CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003086
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Uracil phosphoribosyltransferase 
Protein Synonyms/Alias
 UMP pyrophosphorylase; UPRTase 
Gene Name
 upp 
Gene Synonyms/Alias
 uraP; b2498; JW2483 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
2******MKIVEVKHPacetylation[1]
7*MKIVEVKHPLVKHKacetylation[1]
67PVEIDQIKGKKITVVacetylation[1]
69EIDQIKGKKITVVPIacetylation[1]
70IDQIKGKKITVVPILacetylation[1]
116EPVPYFQKLVSNIDEacetylation[1]
203GLGDAGDKIFGTK**acetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 Catalyzes the conversion of uracil and 5-phospho-alpha- D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. 
Sequence Annotation
 REGION 130 138 5-phospho-alpha-D-ribose 1-diphosphate
 REGION 198 200 Uracil binding (By similarity).
 BINDING 78 78 5-phospho-alpha-D-ribose 1-diphosphate
 BINDING 103 103 5-phospho-alpha-D-ribose 1-diphosphate
 BINDING 193 193 Uracil; via amide nitrogen (By
 BINDING 199 199 5-phospho-alpha-D-ribose 1-diphosphate  
Keyword
 3D-structure; Allosteric enzyme; Complete proteome; Direct protein sequencing; Glycosyltransferase; GTP-binding; Magnesium; Nucleotide-binding; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 208 AA 
Protein Sequence
MKIVEVKHPL VKHKLGLMRE QDISTKRFRE LASEVGSLLT YEATADLETE KVTIEGWNGP 60
VEIDQIKGKK ITVVPILRAG LGMMDGVLEN VPSARISVVG MYRNEETLEP VPYFQKLVSN 120
IDERMALIVD PMLATGGSVI ATIDLLKKAG CSSIKVLVLV AAPEGIAALE KAHPDVELYT 180
ASIDQGLNEH GYIIPGLGDA GDKIFGTK 208 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0000287; F:magnesium ion binding; IEA:HAMAP.
 GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:HAMAP.
 GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
 GO:0006223; P:uracil salvage; IEA:InterPro. 
Interpro
 IPR000836; PRibTrfase_dom.
 IPR005765; Ura_phspho_trans. 
Pfam
 PF00156; Pribosyltran 
SMART
  
PROSITE
  
PRINTS