncF
PRO_0000389001

Regions

Region63 – 653Substrate binding By similarity
Region80 – 823Substrate binding By similarity

Sites

Binding site761Substrate By similarity

Secondary structure

............................. 144
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O31801 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 2E15AE84170ED23B

FASTA14416,410
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
PIRH69888.
RefSeqNP_389649.1. NC_000964.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XCDX-ray1.84A/B/C/D/E/F1-144[»]
2XCEX-ray1.85A/B/C/D/E/F1-144[»]
4AOOX-ray2.30A/B/C/D1-144[»]
4AOZX-ray2.05A/B/C1-144[»]
4APZX-ray2.011/2/3/4/5/6/7/8/9/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j/k/l/m1-144[»]
4B0HX-ray1.18A/B/C1-144[»]
ProteinModelPortalO31801.
SMRO31801. Positions 2-130.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU17660.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13650; CAB13650; BSU17660.
GeneID939541.
KEGGbsu:BSU17660.
PATRIC18975351. VBIBacSub10457_1867.

Organism-specific databases

GenoListBSU17660.

Phylogenomic databases

HOGENOMHOG000028966.
KOK01520.
OMAIEQGDWI.
OrthoDBEOG689HXK.
PhylomeDBO31801.

Enzyme and pathway databases

BioCycBSUB:BSU17660-MONOMER.
UniPathwayUPA00610; UER00666.

Family and domain databases

Gene3D2.70.40.10. 1 hit.
InterProIPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
[Graphical view]
PfamPF00692. dUTPase. 1 hit.
[Graphical view]
SUPFAMSSF51283. SSF51283. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO31801.

Entry information

Entry nameYNCF_BACSU
AccessionPrimary (citable) accession number: O31801
Entry history
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList