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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.

December 2001 / Pattern and text revised.

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

GARS, PS00184; Phosphoribosylglycinamide synthetase signature  (PATTERN)

Consensus pattern: R-[LF]-G-D-P-E-x-[EQIM] Sequences known to belong to this class detected by the pattern: ALL, with a few exceptions Other sequence(s) detected in Swiss-Prot: NONE

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00184 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00184 • Scan Swiss-Prot/TrEMBL entries against PS00184 • view ligand binding statistics

Matching PDB structures: 1VKZ 2QK4 2XCL 2XD4 ... [ALL]

1	Authors	Aiba A., Mizobuchi K.
	Title	Nucleotide sequence analysis of genes purH and purD involved in the de novo purine nucleotide biosynthesis of Escherichia coli.
	Source	J. Biol. Chem. 264:21239-21246(1989).
	PubMed ID	2687276

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