The domain within your query sequence starts at position 163 and ends at position 280; the E-value for the NAD_binding_2 domain shown below is 2.1e-5.

GETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGIERALGLQRVSTLQDLLFHSDCV
TLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDV

NAD_binding_2

NAD_binding_2
PFAM accession number:PF03446
Interpro abstract (IPR006115):

6-Phosphogluconate dehydrogenase ( EC 1.1.1.44 ) (6PGD) is an oxidative carboxylase that catalyses the decarboxylating reduction of 6-phosphogluconate into ribulose 5-phosphate in the presence of NADP. This reaction is a component of the hexose mono-phosphate shunt and pentose phosphate pathways (PPP) [ (PUBMED:2113917) (PUBMED:6641716) ]. Prokaryotic and eukaryotic 6PGD are proteins of about 470 amino acids whose sequence are highly conserved [ (PUBMED:1659648) ]. The protein is a homodimer in which the monomers act independently [ (PUBMED:6641716) ]: each contains a large, mainly alpha-helical domain and a smaller beta-alpha-beta domain, containing a mixed parallel and anti-parallel 6-stranded beta sheet [ (PUBMED:6641716) ]. NADP is bound in a cleft in the small domain, the substrate binding in an adjacent pocket [ (PUBMED:6641716) ].

This family represents the NADP binding domain of 6-phosphogluconate dehydrogenase which adopts a Rossman fold. The C-terminal domain is described in IPR006114 .

This domain can also be found in 3-hydroxyisobutyrate dehydrogenases (HIBADH) and related proteins [ (PUBMED:16466957) ].

GO function:NADP binding (GO:0050661)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry NAD_binding_2