The domain within your query sequence starts at position 3 and ends at position 104; the E-value for the GARS_N domain shown below is 1.4e-40.



PFAM accession number:PF02844
Interpro abstract (IPR020562):

Phosphoribosylglycinamide synthetase (EC (GARS) (phosphoribosylamine glycine ligase) [(PUBMED:2687276)] catalyses the second step in the de novo biosynthesis of purine. The reaction catalysed by phosphoribosylglycinamide synthetase is the ATP-dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide: ATP + 5-phosphoribosylamine + glycine = ADP + Pi + 5'-phosphoribosylglycinamide In bacteria, GARS is a monofunctional enzyme (encoded by the purD gene). In yeast, GARS is part of a bifunctional enzyme (encoded by the ADE5,7 gene) in conjunction with phosphoribosylformylglycinamidine cyclo-ligase (AIRS) [(PUBMED:3097325)]. In higher eukaryotes, GARS is part of a trifunctional enzyme in conjunction with AIRS and with phosphoribosylglycinamide formyltransferase (GART), forming GARS-AIRS-GART [(PUBMED:2147474)].

This entry represents the N-domain, which is related to the N-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (IPR005481).

GO process:purine nucleobase biosynthetic process (GO:0009113)
GO function:phosphoribosylamine-glycine ligase activity (GO:0004637)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry GARS_N