a highly conserved trifunctional enzyme. It has phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase activity which is required for de novo purine biosynthesis. Inhibition of the de novo purine synthesis by folate analogs blocks the p53-dependent G1 checkpoint in human carcinoma cell lines. Two splice variant isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: EC 188.8.131.52; Enzyme, cellular metabolism; Nucleotide Metabolism - purine; EC 184.108.40.206; Methyltransferase; Cofactor and Vitamin Metabolism - one carbon pool by folate; Mitochondrial; EC 220.127.116.11; Ligase
Chromosomal Location of Human Ortholog: 21q22.11
Cellular Component: cytosol
Molecular Function: methyltransferase activity; metal ion binding; phosphoribosylamine-glycine ligase activity; phosphoribosylformylglycinamidine cyclo-ligase activity; phosphoribosylglycinamide formyltransferase activity; ATP binding
Biological Process: methylation; response to organic substance; glycine metabolic process; purine ribonucleoside monophosphate biosynthetic process; tetrahydrofolate biosynthetic process; response to inorganic substance; purine base biosynthetic process; nucleobase, nucleoside and nucleotide metabolic process; cerebellum development; cerebral cortex development; purine base metabolic process; 'de novo' IMP biosynthetic process
SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.