Protein Family Models

This domain precedes the ATP-grasp domain in a number of ribonucleotide synthetases [1-5]. Paper describing PDB structure 1b6r. [1]. 10569930. Three-dimensional structure of N5-carboxyaminoimidazole ribonucleotide synthetase: a member of the ATP grasp protein superfamily. Thoden JB, Kappock TJ, Stubbe J, Holden HM;. Biochemistry. 1999;38:15480-15492. Paper describing PDB structure 1eyz. [2]. 10913290. Molecular structure of Escherichia coli PurT-encoded glycinamide ribonucleotide transformylase. Thoden JB, Firestine S, Nixon A, Benkovic SJ, Holden HM;. Biochemistry. 2000;39:8791-8802. Paper describing PDB structure 1kj8. [3]. 11953435. PurT-encoded glycinamide ribonucleotide transformylase. Accommodation of adenosine nucleotide analogs within the active site. Thoden JB, Firestine SM, Benkovic SJ, Holden HM;. J Biol Chem. 2002;277:23898-23908. Paper describing PDB structure 3eth. [4]. 19053251. Structural analysis of the active site geometry of N5-carboxyaminoimidazole ribonucleotide synthetase from Escherichia coli. Thoden JB, Holden HM, Firestine SM;. Biochemistry. 2008;47:13346-13353. Paper describing PDB structure 3k5h. [5]. 20050602. Structural and functional studies of Aspergillus clavatus N(5)-carboxyaminoimidazole ribonucleotide synthetase . Thoden JB, Holden HM, Paritala H, Firestine SM;. Biochemistry. 2010;49:752-760. (from Pfam)

Date:

2024-10-16

This entry represents the C-terminal domain of the PurK enzyme. (from Pfam)

Date:

2024-08-14

Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines [2]. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. See Pfam:PF00988. The small chain has a GATase domain in the carboxyl terminus. See Pfam:PF00117. The ATP binding domain (this one) has an ATP-grasp fold. [1]. 7915138. Three-dimensional structure of the biotin carboxylase subunit. of acetyl-CoA carboxylase. Waldrop GL, Rayment I, Holden HM;. Biochemistry 1994;33:10249-10256. [2]. 1972379. Mammalian carbamyl phosphate synthetase (CPS). DNA sequence and evolution of the CPS domain of the Syrian hamster multifunctional protein CAD. Simmer JP, Kelly RE, Rinker AG Jr, Scully JL, Evans DR;. Biol Chem 1990;265:10395-10402. [3]. 10089390. The structure of carbamoyl phosphate synthetase determined to 2.1 A resolution. Thoden JB, Raushel FM, Benning MM, Rayment I, Holden HM;. Acta Crystallogr D Biol Crystallogr 1999;55:8-24. (from Pfam)

Date:

2024-10-16

This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity. [1]. 9416615. A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. Galperin MY, Koonin EV;. Protein Sci 1997;6:2639-2643. (from Pfam)

Date:

2024-10-16

Date:

2020-10-26

Date:

2021-07-30

Phosphoribosylaminoimidazole carboxylase is a fusion protein in plants and fungi, but consists of two non-interacting proteins in bacteria, PurK and PurE. This model represents PurK, N5-carboxyaminoimidazole ribonucleotide synthetase (EC 6.3.4.18), which hydrolyzes ATP and converts AIR to N5-CAIR. PurE converts N5-CAIR to CAIR. In the presence of high concentrations of bicarbonate, PurE is reported able to convert AIR to CAIR directly and without ATP.

Gene:

purK

Date:

2021-12-08

5-(carboxyamino)imidazole ribonucleotide synthase catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR)

Date:

2024-11-14