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

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