The domain within your query sequence starts at position 59 and ends at position 491; the E-value for the NAD_binding_5 domain shown below is 4.4e-141.

LGVMLVGWGGNNGSTLTAAVLANRLRLTWPTRTGRKEANYYGSLTQAGTVNLGLDENGRE
VFVPFSALLPMVAPNDLVFDGWDISSLNLAEAMRRAQVLDCGLQEQLWPHMESLRPRPSV
YIPEFIAANQTARADNLIPGTRAQQLEQIRKDIRDFRSSAGLDKVIVLWTANTERFCEVV
PGRNDTAENLLHTIQLGLEVSPSTLFAVASILEDCAFLNGSPQNTLVPGALELASQRHVF
VGGDDFKSGQTKVKSVLVDFLIGSGLKTMSIVSYNHLGNNDGQNLSAPLQFRSKEVTKSS
VVDDMVHSNHVLYAPGERPDHCVVIKYVPYVGDSKRALDEYTSELMLGGTNTLVLHNTCE
DSLLAAPIMLDLVLLTELCQRVSFCTDSDPEPQGFHTVLSLLSFLFKAPLVPPGSPVVNA
LFRQRSCIENIFR

NAD_binding_5

 NAD_binding_5
PFAM accession number:PF07994
Interpro abstract (IPR002587):

1L-myo-Inositol-1-phosphate synthase ( EC 5.5.1.4 ) catalyzes the conversion of D-glucose 6-phosphate to 1L-myo-inositol-1-phosphate, the first committed step in the production of all inositol-containing compounds, including phospholipids, either directly or by salvage. The enzyme exists in a cytoplasmic form in a wide range of plants, animals, and fungi. It has also been detected in several bacteria and a chloroplast form is observed in alga and higher plants. Inositol phosphates play an important role in signal transduction.

In Saccharomyces cerevisiae (Baker's yeast), the transcriptional regulation of the INO1 gene has been studied in detail [ (PUBMED:7975896) ] and its expression is sensitive to the availability of phospholipid precursors as well as growth phase. The regulation of the structural gene encoding 1L-myo-inositol-1-phosphate synthase has also been analyzed at the transcriptional level in the aquatic angiosperm, Spirodela polyrrhiza (Giant duckweed) and the halophyte, Mesembryanthemum crystallinum (Common ice plant) [ (PUBMED:9370339) ].

GO process:inositol biosynthetic process (GO:0006021), phospholipid biosynthetic process (GO:0008654)
GO function:inositol-3-phosphate synthase activity (GO:0004512)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry NAD_binding_5