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Links from Protein

Items: 11

1.

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)

GO Terms:
Molecular Function:
phosphoribosylamine-glycine ligase activity (GO:0004637)
Biological Process:
purine nucleobase biosynthetic process (GO:0009113)
Date:
2024-08-14
Family Accession:
NF014857.5
Method:
HMM
2.

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)

GO Terms:
Molecular Function:
phosphoribosylamine-glycine ligase activity (GO:0004637)
Biological Process:
purine nucleobase biosynthetic process (GO:0009113)
Date:
2024-08-14
Family Accession:
NF014856.5
Method:
HMM
3.

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)

Date:
2024-08-14
Family Accession:
NF013254.5
Method:
HMM
4.
new record, indexing in progress
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5.
new record, indexing in progress
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6.
new record, indexing in progress
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7.
new record, indexing in progress
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8.
new record, indexing in progress
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9.
new record, indexing in progress
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10.

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

Date:
2023-03-17
Family Accession:
11414962
Method:
Sparcle
11.

phosphoribosylamine--glycine ligase

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.

Gene:
purD
GO Terms:
Molecular Function:
phosphoribosylamine-glycine ligase activity (GO:0004637)
Biological Process:
purine nucleobase biosynthetic process (GO:0009113)
Date:
2024-06-10
Family Accession:
TIGR00877.1
Method:
HMM
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