UniProt functional annotation for P08179

UniProt code: P08179.

Organism: Escherichia coli (strain K12).
Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.
 
Function: Catalyzes the transfer of a formyl group from 10- formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate. {ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:2185839, ECO:0000269|PubMed:350869}.
 
Catalytic activity: Reaction=(6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D- ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)- formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide; Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454, ChEBI:CHEBI:143788, ChEBI:CHEBI:147286; EC=2.1.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:2185839, ECO:0000269|PubMed:350869};
Activity regulation: Inhibited by N10-(bromoacetyl)-5,8-dideazafolate. {ECO:0000269|PubMed:2185839}.
Biophysicochemical properties: Kinetic parameters: KM=77.5 uM for (6R)-N10-formyltetrahydrofolate (at pH 8.5) {ECO:0000269|PubMed:2185839}; KM=84.8 uM for (6R)-N10-formyltetrahydrofolate (at pH 7.5) {ECO:0000269|PubMed:2185839}; Note=kcat is 20.7 sec(-1) for (6R)-N10-formyltetrahydrofolate (at pH 8.5). kcat is 13.5 sec(-1) for (6R)-N10-formyltetrahydrofolate (at pH 7.5). {ECO:0000269|PubMed:2185839}; pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:2185839};
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)- formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D- ribosyl)glycinamide (10-formyl THF route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:8688421}.
Subunit: Monomer. Homodimer below pH 6.8. {ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1522592, ECO:0000269|PubMed:1631098, ECO:0000269|PubMed:2185839, ECO:0000269|PubMed:9698564}.
Similarity: Belongs to the GART family. {ECO:0000255|HAMAP- Rule:MF_01930, ECO:0000305}.

Annotations taken from UniProtKB at the EBI.