Domain

Phosphoribosylglycinamide synthetase, N-terminal (IPR020562)

Short name: PRibGlycinamide_synth_N

Domain relationships

None.

Description

Phosphoribosylglycinamide synthetase (EC:6.3.4.13) (GARS) (phosphoribosylamine glycine ligase) [PMID: 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) [PMID: 3097325]. In higher eukaryotes, GARS is part of a trifunctional enzyme in conjunction with AIRS and with phosphoribosylglycinamide formyltransferase (GART), forming GARS-AIRS-GART [PMID: 2147474].

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

GO terms

Biological Process

GO:0009113 purine nucleobase biosynthetic process

Molecular Function

GO:0004637 phosphoribosylamine-glycine ligase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
Pfam