The domain within your query sequence starts at position 10 and ends at position 149; the E-value for the Sacchrp_dh_NADP domain shown below is 2.4e-28.

LVVFGASGFTGQFVTEEVAREQIASEQSSRLPWAVAGRSKEKLQQVLEKAAQKLGRPSLS
SEVGVIICDISNPASLDEMAKQAKLVLNCVGPYRFYGEPVVKACIENGTSCIDICGEPQF
LELMHAKYHEKAAEKGVYII

Sacchrp_dh_NADP

• PFAM accession number: PF03435
• Interpro abstract (IPR005097):

  This entry represents the NADP binding domain of saccharopine dehydrogenase. In some organisms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase [ (PUBMED:11080625) (PUBMED:11354603) ].

  Saccharopine dehydrogenase ( EC 1.5.1.10 ) catalyses the condensation of l-alpha-aminoadipate-delta-semialdehyde (AASA) with l-glutamate to give an imine, which is reduced by NADPH to give saccharopine [ (PUBMED:19449898) ]. In some organisms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase (PF). Saccharopine dehydrogenase can also function as a saccharopine reductase. Saccharopine is an intermediate in lysine metabolism.

  Homospermidine synthase (HSS) ( EC 2.5.1.44 ) catalyses the synthesis of the polyamine homospermidine from 2 putrescine molecules in an NAD ⁺ -dependent reaction [ (PUBMED:8841401) ]. HSS evolved from the alternative spermidine biosynthetic pathway enzyme carboxyspermidine dehydrogenase [ (PUBMED:19196710) (PUBMED:20194510) ] and the structure of HSS is related to lysine metabolic enzymes [ (PUBMED:20194510) ].

• GO process: oxidation-reduction process (GO:0055114)
• GO function: oxidoreductase activity (GO:0016491)

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