The domain within your query sequence starts at position 266 and ends at position 428; the E-value for the NAD_binding_2 domain shown below is 2.6e-41.

DKKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEKCDLFIQEGARLGRTPAEVVSTCDI
TFACVSDPKAAKDLVLGPSGVLQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAP
VSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLGE

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.

GO process:oxidation-reduction process (GO:0055114)
GO function:phosphogluconate dehydrogenase (decarboxylating) activity (GO:0004616)

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