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InterPro: IPR020562 Phosphoribosylglycinamide synthetase, N-domain

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UniProtKB

Matches:

1840 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR020562 PRibGlycinamide_synth_N-dom

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02844	GARS_N	1840
Signatures in BioMart

InterPro Relationships Help

Parent

IPR013817 Pre-ATP-grasp fold

Found in

IPR000115 Phosphoribosylglycinamide synthetase

GO Term annotation Help

Process

GO:0009113 purine base biosynthetic process

Function

GO:0004637 phosphoribosylamine-glycine ligase activity

InterPro annotation

Entry Details in BioMart

Abstract

Phosphoribosylglycinamide synthetase (EC:6.3.4.13) (GARS) (phosphoribosylamine glycine ligase) [1] 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 + P_i + 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) (IPR000728). In higher eukaryotes, GARS is part of a trifunctional enzyme in conjunction with AIRS (IPR000728) and with phosphoribosylglycinamide formyltransferase (GART) (IPR001555 ), forming GARS-AIRS-GART.

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

Structural links Help

PDB - click here

SCOP: c.30.1.1

CATH: 3.40.50.20

Database links Help

Enzyme: EC:6.3.4.13

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR020562

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P00967 Trifunctional purine biosynthetic protein adenosine-3

P07244 Bifunctional purine biosynthetic protein ADE5,7

P22102 Trifunctional purine biosynthetic protein adenosine-3

P52420 Phosphoribosylamine--glycine ligase, chloroplastic

Q64737 Trifunctional purine biosynthetic protein adenosine-3

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013815	ATP-grasp fold, subdomain 1
IPR013816	ATP-grasp fold, subdomain 2
IPR002376	Formyl transferase, N-terminal
IPR013817	Pre-ATP-grasp fold
IPR020559	Phosphoribosylglycinamide synthetase, conserved site
IPR004607	Phosphoribosylglycinamide formyltransferase
IPR016188	PurM, N-terminal-like
IPR016185	PreATP-grasp-like fold
IPR011761	ATP-grasp fold
IPR001555	Phosphoribosylglycinamide formyltransferase, active site
IPR010918	AIR synthase related protein, C-terminal
IPR004733	Phosphoribosylformylglycinamidine cyclo-ligase
IPR011054	Rudiment single hybrid motif
IPR020561	Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain
IPR020560	Phosphoribosylglycinamide synthetase, C-domain
IPR020562	Phosphoribosylglycinamide synthetase, N-domain
IPR000728	AIR synthase related protein
IPR000115	Phosphoribosylglycinamide synthetase
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Aiba A, Mizobuchi K. Nucleotide sequence analysis of genes purH and purD involved in the de novo purine nucleotide biosynthesis of Escherichia coli. J. Biol. Chem. 264 21239-46 1989 [PubMed: 2687276] http://intl.jbc.org/cgi/reprint/264/35/21239.pdf

Additional Reading Open in usermanual
	Wang W, Kappock TJ, Stubbe J, Ealick SE. X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli. Biochemistry 37 1998 15647-62 [PubMed: 9843369] http://dx.doi.org/10.1021/bi981405n

InterPro 23.1