Protein Family Models

This entry represents the PurM_N-like domain of formylglycinamide ribonucleotide amidotransferase (FGAR-AT) and related proteins. FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) to formylglycinamidine ribonucleotide (FGAM) in the fourth step of the purine biosynthetic pathway. This domain consists of an antiparallel beta-sheet with two helices packed on one side [1-5]. Paper describing PDB structure 1vk3. [1]. 16544324. Crystal structure of phosphoribosylformylglycinamidine synthase II (smPurL) from Thermotoga maritima at 2.15 A resolution. Mathews II, Krishna SS, Schwarzenbacher R, McMullan D, Abdubek P, Ambing E, Canaves JM, Chiu HJ, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Jaroszewski L, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, Levin I, Miller MD, Moy K, Nigoghossian E, Paulsen J, Quijano K, Reyes R, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Wilson IA;. Proteins. 2006;63:1106-1111. Paper describing PDB structure 2hru. [2]. 17154526. Complexed structures of formylglycinamide ribonucleotide amidotransferase from Thermotoga maritima describe a novel ATP binding protein superfamily. Morar M, Anand R, Hoskins AA, Stubbe J, Ealick SE;. Biochemistry. 2006;45:14880-14895. Paper describing PDB structure 2z1e. [3]. 17612488. Crystal structures of [NiFe] hydrogenase maturation proteins HypC, HypD, and HypE: insights into cyanation reaction by thiol redox signaling. Watanabe S, Matsumi R, Arai T, Atomi H, Imanaka T, Miki K;. Mol Cell. 2007;27:29-40. Paper d. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

This is the N-terminal domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT), also known as Phosphoribosylformylglycinamidine synthase (EC:6.3.5.3), PurL and formylglycinamidine ribonucleotide (FGAM) synthase. This enzyme catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide and glutamine to formylglycinamidine ribonucleotide, ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway [3]. [1]. 15301531. Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography. Anand R, Hoskins AA, Stubbe J, Ealick SE;. Biochemistry. 2004;43:10328-10342. [2]. 22683785. Formylglycinamide ribonucleotide amidotransferase from Salmonella typhimurium: role of ATP complexation and the glutaminase domain in catalytic coupling. Tanwar AS, Morar M, Panjikar S, Anand R;. Acta Crystallogr D Biol Crystallogr. 2012;68:627-636. [3]. 24223728. Importance of hydrophobic cavities in allosteric regulation of formylglycinamide synthetase: insight from xenon trapping and statistical coupling analysis. Tanwar AS, Goyal VD, Choudhary D, Panjikar S, Anand R;. PLoS One. 2013;8:e77781. (from Pfam)

Date:

2024-10-16

This is the linker domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT), also known as Phosphoribosylformylglycinamidine synthase (EC:6.3.5.3), PurL and formylglycinamidine ribonucleotide (FGAM) synthase. This enzyme catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. The structure analysis of Salmonella typhimurium FGAR-AT reveals that this linker domain is made up of a long hydrophilic belt with an extended conformation [4]. [1]. 16544324. Crystal structure of phosphoribosylformylglycinamidine synthase II (smPurL) from Thermotoga maritima at 2.15 A resolution. Mathews II, Krishna SS, Schwarzenbacher R, McMullan D, Abdubek P, Ambing E, Canaves JM, Chiu HJ, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Jaroszewski L, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, Levin I, Miller MD, Moy K, Nigoghossian E, Paulsen J, Quijano K, Reyes R, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Wilson IA;. Proteins. 2006;63:1106-1111. [2]. 17154526. Complexed structures of formylglycinamide ribonucleotide amidotransferase from Thermotoga maritima describe a novel ATP binding protein superfamily. Morar M, Anand R, Hoskins AA, Stubbe J, Ealick SE;. Biochemistry. 2006;45:14880-14895. [3]. 18597481. Formylglycinamide ribonucleotide amidotransferase from Thermotoga maritima: structural insights into complex formation. Morar M, Hoskins. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

This family captures members that are not found in Pfam:PF00310, Pfam:PF07685 and Pfam:PF13230. [1]. 10966576. The synthetase domains of cobalamin biosynthesis amidotransferases cobB and cobQ belong to a new family of ATP-dependent amidoligases, related to dethiobiotin synthetase. Galperin MY, Grishin NV;. Proteins 2000;41:238-247. (from Pfam)

Date:

2024-10-16

This family includes Hydrogen expression/formation protein HypE Swiss:P24193, AIR synthases Swiss:P08178 EC:6.3.3.1, FGAM synthase Swiss:P35852 EC:6.3.5.3 and selenide, water dikinase Swiss:P16456 EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site [1]. [1]. 10508786. X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution. Li C, Kappock TJ, Stubbe J, Weaver TM, Ealick SE;. Structure Fold Des 1999;7:1155-1166. (from Pfam)

Date:

2024-10-16

phosphoribosylformylglycinamidine synthase catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate

Date:

2023-03-16

This HMM represents a single-molecule form of phosphoribosylformylglycinamidine synthase, also called FGAM synthase, an enzyme of purine de novo biosynthesis. This form is found mostly in eukaryotes and Proteobacteria. In Bacillus subtilis PurL (FGAM synthase II) and PurQ (FGAM synthase I), homologous to different parts of this model, perform the equivalent function; the unrelated small protein PurS is also required and may be a third subunit.

Gene:

purL

Date:

2021-04-27

Gene:

purL

Date:

2021-07-22