Phosphoribosylamine—glycine ligase

Phosphoribosylamine—glycine ligase
phosphoribosylamine-glycine ligase monomer (fragment), Human
Identifiers
EC no.6.3.4.13
CAS no.9032-01-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Phosphoribosylglycinamide synthetase, N domain
glycinamide ribonucleotide synthetase (gar-syn) from e. coli.
Identifiers
SymbolGARS_N
PfamPF02844
InterProIPR020562
PROSITEPDOC00164
SCOP21gso / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain
glycinamide ribonucleotide synthetase (gar-syn) from e. coli.
Identifiers
SymbolGARS_A
PfamPF01071
Pfam clanCL0179
InterProIPR020561
PROSITEPDOC00164
SCOP21gso / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Phosphoribosylglycinamide synthetase, C domain
crystal structure of phosphoribosylamine--glycine ligase (tm1250) from thermotoga maritima at 2.30 a resolution
Identifiers
SymbolGARS_C
PfamPF02843
InterProIPR020560
PROSITEPDOC00164
SCOP21gso / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Phosphoribosylamine—glycine ligase, also known as glycinamide ribonucleotide synthetase (GARS), (EC 6.3.4.13) is an enzyme that catalyzes the chemical reaction

ATP + 5-phospho-D-ribosylamine + glycine ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide

which is the second step in purine biosynthesis. The 3 substrates of this enzyme are ATP, 5-phospho-D-ribosylamine, and glycine, whereas its 3 products are ADP, phosphate, and N1-(5-phospho-D-ribosyl)glycinamide.

This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds.

In bacteria, GARS is a monofunctional enzyme (encoded by the purD gene). The purD genes often contain PurD RNA motif in their 5' UTR. In yeast, GARS is part of a bifunctional enzyme (encoded by the ADE5/7 gene) in conjunction with phosphoribosylformylglycinamidine cyclo-ligase (AIRS). In higher eukaryotes, including humans, GARS is part of a trifunctional enzyme in conjunction with AIRS and with phosphoribosylglycinamide formyltransferase (GART), forming GARS-AIRS-GART.