Protein Family Models

This is the N-terminal domain of bacterial AMP nucleoside phosphorylase (AMNp). The N- and C-termini form distinct domains which intertwine with each other to form a stable monomer which associates with five other monomers to yield the active hexamer. The N-terminus consists of a long helix and a four-stranded sheet with a novel topology. The C-terminus binds the nucleoside whereas the N-terminus acts as the enzymatic regulatory domain. AMNp (EC:3.2.2.4) catalyses the hydrolysis of AMP to form adenine and ribose 5-phosphate. thereby regulating intracellular AMP levels [1]. [1]. 15296732. Structure of Escherichia coli AMP nucleosidase reveals. similarity to nucleoside phosphorylases.. Zhang Y, Cottet SE, Ealick SE;. Structure. 2004;12:1383-1394. (from Pfam)

Date:

2024-07-12

Members of this family include: purine nucleoside phosphorylase (PNP) Uridine phosphorylase (UdRPase) 5'-methylthioadenosine phosphorylase (MTA phosphorylase) [1]. 7920254. Unexpected sequence similarity between nucleosidases and. phosphoribosyltransferases of different specificity.. Mushegian AR, Koonin EV;. Protein Sci 1994;3:1081-1088.. [2]. 9351810. The crystal structure of Escherichia coli purine nucleoside. phosphorylase: a comparison with the human enzyme reveals a. conserved topology.. Mao C, Cook WJ, Zhou M, Koszalka GW, Krenitsky TA, Ealick SE;. Structure 1997;5:1373-1383. (from Pfam)

Date:

2024-07-09

This model represents the AMP nucleosidase from proteobacteria but also including a sequence from Corynebacterium, a gram-positive organism. The species from E. coli has been most well studied [1].

Gene:

amn

Date:

2024-06-10

Catalyzes the hydrolysis of AMP to form adenine and ribose 5-phosphate using water as the nucleophile

Date:

2021-08-24