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HAMAP annotation rule: MF_01218
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General rule information

Accession MF_01218
Dates 30-JUL-2002 (Created)
12-JAN-2011 (Last updated, Version 22)
Data class Protein

case <OC:Bacteria>
Predictors HAMAP; MF_01218_B; [distribution of match scores in UniProtKB];[seed alignment for MF_01218_B]
end case


case <OC:Archaea>
Predictors HAMAP; MF_01218_A; [distribution of match scores in UniProtKB];[seed alignment for MF_01218_A]
end case

Names Upp


Propagated annotation

Identifier, protein and gene names
Identifier UPP
Protein name
RecName: Full=Uracil phosphoribosyltransferase;
EC=2.4.2.9;
AltName: Full=UMP pyrophosphorylase;
AltName: Full=UPRTase;
Gene name upp
Comments
FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate (By similarity).
CATALYTIC ACTIVITY: UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate.
COFACTOR: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP (By similarity).
ENZYME REGULATION: Allosterically activated by GTP (By similarity).
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1.
SIMILARITY: Belongs to the UPRTase family.
Cross-references
Pfam PF00156; Pribosyltran; 1;
TIGRFAMs TIGR01091; upp; 1;
Keywords
Allosteric enzyme, Transferase, Glycosyltransferase, GTP-binding, Magnesium, Nucleotide-binding, Transferase.
Gene Ontology
GO:0000287; Molecular function: magnesium ion binding.
GO:0004845; Molecular function: uracil phosphoribosyltransferase activity.
GO:0008655; Biological process: pyrimidine-containing compound salvage.
Features

case <OC:Bacteria>
From: UPP_BACCL (P70881)
Key     From     To       Description   Condition   FTGroup
REGION     131     139       5-phospho-alpha-D-ribose 1-diphosphate binding (By similarity)      
REGION     199     201       Uracil binding (By similarity)   G-x-[AIC]  
BINDING     79     79       5-phospho-alpha-D-ribose 1-diphosphate (By similarity)   R  
BINDING     104     104       5-phospho-alpha-D-ribose 1-diphosphate (By similarity)   [RK]  
BINDING     194     194       Uracil; via amide nitrogen (By similarity)   [IV]  
BINDING     200     200       5-phospho-alpha-D-ribose 1-diphosphate (By similarity)   D  
end case

case <OC:Archaea>
From: UPP_SULSO (Q980Q4)
Key     From     To       Description   Condition   FTGroup
NP_BIND (Optional)     30     34       GTP (By similarity)   [KR]-x(3)-[RK]  
REGION     140     148       5-phospho-alpha-D-ribose 1-diphosphate binding (By similarity)      
REGION     208     210       Uracil binding (By similarity)   G-x-[AIC]  
BINDING     80     80       5-phospho-alpha-D-ribose 1-diphosphate (By similarity)   R  
BINDING     105     105       5-phospho-alpha-D-ribose 1-diphosphate (By similarity)   [RK]  
BINDING     203     203       Uracil; via amide nitrogen (By similarity)   [IV]  
BINDING     209     209       5-phospho-alpha-D-ribose 1-diphosphate (By similarity)   D  
end case



Additional information


case <OC:Bacteria>
Size range: 206-218 amino acids
end case


case <OC:Archaea>
Size range: 211-232 amino acids
end case

Related UniRules: None
Template: P70881 (UPP_BACCL); P0A8F0 (UPP_ECOLI); Q980Q4 (UPP_SULSO); P39149 (UPP_BACSU): [Recover all]
Scope: Bacteria
Archaea
Fusion: Nter: <Unknown>; Cter: None
Duplicate: None
Plasmid encoded: None
Comments: Divergent PORGI and TREPA; sequences not included in alignment. Possible wrong start in STRCO.

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UniProtKB rule member sequences