- Deposition Date: 2006/03/09
- Description: NADH pyrophosphatase (EC 3.6.1.-).
- Solution Method: X-RAY
- Start: 1 End: 258 Sequence Type: Complete
- Fold Function: NADH pyrophosphatase
- Fold Summary: Class: alpha+beta. Duplication of NUDIX fold - beta(2)-alpha-beta(3)-alpha; 3 layers: alpha/beta/alpha; mixed sheet contains beta-grasp motif.
- Fold Description: NADH pyrophosphatase containing a strongly modified (aa1-124) and a classic (aa 128-256) NUDIX (NUcleoside DIphosphate linked to some other moiety X) hydrolase domain (PF00293) connected by a short linker. The C-terminal NUDIX domain is an alpha/beta/alpha fold with a six-stranded, mixed b-sheet flanked by two a-helices. The N-terminal domain is a novel variation of the NUDIX fold because it does not contain the a-helix between strands b3 and b4. It is fused to a small additional b-domain (residues 96 - 124) that forms a Zn-finger (coordinated by cysteines 98, 101, 116, 119), implicated in nucleic-acid binding. The active site is located in the crevice between the two domains adjacent to the conserved Arg 242 and the EEVxE-motif. The first structure of such enzyme and such combination of domains. Over 50 homologues in Prokaryotes and Eukaryotes.
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