Q65DW6 (UPP_BACLD) 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:	BLi03934, BL03992

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus licheniformis

Protein attributes

Sequence length	209 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 – 209	209	Uracil phosphoribosyltransferase HAMAP-Rule MF_01218		PRO_1000053677
Regions
	Region	131 – 139	9	5-phospho-alpha-D-ribose 1-diphosphate binding By similarity
	Region	199 – 201	3	Uracil binding By similarity
Sites
	Binding site	79	1	5-phospho-alpha-D-ribose 1-diphosphate By similarity
	Binding site	104	1	5-phospho-alpha-D-ribose 1-diphosphate By similarity
	Binding site	194	1	Uracil; via amide nitrogen By similarity
	Binding site	200	1	5-phospho-alpha-D-ribose 1-diphosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q65DW6 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: A542FBC2D3F1EBBD	FASTA	209	23,039
	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

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. , 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.
RefSeq	YP_006715211.1. NC_006322.1. YP_081011.1. NC_006270.3.
3D structure databases
ProteinModelPortal	Q65DW6.
SMR	Q65DW6. Positions 2-209.
ModBase	Search...
Protein-protein interaction databases
STRING	279010.BL03992.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAU25373; AAU25373; BL03992. AAU42748; AAU42748; BLi03934.
GeneID	3028298. 3101272.
KEGG	bld:BLi03934. bli:BL03992.
PATRIC	18953660. VBIBacLic203714_4005.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0035.
HOGENOM	HOG000262754.
KO	K00761.
OMA	IQHKLSH.
ProtClustDB	PRK00129.
Enzyme and pathway databases
BioCyc	BLIC279010:GJ2P-3887-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_BACLD

Accession

Primary (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:	May 29, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program