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HAMAP annotation rule: MF_01208

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General rule information

Accession MF_01208
Dates 30-MAY-2002 (Created)
31-OCT-2008 (Last updated, Version 23)
Data class Protein

case <OC:Bacteria>
Predictors HAMAP; MF_01208_B; [distribution of match scores in UniProtKB];[seed alignment for MF_01208_B]
end case


case <OC:Archaea>
Predictors HAMAP; MF_01208_A; [distribution of match scores in UniProtKB];[seed alignment for MF_01208_A]
end case



Propagated annotation

Identifier, protein and gene names
Identifier PYRE
Protein name
RecName: Full=Orotate phosphoribosyltransferase;
Short=OPRT;
Short=OPRTase;
EC=2.4.2.10;
Gene name pyrE
Comments
FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP) (By similarity).
CATALYTIC ACTIVITY: Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate.
COFACTOR: Magnesium (By similarity).
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 5/6.
SUBUNIT: Homodimer (By similarity).
SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.
Cross-references
Pfam PF00156; Pribosyltran; 1;
TIGRFAMs TIGR00336; pyrE; 1;
PROSITE PS00103; PUR_PYR_PR_TRANSFER; 1;
Keywords
Pyrimidine biosynthesis, Transferase, Glycosyltransferase, Magnesium.
Gene Ontology
GO:0000287; Molecular function: magnesium ion binding.
GO:0004588; Molecular function: orotate phosphoribosyltransferase activity.
GO:0006221; Biological process: pyrimidine nucleotide biosynthetic process.
Features

case <OC:Bacteria>
From: PYRE_SALTY (P08870)
Key     From     To       Description   Condition   FTGroup
REGION (Optional)     34     35       Orotate binding (By similarity)   F-F  
REGION (Optional)     72     73       5-phosphoribose 1-diphosphate binding (By similarity)   Y-K  
REGION     124     132       5-phosphoribose 1-diphosphate binding (By similarity)      
BINDING (Optional)     26     26       5-phosphoribose 1-diphosphate (By similarity)   [KR]  
BINDING (Optional)     99     99       5-phosphoribose 1-diphosphate; shared with dimeric partner (By similarity)   R  
BINDING (Optional)     100     100       5-phosphoribose 1-diphosphate (By similarity)   K  
BINDING (Optional)     103     103       5-phosphoribose 1-diphosphate; shared with dimeric partner (By similarity)   K  
BINDING (Optional)     105     105       5-phosphoribose 1-diphosphate; shared with dimeric partner (By similarity)   H  
BINDING (Optional)     128     128       Orotate (By similarity)   [ST]  
BINDING (Optional)     156     156       Orotate (By similarity)   R  
end case

case <OC:Archaea>
From: PYRE_PYRHO (O58855)
Key     From     To       Description   Condition   FTGroup
REGION     119     127       5-phosphoribose 1-diphosphate binding (By similarity)      
BINDING (Optional)     93     93       5-phosphoribose 1-diphosphate; shared with dimeric partner (By similarity)   R  
BINDING (Optional)     94     94       5-phosphoribose 1-diphosphate (By similarity)   K  
BINDING (Optional)     97     97       5-phosphoribose 1-diphosphate; shared with dimeric partner (By similarity)   [KR]  
BINDING (Optional)     99     99       5-phosphoribose 1-diphosphate; shared with dimeric partner (By similarity)   H  
BINDING (Optional)     123     123       Orotate (By similarity)   T  
BINDING (Optional)     151     151       Orotate (By similarity)   R  
end case



Additional information


case <OC:Bacteria>
Size range: 179-237 amino acids
end case


case <OC:Archaea>
Size range: 166-203 amino acids
end case

Related UniRules: MF_01214 (PYREL)
Template: P0A7E3 (PYRE_ECOLI); P08870 (PYRE_SALTY); P42719 (PYRE_RHILT); P61498 (PYRE_THET2); P46534 (PYRE_BACCL): [Recover all]
Scope: Bacteria
Archaea
Fusion: Nter: MF_01200 (pyrF); Cter: None
Duplicate: in ANASP, RHILO
Plasmid encoded: None

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UniProtKB rule member sequences



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