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Phosphoribosylglycinamide synthetase, N domain
Phosphoribosylglycinamide synthetase 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. This domain is related to the N-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see Pfam:PF00289). This domain is structurally related to the PreATP-grasp domain. [1]. 2687276. Nucleotide sequence analysis of genes purH and purD involved in. the de novo purine nucleotide biosynthesis of Escherichia coli.. Aiba A, Mizobuchi K;. J Biol Chem 1989;264:21239-21246.. [2]. 9843369. X-ray crystal structure of glycinamide ribonucleotide synthetase. from Escherichia coli.. Wang W, Kappock TJ, Stubbe J, Ealick SE;. Biochemistry 1998;37:15647-15662. (from Pfam)
phosphoribosylglycinamide synthetase C domain-containing protein
Phosphoribosylglycinamide synthetase 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. This domain is related to the C-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see Pfam:PF02787). [1]. 2687276. Nucleotide sequence analysis of genes purH and purD involved in. the de novo purine nucleotide biosynthesis of Escherichia coli.. Aiba A, Mizobuchi K;. J Biol Chem 1989;264:21239-21246.. [2]. 9843369. X-ray crystal structure of glycinamide ribonucleotide synthetase. from Escherichia coli.. Wang W, Kappock TJ, Stubbe J, Ealick SE;. Biochemistry 1998;37:15647-15662. (from Pfam)
ATP-grasp domain-containing protein
No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman). (from Pfam)
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain
Phosphoribosylglycinamide synthetase 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. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see Pfam:PF02786). [1]. 2687276. Nucleotide sequence analysis of genes purH and purD involved in. the de novo purine nucleotide biosynthesis of Escherichia coli.. Aiba A, Mizobuchi K;. J Biol Chem 1989;264:21239-21246.. [2]. 9843369. X-ray crystal structure of glycinamide ribonucleotide synthetase. from Escherichia coli.. Wang W, Kappock TJ, Stubbe J, Ealick SE;. Biochemistry 1998;37:15647-15662. (from Pfam)
phosphoribosylamine--glycine ligase
phosphoribosylamine--glycine ligase catalyzes the second step of the de novo purine biosynthetic pathway; the conversion of phosphoribosylamine, glycine, and ATP to glycinamide ribonucleotide (GAR), ADP, and Pi
Phosphoribosylamine--glycine ligase catalyzes the formation of N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-D-ribosylamine and glycine in purine biosynthesis. It is also called glycinamide ribonucleotide synthetase (GARS). This enzyme appears as a monofunctional protein in prokaryotes but as part of a larger, multidomain protein in eukaryotes.
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