phosphoribosylamine-glycine ligase | |||||||||
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Identifiers | |||||||||
EC number | 6.3.4.13 | ||||||||
CAS number | 9032-01-3 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / EGO | ||||||||
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Search | |
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PMC | articles |
PubMed | articles |
NCBI | proteins |
Phosphoribosylglycinamide synthetase, N domain | |||||||||
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glycinamide ribonucleotide synthetase (gar-syn) from e. coli.
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Identifiers | |||||||||
Symbol | GARS_N | ||||||||
Pfam | PF02844 | ||||||||
InterPro | IPR020562 | ||||||||
PROSITE | PDOC00164 | ||||||||
SCOP | 1gso | ||||||||
SUPERFAMILY | 1gso | ||||||||
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Available protein structures: | |
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Pfam | structures |
PDB | RCSB PDB; PDBe; PDBj |
PDBsum | structure summary |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain | |||||||||
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glycinamide ribonucleotide synthetase (gar-syn) from e. coli.
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Identifiers | |||||||||
Symbol | GARS_A | ||||||||
Pfam | PF01071 | ||||||||
Pfam clan | CL0179 | ||||||||
InterPro | IPR020561 | ||||||||
PROSITE | PDOC00164 | ||||||||
SCOP | 1gso | ||||||||
SUPERFAMILY | 1gso | ||||||||
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Available protein structures: | |
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Pfam | structures |
PDB | RCSB PDB; PDBe; PDBj |
PDBsum | structure summary |
Phosphoribosylglycinamide synthetase, C domain | |||||||||
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crystal structure of phosphoribosylamine--glycine ligase (tm1250) from thermotoga maritima at 2.30 a resolution
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Identifiers | |||||||||
Symbol | GARS_C | ||||||||
Pfam | PF02843 | ||||||||
InterPro | IPR020560 | ||||||||
PROSITE | PDOC00164 | ||||||||
SCOP | 1gso | ||||||||
SUPERFAMILY | 1gso | ||||||||
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Available protein structures: | |
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Pfam | structures |
PDB | RCSB PDB; PDBe; PDBj |
PDBsum | structure summary |
In enzymology, phosphoribosylamine-glycine ligase, also known as glycinamide ribonucleotide synthetase (GARS), (EC 6.3.4.13) is an enzyme that catalyzes the chemical reaction
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.