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Q65DW6 (UPP_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Uracil phosphoribosyltransferase

EC=2.4.2.9
Alternative name(s):
UMP pyrophosphorylase
UPRTase
Gene names
Name:upp
Ordered Locus Names:BLi03934, BL03992
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length209 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate By similarity. HAMAP-Rule MF_01218

Catalytic activity

UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_01218

Cofactor

Binds 1 Mg2+ ion per subunit. The magnesium is bound as Mg-PRPP By similarity.

Enzyme regulation

Allosterically activated by GTP By similarity. HAMAP-Rule MF_01218

Pathway

Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1. HAMAP-Rule MF_01218

Sequence similarities

Belongs to the UPRTase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 209209Uracil phosphoribosyltransferase HAMAP-Rule MF_01218
PRO_1000053677

Regions

Region131 – 13995-phospho-alpha-D-ribose 1-diphosphate binding By similarity
Region199 – 2013Uracil binding By similarity

Sites

Binding site7915-phospho-alpha-D-ribose 1-diphosphate By similarity
Binding site10415-phospho-alpha-D-ribose 1-diphosphate By similarity
Binding site1941Uracil; via amide nitrogen By similarity
Binding site20015-phospho-alpha-D-ribose 1-diphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65DW6 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: A542FBC2D3F1EBBD

FASTA20923,039
        10         20         30         40         50         60 
MGKVYVFDHP LIQHKLTYIR DVKTGTKEFR ELVDEVATLM AFEITRDLPL EEVNVETPVQ 

        70         80         90        100        110        120 
MAKSNVIAGK KLGVVPILRA GLGMVDGILK LIPAAKVGHV GLYRDPETLK PVEYYVKLPS 

       130        140        150        160        170        180 
DVEEREFIVV DPMLATGGSA VEALNSLKKR GAKNIRFMCL IAAPEGVDEV QKHHPDVDIY 

       190        200 
IAALDEKLNE KGYIVPGLGD AGDRMFGTK 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000002 Genomic DNA. Translation: AAU25373.1.
AE017333 Genomic DNA. Translation: AAU42748.1.
RefSeqYP_006715211.1. NC_006322.1.
YP_081011.1. NC_006270.3.

3D structure databases

ProteinModelPortalQ65DW6.
SMRQ65DW6. Positions 2-209.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279010.BL03992.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU25373; AAU25373; BL03992.
AAU42748; AAU42748; BLi03934.
GeneID3028298.
3101272.
KEGGbld:BLi03934.
bli:BL03992.
PATRIC18953660. VBIBacLic203714_4005.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0035.
HOGENOMHOG000262754.
KOK00761.
OMATIEGWCG.
OrthoDBEOG6HF5WX.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-3887-MONOMER.
UniPathwayUPA00574; UER00636.

Family and domain databases

Gene3D3.40.50.2020. 1 hit.
HAMAPMF_01218_B. Upp_B.
InterProIPR029057. PRTase-like.
IPR005765. Ura_phspho_trans.
[Graphical view]
SUPFAMSSF53271. SSF53271. 1 hit.
TIGRFAMsTIGR01091. upp. 1 hit.
ProtoNetSearch...

Entry information

Entry nameUPP_BACLD
AccessionPrimary (citable) accession number: Q65DW6
Secondary accession number(s): Q62PD8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 25, 2004
Last modified: June 11, 2014
This is version 75 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

PATHWAY comments

Index of metabolic and biosynthesis pathways