Q8FUZ2 (UPP_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Uracil phosphoribosyltransferase
EC=2.4.2.9

Alternative name(s):
UMP pyrophosphorylase
UPRTase

Gene names

Name:	upp
Ordered Locus Names:	BRA1067, BS1330_II1059

Organism

Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]

Taxonomic identifier

204722 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella suis

Protein attributes

Sequence length	208 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Ligand	GTP-binding Magnesium Nucleotide-binding
Molecular function	Glycosyltransferase Transferase
Technical term	Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological_process	UMP salvage Inferred from electronic annotation. Source: UniProtKB-UniPathway uracil salvage Inferred from electronic annotation. Source: InterPro
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: HAMAP uracil phosphoribosyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 208	208	Uracil phosphoribosyltransferase HAMAP-Rule MF_01218		PRO_0000120807
Regions
	Region	130 – 138	9	5-phospho-alpha-D-ribose 1-diphosphate binding By similarity
	Region	198 – 200	3	Uracil binding By similarity
Sites
	Binding site	78	1	5-phospho-alpha-D-ribose 1-diphosphate By similarity
	Binding site	103	1	5-phospho-alpha-D-ribose 1-diphosphate By similarity
	Binding site	193	1	Uracil; via amide nitrogen By similarity
	Binding site	199	1	5-phospho-alpha-D-ribose 1-diphosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8FUZ2 [UniParc]. Last modified November 7, 2003. Version 2. Checksum: 2497D19976007987	FASTA	208	23,019
	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

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. , 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.
RefSeq	NP_700229.2. NC_004311.2. YP_005614737.1. NC_017250.1.
3D structure databases
ProteinModelPortal	Q8FUZ2.
SMR	Q8FUZ2. Positions 2-208.
ModBase	Search...
Protein-protein interaction databases
STRING	204722.BRA1067.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN34234; AAN34234; BRA1067. AEM20511; AEM20511; BS1330_II1059.
GeneID	1165513. 12139294.
KEGG	bms:BRA1067. bsi:BS1330_II1059.
PATRIC	17794969. VBIBruSui107850_3291.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0035.
HOGENOM	HOG000262754.
KO	K00761.
ProtClustDB	PRK00129.
Enzyme and pathway databases
UniPathway	UPA00574; UER00636.
Family and domain databases
HAMAP	MF_01218_B. Upp_B.
InterPro	IPR000836. PRibTrfase_dom. IPR005765. Ura_phspho_trans. [Graphical view]
Pfam	PF00156. Pribosyltran. 1 hit. [Graphical view]
TIGRFAMs	TIGR01091. upp. 1 hit.
ProtoNet	Search...

Entry information

Entry name

UPP_BRUSU

Accession

Primary (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:	May 1, 2013
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program