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Search results 1 to 6 out of 6 for Gars

Category restricted to ProteinDomain (x)

0.017s

Categories

Category: ProteinDomain
Type Details Score
Protein Domain
Type: Family
Description: Phosphoribosylglycinamide synthetase () (GARS) (phosphoribosylamine glycine ligase) []catalyses the second step in the de novobiosynthesis 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 + Pi+ 5'-phosphoribosylglycinamideIn bacteria, GARS is a monofunctional enzyme (encoded by the purD gene). Inyeast, GARS is part of a bifunctional enzyme (encoded by the ADE5,7 gene) in conjunction with phosphoribosylformylglycinamidine cyclo-ligase (AIRS) []. In higher eukaryotes, GARS is part of a trifunctional enzyme in conjunction with AIRS and with phosphoribosylglycinamide formyltransferase (GART), forming GARS-AIRS-GART [].
Protein Domain
Type: Domain
Description: Phosphoribosylglycinamide synthetase () (GARS) (phosphoribosylamine glycine ligase) []catalyses the second step in the de novobiosynthesis 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 + Pi+ 5'-phosphoribosylglycinamideIn bacteria, GARS is a monofunctional enzyme (encoded by the purD gene). Inyeast, GARS is part of a bifunctional enzyme (encoded by the ADE5,7 gene) in conjunction with phosphoribosylformylglycinamidine cyclo-ligase (AIRS) []. In higher eukaryotes, GARS is part of a trifunctional enzyme in conjunction with AIRS and with phosphoribosylglycinamide formyltransferase (GART), forming GARS-AIRS-GART [].This entry represents the C-domain, which is related to the C-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase ().
Protein Domain
Type: Domain
Description: Phosphoribosylglycinamide synthetase () (GARS) (phosphoribosylamine glycine ligase) []catalyses the second step in the de novobiosynthesis 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 + Pi+ 5'-phosphoribosylglycinamideIn bacteria, GARS is a monofunctional enzyme (encoded by the purD gene). Inyeast, GARS is part of a bifunctional enzyme (encoded by the ADE5,7 gene) in conjunction with phosphoribosylformylglycinamidine cyclo-ligase (AIRS) []. In higher eukaryotes, GARS is part of a trifunctional enzyme in conjunction with AIRS and with phosphoribosylglycinamide formyltransferase (GART), forming GARS-AIRS-GART [].This entry represents the N-domain, which is related to the N-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase ().
Protein Domain
Type: Conserved_site
Description: Phosphoribosylglycinamide synthetase () (GARS) (phosphoribosylamine glycine ligase) []catalyses the second step in the de novobiosynthesis 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 + Pi+ 5'-phosphoribosylglycinamideIn bacteria, GARS is a monofunctional enzyme (encoded by the purD gene). Inyeast, GARS is part of a bifunctional enzyme (encoded by the ADE5,7 gene) in conjunction with phosphoribosylformylglycinamidine cyclo-ligase (AIRS) []. In higher eukaryotes, GARS is part of a trifunctional enzyme in conjunction with AIRS and with phosphoribosylglycinamide formyltransferase (GART), forming GARS-AIRS-GART [].This signature pattern identifies a highly conserved octapeptide.
Protein Domain
Type: Domain
Description: Phosphoribosylglycinamide synthetase () (GARS) (phosphoribosylamine glycine ligase) []catalyses the second step in the de novobiosynthesis 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 + Pi+ 5'-phosphoribosylglycinamideIn bacteria, GARS is a monofunctional enzyme (encoded by the purD gene). Inyeast, GARS is part of a bifunctional enzyme (encoded by the ADE5,7 gene) in conjunction with phosphoribosylformylglycinamidine cyclo-ligase (AIRS) []. In higher eukaryotes, GARS is part of a trifunctional enzyme in conjunction with AIRS and with phosphoribosylglycinamide formyltransferase (GART), forming GARS-AIRS-GART [].This entry represents the A-domain of the enzyme, and is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase.
Protein Domain
Type: Homologous_superfamily
Description: Phosphoribosylglycinamide synthetase () (GARS) (phosphoribosylamine glycine ligase) []catalyses the second step in the de novobiosynthesis 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 + Pi+ 5'-phosphoribosylglycinamideIn bacteria, GARS is a monofunctional enzyme (encoded by the purD gene). Inyeast, GARS is part of a bifunctional enzyme (encoded by the ADE5,7 gene) in conjunction with phosphoribosylformylglycinamidine cyclo-ligase (AIRS) []. In higher eukaryotes, GARS is part of a trifunctional enzyme in conjunction with AIRS and with phosphoribosylglycinamide formyltransferase (GART), forming GARS-AIRS-GART [].This entry represents the C-domain superfamily of the phosphoribosylglycinamide synthetase, which is related to the C-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase ().