PROSITE documentation PDOC00164

Phosphoribosylglycinamide synthetase signature




Description

Phosphoribosylglycinamide synthetase (EC 6.3.4.13) (GARS) (phosphoribosylamine glycine ligase) [1] catalyzes the second step in the de novo biosynthesis of purine, the ATP-dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide.

In bacteria GARS is a monofunctional enzyme (encoded by the purD gene), in yeast it is part, with phosphoribosylformylglycinamidine cyclo-ligase (AIRS) of a bifunctional enzyme (encoded by the ADE5,7 gene), in higher eukaryotes it is part, with AIRS and with phosphoribosylglycinamide formyltransferase (GART) of a trifunctional enzyme (GARS-AIRS-GART).

The sequence of GARS is well conserved. As a signature pattern we selected a highly conserved octapeptide.

Last update:

December 2001 / Pattern and text revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

GARS, PS00184; Phosphoribosylglycinamide synthetase signature  (PATTERN)


Reference

1AuthorsAiba A., Mizobuchi K.
TitleNucleotide sequence analysis of genes purH and purD involved in the de novo purine nucleotide biosynthesis of Escherichia coli.
SourceJ. Biol. Chem. 264:21239-21246(1989).
PubMed ID2687276



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)