Q5PNJ7 (UPP_SALPA) 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:	SPA0369

Organism

Salmonella paratyphi A (strain ATCC 9150 / SARB42) [Complete proteome] [HAMAP]

Taxonomic identifier

295319 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella paratyphi A

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.

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_1000053775
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)
	Q5PNJ7 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 3EE574788F2DEF5B	FASTA	208	22,533
	10 20 30 40 50 60 MKIVEVKHPL VKHKLGLMRE NDISTKRFRE LASEVGSLLT YEATADLETE KVTIEGWNGP 70 80 90 100 110 120 VEIDQIKGKK ITVVPILRAG LGMMEGVLEN VPSARISVVG MYRNEETLEP VPYFQKLVSN 130 140 150 160 170 180 IDERMALIVD PMLATGGSVI ATIDLLKKAG CSSIKVLVLV AAPEGIAALE KAHPDVELYT 190 200 ASIDQGLNEH GYIIPGLGDA GDKIFGTK

References

[1]

"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid." McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K. Nat. Genet. 36:1268-1274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000026 Genomic DNA. Translation: AAV76382.1.
RefSeq	YP_149694.1. NC_006511.1.
3D structure databases
HSSP	HSSP built from PDB template 1I5E based on UniProtKB P70881.
ProteinModelPortal	Q5PNJ7.
SMR	Q5PNJ7. Positions 2-208.
ModBase	Search...
Protein-protein interaction databases
STRING	295319.SPA0369.
Proteomic databases
PRIDE	Q5PNJ7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAV76382; AAV76382; SPA0369.
GeneID	3176496.
KEGG	spt:SPA0369.
PATRIC	32349880. VBISalEnt134188_0397.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0035.
HOGENOM	HOG000262754.
KO	K00761.
OMA	TIEGWCG.
ProtClustDB	PRK00129.
Enzyme and pathway databases
BioCyc	SENT295319:GJBZ-368-MONOMER.
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_SALPA

Accession

Primary (citable) accession number: Q5PNJ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 4, 2005
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program