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O31801

- YNCF_BACSU

UniProt

O31801 - YNCF_BACSU

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Protein

Probable deoxyuridine 5'-triphosphate nucleotidohydrolase YncF

Gene

yncF

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

dUTP + H2O = dUMP + diphosphate.

Cofactori

Magnesium.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei76 – 761SubstrateBy similarity

GO - Molecular functioni

  1. dUTP diphosphatase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. dUMP biosynthetic process Source: UniProtKB-UniPathway
  2. dUTP metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU17660-MONOMER.
UniPathwayiUPA00610; UER00666.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable deoxyuridine 5'-triphosphate nucleotidohydrolase YncF (EC:3.6.1.23)
Short name:
dUTPase
Alternative name(s):
dUTP pyrophosphatase
Gene namesi
Name:yncF
Ordered Locus Names:BSU17660
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU17660.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 144144Probable deoxyuridine 5'-triphosphate nucleotidohydrolase YncFPRO_0000389001Add
BLAST

Interactioni

Subunit structurei

Homotrimer.By similarity

Protein-protein interaction databases

STRINGi224308.BSU17660.

Structurei

Secondary structure

1
144
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119
Beta strandi24 – 296
Beta strandi34 – 363
Beta strandi41 – 455
Beta strandi48 – 514
Beta strandi56 – 627
Helixi66 – 705
Beta strandi72 – 743
Beta strandi77 – 815
Beta strandi93 – 1008
Beta strandi102 – 1043
Beta strandi109 – 1179
Beta strandi122 – 1265
Turni138 – 1414

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliO31801.
SMRiO31801. Positions 2-130.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO31801.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni63 – 653Substrate bindingBy similarity
Regioni80 – 823Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the dUTPase family.Curated

Phylogenomic databases

HOGENOMiHOG000028966.
InParanoidiO31801.
KOiK01520.
OMAiIEQGDWI.
OrthoDBiEOG689HXK.
PhylomeDBiO31801.

Family and domain databases

Gene3Di2.70.40.10. 1 hit.
InterProiIPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
[Graphical view]
PfamiPF00692. dUTPase. 1 hit.
[Graphical view]
SUPFAMiSSF51283. SSF51283. 1 hit.

Sequencei

Sequence statusi: Complete.

O31801-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTMQIKIKYL DETQTRISKI EQGDWIDLRA AEDVTIKKDE FKLVPLGVAM
60 70 80 90 100
ELPEGYEAHV VPRSSTYKNF GVIQTNSMGV IDESYKGDND FWFFPAYALR
110 120 130 140
DTEIKKGDRI CQFRIMKKMP AVELVEVEHL GNEDRGGLGS TGTK
Length:144
Mass (Da):16,410
Last modified:January 1, 1998 - v1
Checksum:i2E15AE84170ED23B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL009126 Genomic DNA. Translation: CAB13650.1.
PIRiH69888.
RefSeqiNP_389649.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13650; CAB13650; BSU17660.
GeneIDi939541.
KEGGibsu:BSU17660.
PATRICi18975351. VBIBacSub10457_1867.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL009126 Genomic DNA. Translation: CAB13650.1 .
PIRi H69888.
RefSeqi NP_389649.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
4AOO X-ray 2.30 A/B/C/D 1-144 [» ]
4AOZ X-ray 2.05 A/B/C 1-144 [» ]
4APZ X-ray 2.01 1/2/3/4/5/6/7/8/9/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/m 1-144 [» ]
4B0H X-ray 1.18 A/B/C 1-144 [» ]
ProteinModelPortali O31801.
SMRi O31801. Positions 2-130.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU17660.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB13650 ; CAB13650 ; BSU17660 .
GeneIDi 939541.
KEGGi bsu:BSU17660.
PATRICi 18975351. VBIBacSub10457_1867.

Organism-specific databases

GenoListi BSU17660.

Phylogenomic databases

HOGENOMi HOG000028966.
InParanoidi O31801.
KOi K01520.
OMAi IEQGDWI.
OrthoDBi EOG689HXK.
PhylomeDBi O31801.

Enzyme and pathway databases

UniPathwayi UPA00610 ; UER00666 .
BioCyci BSUB:BSU17660-MONOMER.

Miscellaneous databases

EvolutionaryTracei O31801.

Family and domain databases

Gene3Di 2.70.40.10. 1 hit.
InterProi IPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
[Graphical view ]
Pfami PF00692. dUTPase. 1 hit.
[Graphical view ]
SUPFAMi SSF51283. SSF51283. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiYNCF_BACSU
AccessioniPrimary (citable) accession number: O31801
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3