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MazG nucleotide pyrophosphohydrolase domain-containing protein
This domain is about 100 amino acid residues in length. It is found in the MazG protein from E. coli. It contains four conserved negatively charged residues that probably form an active site or metal binding site. This domain is found in isolation in some proteins as well as associated with Pfam:PF00590. This domain is clearly related to Pfam:PF01503 another pyrophosphohydrolase involved in histidine biosynthesis. This family may be structurally related to the NUDIX domain Pfam:PF00293 (Bateman A pers. obs.). [1]. 12218018. MazG, a nucleoside triphosphate pyrophosphohydrolase, interacts with Era, an essential GTPase in Escherichia coli. Zhang J, Inouye M;. J Bacteriol 2002;184:5323-5329. (from Pfam)
Phosphoribosyl-ATP pyrophosphohydrolase
This enzyme catalyses the second step in the histidine biosynthetic pathway. [1]. 379004. The product of the his4 gene cluster in Saccharomyces cerevisiae. A trifunctional polypeptide. Keesey JK Jr, Bigelis R, Fink GR;. J Biol Chem 1979;254:7427-7433. [2]. 3528746. Primary and secondary structural homologies between the HIS4 gene product of Saccharomyces cerevisiae and the hisIE and hisD gene products of Escherichia coli and Salmonella typhimurium. Bruni CB, Carlomagno MS, Formisano S, Paolella G;. Mol Gen Genet 1986;203:389-396. (from Pfam)
phosphoribosyl-ATP diphosphatase
phosphoribosyl-ATP diphosphatase (PRA-PH) catalyzes the hydrolysis of 1-(5-phosphoribosyl)-ATP to form 1-(5-phosphoribosyl)-AMP and diphosphate, which is the second step in the histidine biosynthetic pathway
This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, catalyses the second step in the histidine biosynthesis pathway. It often occurs as a fusion protein. This model a somewhat narrower scope than Pfam model PF01503, as some paralogs that appear to be functionally distinct are excluded from this model.
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