Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8FUZ2 (UPP_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Uracil phosphoribosyltransferase

EC=2.4.2.9
Alternative name(s):
UMP pyrophosphorylase
UPRTase
Gene names
Name:upp
Ordered Locus Names:BRA1067, BS1330_II1059
OrganismBrucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]
Taxonomic identifier204722 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length208 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 caution

The sequence AAN34234.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 208208Uracil phosphoribosyltransferase HAMAP-Rule MF_01218
PRO_0000120807

Regions

Region130 – 13895-phospho-alpha-D-ribose 1-diphosphate binding By similarity
Region198 – 2003Uracil binding By similarity

Sites

Binding site7815-phospho-alpha-D-ribose 1-diphosphate By similarity
Binding site10315-phospho-alpha-D-ribose 1-diphosphate By similarity
Binding site1931Uracil; via amide nitrogen By similarity
Binding site19915-phospho-alpha-D-ribose 1-diphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FUZ2 [UniParc].

Last modified November 7, 2003. Version 2.
Checksum: 2497D19976007987

FASTA20823,019
        10         20         30         40         50         60 
MGVTVVSHPL VQHKLTIMRK KETSTASFQR LLKEISLLLC YEVTRNLELT TMSIETPLMP 

        70         80         90        100        110        120 
MEAPVLEGKK LVFASILRAG NGLLEGMLDL VPAARVAHIG LYRDHDTLQP IEYYFKAPED 

       130        140        150        160        170        180 
IVNRLVIVVD PMLATANSAI AAIDKLKERG ATNIRFLCLL AAPEGIERFT KAHPDVEVFT 

       190        200 
ASIDERLDEK GYIVPGLGDA GDRMYGTK 

« Hide

References

[1]"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts."
Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. expand/collapse author list , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.
[2]"Revised genome sequence of Brucella suis 1330."
Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.
J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014292 Genomic DNA. Translation: AAN34234.1. Different initiation.
CP002998 Genomic DNA. Translation: AEM20511.1.
RefSeqNP_700229.2. NC_004311.2.
YP_005614737.1. NC_017250.1.

3D structure databases

ProteinModelPortalQ8FUZ2.
SMRQ8FUZ2. Positions 2-208.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING204722.BRA1067.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN34234; AAN34234; BRA1067.
AEM20511; AEM20511; BS1330_II1059.
GeneID1165513.
12139294.
KEGGbms:BRA1067.
bsi:BS1330_II1059.
PATRIC17794969. VBIBruSui107850_3291.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0035.
HOGENOMHOG000262754.
KOK00761.
OrthoDBEOG6HF5WX.
ProtClustDBPRK00129.

Enzyme and pathway databases

UniPathwayUPA00574; UER00636.

Family and domain databases

HAMAPMF_01218_B. Upp_B.
InterProIPR005765. Ura_phspho_trans.
[Graphical view]
TIGRFAMsTIGR01091. upp. 1 hit.
ProtoNetSearch...

Entry information

Entry nameUPP_BRUSU
AccessionPrimary (citable) accession number: Q8FUZ2
Secondary accession number(s): G0KE73
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: November 7, 2003
Last modified: February 19, 2014
This is version 66 of the entry and version 2 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

Brucella suis

Brucella suis (strain 1330): entries and gene names